Datasets:

lhallee

/

exp_new_unprocessed

like 0

A0A0H3JUU7

MRQWTAIHLAKLARKASRAVGKRGTDLPGQIARKVDTDVLRKLAEQVDDIVFISGTNGKTTTSNLIGHTLKANNIQIIHNNEGANMAAGITSAFIMQSTPKTKIAVIEIDEGSIPRVLKEVTPSMMVFTNFFRDQMDRFGEIDIMVNNIAETISNKGIKLLLNADDPFVSRLKIASDTIVYYGMKAHAHEFEQSTMNESRYCPNCGRLLQYDYIHYNQIGHYHCQCGFKREQAKYEISSFDVAPFLYLNINDEKYDMKIAGDFNAYNALAAYTVLRELGLNEQTIKNGFETYTSDNGRMQYFKKERKEAMINLAKNPAGMNASLSVGEQLEGEKVYVISLNDNAADGRDTSWIYDADFEKLSKQQIEAIIVTGTRAEELQLRLKLAEVEVPIIVERDIYKATAKTMDYKGFTVAIPNYTSLAPMLEQLNRSFEGGQS

Staphylococcus aureus (strain N315)

FUNCTION: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide (PubMed:22291598, PubMed:30154570). The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue (PubMed:22291598). {ECO:0000269|PubMed:22291598, ECO:0000269|PubMed:30154570}.

6.3.5.13

CATALYTIC ACTIVITY: Reaction=ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:57928, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:60033, ChEBI:CHEBI:62233, ChEBI:CHEBI:456216; EC=6.3.5.13; Evidence={ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:22291598, ECO:0000269|PubMed:30154570}; CATALYTIC ACTIVITY: Reaction=ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-O-P-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate; Xref=Rhea:RHEA:59488, ChEBI:CHEBI:30616, ChEBI:CHEBI:60033, ChEBI:CHEBI:143132, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:22291598}; CATALYTIC ACTIVITY: Reaction=beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-O-P-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + NH4(+) = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:57932, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:43474, ChEBI:CHEBI:62233, ChEBI:CHEBI:143132; Evidence={ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:22291598};

PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:22291598}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-7.8 for isoglutaminyl synthase activity. {ECO:0000269|PubMed:22291598};

3D-structure;ATP-binding;Cell shape;Cell wall biogenesis/degradation;Ligase;Metal-binding;Nucleotide-binding;Peptidoglycan synthesis;Zinc

cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]

acid-amino acid ligase activity [GO:0016881]; ATP binding [GO:0005524]; carbon-nitrogen ligase activity on lipid II [GO:0140282]; zinc ion binding [GO:0008270]

DOMAIN: Composed of two domains: a Mur ligase middle domain containing the canonical ATP binding site and a ribbon-type zinc finger, and a C-terminal Mur ligase domain. The GatD/MurT complex has an open, boomerang-shaped conformation in which GatD is docked onto one end of MurT. Both proteins contribute to the catalytic triad. {ECO:0000269|PubMed:30154570}.

IPR043703;IPR036565;IPR013221;IPR013564;

3.40.1190.10;

A0A0H3KB22

MTYAVKEIFYTLQGEGANAGRPAVFCRFAGCNLWSGREEDRAQAVCRFCDTDFVGTDGENGGKFKDADALVATIAGLWPAGEAHRFVVCTGGEPMLQLDQPLVDALHAAGFGIAIETNGSLPVLESIDWICVSPKADAPLVVTKGNELKVVIPQDNQRLADYAKLDFEYFLVQPMDGPSRDLNTKLAIDWCKRHPQWRLSMQTHKYLNIP

Burkholderia multivorans (strain ATCC 17616 / 249)

FUNCTION: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}.

4.3.99.3

CATALYTIC ACTIVITY: Reaction=6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-deazaguanine + NH4(+); Xref=Rhea:RHEA:27974, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:61032, ChEBI:CHEBI:61036; EC=4.3.99.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703};

COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}; COFACTOR: Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}; Note=Binds 1 S-adenosyl-L-methionine per subunit. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703};

PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000305|PubMed:24362703}.

3D-structure;4Fe-4S;Iron;Iron-sulfur;Lyase;Magnesium;Metal-binding;Queuosine biosynthesis;Reference proteome;S-adenosyl-L-methionine

queuosine biosynthetic process [GO:0008616]

4 iron, 4 sulfur cluster binding [GO:0051539]; carbon-nitrogen lyase activity [GO:0016840]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; S-adenosyl-L-methionine binding [GO:1904047]

IPR024924;IPR013785;IPR030977;IPR007197;

3.20.20.70;

A0A0H3LCC3

MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKGAKEVETKEQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDPERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIGAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLTLENADLSLLGKARKVVVTKDETTIVEGAGDTDAIAGRVAQIRQEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVTLLQAAPTLDELKLEGDEATGANIVKVALEAPLKQIAFNSGLEPGVVAEKVRNLPAGHGLNAQTGVYEDLLAAGVADPVKVTRSALQNAASIAGLFLTTEAVVADKPEKEKASVPGGGDMGGMDF

Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)

FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000256|HAMAP-Rule:MF_00600, ECO:0000256|RuleBase:RU000419}.

5.6.1.7

CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00600};

ATP-binding;Chaperone;Coiled coil;Cytoplasm;Isomerase;Nucleotide-binding;Reference proteome

adhesion of symbiont to host [GO:0044406]; chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of type II interferon production [GO:0032729]; protein import into mitochondrial intermembrane space [GO:0045041]; protein refolding [GO:0042026]; response to heat [GO:0009408]

capsule [GO:0042603]; cell surface [GO:0009986]; GroEL-GroES complex [GO:1990220]; host cell surface [GO:0044228]

ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; host cell surface binding [GO:0046812]; isomerase activity [GO:0016853]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]

SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}. Secreted, capsule {ECO:0000256|ARBA:ARBA00025702}. Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.

IPR018370;IPR001844;IPR002423;IPR027409;IPR027413;IPR027410;

3.50.7.10;1.10.560.10;3.30.260.10;

A0A0H3LHU4

MTEKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGLAFDGSSIRGFQSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLEPYSRDPRNIARKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGSFYEVDAISGWWNTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDKMLTNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKNTAWQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDTARHYIGGLLHHAPSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACVRIPITGSNPKAKRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPVDKDLYELPPEEAASIPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETWISFKRENEIEPVNIRPHPYEFALYYDV

Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)

6.3.1.2

CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000256|ARBA:ARBA00000777, ECO:0000256|RuleBase:RU004356};

ATP-binding;Cytoplasm;Ligase;Magnesium;Nucleotide-binding;Phosphoprotein;Reference proteome

glutamine biosynthetic process [GO:0006542]; nitrogen utilization [GO:0019740]; protein homooligomerization [GO:0051260]

cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]

ADP binding [GO:0043531]; ATP binding [GO:0005524]; cobalt ion binding [GO:0050897]; GDP binding [GO:0019003]; glutamine synthetase activity [GO:0004356]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU000387}.

IPR008147;IPR036651;IPR014746;IPR008146;IPR027303;IPR004809;IPR001637;IPR027302;

3.10.20.70;3.30.590.10;

A0A0H3NK84

MIPPLNRYVPALSKNELVKTVTNRDIQFTSFNGKDYPLCFLDEKTPLLFQWFERNPARFGKNDIPIINTEKNPYLNNIIKAATIEKERLIGIFVDGDFFPGQKDAFSKLEYDYENIKVIYRNDIDFSMYDKKLSEIYMENISKQESMPEEKRDCHLLQLLKKELSDIQEGNDSLIKSYLLDKGHGWFDFYRNMAMLKAGQLFLEADKVGCYDLSTNSGCIYLDADMIITEKLGGIYIPDGIAVHVERIDGRASMENGIIAVDRNNHPALLAGLEIMHTKFDADPYSDGVCNGIRKHFNYSLNEDYNSFCDFIEFKHDNIIMNTSQFTQSSWARHVQ

Salmonella typhimurium (strain SL1344)

FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis (PubMed:30327479, PubMed:32766249). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins TRADD and, to a lower extent, FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling (PubMed:30327479, PubMed:30902834, PubMed:32766249). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host GAPDH protein, thereby preventing GAPDH interaction with TRAF2, leading to inhibit NF-kappa-B signaling (By similarity). Catalyzes GlcNAcylation of host tubulin-folding cofactor TBCB, thereby promoting microtubule stability (By similarity). Also mediates auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (PubMed:32432056). {ECO:0000250|UniProtKB:Q9L9J3, ECO:0000269|PubMed:30327479, ECO:0000269|PubMed:30902834, ECO:0000269|PubMed:32432056, ECO:0000269|PubMed:32766249}.

2.4.1.-

CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP; Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:167322; Evidence={ECO:0000269|PubMed:30327479, ECO:0000269|PubMed:30902834, ECO:0000269|PubMed:32432056, ECO:0000269|PubMed:32766249}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66633; Evidence={ECO:0000269|PubMed:30327479, ECO:0000269|PubMed:30902834, ECO:0000269|PubMed:32432056, ECO:0000269|PubMed:32766249};

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:30327479};

3D-structure;Glycoprotein;Glycosyltransferase;Host cytoplasm;Manganese;Metal-binding;Secreted;Toxin;Transferase;Virulence

extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell cytosol [GO:0044164]

manganese ion binding [GO:0030145]; protein-arginine N-acetylglucosaminyltransferase activity [GO:0106362]; toxin activity [GO:0090729]

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9L9J3}. Host cytoplasm, host cytosol {ECO:0000305|PubMed:32432056}. Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 T3SS). {ECO:0000250|UniProtKB:Q9L9J3}.

PTM: Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins. {ECO:0000269|PubMed:32432056}.

DOMAIN: Adopts a GT-A fold and acts as an inverting enzyme that converts the alpha-configuration in the UDP-N-acetyl-alpha-D-glucosamine donor to the beta configuration in the N-linked (GlcNAc) arginine product. {ECO:0000269|PubMed:30327479, ECO:0000269|PubMed:30463645}.

A0A0H3PEK7

MRFDFFVSKRLNISRNKALELIENEEVLLNGKSFKASFDVKNFLENLKKTQDLNPEDILLTDGLKLDLLSEIYVSRAALKLKNFLEENGIEIKHKNCLDIGSSTGGFVQILLENQALKITALDVGNNQLHLSLRTNEKIILHENTDLRTFKSEEKFELITCDVSFISLINLLYYIDNLALKEIILLFKPQFEVGKNIKRDKKGVLKDDKAILKARMDFEKACAKLGWLLKNTQKSSIKGKEGNVEYFYYYIKN

Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)

FUNCTION: Catalyzes the 2'-O-methylation at nucleotide C1920 in 23S rRNA (PubMed:24796671, PubMed:29404277). Enhances motility (PubMed:24796671, PubMed:29404277, PubMed:32134554). Enhances biofilm formation (PubMed:29404277, PubMed:32134554). Involved in the assembly of 70S ribosomes (PubMed:24796671). Involved in virulence by promoting adherence and invasion to host cells (PubMed:18389311, PubMed:23971210, PubMed:32134554). Involved in pathogenicity by modulating secretion of host-protective chemokine interleukin 8 (IL-8) (PubMed:32134554). Involved in susceptibility to antibiotic capreomycin (PubMed:24796671, PubMed:32134554). {ECO:0000269|PubMed:18389311, ECO:0000269|PubMed:23971210, ECO:0000269|PubMed:24796671, ECO:0000269|PubMed:29404277, ECO:0000269|PubMed:32134554}.

2.1.1.226

CATALYTIC ACTIVITY: Reaction=cytidine(1920) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1920) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43200, Rhea:RHEA-COMP:10403, Rhea:RHEA-COMP:10404, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.226; Evidence={ECO:0000269|PubMed:24796671, ECO:0000269|PubMed:29404277}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43201; Evidence={ECO:0000269|PubMed:24796671, ECO:0000269|PubMed:29404277};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.8 uM for 50S ribosomal subunit (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:24796671}; KM=5.8 uM for S-adenosyl-L-methionine (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:24796671}; Note=kcat is 0.0048 min(-1) for 50S ribosomal subunit. kcat is 0.0044 min(-1) for S-adenosyl-L-methionine. {ECO:0000269|PubMed:24796671};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: High methylation activity of the 50S ribosomal subunit at 37 degrees Celsius. Loss of activity at 42 degrees Celsius. {ECO:0000269|PubMed:24796671};

Methyltransferase;RNA-binding;rRNA processing;S-adenosyl-L-methionine;Transferase;Virulence

cell motility [GO:0048870]; cellular response to antibiotic [GO:0071236]; cytosolic ribosome assembly [GO:0042256]; rRNA 2'-O-methylation [GO:0000451]; viral process [GO:0016032]

RNA binding [GO:0003723]; rRNA methyltransferase activity [GO:0008649]

IPR002877;IPR036986;IPR029063;IPR047048;

3.10.290.10;3.40.50.150;

A0A0J9UVG7

MRLLRPTPRLSSIFSSKTATSNLRFFTAMAPHNDVGAFHEALRSSKRILALCGAGLSASSGLPTFRGAGGLWRNHDATSLATLSAFKNDPGLVWLFYNYRRHMCLRAEPNPAHYALAALAEKNKDFLCLTQNVDNLSQQAGHPQDQLRTLHGSLFDIKCTNCDWIQRGNYDDPFCPALAPASVDVEPGKPFPLLDASLPLDPISPDDIPKCPQCKIGFQRPGVVWFGENLDEVMMMGITNWLLEDKVDLMLVIGTSAQVYPAAGYIDKAKRKGARIAVINPEAENEEEMYKVKPGDFAFGKDAAEYLPLLLEPVIGKLETDKKERS

Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato)

FUNCTION: NAD-dependent protein-lysine deacylase that decrotonylates the PDC (pyruvate dehydrogenase complex) subunit LAT1 at 'Lys-148' to inhibit PDC activity and consequently ATP production (PubMed:34927582). Also decrotonylates histone H3 crotonylated at 'Lys-18' (H3K18cr), to repress the expression of genes involved in aerobic respiration (PubMed:34927582). May also act as a NAD-dependent deacetylase (By similarity). Does not mediate desuccinylation, demalonylation, or deglutarylation of LAT1 (PubMed:34927582). {ECO:0000250|UniProtKB:P06700, ECO:0000269|PubMed:34927582}.

2.3.1.-; 2.3.1.286

CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:35899, ChEBI:CHEBI:137954; Evidence={ECO:0000269|PubMed:34927582};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9NXA8}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NXA8};

Chromatin regulator;Chromosome;Cytoplasm;Metal-binding;Mitochondrion;NAD;Nucleus;Reference proteome;Transferase;Transit peptide;Zinc

negative regulation of cellular respiration [GO:1901856]

chromosome [GO:0005694]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]

metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; NAD-dependent histone decrotonylase activity [GO:0160012]; NAD-dependent protein decrotonylase activity [GO:0160011]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuccinylase activity [GO:0036055]

SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:34927582}. Cytoplasm, cytosol {ECO:0000269|PubMed:34927582}. Nucleus {ECO:0000269|PubMed:34927582}. Chromosome {ECO:0000269|PubMed:34927582}.

IPR029035;IPR003000;IPR026591;IPR027546;IPR026590;

3.30.1600.10;3.40.50.1220;

A0A0K0JFP3

MLGLLTITSVFRNWRNSLQRKEDYDECHMRGINNENEISGKSEKNFKLDEPPISLETVMAEFKLSNETLRRMMAHMSRNMDKGLEGGPENSTISMLPSFVPELPNGTEEGRFIAMDLGGTNLRVMLMDIKPGEELKTEQFNTRIPNWAMRGTGEQLFDYITKCLAEFLIEKGIENDGLPVGFTFSYPCDQKSLRSATLLRWTKGFETTGVVGEDVVELLEQSIARRGDIKVEVVALINDTVGTMVAAAHESGGECHIGVIIATGTNASYMEDTSKIKYGLSKAIAAYNYPEMIIDTEWGGFGDRSEADYILTQYDKIVDSRSEHPGVNTFDKLVGGKCMGEVVRVVLEKLTRARVLFNGKGSDALFQQDSFPTKYISEILRDESGSYVHTRDILGELGIDHYSFSDMLLLREVCVVVSRRSANLGAAAIACVLNRVRKQNMVVGIDGSTYKYHPFFDFWVHDKLKELVDPGLKFKLLQTADGSGKGAALITAIVARLKKRNLKQQQQQQQQQQQHVTMVEQNVVEQIAETKGSREQFMNGNQKINLVTNDIPIYDSFNGDIENGVIHLSTDH

Brugia malayi (Filarial nematode worm)

FUNCTION: Active against glucose, fructose, mannose, maltose and galactose. {ECO:0000269|PubMed:18499511}.

2.7.1.1

CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000269|PubMed:18499511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidence={ECO:0000269|PubMed:18499511}; CATALYTIC ACTIVITY: Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+); Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:18499511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029; Evidence={ECO:0000269|PubMed:18499511}; CATALYTIC ACTIVITY: Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:18499511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; Evidence={ECO:0000269|PubMed:18499511}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:18499511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence={ECO:0000269|PubMed:18499511};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.035 mM for glucose {ECO:0000269|PubMed:18499511}; KM=75 mM for fructose {ECO:0000269|PubMed:18499511}; KM=1.09 mM for ATP {ECO:0000269|PubMed:18499511};

PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000269|PubMed:18499511}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000269|PubMed:18499511}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.4. {ECO:0000269|PubMed:18499511};

ATP-binding;Glycolysis;Kinase;Nucleotide-binding;Reference proteome;Transferase

glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; hexose metabolic process [GO:0019318]; intracellular glucose homeostasis [GO:0001678]

cytosol [GO:0005829]; mitochondrion [GO:0005739]

ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; mannokinase activity [GO:0019158]

IPR043129;IPR001312;IPR022673;IPR022672;

3.30.420.40;3.40.367.20;

A0A0K0PVW1

MKSELIFLPVPAFGHLVGMVEMAKLFISRHENLSVTVLISKFFIDTGIDNYNKSLLAKPTPRLTIINLPEIDPQKYLLKPRCAIFPSLIENQKTHVRDVMSRMTQSESTRVVGLLADILFVDIFDIADEFNVPTYVYSPAGAGFLGLAFHLQTLNDDKKQDVTEFRNSDTELLVPSFANPVPAEFLPSIFLEKDGRHDVLLSLYWRCREAKGIIVNTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGEGQNSDEAAVILGWLDDQPPSSVVFLCFGSFGSFPENQVKEIAMGLERSGHRFLWSLRPCISEGETTLQLKYSNLELPAGFLDRTSCVGKVIGWAPQMAILAHEAVGGFVSHCGWNSVLESVWYGMPVATWPMYGEQQLNAFEMVKELGLAVEIEVDYRNEYNKSDFIVKADEIETKIKKLMMDGKNSKIRKKVKEMKEKSRVAMSENGSSYTSLAKLFEEIM

Panax ginseng (Korean ginseng)

FUNCTION: Component of the dammarane-type triterpene saponins (e.g. PPT-type ginsenosides or panaxosides) biosynthetic pathway (PubMed:26032089, PubMed:27746309, PubMed:29378087). Glycosyltransferase that catalyzes the biosynthesis of ginsenoside Rh1 from protopanaxatriol (PPT) and the conversion of ginsenoside F1 to ginsenoside Rg1 (PubMed:26032089, PubMed:27746309). {ECO:0000269|PubMed:26032089, ECO:0000269|PubMed:27746309, ECO:0000303|PubMed:29378087}.

2.4.1.367

CATALYTIC ACTIVITY: Reaction=(20S)-protopanaxadiol + UDP-alpha-D-glucose = (20S)-ginsenoside C-K + H(+) + UDP; Xref=Rhea:RHEA:57976, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75950, ChEBI:CHEBI:77146; Evidence={ECO:0000269|PubMed:26032089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57977; Evidence={ECO:0000269|PubMed:26032089}; CATALYTIC ACTIVITY: Reaction=(20S)-protopanaxatriol + UDP-alpha-D-glucose = (20S)-ginsenoside Rh1 + H(+) + UDP; Xref=Rhea:RHEA:58952, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75951, ChEBI:CHEBI:142487; EC=2.4.1.367; Evidence={ECO:0000269|PubMed:26032089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58953; Evidence={ECO:0000269|PubMed:26032089}; CATALYTIC ACTIVITY: Reaction=(20S)-ginsenoside F1 + UDP-alpha-D-glucose = (20S)-ginsenoside Rg1 + H(+) + UDP; Xref=Rhea:RHEA:58008, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:67987, ChEBI:CHEBI:77150; EC=2.4.1.367; Evidence={ECO:0000269|PubMed:26032089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58009; Evidence={ECO:0000269|PubMed:26032089};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305}.

Glycosyltransferase;Hydrolase;Isoprene biosynthesis;Transferase

response to molecule of fungal origin [GO:0002238]; terpenoid biosynthetic process [GO:0016114]

hydrolase activity [GO:0016787]; UDP-glycosyltransferase activity [GO:0008194]

IPR002213;IPR035595;

3.40.50.2000;

A0A0K1TQQ0

MAENSILLAVLSLLSACQQSYFALQVGKARLKYKVMPPAVSGSPEFERIFRAQQNSLEFYPVFIITLWVAGWYFNQVFATCLGLVYIYARHRYFWGYSEAPKKRITGFRLSLGVLALLAVLGAVGITNSFLDEYLDLNIAKKLRHF

Sus scrofa (Pig)

FUNCTION: Catalyzes several different glutathione-dependent reactions. Catalyzes the glutathione-dependent reduction of lipid hydroperoxides, such as 5-HPETE. Has glutathione transferase activity, toward xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB). Catalyzes also the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4 (LTC4). Involved in oxidative DNA damage induced by ER stress and anticancer agents by activating LTC4 biosynthetic machinery in nonimmune cells. {ECO:0000256|RuleBase:RU369123}.

1.11.1.-; 2.5.1.18; 4.4.1.20

CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000256|RuleBase:RU369123}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718, ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18; Evidence={ECO:0000256|RuleBase:RU369123}; CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000256|RuleBase:RU369123}; CATALYTIC ACTIVITY: Reaction=leukotriene C4 = glutathione + leukotriene A4; Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925, ChEBI:CHEBI:57973; EC=4.4.1.20; Evidence={ECO:0000256|RuleBase:RU369123};

Endoplasmic reticulum;Leukotriene biosynthesis;Lipid metabolism;Lyase;Membrane;Microsome;Oxidoreductase;Proteomics identification;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix

glutathione biosynthetic process [GO:0006750]; leukotriene biosynthetic process [GO:0019370]; membrane lipid catabolic process [GO:0046466]

endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]

enzyme activator activity [GO:0008047]; glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; leukotriene-C4 synthase activity [GO:0004464]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369123}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369123}. Microsome membrane {ECO:0000256|RuleBase:RU369123}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369123}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR001446;IPR023352;IPR001129;

1.20.120.550;

A0A0K3AUJ9

MSLAPKMSKAFIGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEKHGEVCPAGWTPGSDTIKPGVKESQEYFKKH

Caenorhabditis elegans

FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:15099742). In I2 pharyngeal neurons, required for the inhibition of feeding in response to light and hydrogen peroxide (PubMed:25640076). In the intestine, plays a role in protecting cells against oxidative stress by detoxifying peroxides such as hydrogen peroxide (PubMed:15099742, PubMed:19064914, PubMed:20649472). In addition, plays a role in the recovery from oxidative stress induced by hydrogen peroxide (PubMed:20649472). In its hyperoxidized form (induced by hydrogen peroxide), confers protection against heat stress (PubMed:19064914). However, has a low tendency for overoxidation during the normal lifespan (PubMed:20964547). Increases sensitivity to cytotoxity caused by metalloids and heavy metals such as arsenic and cadmium by playing a role in inhibiting the expression of phase II detoxification genes such as gcs-1 in intestinal cells (PubMed:19064914, PubMed:25204677). In addition, in response to arsenite, promotes the secretion of the insulin ligand daf-28 into the pseudocoelom, which negatively regulates the activities of daf-16 and skn-1 (PubMed:25808059). Plays a role in promoting longevity (PubMed:19064914, PubMed:24889636). Plays a role in the mitohormetic pathway by promoting the activation of pmk-1 in response to the drug metformin (PubMed:24889636). {ECO:0000269|PubMed:15099742, ECO:0000269|PubMed:19064914, ECO:0000269|PubMed:20649472, ECO:0000269|PubMed:20964547, ECO:0000269|PubMed:24889636, ECO:0000269|PubMed:25204677, ECO:0000269|PubMed:25640076, ECO:0000269|PubMed:25808059}.

1.11.1.24

CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:15099742};

Alternative splicing;Antioxidant;Cytoplasm;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome

cell redox homeostasis [GO:0045454]; cellular response to hydrogen peroxide [GO:0070301]; determination of adult lifespan [GO:0008340]; heat acclimation [GO:0010286]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of brood size [GO:0090727]; regulation of response to oxidative stress [GO:1902882]; removal of superoxide radicals [GO:0019430]; response to hydrogen peroxide [GO:0042542]; response to metal ion [GO:0010038]; response to oxidative stress [GO:0006979]

cytoplasm [GO:0005737]; cytosol [GO:0005829]

thioredoxin peroxidase activity [GO:0008379]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19064914}.

PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. {ECO:0000250|UniProtKB:Q06830}.

IPR000866;IPR024706;IPR019479;IPR036249;IPR013766;

3.40.30.10;

A0A0K3AV08

MEQASVPSYVNIPPIAKTRSTSHLAPTPEHHRSVSYEDTTTASTSTDSVPEVRIRSESSQVSRESPPIRASKAFVASYEYEAQKDDELNLPLGAIITLVTVETNEDGWYRGELNGKVGLFPSNYAREVTYKDNLVEFKQDEIMLPVAVRTLSDCQIGHGATATVFKMDIKIKKELQNGRMGEAVGDQMKAALKRFNRHASNFRADVVSTDEQLEQLKREANLVNGLSHNNIVRLLGICLEDPYFGLLLELCEGSSLRNVCRNLNSDAAIPLGVLIDWATQVAEGMEYLTKQGYVHRDLKADNVLVKEEVCLCMDEEMFQYAYCLKCGKRPFDKLQLKITDFGVTRKMTADANRFSTAGTYAWLAPEAFKEGTWSEASDVWSYGVVLWELLTREEPYQGHIPATIAFQIANKGQNLSIGDSCPDRWKKLMQDCWNLEPNFRPKFSTLAISFKQYAKEFKDTHLQRAPSKMAVKELYSECFADKTKEEFEKRFHDLYAGSGDINRKNRHSIAPETKARRLKHHKPKKADITGPTEVKHILSVQKDDKNFRVKTYDQSSTGGTLPRLNERQSTLSLSSPDLFHISNLISGSNTVGHSAHRISRKNAIRHKKNQHRMFESPVVSPTMDDSNTFSTIDNADEVDPNHSKESKKGGTLSRAWAKLPWNKRDSKEDHDERAVAGSISSRSSSTTSSNRLITGQTTRGASAAGLLEIGARSRAQSTADGWEDPNTTKKHKVSPSDKRPVKTTNQTERYVKDLEKDTPLRPAQLPPTHRKSALDQTIPASPNSPDSINNFHPMPLSSRRTTANSSSDGAPCYDALVSHSYGAGHGHKNHFGLSDTIPLFPEEPTHYDMGPGRPFGTNGRAIVNQGGDYYGNISGQNYEGFGHGRSINQSTQYYPVGGGCDDYIPIVQKTVIKPTVGEVGNSPYSENIRCATRNVQNPQYIQCKKNQNPRRIPALPMKIQSESNLVTSGMVFTPRDEQLNGIGNSLSSLSLNEPPDIPAPLPPVVTYPIPASLISPSNRVSMSPPTRMAPVLPLGAMSSPRIMDKEILKNSSVEGTEIY

Caenorhabditis elegans

FUNCTION: Serine/threonine-protein kinase which, by phosphorylating and activating mek-1, plays an important role in the activation of the JNK pathway composed of mlk-1, mek-1 and kgb-1 (PubMed:15116070, PubMed:20008556). Involved in the response to environmental stress such as heavy metals (PubMed:15116070, PubMed:18809575). By activating the JNK pathway downstream of tyrosine receptor svh-2, plays a role in axon regeneration after injury (PubMed:21670305, PubMed:22388962, PubMed:23072806). {ECO:0000269|PubMed:15116070, ECO:0000269|PubMed:18809575, ECO:0000269|PubMed:20008556, ECO:0000269|PubMed:21670305, ECO:0000269|PubMed:22388962, ECO:0000269|PubMed:23072806}.

2.7.11.25

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000269|PubMed:15116070, ECO:0000269|PubMed:20008556}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000269|PubMed:15116070, ECO:0000269|PubMed:20008556};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P80192};

Alternative splicing;ATP-binding;Coiled coil;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;SH3 domain;Stress response;Transferase;Ubl conjugation

axon regeneration [GO:0031103]; defense response to Gram-negative bacterium [GO:0050829]; determination of adult lifespan [GO:0008340]; JNK cascade [GO:0007254]; MAPK cascade [GO:0000165]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of axon regeneration [GO:0048680]; positive regulation of protein phosphorylation [GO:0001934]; response to copper ion [GO:0046688]; response to starvation [GO:0042594]; signal transduction [GO:0007165]

cytoplasm [GO:0005737]

ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; protein serine kinase activity [GO:0106310]; receptor tyrosine kinase binding [GO:0030971]; scaffold protein binding [GO:0097110]

PTM: May be phosphorylated on tyrosine residues by svh-2. {ECO:0000269|PubMed:22388962, ECO:0000269|PubMed:27984580}.; PTM: May be ubiquitinated and targeted for proteasomal degradation by E3 ubiquitin ligase rpm-1. {ECO:0000269|PubMed:21670305}.

IPR011009;IPR000719;IPR001245;IPR008271;IPR036028;IPR001452;

2.30.30.40;1.10.510.10;

A0A0K8P6T7

MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS

Piscinibacter sakaiensis (Ideonella sakaiensis)

FUNCTION: Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with MHETase to depolymerize PET (PubMed:26965627). Catalyzes the hydrolysis of PET to produce mono(2-hydroxyethyl) terephthalate (MHET) as the major product (PubMed:26965627, PubMed:29235460, PubMed:29374183, PubMed:29603535, PubMed:29666242, PubMed:32269349). Also depolymerizes another semiaromatic polyester, poly(ethylene-2,5-furandicarboxylate) (PEF), which is an emerging, bioderived PET replacement with improved gas barrier properties (PubMed:29666242). In contrast, PETase does not degrade aliphatic polyesters such as polylactic acid (PLA) and polybutylene succinate (PBS) (PubMed:29666242). Is also able to hydrolyze bis(hydroxyethyl) terephthalate (BHET) to yield MHET with no further decomposition, but terephthalate (TPA) can also be observed (PubMed:26965627, PubMed:29374183, PubMed:29603535). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) in vitro (PubMed:26965627, PubMed:30502092). {ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:29235460, ECO:0000269|PubMed:29374183, ECO:0000269|PubMed:29603535, ECO:0000269|PubMed:29666242, ECO:0000269|PubMed:30502092, ECO:0000269|PubMed:32269349}.

3.1.1.101

CATALYTIC ACTIVITY: Reaction=(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+); Xref=Rhea:RHEA:49528, Rhea:RHEA-COMP:12420, Rhea:RHEA-COMP:12421, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131701, ChEBI:CHEBI:131704; EC=3.1.1.101; Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:29235460, ECO:0000269|PubMed:29374183, ECO:0000269|PubMed:29603535, ECO:0000269|PubMed:29666242, ECO:0000269|PubMed:32269349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529; Evidence={ECO:0000269|PubMed:26965627}; CATALYTIC ACTIVITY: Reaction=(2,5-ethylene furandicarboxylate)(n) + 2 H2O = (2,5-ethylene furandicarboxylate)(n-1) + 2,5-dicarboxyfuran + ethylene glycol + 2 H(+); Xref=Rhea:RHEA:42648, Rhea:RHEA-COMP:14671, Rhea:RHEA-COMP:14672, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30742, ChEBI:CHEBI:83389, ChEBI:CHEBI:140646; Evidence={ECO:0000269|PubMed:29666242}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30502092}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30502092}; CATALYTIC ACTIVITY: Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656; Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30502092}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30502092}; CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:30502092};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.431 mM for pNP-acetate {ECO:0000269|PubMed:30502092}; KM=0.315 mM for pNP-butanoate {ECO:0000269|PubMed:30502092}; KM=0.053 mM for pNP-hexanoate {ECO:0000269|PubMed:30502092}; KM=0.048 mM for pNP-octanoate {ECO:0000269|PubMed:30502092}; KM=2.283 mM for pNP-dodecanoate {ECO:0000269|PubMed:30502092}; Note=kcat is 1590 sec(-1) for the hydrolysis of pNP-acetate. kcat is 1353 sec(-1) for the hydrolysis of pNP-butanoate. kcat is 1345 sec(-1) for the hydrolysis of pNP-hexanoate. kcat is 519 sec(-1) for the hydrolysis of pNP-octanoate. kcat is 1531 sec(-1) for the hydrolysis of pNP-dodecanoate. {ECO:0000269|PubMed:30502092};

PATHWAY: Xenobiotic degradation. {ECO:0000305|PubMed:26965627}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9 for PET film hydrolysis (PubMed:26965627). Optimum pH is 9 for PET (commercial drinking bottle) hydrolysis. Optimum pH is 6.5-8.0 for BHET hydrolysis (PubMed:29603535). Optimum pH is 8.0 for the hydrolysis of pNP-esters. The enzyme is active at pH 6-10, has an optimal pH range of 7-9 and it is rapidly inactivated below pH 7.0 or above pH 9.0 (PubMed:30502092). {ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:29603535, ECO:0000269|PubMed:30502092};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius for PET film hydrolysis (PubMed:26965627). Optimum temperature is 30 degrees Celsius for PET (commercial drinking bottle) hydrolysis and BHET hydrolysis (PubMed:29603535). Optimum temperature is 35-45 degrees Celsius for the hydrolysis of pNP-esters. Remains active even at 65 degrees Celsius (about 60% of maximum activity) (PubMed:30502092). {ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:29603535, ECO:0000269|PubMed:30502092};

3D-structure;Disulfide bond;Hydrolase;Reference proteome;Secreted;Serine esterase;Signal

cellular response to organic substance [GO:0071310]; xenobiotic catabolic process [GO:0042178]

extracellular region [GO:0005576]

acetylesterase activity [GO:0008126]; carboxylic ester hydrolase activity [GO:0052689]

SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26965627}.

DOMAIN: PETase retains the ancestral alpha/beta-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases. {ECO:0000269|PubMed:29666242}.

IPR029058;IPR002925;

3.40.50.1820;

A0A0K8P8E7

MQTTVTTMLLASVALAACAGGGSTPLPLPQQQPPQQEPPPPPVPLASRAACEALKDGNGDMVWPNAATVVEVAAWRDAAPATASAAALPEHCEVSGAIAKRTGIDGYPYEIKFRLRMPAEWNGRFFMEGGSGTNGSLSAATGSIGGGQIASALSRNFATIATDGGHDNAVNDNPDALGTVAFGLDPQARLDMGYNSYDQVTQAGKAAVARFYGRAADKSYFIGCSEGGREGMMLSQRFPSHYDGIVAGAPGYQLPKAGISGAWTTQSLAPAAVGLDAQGVPLINKSFSDADLHLLSQAILGTCDALDGLADGIVDNYRACQAAFDPATAANPANGQALQCVGAKTADCLSPVQVTAIKRAMAGPVNSAGTPLYNRWAWDAGMSGLSGTTYNQGWRSWWLGSFNSSANNAQRVSGFSARSWLVDFATPPEPMPMTQVAARMMKFDFDIDPLKIWATSGQFTQSSMDWHGATSTDLAAFRDRGGKMILYHGMSDAAFSALDTADYYERLGAAMPGAAGFARLFLVPGMNHCSGGPGTDRFDMLTPLVAWVERGEAPDQISAWSGTPGYFGVAARTRPLCPYPQIARYKGSGDINTEANFACAAPP

Piscinibacter sakaiensis (Ideonella sakaiensis)

FUNCTION: Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with PETase to depolymerize PET. Catalyzes the hydrolysis of mono(2-hydroxyethyl) terephthalate (MHET) into its two environmentally benign monomers, terephthalate and ethylene glycol. Does not show activity against PET, bis(hydroxyethyl) terephthalate (BHET), pNP-aliphatic esters or typical aromatic ester compounds catalyzed by the tannase family enzymes, such as ethyl gallate and ethyl ferulate. {ECO:0000269|PubMed:26965627}.

3.1.1.102

CATALYTIC ACTIVITY: Reaction=4-[(2-hydroxyethoxy)carbonyl]benzoate + H2O = ethylene glycol + H(+) + terephthalate; Xref=Rhea:RHEA:49532, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30043, ChEBI:CHEBI:30742, ChEBI:CHEBI:131704; EC=3.1.1.102; Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30979881}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49533; Evidence={ECO:0000269|PubMed:26965627};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.3 uM for mono(2-hydroxyethyl) terephthalate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:26965627}; Note=kcat is 31 sec(-1) for the hydrolysis of mono(2-hydroxyethyl) terephthalate (at pH 7 and 30 degrees Celsius). {ECO:0000269|PubMed:26965627};

3D-structure;Calcium;Cell outer membrane;Disulfide bond;Hydrolase;Lipoprotein;Membrane;Metal-binding;Palmitate;Reference proteome;Serine esterase;Signal

cellular response to organic substance [GO:0071310]; xenobiotic catabolic process [GO:0042178]

cell outer membrane [GO:0009279]

carboxylic ester hydrolase activity [GO:0052689]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:26965627}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:26965627}.

IPR029058;IPR011118;

A0A0L7KF24

MNLTKLMKVFGYINIITNCVQSFTNRADKKRYNVFAKSFINTINTNLYTFKAVMSKTPEWIHEKSPKHNSYDIIEKRYNEEFKMTYTVYQHKKAKTQVISLGTNDPLDVEQAFAFYVKTLTHSGKGIPHILEHSVLSGSKNYNYKNSIGLLEKGTLHTHLNAYTFNDRTVYMAGSMNNKDFFNIMGVYMDSVFQPNVLENKYIFETEGWTYEVEKLKEDEKGKAEIPQMKDYKVSFNGIVYNEMKGALSSPLEDLYHEEMKYMFPDNVHSNNSGGDPKEITNLTYEEFKEFYYKNYNPKKVKVFFFSKNNPTELLNFVDQYLGQLDYSKYRDDAVESVEYQTYKKGPFYIKKKYGDHSEEKENLVSVAWLLNPKVDKTNNHNNNHSNNQSSENNGYSNGSHSSDLSLENPTDYFVLLIINNLLIHTPESVLYKALTDCGLGNNVIDRGLNDSLVQYIFSIGLKGIKRNNEKIKIFDKVHYEVEDVIMNALKKVVKEGFNKSAVEASINNIEFILKEANLKTSKSIDFVFEMTSKLNYNRDPLLIFEFEKYLNIVKNKIKNEPMYLEKFVEKHFINNAHRSVILLEGDENYAQEQENLEKQELKKRIENFNEQEKEQVIKNFEELSKYKNAEESPEHLNKFPIISISDLNKKTLEVPVNVYFTNINENNNIMETYNKLKTNEHMLKDNMDVFLKKYVLKNDKHNTNNNNNNNNNMDYSFTETKYEGNVPILVYEMPTTGIVYLQFVFSLDHLTVDELAYLNLFKTLILENKTNKRSSEDFVILREKNIGSMSANVALYSKDDHLNVTDKYNAQALFNLEMHVLSHKCNDALNIALEAVKESDFSNKKKVIDILKRKINGMKTTFSEKGYAILMKYVKAHLNSKHYAHNIIYGYENYLKLQEQLELAENDFKTLENILVRIRNKIFNKKNLMVSVTSDYGALKHLFVNSNESLKNLVSYFEENDKYINDMQNKVNDPTVMGWNEEIKSKKLFDEEKVKKEFFVLPTFVNSVSMSGILFKPGEYLDPSFTVIVAALKNSYLWDTVRGLNGAYGVFADIEYDGSVVFLSARDPNLEKTLATFRESAKGLRKMADTMTENDLLRYIINTIGTIDKPRRGIELSKLSFLRLISNESEQDRVEFRKRIMNTKKEDFYKFADLLESKVNEFEKNIVIITTKEKANEYIANVDGEFKKVLIE

Plasmodium falciparum (isolate HB3)

FUNCTION: In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains (PubMed:10542284, PubMed:12876284). In the apicoplast, degrades apicoplast transit peptides after their cleavage (By similarity). Prefers bulky hydrophobic amino acids in the P1' position at both acidic and neutral pH (PubMed:12876284). At P2', prefers hydrophobic residues at acidic pH; at neutral pH, these same residues are abundant but prefers Arg (PubMed:12876284). At P3', prefers hydrophobic residues, especially Met, at both pH conditions. At P4' and P5', prefers acidic residues at acidic pH, however, at neutral pH, the enzyme is less selective at these positions (PubMed:12876284). The optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH, MKRHS-|-FRMRG (PubMed:12876284). {ECO:0000250|UniProtKB:Q76NL8, ECO:0000269|PubMed:10542284, ECO:0000269|PubMed:12876284}.

3.4.24.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10542284}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q76NL8};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5 (food vacuole) (PubMed:12876284). Optimum pH is 7 (PubMed:12876284). {ECO:0000269|PubMed:12876284};

Apicoplast;Coiled coil;Direct protein sequencing;Hydrolase;Membrane;Metal-binding;Metalloprotease;Plastid;Protease;Reference proteome;Vacuole;Zinc

acquisition of nutrients from host [GO:0044002]; protein processing [GO:0016485]

apicoplast [GO:0020011]; chloroplast [GO:0009507]; food vacuole [GO:0020020]; mitochondrial matrix [GO:0005759]; vacuolar membrane [GO:0005774]

metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]

SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10542284}; Peripheral membrane protein {ECO:0000269|PubMed:12876284}. Plastid, apicoplast {ECO:0000250|UniProtKB:Q76NL8}. Vesicle {ECO:0000269|PubMed:12876284}. Note=Localizes to the food (or digestive) vacuole, an acidic vacuole where host hemoglobin is digested (PubMed:10542284, PubMed:12876284). During the trophozoite and early to mid-schizont stages, localizes to the apicoplast (By similarity). {ECO:0000250|UniProtKB:Q76NL8, ECO:0000269|PubMed:10542284, ECO:0000269|PubMed:12876284}.

PTM: Does not require processing for targeting to the food vacuole or maturation. {ECO:0000269|PubMed:12798513, ECO:0000269|PubMed:12876284}.

IPR011249;IPR011765;IPR007863;IPR013578;

3.30.830.10;

A0A0M3Q1Q3

MRRSGNYQAPVWNNDFIQSFSTDKYKDEKFLKKKEELIAQVKVLLNTKMEAVKQLELIEDLRNLGLTYYFEDEFKKILTSIYNEHKGFKNEQVGDLYFTSLAFRLLRLHGFDVSEDVFNFFKNEDGSDFKASLGENTKDVLELYEASFLIRVGEVTLEQARVFSTKILEKKVEEGIKDEKLLAWIQHSLALPLHWRIQRLEARWFLDAYKARKDMNPIIYELGKIDFHIIQETQLQEVQEVSQWWTNTNLAEKLPFVRDRIVECYFWALGLFEPHEYGYQRKMAAIIITFVTIIDDVYDVYDTLDELQLFTDAIRKWDVESISTLPYYMQVCYLAVFTYASELAYDILKDQGFNSISYLQRSWLSLVEGFFQEAKWYYAGYTPTLAEYLENAKVSISSPTIISQVYFTLPNSTERTVVENVFGYHNILYLSGMILRLADDLGTTQFELKRGDVQKAIQCYMNDNNATEEEGTEHVKYLLREAWQEMNSAMADPDCPLSEDLVFAAANLGRTSQFIYLDGDGHGVQHSEIHNQMGGLIFEPYV

Thymus vulgaris (Thyme)

FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (PubMed:26750479). Monoterpene synthase which catalyzes the conversion of geranyl diphosphate (GPP) to gamma-terpinene and the minor products alpha-thujene, alpha-terpinene, myrcene, sabinene, (+)-R-limonene, alpha-pinene and alpha-phellandrene (PubMed:26750479). {ECO:0000269|PubMed:26750479}.

4.2.3.114; 4.2.3.115

CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene; Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.114; Evidence={ECO:0000269|PubMed:26750479}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560; Evidence={ECO:0000269|PubMed:26750479}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = alpha-terpinene + diphosphate; Xref=Rhea:RHEA:32563, ChEBI:CHEBI:10334, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.115; Evidence={ECO:0000250|UniProtKB:E2E2P0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32564; Evidence={ECO:0000250|UniProtKB:E2E2P0};

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:E2E2P0}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:E2E2P0}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:E2E2P0};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:26750479}.

3D-structure;Lyase;Magnesium;Manganese;Metal-binding

diterpenoid biosynthetic process [GO:0016102]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to UV-C [GO:0010225]

gamma-terpinene synthase activity [GO:0102903]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; terpene synthase activity [GO:0010333]

DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+). {ECO:0000250|UniProtKB:Q9X839}.

IPR008949;IPR044814;IPR001906;IPR036965;IPR005630;IPR008930;

1.10.600.10;1.50.10.130;

A0A0N4SWI8

MDESALTLGTIDVSYLPNSSEYSIGRCKHASEEWGECGFRPPVFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDRFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKKILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATEMNLPLIFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGQKDILYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNTIPDILIIPVGISYDRIIEGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSAPLSLEQALLPAILPSRPSDAVDEGTDMSINESRNADESFRRRLIANLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCITITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLKKRGSGGPASPSLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQICHETVGRFIQYGILTVAEQDDQEDISPSLAEQHWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAIFIHNFSGPVPEPEYLQKLHKYLINRTERRVAVYAESATYCLVKNAVKMFKDIGVFKETKQKKVSVLELSSTFLPQCNRQKLLEYILSFVVL

Sus scrofa (Pig)

FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipids biosynthesis such as triglycerides, phosphatidic acids and lysophosphatidic acids. {ECO:0000256|ARBA:ARBA00023435}.

2.3.1.15

CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597, ChEBI:CHEBI:74544; Evidence={ECO:0000256|ARBA:ARBA00023362}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200; Evidence={ECO:0000256|ARBA:ARBA00023362}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:57597, ChEBI:CHEBI:74547; Evidence={ECO:0000256|ARBA:ARBA00023344}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204; Evidence={ECO:0000256|ARBA:ARBA00023344}; CATALYTIC ACTIVITY: Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:33203, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64716, ChEBI:CHEBI:64840; Evidence={ECO:0000256|ARBA:ARBA00023355}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204; Evidence={ECO:0000256|ARBA:ARBA00023355}; CATALYTIC ACTIVITY: Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15; Evidence={ECO:0000256|PIRNR:PIRNR000437}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + sn-glycerol 3-phosphate = 1-dodecanoyl-sn-glycerol 3-phosphate + CoA; Xref=Rhea:RHEA:35727, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:57597, ChEBI:CHEBI:72682; Evidence={ECO:0000256|ARBA:ARBA00023335}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728; Evidence={ECO:0000256|ARBA:ARBA00023335}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518, ChEBI:CHEBI:57597; Evidence={ECO:0000256|ARBA:ARBA00023405}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724; Evidence={ECO:0000256|ARBA:ARBA00023405}; CATALYTIC ACTIVITY: Reaction=octadecanoyl-CoA + sn-glycerol 3-phosphate = 1-octadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37195, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57597, ChEBI:CHEBI:74565; Evidence={ECO:0000256|ARBA:ARBA00023374}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196; Evidence={ECO:0000256|ARBA:ARBA00023374};

PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.; PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|PIRNR:PIRNR000437}.

Acetylation;Acyltransferase;Lipid biosynthesis;Lipid metabolism;Membrane;Mitochondrion;Phospholipid biosynthesis;Phospholipid metabolism;Phosphoprotein;Reference proteome;Transferase;Transmembrane;Transmembrane helix

activated T cell proliferation [GO:0050798]; activation-induced cell death of T cells [GO:0006924]; acyl-CoA metabolic process [GO:0006637]; CDP-diacylglycerol biosynthetic process [GO:0016024]; defense response to virus [GO:0051607]; fatty acid homeostasis [GO:0055089]; fatty acid metabolic process [GO:0006631]; glycerol-3-phosphate metabolic process [GO:0006072]; negative regulation of activation-induced cell death of T cells [GO:0070236]; phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid biosynthetic process [GO:0008654]; phospholipid homeostasis [GO:0055091]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of multicellular organism growth [GO:0040018]; regulation of cytokine production [GO:0001817]; response to glucose [GO:0009749]; triglyceride biosynthetic process [GO:0019432]

mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886]

glycerol-3-phosphate O-acyltransferase activity [GO:0004366]; sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity [GO:0102420]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004374}.

IPR022284;IPR045520;IPR041728;IPR028354;IPR002123;

A0A0N9E2K8

MLTVIRRIFIIQTFIFITAEKIFHSRDHSDVLNNIHQAELITDTDTAQRFLSKYGFIKAAGSEESQLSESSGDLDFSLSLDLHEGGTTSGSSSSDLQFVSALRDFQRLSDLPVTGVFDDATKAAMNKPRCGVMDDDQELKDVTGSNSTRNHIRTSTNTSHNHEHQAPVRKKRHLSALLKNTSLQKRDVSKWTGHMAFSKSVLKWRLIGEGYSSQLSIQEQKYIFRLAFRMWSEISPLQFIEDLHSPLENIDIRLGFGTGRHLGCSQRFDGAGREFAHAWFLGDIHFDDDEHFTVPNTGSGISLLKVAVHEIGHVLGLPHIYRPGSIMQPSYLPQDAGFEIDWMDRKSIQRLYGVCTGRFSTVFDWIRKEQTPYGEVVVRFNTYFMRDGLYWLYENRNNRTRYGDPVAVQVGWHGLPSGGVDAYVHVWNRKTDAVYFFKGMQYWRYDSENDHVFSHAPDGRLYPRLISEDFPGVSGPLDTAYYDRRDAHIYFFKGSQVFRFDVRMRRLASSSPQEMTEVFPAIVSGDHPVRSLDAAYFSYTHNTVFLLKGSLFWRVLSGKERRRRAFLPMNGLLAHRRVHEQWFDICDVHSSSLRTTRRR

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway. {ECO:0000269|PubMed:26429889, ECO:0000269|PubMed:26437028}.

3.4.24.-

Calcium;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Signal;Zinc

collagen catabolic process [GO:0030574]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right symmetry [GO:0007368]; embryonic heart tube left/right pattern formation [GO:0060971]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; regulation of heart looping [GO:1901207]

extracellular matrix [GO:0031012]; extracellular space [GO:0005615]

metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]

PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.

IPR036375;IPR018487;IPR033739;IPR024079;IPR001818;IPR021190;IPR006026;IPR002477;IPR036365;

3.40.390.10;2.110.10.10;

A0A0N9HMN6

MEMAPTMDLEIRNGNGYGDSGEELLAAQAHIYNHIFNFISSMALKCAVELNIPEILHNHQPKAVTLSELVQALQIPQAKSACLYRLLRILVHSGFFAITKIQSEGDEEGYLPTLSSKLLLKNHPMSMSPCLLGLVNPTMVAPMHFFSDWFKRSDDMTPFEATHGASLWKYFGETPHMAEIFNEAMGCETRLAMSVVLKECKGKLEGISSLVDVGGGTGNVGRAIAEAFPNVKCTVLDLPQVVGNLKGSNNLEFVSGDMFQFIPPADVVFLKWILHDWNDEECIKILKRCKEAIPSKEEGGKLIIIDMVVNDHNKGSYESTETQLFYDLTLMALLTGTERTETEWKKLFVAAGFTSYIISPVLGLKSIIEVFP

Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum)

FUNCTION: O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the methylation of (-)-pluviatolide to produce (-)-bursehernin (PubMed:26359402). {ECO:0000269|PubMed:26359402}.

2.1.1.323

CATALYTIC ACTIVITY: Reaction=(-)-pluviatolide + S-adenosyl-L-methionine = (-)-bursehernin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49036, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90893, ChEBI:CHEBI:90896; EC=2.1.1.323; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49037; Evidence={ECO:0000269|PubMed:26359402};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for (-)-pluviatolide {ECO:0000269|PubMed:26359402}; Vmax=1.7 nmol/min/mg enzyme with (-)-pluviatolide as substrate {ECO:0000269|PubMed:26359402}; Note=kcat is 0.72 sec(-1) with (-)-pluviatolide as substrate. {ECO:0000269|PubMed:26359402};

PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26359402}.

Methyltransferase;S-adenosyl-L-methionine;Transferase

aromatic compound biosynthetic process [GO:0019438]; melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]; phenylpropanoid biosynthetic process [GO:0009699]; response to wounding [GO:0009611]

acetylserotonin O-methyltransferase activity [GO:0017096]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;

3.40.50.150;1.10.10.10;

A0A0N9HTA1

MDTRADAEIKAMELIGIGVLPLAMKAIIELNVLEILSKAGPDTQLTAAQIVTDIPTTNPNAGFQLDRILRLLASHSVLSSSITKSGERVYGLTPMCKYFLPDQDGVSLAPMVVTIHDKVLLQSWHYLKDSVLKQGSLPFTEAFGMSPFEYSVSDTRFNKVFNAGMFDHSTLCMRDVLQRYKGFQGLGELVDVGGGTGGSLKMILSQYPNLKGINFDLPHVVADAPSFPGVKHIGGDMFESVPSGDAIFMKWILHDWDDGRCLTLLKNCWNALPEHGKVIIVEWILPSDAATDPTSRRVFTADLMMLAFSEGGKERTLGDYGALAKEAGFTTVKDFPCANGISVIEFHKK

Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum)

FUNCTION: O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the methylation of (-)-5'-demethylyatein to produce (-)-yatein (PubMed:26359402). {ECO:0000269|PubMed:26359402}.

2.1.1.330

CATALYTIC ACTIVITY: Reaction=(-)-5'-demethylyatein + S-adenosyl-L-methionine = (-)-yatein + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49040, ChEBI:CHEBI:4553, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90894; EC=2.1.1.330; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49041; Evidence={ECO:0000269|PubMed:26359402};

PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26359402}.

Methyltransferase;S-adenosyl-L-methionine;Transferase

aromatic compound biosynthetic process [GO:0019438]; methylation [GO:0032259]; phenylpropanoid biosynthetic process [GO:0009699]; response to wounding [GO:0009611]

O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;

3.40.50.150;1.10.10.10;

A0A0N9NCU6

MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGENPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV

Yersinia pseudotuberculosis

FUNCTION: Serine/threonine-protein acetyltransferase translocated into infected cells, which inhibits the host immune response and induces cell death by mediating acetylation of target proteins (PubMed:10489373, PubMed:12433923, PubMed:16728640, PubMed:22563435, PubMed:26810037). Inhibits the MAPK and NF-kappa-B signaling pathways by acetylating protein-kinases such as MAP2K1, MAP2K6, MAP3K7/TAK1 and I-kappa-B kinase (CHUK/IKKA and IKBKB) on serine and threonine residues critical for their activation by phosphorylation, thereby preventing protein-kinase activation (PubMed:16728640, PubMed:30361383, Ref.9). Promotes pyroptosis, a programmed cell death, in host cells by mediating acetylation of MAP3K7/TAK1: MAP3K7/TAK1 inactivation triggers activation of caspase-8 (CASP8), followed by CASP8-dependent cleavage of gasdermin-D (GSDMD) and induction of pyroptosis (PubMed:30361383, PubMed:30381458). Also able to induce intestinal barrier dysfunction by acetylating and inhibiting host protein-kinases RIPK2/RICK and MAP3K7/TAK1, thereby promoting cell death (By similarity). {ECO:0000250|UniProtKB:P0DUD0, ECO:0000269|PubMed:10489373, ECO:0000269|PubMed:12433923, ECO:0000269|PubMed:16728640, ECO:0000269|PubMed:22563435, ECO:0000269|PubMed:26810037, ECO:0000269|PubMed:30361383, ECO:0000269|PubMed:30381458, ECO:0000269|Ref.9}.

2.3.1.-

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-threonyl-[protein] = CoA + O-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:65340, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:16780, ChEBI:CHEBI:30013, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141025; Evidence={ECO:0000269|PubMed:16728640}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65341; Evidence={ECO:0000269|PubMed:16728640}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-seryl-[protein] = CoA + O-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:59392, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15352, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141128; Evidence={ECO:0000269|PubMed:16728640}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393; Evidence={ECO:0000269|PubMed:16728640};

COFACTOR: Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130; Evidence={ECO:0000250|UniProtKB:O68718};

Acyltransferase;Allosteric enzyme;Plasmid;Secreted;Transferase;Virulence

negative regulation of JNK cascade [GO:0046329]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of p38MAPK cascade [GO:1903753]; peptidyl-serine O-acetylation [GO:0030919]; peptidyl-threonine O-acetylation [GO:0120258]

extracellular region [GO:0005576]

O-acetyltransferase activity [GO:0016413]; toxin activity [GO:0090729]

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DUD0}. Note=Secreted via type III secretion system (T3SS). {ECO:0000250|UniProtKB:P0DUD0}.

IPR005083;

A0A0P0UQI8

MLSNKKSDPGSSSSSGGNGGDRAPETLAAPQAGPAGPSGPISADVKKKERASPSGEPGGPPLPHPPGPGGIDQDSAEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKERKQVIPPPAPPIEEENDSEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIINGPQHTQKVFLYIRNRTLQLWLDNPKVQLTFEATVQQLEAPYNSDAVLVHRIHSYLERHGFINFGIYKRVKPLPTKKTGKVIVIGAGVSGLAAARQLQSFGMDVTVLESRDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAGERCTSVPKEKDEMVEQEFNRLLEATSYLSHQLDFNFLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKDLLNKMVTTKEKVKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELVEMQVKLEERLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTSSGCEVIAVNTRSTTQTFIYKCDAVLCTLPLGVMKQQPPAVQFVPPLPEWKTAAIQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALMAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPAIPGASQPVPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTMPRQATANPNPQPSPSIQ

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. {ECO:0000256|PIRNR:PIRNR038051}.

1.14.99.66

CATALYTIC ACTIVITY: Reaction=2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2 AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60244, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499, ChEBI:CHEBI:29969, ChEBI:CHEBI:61976; EC=1.14.99.66; Evidence={ECO:0000256|PIRNR:PIRNR038051};

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974, ECO:0000256|PIRNR:PIRNR038051, ECO:0000256|PIRSR:PIRSR038051-1};

Chromatin regulator;Coiled coil;FAD;Flavoprotein;Methyltransferase;Nucleus;Oxidoreductase;Proteomics identification;Reference proteome;Repressor;Transcription;Transcription regulation;Transferase

methylation [GO:0032259]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of hemopoiesis [GO:1903706]; regulation of retinoic acid biosynthetic process [GO:1900052]

nucleus [GO:0005634]

chromatin binding [GO:0003682]; FAD-dependent H3K4me/H3K4me3 demethylase activity [GO:0140682]; flavin adenine dinucleotide binding [GO:0050660]; histone deacetylase activity [GO:0004407]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038051}.

DOMAIN: The SWIRM domain may act as an anchor site for a histone tail. {ECO:0000256|PIRNR:PIRNR038051}.

IPR002937;IPR036188;IPR017366;IPR009057;IPR007526;IPR036388;

3.90.660.10;1.10.287.80;3.50.50.60;1.10.10.10;

A0A0P0VIP0

MPPRCRRLPLLFILLLAVRPLSAAAASSIAAAPASSYRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFGFPNSSYAPPPTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPHPNHRRRHLFYKVLGGVLGGMVLLGLVVVGSAVLLGRSVRRKNQEHAVASEDMGEATLSMEVARAATKGFDSGNVIGVGGSGATVYEGVLPSGSRVAVKRFQAIGSCTKAFDSELKAMLNCPHHPNLVPLAGWCRSKDELVLVYEFMPNGNLDSALHTLGGATLPWEARFRAVYGVASALAYLHDECENRIIHRDVKSSNVMLDAEFNARLGDFGLARTVSHGGLPLTTQPAGTLGYLAPEYVHTGVATERSDVYSFGVLALEVATGRRPAERGISVVNWVWTLWGRRRLVDAADRRLQGRFVADEMRRVLLVGLCCVHPDCRKRPGMRRVVSMLDGTAPLILVPDKMPPVLLQPVPNASSMNSADTANTAFFSCR

Oryza sativa subsp. japonica (Rice)

FUNCTION: Legume-lectin receptor-like kinase required for normal pollen development and male fertility (PubMed:31833176, PubMed:32284546). Regulates pollen exine assembly and aperture development (PubMed:31833176, PubMed:32284546). Plays a critical role in annulus formation, and may participate in the formation of the fibrillar-granular layer underneath the operculum (PubMed:32284546). May function by regulating the expression of genes involved in pollen exine development (PubMed:31833176). Kinase activity is required for its function in pollen development (PubMed:31833176). {ECO:0000269|PubMed:31833176, ECO:0000269|PubMed:32284546}.

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:31833176}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:31833176}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:31833176}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:31833176};

ATP-binding;Cell membrane;Cytoplasm;Glycoprotein;Kinase;Lectin;Membrane;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Signal;Transferase;Transmembrane;Transmembrane helix

defense response to bacterium [GO:0042742]; defense response to oomycetes [GO:0002229]; pollen aperture formation [GO:0062075]; pollen development [GO:0009555]; protein autophosphorylation [GO:0046777]

cytosol [GO:0005829]; plasma membrane [GO:0005886]; pollen aperture [GO:0062074]

ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; kinase activity [GO:0016301]; protein serine/threonine kinase activity [GO:0004674]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31833176, ECO:0000269|PubMed:32284546}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:32284546}. Note=During meiosis, localizes diffusely in the cytosol and plasma membrane of microspore mother cells (MMCs). During tetrad development, localizes at the corners. At late tetrad stage, accumulates to the four corners of the tetrad, assembled into ring-like structures marking future aperture sites. When microspores are released from tetrads and preliminary aperture structures has formed, remains in a distinctly ring-shaped distribution beneath the aperture in the plasma membrane between the annulus and operculum. {ECO:0000269|PubMed:32284546}.

PTM: Autophosphorylated at Thr-376; Ser-378; Thr-386; Thr-403 and Thr-657. {ECO:0000269|PubMed:31833176}.

IPR013320;IPR011009;IPR001220;IPR000719;IPR008271;

2.60.120.200;1.10.510.10;

A0A0P0WGX7

MASPPPFDICGDLDDDPTPPAPTPLAAPTPNGLNDRLLRLTRTHQRGPSQNPNPNPNPNPKPPPPPPPQEPEPAKVKLAGRRRLCKLSTAGDESAGDDDSIRDILDDLTTRLDSLSVDRPTARPRPHVSPLPCALHADPDPSQSQLNDGTKPSSSFVDCDDDDDDAGGAYGGFGVKEEVTRKVFKASSSFGGRGNDDKMKAKGAYAFDTVSRKTTTESKASKFFGDYDDEDDIDQDAENGKENHADDVGWEKTEDFKMEPTGTGVTRKPYNLPGRIFNMLYPHQREGLRWLWVLHCRGTGGILGDDMGLGKTMQVSAFLAGLFHSRLIKRVLVVAPKTLLTHWTKELSVVSLKDKIRDYSGPNANARNYELKYAFKEGGILLTTYDIVRNNFKMIKGNFTNDFDDEEETLWNYVILDEGHIIKNPKTQRAQSLFEIPCAHRIVISGTPIQNNLKEMWALFYFCCPEVLGDKEQFKARYEHAIIQGNDKNATNRQKHIGSNVAKELRERIKPYFLRRMKNEVFLDSGTGEDKKLAKKNELIIWLKLTSCQRQLYEAFLNSELVHSSMQGSPLAAITILKKICDHPLLLTKKAAEGVLEGMDAMLNNQEMGMVEKMAMNLADMAHDDDDVELQVGQDVSCKLSFMMSLLQNLVSEGHNVLIFSQTRKMLNIIQEAIILEGYKFLRIDGTTKISERERIVKDFQEGPGAPIFLLTTQVGGLGLTLTKAARVIVVDPAWNPSTDNQSVDRAYRIGQMKDVIVYRLMTSGTIEEKIYKLQVFKGALFRTATEHKEQTRYFSKRDIQELFSLPEQGFDVSLTQKQLQEEHGQQLVMDDSLRKHIQFLEQQGIAGVSHHSLLFSKTAILPTLNDNDGLDSRRAMPMAKHYYKGASSDYVANGAAYAMKPKEFIARTYSPNSTSTESPEEIKAKINRLSQTLANTVLVAKLPDRGDKIRRQINELDEKLTVIESSPEPLERKGPTEVICLDDLSV

Oryza sativa subsp. japonica (Rice)

FUNCTION: DNA helicase that acts as an essential component of the spindle assembly checkpoint (By similarity). Plays an indispensable role in the development of seed endosperm (PubMed:25327517). Is required to secure sister chromosome separation during endosperm syncytial mitosis, which involves extremely rapid free nuclear cycles (PubMed:25327517). {ECO:0000250|UniProtKB:Q2NKX8, ECO:0000269|PubMed:25327517}.

3.6.4.-

ATP-binding;Cell cycle;Cell division;Chromosome;Cytoplasm;DNA recombination;Helicase;Hydrolase;Mitosis;Nucleotide-binding;Reference proteome

cell division [GO:0051301]; double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; reciprocal meiotic recombination [GO:0007131]; regulation of endosperm development [GO:2000014]; regulation of mitotic sister chromatid separation [GO:0010965]; transcription-coupled nucleotide-excision repair [GO:0006283]

chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]

ATP binding [GO:0005524]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA translocase activity [GO:0015616]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25327517}. Chromosome {ECO:0000269|PubMed:25327517}. Note=Localizes to the cytoplasm during interphase, but moves to the chromosome arms during mitosis. {ECO:0000269|PubMed:25327517}.

IPR014001;IPR001650;IPR027417;IPR038718;IPR049730;IPR000330;

3.40.50.300;3.40.50.10810;

A0A0P0XCU3

MEMALRPQSLLCPRSRLKVVIRPASSASGGGLAQYFLMTRRYTGSRIVRCMVSSSDCPNRKAKRTISLHTEVASSRGYAPRIAAESSIQEREHINSDEETFDTYNRLLRNESTEWKKLDTTEVDLSQDVSSSSMRKVDATDEAKLDILEDDLPRNLLNGVTMGEVDMLDEAGAEDDVFEVDLSALHNSTVGKMDAVNEVGTENDLFEVDLSALHSAAVGKVDVVDGAKAKEDLFEMDSLALHSVTMGKVDAINAAGAEGDKFEVDLSALASNNSMIEAVNVMDEAKAIEDTLEVDLSGNATSSSTYGEVKFEVDSLGNTSSTVMYGPADGAYEPRSDEVTFKVDSSENASNNVMYGRADVVDESWADEGIFEVDFFTNASSGAEYGKVDVVDEAKTDDFTFEIDSLEKDSNNKMHGKAHMVDEAWDDEAIFEVDLFGNASSIPIYGEVNVLDEARADDGKFEVDLLGNTSSNSTHEEVDVVDEAQTGEATFEVDLLGNALSSAIYKEVPVMGGAQDDEVDVDFSINASITETEKEADAVDEARVEDETFDMDLVGKQISIDSMNDDVVEEGTKHHRYPMLSSAFIEVKTIHETPVSLKPELMSVVMDQEQDKPISSVYQQEGSIFNLHAENQSTVDFHEREQMAITFDKQKESVAKLSKEDQQTAGLPEQNMSFDGVHRKSQSIIGLPFQHQSIVSSPEKYRSIVGFHGQNQSIISSHKQDKSIVGVPKKIQSIVGSTKHDDSIVGFRKQDRSIVSVPEQKQSIVGFHKQDLSIVAVSEQNLSIVAIPRESQSKQISIVRRHDPLHLKEVETKDRDGISKKSGGDDDLPHMLFEEELSQVEDVARAIAYKKQHEVDVISLTPDIQESPQDNIDPQELRRMLQELADQNCSMGNKLFVFPEAVKANSTIDVYLNRNLSALANEPDVHIKGAFNSWRWRPFTERLHKSELSGDWWSCKLHIPKEAYRLDFVFFNGRLVYDNNDSNDFVLQVESTMDEDSFEEFLVEEKKRELERVATEEAERRRHAEEQQRMGEQRAAEQAAREQAKKEIELKKNKLQNLLSSARTHVDNLWHIEPSTYRQGDTVRLYYNRNSRPLMHSTEIWMHGGCNSWTDGLSIVERLVECDDENGDWWYANVHIPEKAFVLDWVFADGPPGNARNYDNNGRQDFHAILPNAMTNEEYWVEEENCIYTRLLHEIREREEAIKIKVEKRAKMKSEMKEKTMRMFLLSQKHIVYTEPLEIRAGTTVDVLYNPSNTVLNGKPEVWFRWSFNRWMHPSGVLPPKKMVKTEDGCHLKATVSVPSDAYMMDFVFSESEEGGIYDNRNGTDYHIPVSGSNAKEPPIHIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLHVRQSFSLGGTEIKVWFGLVEDLSVYFLEPQNGMFGGGWVYGGNDAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATARIIFTIHNLEFGAHFIGKAMTYCDKATTVSHTYSKEVAGHGAIAPHRGKFYGILNGIDPDIWDPYTDNFIPMHYTSENVVEGKNAAKRALQQRFGLQQTDVPIVGIITRLTAQKGIHLIKHALHRTLERNGQVVLLGSAPDPRIQSDFCRLADSLHGENHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGSIPIVRKTGGLYDTVFDVDHDKDRARVLGLEPNGFSFDGADCNGVDYALNRQQSLLGLKPAVGSTPSAKGSWSKTGPGTGLPWTTLNCTIQLTNFEAPIQRWQEKASIGRYYKLNETWLKVKIFYLSCRYKLTQTWFKVKIFYLSYTYICRIKTLYSMHKQLWEYVSAMFPILSFNYEYLI

Oryza sativa subsp. japonica (Rice)

FUNCTION: Involved in starch synthesis in endosperm amyloplasts (PubMed:17297616, PubMed:17586688, PubMed:21417378, PubMed:21595523, PubMed:21730357). Plays an important role in the elongation of amylopectin B chains (PubMed:17297616, PubMed:17586688, PubMed:21417378, PubMed:21595523, PubMed:21730357). {ECO:0000269|PubMed:17297616, ECO:0000269|PubMed:17586688, ECO:0000269|PubMed:21417378, ECO:0000269|PubMed:21595523, ECO:0000269|PubMed:21730357}.

2.4.1.21

CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21; Evidence={ECO:0000305};

PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.

Alternative splicing;Amyloplast;Chloroplast;Coiled coil;Glycosyltransferase;Plastid;Reference proteome;Starch biosynthesis;Transferase;Transit peptide

amylopectin biosynthetic process [GO:0010021]; endosperm development [GO:0009960]; starch biosynthetic process [GO:0019252]

amyloplast [GO:0009501]; chloroplast [GO:0009507]

alpha-1,4-glucan synthase activity [GO:0033201]; glycogen (starch) synthase activity [GO:0004373]; starch binding [GO:2001070]; starch synthase activity [GO:0009011]

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. Plastid, amyloplast {ECO:0000305}. Note=Amyloplast or chloroplast, soluble. {ECO:0000305}.

IPR005085;IPR001296;IPR011835;IPR013783;IPR013534;

3.40.50.2000;2.60.40.10;

A0A0R4I9Y1

MTRKRKSGKKGKPLAQKKEAQKRGGSTSSSTTQKEGAQKGDGSSSSSTTQKDGAQKRDDSTSSSSTAQKEEGQKSDGSTSSSTTNKEGAQKRDGSTSSRLQKKGPQKRKGSTSSSRAHSRSRSKSKQTSYPSQARSRSHGQHNISTTESGPLSKEAQTQTSASLLVDKDTQTETVGQASQQTQTEINGNTETAEVSQPPQLSHEDVEMEGTVQPRTKGSESDGEKEESVKRKKRKLSEIGEPAKETEDSTKLSHECEEKVGDNQKNEDTNKHYGGDSLKDLKSVTEEPKSYAAAAATGKTGKVSKEQTNQIEANQDSTMESKSTQRKPSPVRAPAGPPMLTFYIYAVLDKRFRFNEQYDSLFLDYGNGNIKLQMKHFNIGKDGYLIEATFSVEDSAVRGGTIQYKYVVQQRQNQKSEIAVRYIEVPSYTTEKEFHLYEGYISCSSTVSITEWMMSLFHSEQKAVYKGWETSAHVLLDRIFLKWHPSNEESNMTFVQHLRSYKNAFESGFVEFPGNYTPFPIKVSELISAKLRMILKKESEALRTSESLDGVKSEALSVALSVFKVCCGCDVDLSLKDWGKLCQVVSECMGSFGEIQTTQTAPFINTVTGLMNLCAKKLITEVVLLVPVLHLLRNSEVNEAGPGSSMDEQRWTGLENISYQSFRERIRGLPDKRRMILKLIKDNLPMTKDNPKLLKSWLSLVAFEDVSEFVQLTGSFPELLIQSLMCRIIEAEKNTDANRTEKNLEVTGKVLNLLLKSIKKDRERIMKTEQLKLILQCCCNVHKSVCKTARLVPQYKVTVLSFQLLLKMAEIVYDGFFKGGEQMKQHQNEVLSKLNIIQEDFRKWRVELLLKPLMQTTGFTYPREMELWNDLYGIESSIPGVTERWKGFLDHDLRRRISQISDTDKIVVYVLVTSAKAVENSHANIQSCLKELCEAAIKNQCQSKKEGTLLCHLFSKTISWPVLSSIIVESAACFGEDHKGRLLDPQSAINFFLSQDKWNEWKLEDGASQLIAESQSFLGRLIQTLCQGSIPLGHLKTIFKYKTQFQKLYNQYKNNNKEMNVSISVSDLLSQREDDLKAFEQQKGYMTNLINMLGKISDVINVPELSSLEEIAKTNVQEVALDKLVEVETYFSKDDLKKNNTRRVLFYSDDQQVQDMAREMHDVNSSNLILSFWQEKAKDYFMAGPELLSLDLTEIYEDIWTPCLTKFLNFGNRIAVGQACFKEVEEALVGCGETGEGDRLKKEFMLMATMLDGHNENWPEQRLKQIREYRCLYDAAESAEVILKLKDRLGLQGDFSHIHSLTLVRDDSFKQNTLGSLSEDLIKARQKLADVERRHTACLEAFLKSDTLIKWIKAEIPSLKELKVFMELATISAGENDADIDRLASFETAVMGYAPLLYSLPQNVGFEEFFDYAKQVLDTLNKDEKLGDKLVDSNRWLDWLKGLRETHGSVEQSSLSLASAINTGGVYHVGWPDDFNGKTGLDNIFYVKVTKNNEEKTYRLNELLELQNKLMLMSSKGEKGKEQVIKFTQVFEGIQRMGRILLQLHRSGNMLFRNWAAEITCNHQNQPCIQVKFPLLSKCIVYQGEVEEELQKLSRSLEDFHKDWCNHLTKMRSQYYPLNHYSSEQIVYLCEWINSINIKKKPVPQQVWHLLTPIKPDCMLNDIKEAFEIATEPQSILQEDTAEELGPNSDFDLPLSFSLLDVSTECLEDLWKQFKENMSGFLTHHVDVETLGRFLSNLSNMNQLHIKRKIPSFLQEGRPNLVQCPAAELMSTTLSFYMESPENPLPTTDEVLMCQEETTEEEVEIFLRRCLGGAASNHKKIYTLVNPGSMSYDVSVALVEYFETQEVCAGPYYRLVMVCPVNQDRYIPSFFSNYKVQTGITISAERSQKYIRHHFKISYELATHSSVYPERLSVWMIASKRPAVGKSLYVRRLFEKFKGEFPRATLLTIRLIDPYIDMDGFVQTLSERLAPLRQQDPVLLHIDVAAVCHGLEEFLFKLLILECISDSKGTIWRRNKAHLVVIETLQRGHKTQTKMEPSHGFLNTLPTIFCRPPKDIKEIMKTNESFRSLDPLMDKEEFESEDIQRPYQYLRRFNRSMNLDRFTYQAHSVEGDPVDCLHHLLSNYGLKDPSWAELKHFTWFLNLQLKDCEKSLFCDSDFCGETLSGFKDFIVKFMIHMARDFASPSIDISDQSPSFFSKNEDEEEILSFRKRWENESHPYIFFNADHVSMSFLGFHVKQNGTILNAVDSKSGKVLMRNVMTQELFSDIQRQMINLSKDFDDLTREDKLQKMSFVVGAEKGCEKGKFDPDPTYELTTDNVMKMLAIHMRFRCEIPVIIMGETGCGKTRLVRFLCDLQREGRDVENMKLVKVHGGTTSETIYKKVREAEELAQKNRQKYKLDTVLFFDEANTTEAIFAIKEVLCDKTVKGYPLKKNSGLKIIAACNPYRRHTTKMVDRLERAGLGYRVKAEETEDRLGKVPMRQLVYRVHPLPPSMVPLVWDFGQLSDSTELSYIRQIVKKKMRDHRLPLSCQNVITNVLAASQKYMRNQADECSFVSLRDVERSMGVLLWFYNHRDIFFPSQDFPRFENVQMVLKCLVLAVGVCYYPSLENKRPYLATISKCFPDQFNSEESLEQEIASCQDFLLKNIQTRETIAKNMALKENVFLMVVCIELRIPLFLVGKPGSSKSLAKTVIADAMQRQASHCDLFKKLKEVHMVSFQCSPHSSPEGIIGTFRNCARFQKDKNLDEYVSVVVLDEIGLAEDSPQMPLKTLHPLLEDGCIDSDNPESYMKVGFVGISNWALDPAKMNRGIFVSRWDPSEKDLVETAEGICSSSQPVLLKIKHLLSKLAKCFLSICKTDSEQFFGLRDYYGLIKMLFDTVKCSDQEPSDKELAEAVLRNFSGQRDGFDPLDYFKDIFQNIQNVQRPNTLNMIEQNLDHHIDKECRYLLLLTTNNAALYIIQHHIFSKENYTQKCPEIVFGSGFPKDQEYAQICRNVSRIKACMETGRTVILLNLLNLYESLYDALNQYYVYFSGQQYVDLGLGSHRVKCRVHRDFRLVVVEDQEKVYKKFPVPLKNRLEKHKVDRSTDLAPWQHRVLEKLKKWAREFSKIQHSDSSEANFSVTDAFVGFHGDACASALLQALKKIDKLHHNKEENREESEAHHIDREFTEFQEKVNKFPDEAQEDDASMEVDKVQDAEIDEEMETLEDDSDLVKMVEGPVFVETRDKIESNKTMDEEEVYEIAKSFLLNCSTPDSVLRLKYSEFGNQETEELQKMYFHLQTHQSLRDLLNNHLNKTNQDKNRFLEVTTFSNLLTGADVRNLGPALGLSTERFLLLSLHQFDTEASFCNKIQSFLRESGPSVHILLIQMDMEESLCKNELIASAKYCTMNEILHLKSDECNIYTVFITKLSRIGEQCTSITGDKYIGFQGGVWLSAHIDDLRDSDDLCLNLKAFCGIPISQLISQTIESDVKESDEMNTNRQQSEKGDSVHLHSLSLLRSCTQKAVSLLRDTDEKTSRSMERMNILLGLLACDPGRTGARFQQVLLKRLVFALIQKEELIPNAKDWVYKVAKNHEALQECGTLRHTLWRYLQDFLTPVLARILEVIDRDCNLYQLYGEGLSEGLTQFWLDIFEDQQLLDLIPSQNTRAPDQEINVQCHLFVGEVEQPCAAPYSWLIKTYCQSLWEESEFVRSSEQDIKARIQQFVSAVSGSRLGSYIQKLSDVENVELGQRYLTDYVLLAFKVNSEDEHWVLQSAVLGCVFTLQTMMSVSPELSPSWIHAAAQIYNPRMDTLSHVLQLNPQLVSLIQQERPKRESPDMCEDILAVGICVEETKLLPVTSLTECLTFLQRVEQLQPCIERVLSPDYSALCSPGCLKYLETIQSVWQGILLVAVFIEKVVIKMKKGDERIIALTLKHCSQLHGLVEGSPDFRSKDNLQQIIRILNDYHEESISSELRYGVKCRVCLMELSEPFALPCEHVFCRSCLRRSMEREEAQHCPVCREPLSNNYQPTVSTTLNYSFALKQHKEIIKCCNTFFLEVVSRFCLTDDQDPPDDLVELLFSLLISAQGDVYKTRELTPFLECVDQSPVVRSVLPKLLMQYSLKQVKKHIQSYLEDLENKLLDKEDRTELYRLFVNCFQDTLLCSDSNGDHKHLRENTNFLSRLARKQTPSRQNDPAEFLMSMARLRMCLDSAAYILSKAICQKNNFVEAEFKFMEQVKAVCDYCDNDWYRVYLLRALNRQAGMDFLQALINSTDYEWIFPAEMMRLHRLIPAEVDRFLCCGQSYRALRDGVGESTQVGTTDGLKEALQASVGSSPLKNALLTLAVFRQVTCHFMSPERTLHPQEQQISILEKVIRDNMSGHAREFCTALLSNHIGGPGSNLRLGTGVPAQRRPVLELLVHACTVFYSGNRLISPLFNIASQPQNMTGAFLPTMPDDHTSEAKQWLSEKKLKMYFCSNSHACFVGECGRPMAKSKCATCGVEIGGEGHIPVPGFTEAYGDYDRTRPGHILGQARTRSEAPNRKLTLAQSCVLRLCLHLAMLQGLIHYQQGIRNMIHPEVSDVYQFLWQHLEKDMEVLGKTLTLNIDDSAIVIHLIFSRFLQTTPVANVDLSTRKSREQWEITVCKTAISPVLQNLDRELNNAQDLIAADNRLSNSPLVKVLRGDPQRMLQLPANCPTEHSAFWSPSSVLAVESISQQIDQAQAPLLTLFVQKVHYIRQLDCLPALAALLSDLIKVLPPGSETQNHTIASLLHCIPAGHQKKLMSERVEIYMKVWNQLRMEISSNASLGLDSTHCEKDITSESSGQFLFPSRKGAGSCLHAVIDVLSETHNSLVREARKLCQQTDSDYKVPLAVLSKSQLALCHPEREFLPLVLANCHYTLEKGQQTVSSYDHQGIERELSRRFFAGKPRIQTDTEKYLRRHHQNFTEVLNEVRAKIPQEMFWNPKQIHQAFSTNYHSTNRHKGLSRFYPDQPLSITTVPDLVIPRRPVGFQTQERHTLTPPGSHLTALNSLPAFSFCAPPISIRSTMELHLEEKDITSFPGLDSLPEELTWAKAAEIWRLAVQFKH

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity. Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS. Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (By similarity). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (By similarity). Also regulates lipotoxicity by inhibiting desaturation of fatty acids. Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger. Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of proteins downstream of rspo3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression. Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (By similarity). {ECO:0000250|UniProtKB:A0A0R4IBK5, ECO:0000250|UniProtKB:Q63HN8}.

2.3.2.-; 2.3.2.27; 3.6.4.-

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q63HN8}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q63HN8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q63HN8};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}.

Angiogenesis;ATP-binding;Cytoplasm;Hydrolase;Immunity;Lipid droplet;Lipid metabolism;Metal-binding;Multifunctional enzyme;Nucleotide-binding;Reference proteome;Transferase;Ubl conjugation pathway;Zinc;Zinc-finger

defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; lipid droplet formation [GO:0140042]; lipid ubiquitination [GO:0120323]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; protein K63-linked ubiquitination [GO:0070534]; regulation of lipid metabolic process [GO:0019216]; sprouting angiogenesis [GO:0002040]; ubiquitin-dependent protein catabolic process [GO:0006511]; xenophagy [GO:0098792]

cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleolus [GO:0005730]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}.

DOMAIN: Composed of an N-terminal stalk, a dynein-like core comprised of two catalytically active and four inactive ATPase domains, and a C-terminal E3 module. The ATPase regions do not generate movement but rather act like an intricate molecular 'switch'. {ECO:0000250|UniProtKB:E9Q555}.; DOMAIN: The RING-type zinc finger domain is required for the ubiquitin-protein ligase activity. {ECO:0000250|UniProtKB:Q63HN8}.; DOMAIN: The RZ-type (RNF213-ZNFX1) zinc-finger is required for the ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS). {ECO:0000250|UniProtKB:Q63HN8}.

IPR003593;IPR027417;IPR031248;IPR046439;IPR001841;IPR013083;IPR017907;

3.40.50.300;3.30.40.10;

A0A0R4IAH0

MTSHSRPDGLPSKEQPLELLKPSGVNHIPPVDVSVALPLQVPPSAIPMDLRVDHQFALAPTDPAQREHQLQQELLALKQKQQIQRQLLIEEFQRQHEQLSRQHEAQLQEHVKHQQDLLALKHQQELLEHQRKLERHRQEQEMEKQQREQKLQLLKNKERGQESAVASTEVKMRLQEFVLNKKKALAQRSLNHCLPSDPRYWYGKTQHSSLDQSSPPQTGISTYNHPVLGMYDPKDDFPLRKTASEPNLKLRSRLKQKVSERRSSPLLRRKDGPITTAKKRSLDMAESACSSAPGSGPSSPNNSSNNITNENGIAGSISNSAVEPSLAHRLTGREGPVSQLSLYTSPSLPNITLGLPATGPSSVASGQQDGDRMAVPGLQPGIPITTPFMPGAHLPSYLAASSLERESGSAHNTLLQHMVLLEQSAAQNSLVAGLSGVPLQSHSIHKLRQHRPLGRTQSAPLPQNSQALQQLVVQQQHQQFLEKHKQQFQQQQLHISKMMVKPSEPNRQHESHPEETEEELREHQGLGDPADPLPHGVTIKQEPPDEQDEDFQQRERQAEEELLFRQQALLLEQQRIHQLRNYQASMEAAGLSVSFPVHRPLSRAQSSPASATFPIVVQEPPAKPRFTTGLVYDTLMQKHQCMCGNSNIHPEHAGRIQSIWSRLQETGLRGQCECIRGRKATLEELQTVHSEAHVLLYGTNPLRQKLDSSVTPMFVRLPCGGIGVDSDTIWNEVHSSSAARLAVGSVVDLVFKVASGELRNGFAVVRPPGHHAEESTPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYLSLHRYDDGNFFPGSGAPDEVGIGPGVGFNVNMAFTGGLEPPMGDADYLAAFRSVVMPIANEFSPDVVLVSSGFDAVEGHPPPLGGYKLTAKCFGYLTKQLMGLAGGRLVLALEGGHDLTAICDASEACVSALLGNELDPIPEDILQQRPNANAIQSMEKVLEVQSKYWRSLQRSVSTLGYSLREAQRCENEEAETVTAMASLSVANKHMGKRPEEEPMEEEPPL

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. {ECO:0000256|PIRNR:PIRNR037911}.

3.5.1.98

CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000256|PIRNR:PIRNR037911};

Chromatin regulator;Coiled coil;Hydrolase;Metal-binding;Nucleus;Proteomics identification;Reference proteome;Repressor;Transcription;Transcription regulation;Zinc

embryonic cranial skeleton morphogenesis [GO:0048701]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural crest cell migration [GO:0001755]; perichondral ossification [GO:0036073]; pronephros morphogenesis [GO:0072114]; regulation of neural crest formation [GO:0090299]; response to stimulus [GO:0050896]

histone deacetylase complex [GO:0000118]

histone deacetylase activity [GO:0004407]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.

IPR046949;IPR000286;IPR023801;IPR037138;IPR024643;IPR023696;

6.10.250.1550;3.40.800.20;

A0A0R4IBK5

MKCPKCSHEALEKAPKFCSECGHKLQSQSYETTQGTPHDKSQTPSIVPQITNAEMDETGSESKSLEIQNANVSPKRPNENTSPNPKKKKRKKRKKEKKKKSGVSEGPSSLTSDLSDISLTDKEKKMDTDQSSDSDCSSCIVEDTPTPAEPSSHLSPPENETAGPAQLSASALTTGSSKDGEESIGTTQKPVSASASKAPLGVDQQTKEEKVKCKDEGQKSLSAKAQHTPNANVDQNANVQSDANIDKDSQNVEPQKSSSVKTKPSKSTVADPKKTESEKQKSGERDNENSTQPVSSPKLKRNQTEESQKMVFGPNSAPKKNRGSSADSAMKVEKKPAGGKKDSSADQKSKESEDTESQCVTLPKRNTRSTQHISSSDRLTIYFHAVLSKDFKFNPEEDLIFIRAGGPIGNWEENLVELSVSRDLKEHGFLVEGKFICRKIDAEAVSIPYKYVVYKQKKNKYDYEYIYKLDAEVPTNRCLFIKSHLLNDEGEWHQYDDIICAQPAKNMFEWVKKTIWSDEKKNVLQGRKIAGTIMLETIFDLLRSWSKINLNNFFSQLRQFYEIYRNPFVFEKKQTKWYQLDYDEKDVRELLKNFMLMHVTPELQKDSNEKSKFIQEPLKAGLIMLYVWKQYDLKLDYGTLSRLCTAVCLPNLPKDEFLSLWTDITESFSVINSFSDMVEALISKLKAENMPRWIIVIPLLHLLKGTSKPFEQVITKVNSKYEQSWAGLQGLRSNILSPGPQERRAMLNLMKTYGHLVEVDRLLIRSWMYLMPLDDLVECGSIFPVELLDILQLFTMKCPNNISFTSSESTAEALAHIQSQLLQHRYSCPDVDYGIQCIQAACKLLEKICSLVRYFGHSQNFTDIPVACMNLVASVSGFAQTKQEADTFAEKTLVLLNDTKQTVRAWMRQTFKGRLLNSHLFSSHLTGTSFSTETEVWNNIIAIDFVCKDFIKEWRDTFTTDFEGKYQQEDHLDQIEAYCSNIEKLKVSQPYLVNSVEKCALQAVSTICQTKSEWKLFARFNKFRINWRFGNLVSTIILKSWPKDDKGTYFEEEEAVLKHLLGWAAAKNIFQLHGADEKLIDQLSDEAKEKFAMATSLFTNVLNQLVTGKIKMKLLNHILEKKSVFLELLTLDCFSEEEQYKDIDAMKALIQTRQEEVKAIYHERALAGALIAMCHNVEEHVKVDYKYLEDLYSNDMNEMDLDLFMDVHELNQIPTEASLEVPYFELQDDVRSMAEILNIFKDSYIFKLRWGNEAALFVERAEDEELDELDELPITLDVLNEEIFLPCHAAYRNIYTSLKDGSIDFEDIDEIFRAYKGKYEKLAAEVAIMSKQDFNDDQHWVQTRIQQIKQYHELHLAVESAKVVMMVKETLCLQGDFQVLEKLLITTHSDFKSERLDSIDNELIQAKNVLVDITEPRRLCLQELGHRKNFVIWVKEALEDINELKVFVDLASISAGENDLDVDRVACFHDAVLGYSSMLYDLKPDAGFSLFNEMLKKLWKALDNDSNLPKKLCDSARHIEWLKTVKDSHGSVELSSLSLASAINSKGIYVINAQNQKKLALENILKLHIMEEHDGGCETRVYSLEDLRDLQNKLMLMSGKGEQGQCEVDQFAEVFASVQRLVSAFIDLYVAGNPLFRHWEANINCNSKEACIIIDFNLGSVVSVVMVEGDVTEQLPEVCKKMESCLRFWQDFMDKQRSQHYYLNYYTAEQLVYLCHQLAHNNMEEIDDQVLMMLSFIKPSCSTSDLRKAWHILQYDLIRKGPDQNDDLDFQTFVEVSSMTENESTEKSCPTSDDLIQQLGDASGSTKLGVIWNNYMRDMKAFLPDSLDVPSLGYLLEILANSHREDEGDMSQRDKTRTILRELPNGIASGRPNLIICPSEEILISCISIYMNSKNEPLPTYDEVLLCSATTPYEEVELFLRRCLSAGYRGKKIYTMLYVNQLNYEVSYKVEKFFQNQNAHTTNDYRLVLICESNKEHAYLPSAFSQFRLHLIPQQPIPSIQQYLHRHFAVPVGISSAAAVFKDRQNVGVVSSERSGVGKSLYIKRLYEKLKLNSKKPSQLKCIRLTEPKVDENVIIQSLISVLKKNDLSVYHFDVTTMVKKGLHEFLFRLLILGYLMDSKGNMWKSSNKHLYVIEILRPGLSQNDRRAGAKVSFNFLDVFPIVYCRSPKEVLELEMRMEEHPSFGLSDDPLMDDQEFRSEAYQRPYQYLQRFYNGINLDEFLYQGVEGSHVECLQMLFEYCGIIDPSWAELRNFAWFLNLQLQDCEKSVFCDFSFVGDTLLGFKNFVVEFMILMAKDFATPSLSISDQSPGRLHEDFSSANEEDLAPFKIRKRWESEPHPYIFFNDDHDSMTFIGFHLQPNAQKGVDAVDPSNNRVIKQNIMTMELYEGLKLQRVPFNIDFDQLPRWEKIERLSRVLGIQWPLDPDETYELTTDNMLKMLAVHMRFRCGIPVIIMGETGCGKTRLIKFLCEMHRSGVATDNMKLVKVHGGTSSEMIYTKVREAEAMALRNKLDYGFDTVLFFDEANTTEAISSIKEILCDNSAEGQNLTENTGLKIIAACNPYRKHTDVMIKRLESAGLGYRVRAEETDEKLGSIPLRQLVYRVQALPPSMIPLIWDFGQLNDHTEKMYIKQIVERVAETHSIDSGYITVITDVLSASQKYMRTRQDECSFVSLRDVERCMQVFGWFYKKHLMLLSELDKFESIQRTEKTDQHPKDTDERNPILWSLLMAVGVCYHACLEDKEKYRKKICKYFPAAYSPMKVMQEISVIQDIFLEGVPMGENIARNNALKENVFMMVICIELRIPLFLVGKPGSSKSLSKTLVADGMQGQAAHSDLFRKLKQIHLVSFQCSPHSTPEGIINTFKQCARFQEGKNLSEYVSVVVLDEIGLAEDSQKMPLKTLHPLLEEGCIDDQPSPHKKVGFIGISNWALDPAKMNRGIFVSRGDPDENELIESAKGICSSDVMILEKVRECFKPFAHAYLRICKKQEKGFFGLRDYYSLIKMMFAVAKACDQKPSAEQIVKAVLRNFSGKDDVDAVTFFTSRLNIKPELETISAIELVRENVTAIGQDEECRYLLVLTKNYAALRILQQTFFSDQCQPEIIFGSSFPKDQEYTQICRNINRVKICMETGQTIVLLNLQNLYESLYDALNQYYVTLGGQKYVDLGLGTHRVKCRVHKDFRLIVIEEKDIVYKQFPIPLINRLEKHYLDLNTLLKSEQKDIVKNLEQWVQCFTDVKNKHSVAPSARRYSPADAFIGYHTDTCASVVMQVTEQLKGQELSDPRKGILDESKLILLNCATPDAVVRLDCTSLFNVESEHLSRVYFEDQMHNSLAEFILSHIQQEGCSGAFFTEVTTFSRLLTASETQQLQNVVQNIELLSLQQFDTEQSFLKKIKNYLENTTGDKILLIQTDFDEGFQKLNVIASAKYSSINEINKFKKEGSGKIFVYFITKLPRMDGGTSYIGFNGGPWKSIHIDDLRRPKDIVSDIKALQGLTISQLFEEKAEKVDETEAMEVEDMYAGGEDEEDEEKMELEENNGCKDVLDTTALVRSCVQSAVGMLRDQTEGGMRSTKRVEILLMLLAEDQTLQAEFLKTLKTRLHSLLVAHDDNTISAKSWVSREALNVDALHEGGTFRHALWRRVQAVVTPFLAQLVSVVDRDCNLDLLLDRNSGEPLKKLWLEIFRDDKFLSVSPYTRTENNSATKTILVQNYMSVDRNKGCTMPFSWRIKDYLEDLWKHALQQEGHTVKQFEEFFWKTPLGRYISEATNEMQMEFFYRYLQDFISMTMNVTSEVDFEVLRGAFTSSVNEVRIAHEAHESEALSLVWIHVAYHHFKNRIQNLHRMMSLEPQISQMLLENRYASEGKELVLDVLAAVACIEYLEPQNLDGDDQSLAWLRRVKKLQVPVELVCSLESLHNRGDRCRQMVTNIQHGWRRIYSLVLFVEHMLLGVGDLQQKLKPVVLEHTQLLAQVLEQDSNLKKKKPFEAVITVLKTCKDKASQRIIRFGLQLCPVCMGDPRDPLSLPCDHIYCLTCIRQWLVPGQMHCPLCVQEVPDNFELKPSDELRRLISQNASFRMRCNAFFIDLVSTMCFKDNTPPSKDIILHLLSLLMVEASSLPPFKGRDRRFLTKALSPFDDSVDKNPVVRSVVLKLLLNYSFDHVKDYLQQHLTEVEQSKILEETDKAELYCLYMNCLEDSMYDRTQWHTVAEQQNCFLEETRFLLEFLQSDSVSAHTATVEHLQRLARVRLCLDMAADLLVANAGIHDDPSAFIQAFWNNVVNLCRQSRNDWYRVYLIRKLCSLQGVECVKNLLLQETYRWLFPQEILEMNQDDSQIDQYLACGADYKTIRDAVAKFMLDLHINGIQKAIEDCNCTPMKKAVYVLMAFFREVTSLHRTGNPNMHPKPEHCAGLEHFIKNSAIFVNNEMKAFAEKLVRNQLGALRVRPHMPSRDLSLVEVTIHMAAVLLCGNLLLLQPLQKLALSPNNMMASFIPTMPDDMLAVAQQAMGHLQWYFCPNGHPCTVGECGQPMEVSRCPDCDAEIGGSNHRPVDGFRAMQIQADRTQSGHILGDAQRRDLPDMQDTKNMSPAPFALLRLLTHMSMLIGTQNNPQSIMQIIKPAVVHPDAFLMQHLLKDMEQLSKALGKGVDDTVSTIHLAIHSLLEPHQTSQWPDPYDPNLSTKDARNGWENAMNNDVITHHLKVLEHQLKEVNAFIREDERVSSNPVMKLTFGEPGRFLRSLPQNSLIHNSSIWSCRNKVSLMSLTHIVEQNNGRDTLPVLWRFLQREAELRLVRFLPDILVLQRDLVKKFQNITDLTYKTIREFLQDQKAASLTAWYEKRIKIFLTTWNQIRVSLANTGEIKLPADYTEKDLGLDADLQVLLPQRRGLGLCSTALVSYLITIHNDLMYTVEKHTGDDSDYKISPAELTELHVIRYEYDRDLLPLVLANCQYSMECGQETLLEYDLPKIQQQILTRFLQGKPLITINGIPTLVNRQDRNYEIIFKDVKGKVQQELLQPLTQYDLVKELQSYSDVCEALSTVELAVGFLAMTGGEPNMQLGVYLKDVLQMTDHMATHVFKALSRCSLKHCVALWQLLSSLKSETMLRLKRDPFVGISKEYKQPLQEEHKRLLTSFFTKSSADAFLLEMHEFLLLVLKSPKATDTYRPDWRLKHTVVSYMERKDLDVPPEVEEFFPKEILLSEYTSTWNFSVNLRQKRSQS

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (By similarity). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS (By similarity). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (By similarity). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (PubMed:30705059). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (By similarity). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger (By similarity). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of proteins downstream of rspo3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression (By similarity). Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (By similarity). Also involved in neuromuscular regulation (PubMed:26530008). {ECO:0000250|UniProtKB:Q63HN8, ECO:0000269|PubMed:26530008, ECO:0000269|PubMed:30705059}.

2.3.2.-; 2.3.2.27; 3.6.4.-

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q63HN8}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q63HN8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q63HN8};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}.

Angiogenesis;ATP-binding;Cytoplasm;Hydrolase;Immunity;Lipid droplet;Lipid metabolism;Metal-binding;Multifunctional enzyme;Nucleotide-binding;Reference proteome;Transferase;Ubl conjugation pathway;Zinc;Zinc-finger

blood circulation [GO:0008015]; defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; lipid droplet formation [GO:0140042]; lipid ubiquitination [GO:0120323]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; protein K63-linked ubiquitination [GO:0070534]; regulation of angiogenesis [GO:0045765]; regulation of lipid metabolic process [GO:0019216]; sprouting angiogenesis [GO:0002040]; ubiquitin-dependent protein catabolic process [GO:0006511]; xenophagy [GO:0098792]

cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleolus [GO:0005730]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}.

DOMAIN: Composed of an N-terminal stalk, a dynein-like core comprised of two catalytically active and four inactive ATPase domains, and a C-terminal E3 module. The ATPase regions do not generate movement but rather act like an intricate molecular 'switch'. {ECO:0000250|UniProtKB:E9Q555}.; DOMAIN: The RING-type zinc finger domain is required for the ubiquitin-protein ligase activity. {ECO:0000250|UniProtKB:Q63HN8}.; DOMAIN: The RZ-type (RNF213-ZNFX1) zinc-finger is required for the ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS). {ECO:0000250|UniProtKB:Q63HN8}.

IPR003593;IPR027417;IPR031248;IPR046439;IPR018957;IPR001841;IPR013083;IPR017907;

3.40.50.300;3.30.40.10;

A0A0R4IKJ1

MTSENHTTIKADSALVMSPTGSTSQAAPFSPSTSKPIQELPDELIQAGWSKCWSKRENRPYYFNRFTNQSLWEMPVLGQHDVISDPLGLNAAPASGEANADAGLGNGQRKRHPSEDASQAGPNSFKRPKVEIPATPTTPTVPISPSTPGVKPWVNTTTDEKQGQASTPAPAPYRPSVVYWDLDIQTNAVIRERAPADHLPPHPEIELQRAQLTTKLRQHYHELCSQREGIEPPRESFNRWLLERKVVDKGLDPLLPSECDPVISPSMFREIMNDIPIRLSRIKYKEEARKLLFKYAEAAKKMIDSRNATPESRKVVKWNVEDTMNWLRRDHSASKEDYMDRLEHLRKQCGPHVASVAKDSVEGICSKIYHISAEYVRRIRQAHLTLLKECNISVDGTESAEVQDRLVYCYPVRLSIPAPPQTRVELHFENDIACLRFKGEMVKVSRGHFNKLELLYRYSCIDDPRFEKFLSRVWCLIKRYQVMFGSGVNEGSGLQGSLPVPVFEALNKQFGVTFECFASPLNCYFKQFCSAFPDIDGFFGSRGPFLSFSPASGSFEANPPFCEELMDAMVTHFEDLLGRSSEPLSFIIFVPEWRDPPTPALTRMEASRFRRHQMTVPAFEHEYRSGSQHICKREEIYYKAIHGTAVIFLQNNAGFAKWEPTTERIQELLAAYKVSGRSLPSPGPSSTNTGEKDSKPAPERTAPSQDNSSPVDKTAQDTTNT

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs (PubMed:30467178). {ECO:0000269|PubMed:30467178}.

2.1.1.62

CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:22744, Rhea:RHEA-COMP:11518, Rhea:RHEA-COMP:11519, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85958, ChEBI:CHEBI:85959; EC=2.1.1.62; Evidence={ECO:0000269|PubMed:30467178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22745; Evidence={ECO:0000269|PubMed:30467178};

3D-structure;Methyltransferase;Nucleus;Reference proteome;Transferase

mRNA methylation [GO:0080009]; positive regulation of translation [GO:0045727]

nucleus [GO:0005634]

mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity [GO:0016422]; RNA polymerase II C-terminal domain binding [GO:0099122]; S-adenosyl-L-methionine binding [GO:1904047]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4Z3}.

IPR029048;IPR039881;IPR022035;IPR001202;IPR036020;

1.20.1270.10;2.20.70.10;

A0A0R4ILA2

MTAGVRGMACWGLCGFLFGLLRISSACPVSCFCNASRISCIDQEPGIEDFPVLMPESDMENITDIYISNQKRLFTINEDHMKFYSNLRNLTVTNTHLTYVSTMAFFNNSKLQYLNLGDNNLSTLSWMAMRNSNVSTLLLSGNPLQCACENIWIKLWLDDSERDVLQCLQEGGKAKTLSRLTLPLCEHPRVEVFPTDVSQMAGSDATVICNASGSPTPELTWTLNSSEHPPLSTSHEISKMDLQSVLTLNGLSPNDNGRKLICSAENIVGQIEATVMLNISFPPTVLELYLPERSQDWCIPFVVTGNPRPDLHWYHEGKPLEEQEYIRTEIHDITNTEYHGCLKLDTPTHIHNGIYTLVASNEFGEDRGNVTAHFMRIPDVDHSGIEGVFYYDTTVSPDIPPLEDRVAVYIVVGIAGVALTGCILMLVFLKYGRSSKFGMKGSSSVISNDDDSASPLHHVSNGNNTPSSSEMGPDAVIIGMTKIPVIENPQYFRNPGSMLKSDTLVQHIKRHNILLKRELGEGAFGKVFLAECYNLSPDQEKILVAVKTLKEASESGRADFHREAELLTNLQHEHIVKFYGVCVESDPLIMVFEYMKHGDLNKFLRAHGPDAVLMADGQQSLLVELTQPQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRRFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPKEVYDLMLGCWQREPYMRLNIKEIHNLLQSLAKASPVYLDILG

Danio rerio (Zebrafish) (Brachydanio rerio)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171, ECO:0000256|RuleBase:RU000312};

ATP-binding;Developmental protein;Differentiation;Disulfide bond;Glycoprotein;Immunoglobulin domain;Kinase;Leucine-rich repeat;Membrane;Neurogenesis;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

cell differentiation [GO:0030154]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; lateral line development [GO:0048882]; nervous system development [GO:0007399]; neuromast primordium migration [GO:0048883]; positive regulation of neuron projection development [GO:0010976]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; trans-synaptic signaling by neuropeptide, modulating synaptic transmission [GO:0099551]

axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; synapse [GO:0045202]

ATP binding [GO:0005524]; brain-derived neurotrophic factor binding [GO:0048403]; brain-derived neurotrophic factor receptor activity [GO:0060175]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR007110;IPR036179;IPR013783;IPR013098;IPR003599;IPR011009;IPR001611;IPR032675;IPR020777;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;IPR002011;

2.60.40.10;3.80.10.10;1.10.510.10;

A0A0R4IPY6

MMEPSFGISESQCIATVRGHEIRSGQKEPRLLSLLECSGQFKLDILSNPDAIVLSPVSQLSIPINNHFRIIREAEEALLIDIDSISKTVRIRLRGERTPELLLELQDDGQTQSFLEHVTKAKQQAERSSLPRKMEPVVPAPVKDCVPVPPQRGTSKSFSNNINNSTLANPSNTDSTRSLATDFGFEENFNHVLKVEEKKNKQNRLVAQREPPPPPIPPLPPRKGTNTSLTGPATKERPPSVQNATPVRNEFQSVDRSVSWSESPSNSTIRQAMMSSHAGSREGLLKYRLSKKEKEYVDIKNFKFFVGTWNVNGQSPDSSLGPWLSSDPDPPDVYALGFQELDLSTEAFFYMDSSKEQLWVDAVERGLHQKARYIQVRIIRLVGMMLVVYIKKEHKDQIREIASESVGTGLMNKMGNKGGVAVRFVFHNTSFCFVNSHLAAHVDDFERRNQDYKDICARMSFHLLEYPPVSIVKHDVVIWLGDLNYRLCLPDAGEVKRLIAEKELRRLQEYDQLNLQRKTKRVFTDFMEGEINFIPTYKYDAKSDRWDSSGKCRIPAWCDRILWRGSNVKQLHYRSHMELKTSDHKPVSSVFSIGVKMVIEQRYKKIFEEIVRDMDRMENDFLPSLSLTRREFTFENVKFRQLQRQSFLITNDGQVACTFAFIPKLNDSQYCKPWLRAEPCEGVLDPNEKIEIFLEVYVSKDSVTLLNSGEDNIEDILVLHLDRGKDYFITVSGNYLPSCFGTSLETLCRMKKPIREIPITKLIDLGEDSCMEKEKARMTFLLDSAGTEDKPLKIPKEVWLLVNHLYTKACQQEDLFQTPGLQDELQSIIDCLDTSIPDSIPGCNHSVAEALLIFLEALPEPVLCYELFQRCLECSHDSRLCKQLISQLPRAHRNVFRYLMAFLRELLKHSIDNNLNANLLATLFASLLIRPPPNLAGKQTQHDRQKANDFILGFLMAGDED

Danio rerio (Zebrafish) (Brachydanio rerio)

3.1.3.36

Coiled coil;Cytoplasmic vesicle;Endosome;Hydrolase;Lipid metabolism;Proteomics identification;Reference proteome

brain development [GO:0007420]; chordate embryonic development [GO:0043009]; cilium assembly [GO:0060271]; cilium movement [GO:0003341]; cilium organization [GO:0044782]; embryonic cranial skeleton morphogenesis [GO:0048701]; endocytosis [GO:0006897]; glomerular filtration [GO:0003094]; melanosome transport [GO:0032402]; neural crest cell migration [GO:0001755]; neuromast development [GO:0048884]; phosphatidylinositol dephosphorylation [GO:0046856]; pigmentation [GO:0043473]; pronephric proximal tubule development [GO:0035776]; regulation of endocytosis [GO:0030100]; regulation of receptor recycling [GO:0001919]; regulation of receptor-mediated endocytosis [GO:0048259]; renal filtration [GO:0097205]; response to epinephrine [GO:0071871]; signal transduction [GO:0007165]

cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; membrane [GO:0016020]; phagocytic vesicle membrane [GO:0030670]

inositol phosphate phosphatase activity [GO:0052745]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]

SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000256|ARBA:ARBA00004580}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004146}. Endosome membrane {ECO:0000256|ARBA:ARBA00004608}. Membrane {ECO:0000256|ARBA:ARBA00004370}.

IPR036691;IPR005135;IPR013783;IPR046985;IPR000300;IPR048869;IPR037793;IPR037787;IPR031995;IPR008936;IPR000198;IPR047078;

2.30.29.110;3.60.10.10;2.60.40.10;1.10.555.10;

A0A0R4IQG7

MQESEPSVCQLQPNIISVRLFKRKIGGLGFLVKQRVCKPPVIVSDLIRGGAAEECGLVQVGDIVLAVNNKPLVDMSYERALETLKNVSPESHAVLILRGPEGFTTHLETTLSSDGKTKTIRVTRPVNPAQSRPCERCSPLTPNMTKELRAIENLSSSSTPRKESRDDKPLIPLLSQDSLLREGGHAGLLLNGVEDNNDLLKEIEPVLKLIKNSKKEINGEGQRVIDRKDAEVQVERDLGVGNGQNAQLASDNDRVFDDLWRKDNMPTVLNNPYSESDKPQSYERVSPTKAVQNGSPSKCPRFMKVKNWETGALYNDTLHHSSSKVPICTEHVCIGSIMVPNQHAHKPDEDRRKEELLPLATDFIDQYYTSIKRCCSKAHVDRLEEVKKEIETSGTYQLKDTELIYGAKHAWRNAARCVGRIQWSKLQVFDARDCTTAHGMFNYICNHIKYATNKGNLRSAITIFPQKTDGKHDFRVWNSQLIRYAGYKQPDGSILGDPASVELTEICMQQGWKAPKGRFDVLPLLLQANGNDPELFEIPDDLVLEVPIIHPKFEWFKELNLKWYGLPAVSNMLLEIGGLEFTACPFSGWYMGTEIGVRDFCDSSRYNILEEVATMMGLDTRKTSSLWKDQALVEINIAVLYSYQMSKVTIVDHHSATESFMKHMENEYRVRGGCPGDWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGVNGTPTKKRAIGFKKLAKAVKFSAKLMGQAMAKRVKATILFATETGKSQDYAKTLCEIFKHAFDAKVMSMDEYDTVDLEHETLVIVVTSTFGNGDPPENGEKFGAALMEMRHPTTSVEDRKTYKVRFNSVSSYSDTRKSSSDEPESKANFESTGPLANVRFSVFGLGSRAYPHFCAFAHAVDTLFEELGGERILRMGEGDELCGQEESFRTWAKKVFKAACDVFCVGDDVNIEKANDSLISNDRSWKKSKFRMTYTAEAPTLTQALYSIHKKKVYGAKVVQRQNLQSARSNRLTIFVRLDANNHESLKYLPGDHLGVFPGNNEDLVTTLIEKLEDAPPVNQIVKVEFLEERNTALGVISNWTDESRIPPCTIYQAFKYFLDITTPPSPVLLQQFAPLATNEKQRKRLEVLSKGLQEYEEWKWYNNPTMVEVLEEFPSLQIPSTLLLTQLPLLQPRYYSISSSPDLYPGEIHLTVAVVSYRPRDGEGPIHHGVCSSWLNSLDEGDTVPCFVRGAPSFRMPKDSQVPCILIGPGTGIAPFRAFWQQRQYDVENKGIKACPMILVFGCRQSQIDHIYKEQTIQAKNKEVFKELYTAYSREPGRPKKYVQDVLREQLSETVYKCLREEGGHIYVCGDVTMAGDVLKTVQQIFKLHGNMSLEDAGFYISKLRDENRYHEDIFGVTLRTYEVTNRLRSESIAYIEESKKDIDEVFCS

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions. {ECO:0000256|PIRNR:PIRNR000333}.

1.14.13.39

CATALYTIC ACTIVITY: Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; Evidence={ECO:0000256|ARBA:ARBA00035595}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898; Evidence={ECO:0000256|ARBA:ARBA00035595};

COFACTOR: Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin; Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000256|ARBA:ARBA00001950}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|PIRNR:PIRNR000333}; Note=Binds 1 FAD. {ECO:0000256|PIRNR:PIRNR000333}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|PIRNR:PIRNR000333}; Note=Binds 1 FMN. {ECO:0000256|PIRNR:PIRNR000333}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|ARBA:ARBA00001970, ECO:0000256|PIRNR:PIRNR000333};

Calmodulin-binding;FAD;Flavoprotein;FMN;Heme;Iron;Metal-binding;NADP;Oxidoreductase;Proteomics identification;Reference proteome;Ubl conjugation

arginine catabolic process [GO:0006527]; collateral sprouting [GO:0048668]; hematopoietic stem cell differentiation [GO:0060218]; liver development [GO:0001889]; muscle contraction [GO:0006936]; negative regulation of blood pressure [GO:0045776]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide mediated signal transduction [GO:0007263]; response to hormone [GO:0009725]; response to lipopolysaccharide [GO:0032496]; retrograde trans-synaptic signaling by nitric oxide [GO:0098924]; serotonin receptor signaling pathway [GO:0007210]; ventral spinal cord development [GO:0021517]

cytosol [GO:0005829]; dendritic spine [GO:0043197]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; sarcolemma [GO:0042383]

calmodulin binding [GO:0005516]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitric-oxide synthase activity [GO:0004517]

SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004468}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004468}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}.

IPR003097;IPR017927;IPR001094;IPR008254;IPR001709;IPR029039;IPR039261;IPR023173;IPR044943;IPR044940;IPR044944;IPR012144;IPR004030;IPR036119;IPR001433;IPR001478;IPR036034;IPR017938;

2.30.42.10;3.40.50.360;6.10.250.410;3.90.440.10;3.40.50.80;2.40.30.10;

A0A0R4IVA4

MTLDNLKHSAILSTLFKMADDNDLLGASEFIKDRLYFATLRSKPKSTANTHYFSTDEEFVYENFYADFGPLNLAMLYRYCCKLNKKLKSFTLTRKRIVHYTSFDQRKRANAAVLIGAYAVIYLKKTPEEAYRALISGSNASYLPFRDASFGNCTYNLTVLDCLQGIRKALQHGFLNFETFDVNEYEHYERVENGDLNWITPGKLLAFSGPHPKSKVENGYPLHAPEAYFPYFRKHNVTTIVRLNKKIYDAKRFTDAGFDHYDLFFVDGSTPSDIITRRFLHICESTSGAVAVHCKAGLGRTGTLIGCYLMKHYRFTSAEAIAWIRICRPGSIIGPQQHYLEEKQASLWAHGDSLRSKQRQYQDRSVPQLISSMDNLSISTSIFKSHSLDRMEENDYAENDLGMTQGDKLRALKGRRQPRSATTGAIRVEDVKVHTRSPSQPLSRMKPPASSQGSISPLKSSKVPASSSSSSSSSSVSASAKRIGRSSSSSTNLKSTRLASSLGNLYEPNTESISSGKPPSPSSFTPHPVRTTYNYHYEVNNNNNQYSTTSSPSKSLGYNLNHSGPSGASANARLSAGEQGHQRNPPAGLSGLSTRHLSRSIPSLQSEYVQY

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis. {ECO:0000250|UniProtKB:Q9UNH5}.

3.1.3.16; 3.1.3.48

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:Q9UNH5}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:Q9UNH5};

Cell cycle;Cell division;Cell projection;Cytoplasm;Cytoskeleton;Hydrolase;Nucleus;Phosphoprotein;Protein phosphatase;Reference proteome

cell cycle [GO:0007049]; cell division [GO:0051301]; cilium assembly [GO:0060271]; dephosphorylation [GO:0016311]; microtubule cytoskeleton organization [GO:0000226]; positive regulation of cytokinesis [GO:0032467]; regulation of exit from mitosis [GO:0007096]

centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinocilium [GO:0060091]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]; spindle pole [GO:0000922]

myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UNH5}. Cell projection, kinocilium {ECO:0000250|UniProtKB:Q6GQT0}. Note=Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the mitotic spindle pole and at the central spindle (By similarity). Present along both the transient kinocilia of developing cochlear hair cells and the persistent kinocilia of vestibular hair cells (By similarity). {ECO:0000250|UniProtKB:Q6GQT0, ECO:0000250|UniProtKB:Q9UNH5}.

DOMAIN: Composed of two structurally equivalent A and B domains that adopt a dual specificity protein phosphatase (DSP) fold. {ECO:0000250|UniProtKB:Q9UNH5}.

IPR044506;IPR029260;IPR000340;IPR029021;IPR016130;IPR000387;IPR020422;

3.90.190.10;

A0A0R4IVA6

MAGAKPGVHALQLKPVSVNEVLKRGSKFIKWDEEANSTPSLITLRVDPNGFFLYWTGGTSMEAEILDMSHIRDTRTGKFAKTPKDQRIREMLFSGKADGNSDSRLLTVVYGNDLVNISFLNFQAVQDGYCKLWTDELFKLATNMLSQNASRNTFLLKAYTKLKLQVTQDGKIPVKNILKMFSDKKRVEMALEHCGLIFNRVDGIKPDDFTWEMFQNFLNKLSPRPEVERIFVDLGSKGKPFLSLDQLMDFINRKQRDSRLNEVLYPPLKRDQVRQLMEKYETNTSQLERDQISLMSFTKYLGGEENTVVPPERLDIIDDMNQPLSHYFINSSHNTYLTVGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPIITHGFTMTTEIPFKDVIEAIAESAFKTSPYPLILSFENHVDSAKQQAKMAEYCRSMFGDALLIDPLDKYPLVPGQQLPSPQELLGKILIKNKKKHHHRASNGGSIRRKDGTDEQSSPLNDCPLSDGDVGQLMSNGGEKLAERMAKDHDNSKSIDRGDGESDEEEEEEPIPDPKKHNNTDEGTAYSEVNATEEMSTLVNYIEPVKFKSFEVAAKRKKFFEMSSFVETKGMDTLKNSPTEFVEYNKKQMSRIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQTLDLAMQLNMGVFEYNGRCGYLLKPEFMRRTDKHFDPFTTDIVDGIVANTVKVKIISGQFLNDKKVGVYVEVDMFGLPADTKRKYRTKTSNNNSLDPVWDDETFVFNKVVLPTLASLRVAVYEENGKFIGHRILPVSALRPGYHYICLKNELNQPLMLPSLLVYTEVQDYIPNEHQEYAEALTNPIKHLSLLAQRESQLLALMEDPTEGGPTKQEEGDGTDSSCVTSADPIFPLPSSPTLPSVPTDLNPPPSGQKEDLVNNVLKVIEPESVDELKQHNSYLKLLKKQCKEFKELSKKHLKKMLALSKEQKTLFNQQSSELQRKRSQIEKRIRTSLKKNGSEDSVHRELNELDLELQKQMEQFREEHMQKLLVLRQGQLQMEKEVKQFHLKEANQKLKDIAIECQAAQIKKLKDVCDKEKKELQKMLDRKRLNSIVEARKAEKEIRDVNEINRKHIQESVSLIRQLEVSQGKRQEKLKALHKDILQKIEEEIPMNQARLTRDFEAELKRLPEEISQYLQELESKGSRKDSLMGQTNDGPNSGPPSNCSTPPYSSPNHSWSNIANVSSLLLDSSTSSSSAKSETDTTGVY

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. {ECO:0000256|PIRNR:PIRNR000956}.

3.1.4.11

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433; Evidence={ECO:0000256|ARBA:ARBA00023726}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485; Evidence={ECO:0000256|ARBA:ARBA00023726}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={ECO:0000256|ARBA:ARBA00023674}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; Evidence={ECO:0000256|ARBA:ARBA00023674};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR000956-2}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000956-2};

Calcium;Coiled coil;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Phosphoprotein;Proteomics identification;Reference proteome;Transducer

cartilage morphogenesis [GO:0060536]; embryonic viscerocranium morphogenesis [GO:0048703]; G protein-coupled receptor signaling pathway [GO:0007186]; lipid catabolic process [GO:0016042]; negative regulation of calcium ion import [GO:0090281]; negative regulation of vascular permeability [GO:0043116]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; release of sequestered calcium ion into cytosol [GO:0051209]

cytoplasm [GO:0005737]

calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; phosphatidylinositol phospholipase C activity [GO:0004435]

IPR000008;IPR035892;IPR011992;IPR001192;IPR016280;IPR014815;IPR042531;IPR009535;IPR037862;IPR017946;IPR015359;IPR000909;IPR001711;

2.30.29.240;2.60.40.150;1.10.238.10;3.20.20.190;1.20.1230.10;

A0A0R4IVY5

MEMSIGESLTARFEKIDAMLKDPKSEVNTDCLLDSLDALVYDLDFPALRKNKSIDDFLKRYKDTISKIRELRMKAEDYEVVKVIGRGAFGEVQLVRHKATRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSNWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDGIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKDGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNALTFPEDSDISKDAKSLICAFLTDREVRLGRNGVDEIKRHGFFKNDQWTWENIRETAAPVVPELSCDTDTSNFDDIEEDRGEEETFPIPKAFVGNQLPFVGFTYYSNNLFSQESTIKTSDKRSSTKEDKSLLENLQKRIYQLEEQVHSEMQLRDEMEQKCRASNTKLDKIMKELDEESNLRKSVEANMSILEKDKIMIQHRATEYQRKADQEAEKRRNLENEVSTLKEQLEDLRKISQNNDKIAQLQNQLGEANDLLRAESDTVMRLRKSHTEMGKTMSQLESINRELQEKIRAAESVKQQLEKELLQLQTTLDTERRSCSQGSEEIRELQVRIMGLQEDNKNLKQSLTKVETERKHVQERCNILEKEKNSLEIDLNYKLKTLQQRLDQELTEHRITKAQLTDKYESIEESKSAAMHAVEQKVSEETTLRMRAESRVVEVEKQCSMLEFDLKQSVQKMEQLMKQKERLEDEVKDLRVQLEQETGKRVMSQNELKNWKMDSERLKGTEKQLKQEINAALENKRSVEFQLAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKDEIEEKNRQTQEALKRVQDLNSEKESLSAQLDLTMTKAESEQLARALQEEQYVELSQEYKKAVSRYKQEISEKDSTISQLEDSNKTLTKDVEILSKEKTEFNERIQAQEQEFAAEREELTNSIKANYEKALNIERTLKTQAVNKLAEIMNRKDMKDQKKRGSTTDLRKKEKENRKLQLELNQEKEKFNHMAFKYQKELNEMQAQWAEECTYRNELQMQLDSKESDIEQLREKLNDLQLRVDNSSVTSLQPDELDSNIAESRLEGWLAIPNRANIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETDEIPRIFQILYANEGECRKETDVESVPQGDKANCLPHKGHEFIPTLYHFPTNCEACSKPLWHVFKPPPALECRRCHVKCHKDHLDKKEDMITPCKVNYDVTSARDMLLLALSQDEQKKWIGHLGKKIPKTPPSTFARQSPRSMSVRSGANQSFRKNPKNVPGKPS

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. {ECO:0000256|PIRNR:PIRNR037568}.

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001127}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000256|ARBA:ARBA00001127}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001416}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000256|ARBA:ARBA00001416};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR037568};

ATP-binding;Cell membrane;Cell projection;Coiled coil;Cytoplasm;Cytoskeleton;Golgi apparatus;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc;Zinc-finger

actomyosin structure organization [GO:0031032]; cell development [GO:0048468]; cortical actin cytoskeleton organization [GO:0030866]; embryonic morphogenesis [GO:0048598]; epicardial cell to mesenchymal cell transition [GO:0003347]; mitotic cytokinesis [GO:0000281]; negative regulation of adherens junction organization [GO:1903392]; phosphorylation [GO:0016310]; positive regulation of stress fiber assembly [GO:0051496]; regulation of cell junction assembly [GO:1901888]; regulation of cytoskeleton organization [GO:0051493]; Rho protein signal transduction [GO:0007266]

bleb [GO:0032059]; centriole [GO:0005814]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; ruffle [GO:0001726]

ATP binding [GO:0005524]; metal ion binding [GO:0046872]; Rho-dependent protein serine/threonine kinase activity [GO:0072518]; small GTPase binding [GO:0031267]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cell projection, bleb {ECO:0000256|ARBA:ARBA00043945}. Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Membrane {ECO:0000256|ARBA:ARBA00004370}.

IPR000961;IPR046349;IPR011009;IPR002219;IPR011993;IPR001849;IPR000719;IPR017441;IPR020684;IPR037310;IPR015008;IPR008271;

1.20.5.340;3.30.60.20;2.30.29.30;1.20.5.730;1.10.510.10;

A0A0R4IXF6

MADPAAQSSAQPRLQQAQSSGPTGSNSNPGAGSSDPARPGLSQQQWSSQKKAQVRSFPRAKKLEKLGVFSSCKANDACKCNGWKNPNPPTAARMELQQQAASLTETCRSCGHSLAEHVSHLENVSEEEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMGKPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPKERQTMYELSKMFLLCLNYWKLETPSQFRQRAQKEDAAAYKVDYTRWLCYCHVPQSNDSLPRYETCQVFGRSLLKSIFTVTRRQLLEKFRVEKDKLPPEKRTLILTHFPKFLSMLEEEIYGENSPIWEADFTMPASEGTQLGHQTVLSPVSISGSPHSKGSSASALGVTGLDVASSEPTIGEKRKLPEALTLEDAKRIRVMGDIPMELVNEVMKTITDPAAMLGPETSLLSANAARDETARLEERRGIIEFHVIGNSLSQKSNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHGILYFLTYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIPYTELSHIIKRQKEIIKKLIERKQNQIRKVYPGLTCFKEGVRQIPVESIPGIRETGWKPSAKEKSKELKDPDLLYNMLKNLLAQIKTHPDAWPFMEPVKKSEAPDYYEVIRFPIDLKTMTERLKNRYYVTKKLFIADLQRVITNCREYNPPDSEYCKSANTLEKFFYFKLKEAGLIDK

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Protein lysine acyltransferase that can act as a acetyltransferase, glutaryltransferasesucc, succinyltransferase or malonyltransferase, depending on the context (By similarity). Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequency around the transcription start sites of genes (By similarity). Succinylation of histones gives a specific tag for epigenetic transcription activation (By similarity). Association with the 2-oxoglutarate dehydrogenase complex, which provides succinyl-CoA, is required for histone succinylation (By similarity). In different complexes, functions either as an acetyltransferase (HAT) or as a succinyltransferase: in the SAGA and ATAC complexes, acts as a histone acetyltransferase (By similarity). Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles (By similarity). Has a a strong preference for acetylation of H3 at 'Lys-9' (H3K9ac) (By similarity). Acetylation of histones gives a specific tag for epigenetic transcription activation (By similarity). Also acetylates non-histone proteins, such as tbx5 (PubMed:29174768). Involved in heart and limb development by mediating acetylation of tbx5 (PubMed:29174768). Together with kat2b, required for growth and differentiation of craniofacial cartilage and bone by regulating acetylation of histone H3 at 'Lys-9' (H3K9ac) (PubMed:30424580). Also acts as a histone glutaryltransferase: catalyzes glutarylation of histone H4 on 'Lys-91' (H4K91glu), a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes (By similarity). {ECO:0000250|UniProtKB:Q92830, ECO:0000269|PubMed:29174768, ECO:0000269|PubMed:30424580}.

2.3.1.-; 2.3.1.48

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:Q92830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000250|UniProtKB:Q92830}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:Q92830}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + succinyl-CoA = CoA + H(+) + N(6)-succinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:16261, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:87830; Evidence={ECO:0000250|UniProtKB:Q92830}; CATALYTIC ACTIVITY: Reaction=glutaryl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-glutaryl-L-lysyl-[protein]; Xref=Rhea:RHEA:18009, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11875, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57378, ChEBI:CHEBI:87828; Evidence={ECO:0000250|UniProtKB:Q92830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18010; Evidence={ECO:0000250|UniProtKB:Q92830};

Acyltransferase;Bromodomain;Chromosome;Cytoplasm;Cytoskeleton;Nucleus;Reference proteome;Transcription;Transcription regulation;Transferase

bone morphogenesis [GO:0060349]; chromatin remodeling [GO:0006338]; epigenetic regulation of gene expression [GO:0040029]; heart development [GO:0007507]; histone succinylation [GO:0106077]; internal peptidyl-lysine acetylation [GO:0018393]; limb development [GO:0060173]; long-term memory [GO:0007616]; peptidyl-lysine glutarylation [GO:0106227]; positive regulation of cytokine production [GO:0001819]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of bone development [GO:1903010]; regulation of cartilage development [GO:0061035]; regulation of regulatory T cell differentiation [GO:0045589]; regulation of synaptic plasticity [GO:0048167]; regulation of T cell activation [GO:0050863]

ATAC complex [GO:0140672]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; histone acetyltransferase complex [GO:0000123]; nucleus [GO:0005634]

chromatin binding [GO:0003682]; histone acetyltransferase activity [GO:0004402]; histone glutaryltransferase activity [GO:0106229]; histone H3 acetyltransferase activity [GO:0010484]; histone H3K9 acetyltransferase activity [GO:0043992]; histone succinyltransferase activity [GO:0106078]; peptide-lysine-N-acetyltransferase activity [GO:0061733]; transcription coactivator activity [GO:0003713]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92830}. Chromosome {ECO:0000250|UniProtKB:Q92830}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q92830}.

DOMAIN: Loop3 is required for substrate specificity and adopts different structural conformations in succinyl-CoA-bound and acetyl-CoA-bound forms. Tyr-603 has an important role in the selective binding of succinyl-CoA over acetyl-CoA. {ECO:0000250|UniProtKB:Q92830}.

IPR016181;IPR001487;IPR036427;IPR018359;IPR037800;IPR016376;IPR000182;IPR009464;

3.40.630.30;1.20.920.10;

A0A0R4IY06

MDNQQRRTDNMASGETDHLQCVEEPQPGDLIEIFRPAYQHWALYLGDGYIINLTPVDEGQATAVSSVKSVFSRKAVVRMQLLKEVVGADSYRINNKYDDDHTPLPVSEIIQRAQMLIGQEVSYDLLGSNCEHFVTLLRYGEGVSEQASRAIGAISLVTAAASAFSVLGLINTRSRNRPF

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid. Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE) which serves as precursor for N-acylethanolamines (NAEs) (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light (PubMed:33854238). Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity) (PubMed:33854238). {ECO:0000250|UniProtKB:Q9HDD0, ECO:0000269|PubMed:33854238}.

2.3.1.-; 3.1.1.32; 3.1.1.4

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40487, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41348, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73009, ChEBI:CHEBI:76091; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = H(+) + hexadecanoyl-sn-glycero-3-phosphocholine + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:41360, ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999, ChEBI:CHEBI:74986, ChEBI:CHEBI:78097; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41361; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + a 2-acyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + 2-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41364, ChEBI:CHEBI:57875, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078, ChEBI:CHEBI:77369; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41365; Evidence={ECO:0000250|UniProtKB:Q9HDD0};

Cytoplasm;Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid metabolism;Lysosome;Membrane;Mitochondrion;Reference proteome;Transferase;Transmembrane;Transmembrane helix

lens fiber cell differentiation [GO:0070306]; lipid catabolic process [GO:0016042]; N-acylphosphatidylethanolamine metabolic process [GO:0070292]; organelle disassembly [GO:1903008]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]

N-acyltransferase activity [GO:0016410]; phospholipase A1 activity [GO:0008970]; phospholipase A2 activity [GO:0004623]

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:33854238}. Mitochondrion membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain. {ECO:0000269|PubMed:33854238}.

DOMAIN: The C-terminal transmembrane domain is required for the targeting of the protein to damaged organelles. {ECO:0000269|PubMed:33854238}.

IPR007053;

3.90.1720.10;

A0A0R4IZ84

MADELERVRISAAELRAQASSFNIHGDDVKDLREEGKKQRQRDSKRPDLQLYKPGVGHPNRRMDSVEGAGSDTLIQPDGFGNDPKMSDESPTSPGCSYMPGTGNEDYLNDHSKPETNHKTDGHIGGDKHKLVDENAVKIIERAGTPKSPKQSRKMRKPDRQIYQPGGRRSQGNKEVGASKELDRDRSREEEVDGKSIETPLKCEKEEKRKNRRGKNDRKKQASVETPSANKTENAVENISNKVSNLHLETVESKDRDRQDDTNQIKHSEEGRKIQTGGANRGMGEDKKKERGNGKSRPGKEKGNNQVFDKKEEGEAGGKASEAPHLEGRKQRNFGAKEASRDQNLNHEKQQGNRPKEKGKPSERTDSKRVNAASKRYSQSDIRRPRNRTYSTSSASSGTSMDGLAEAERLKAEGQQFSARTLERATGQREFVRGGQTRSRRRTARTLSSTDSLEENEVWEREGRRSRAAEEAKSSTRKEGGILRVSLDKREEQASRKSTRGRGRGILVLPAHTDLTQTPDPAPPLGGMRGGMGLGRGRGGRGGGTRRLWDPNNPDKKPALVSSQQSQHASQHQALYLQQGGCGPLHFLDTDDETVGSPPVRQGEFFQNQQAAAMAYYKFQNSDNPYCYPVSANSPNTPPRYPYPYQIPYQIPGSNGMYPASAMTSFYGPYGQGGPGYPSPTVSALTPEEAEVQTRGELGKFLRLADSQELQLSNLLSRERLSQEGLERMAQLRAELLTIYERVILTDIEFSDSQNVDQTLWKNVFYQVIERFRQLLKDQNSDTAPQIKTMLMTILEEGAVFFDSLLQKLQSVFQFKLQDYMDCMAIRARPLRKTVKYALISAQRCMICQGDIARYREQASESANYGKARSWYLKAQQIAPKNGRPYNQLALLAVYTKRKLDAVYYYMRSLAASNPILTAKESLMSLFEEAKRKADQVERRLKQDSDGSAHGPKGHTGGRRGEDAARVEIWIRPSEVSGTSRPTGSESGKDSEQDGELGALSASDLNKRFILSFLHAHGKLFTKVGMESFPAVANRVLLEFRALLQHSPSPLGSTRMLQIITINMFTIYNAQIRAKGQGETRSALEEQAISLGLAMFGLLVQRCTELLKETPTEPIPAEELGEFDEMDDEEGMVRVSVFPHDLRELLPSMKVWSDWMLGHPEKWNPPPCSMQGSPDVWQCLADLCNSFSRVYHGEVLLYKADADGEGDEELRVLQLEEDKMLSGFVPLLAAPQDACYTDQGTDAAIAADCKRVTVLKYFLEALCGQEEPLLAFKGGKYISMAAPLTPSINTENKAQEQEDDVIVEESSLSASEGEIDGEMEGDGSEDDIRELRARRHALAHKLAQQQKRRDKIQAVLQTGGQLEIEVRPFYLVPDTNGFIDHLEGLRKLLACGTYILVVPLIVITELDGLAKGQDSREGVGNGAHARQVQDRARAAVMFLEKAFESRDPSIRALTSRGNTLESIAFRSEDTSGQKGNNDDVILSCCLHYCQDKAKDFMPAERNGPVRLRREVVLLTDDRNLRVKALTRNVPVRDIPAFLIWAKVG

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini (By similarity). Required for normal embryonic development (PubMed:19414594). {ECO:0000250|UniProtKB:Q86US8, ECO:0000269|PubMed:19414594}.; FUNCTION: Plays a role in nonsense-mediated mRNA decay. {ECO:0000250|UniProtKB:Q86US8}.

3.1.-.-

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q86US8};

Chromosome;Cytoplasm;Endonuclease;Hydrolase;Nonsense-mediated mRNA decay;Nuclease;Nucleus;Reference proteome;Telomere

chordate embryonic development [GO:0043009]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]

chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; nucleolus [GO:0005730]; telomerase holoenzyme complex [GO:0005697]

endonuclease activity [GO:0004519]; telomerase RNA binding [GO:0070034]; telomeric DNA binding [GO:0042162]

SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q86US8}. Chromosome, telomere {ECO:0000250|UniProtKB:Q86US8}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q86US8}.

DOMAIN: The PINc domain confers endonuclease activity and is expected to bind the catalytic metal ion. {ECO:0000250|UniProtKB:Q86US8}.

IPR018834;IPR019458;IPR045153;IPR029060;IPR002716;IPR011990;

3.40.50.1010;1.25.40.10;

A0A0R4J8U1

MPDPAAHLPFFYGSISRAEAEEHLKLAGMADGLFLLRQCLRSLGGYVLSLVHDVRFHHFPIERQLNGTYAIAGGKAHCGPAELCQFYSQDPDGLPCNLRKPCNRPPGLEPQPGVFDCLRDAMVRDYVRQTWKLEGDALEQAIISQAPQVEKLIATTAHERMPWYHSSLTREEAERKLYSGQQTDGKFLLRPRKEQGTYALSLVYGKTVYHYLISQDKAGKYCIPEGTKFDTLWQLVEYLKLKADGLIYRLKEVCPNSSASAEAAAPTLPAHPSTFTQPHRRIDTLNSDGYTPEPARLDKPRPMPMDTSVYESPYSDPEELKDKKLFLKRENLLVADIELGCGNFGSVRQGVYRMRKKQIDVAIKVLKQSTEKADKDEMMREAQIMHQLDNPYIVRLIGVCQAEALMLVMEMAGGGPLHKFLIGKKEEIPVSNVAELLHQVAMGMKYLEEKNFVHRDLAARNVLLVNRHYAKISDFGLSKALGADDSYYTARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVLDFIKQGKRMECPPECPPEMYALMSDCWIYKWEDRPDFVAVEQRMRTYYYSMASRAEGPPQCEQVAEAACG

Rattus norvegicus (Rat)

2.7.10.2

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000256|ARBA:ARBA00001149, ECO:0000256|PIRNR:PIRNR000604};

ATP-binding;Cytoplasm;Immunity;Kinase;Nucleotide-binding;Reference proteome;SH2 domain;Transferase;Tyrosine-protein kinase

alpha-beta T cell differentiation [GO:0046632]; beta selection [GO:0043366]; calcium-mediated signaling [GO:0019722]; cell differentiation [GO:0030154]; immune response [GO:0006955]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; negative thymic T cell selection [GO:0045060]; phosphorylation [GO:0016310]; positive regulation of alpha-beta T cell differentiation [GO:0046638]; positive regulation of alpha-beta T cell proliferation [GO:0046641]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of T cell differentiation [GO:0045582]; positive thymic T cell selection [GO:0045059]; T cell differentiation [GO:0030217]; T cell receptor signaling pathway [GO:0050852]; thymic T cell selection [GO:0045061]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]

cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; immunological synapse [GO:0001772]; membrane [GO:0016020]; plasma membrane [GO:0005886]; T cell receptor complex [GO:0042101]

ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; protein kinase activity [GO:0004672]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102]

IPR011009;IPR023420;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR035838;IPR008266;IPR020635;IPR012234;

3.30.505.10;1.10.510.10;

A0A0R6Y3I5

MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCQFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVPNKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALEELVFGDNDRLSALVAHHFKANLLVILSDIDGYYTENPRTSTNATIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLEKARQFLLGGSHEIGTLFYSRVSS

Leishmania donovani

FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate (PubMed:29777624). May be important for growth and survival (PubMed:29777624). {ECO:0000269|PubMed:29777624}.

2.7.2.11

CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11; Evidence={ECO:0000269|PubMed:29777624}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14878; Evidence={ECO:0000269|PubMed:29777624};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:29777624};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for L-glutamate {ECO:0000269|PubMed:29777624}; KM=0.6 mM for ATP {ECO:0000269|PubMed:29777624};

PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000269|PubMed:29777624}.

Amino-acid biosynthesis;ATP-binding;Kinase;Magnesium;Nucleotide-binding;Proline biosynthesis;Transferase

L-proline biosynthetic process [GO:0055129]; phosphorylation [GO:0016310]

cytosol [GO:0005829]

ATP binding [GO:0005524]; glutamate 5-kinase activity [GO:0004349]; identical protein binding [GO:0042802]

IPR036393;IPR001048;IPR041739;IPR001057;IPR011529;IPR005715;IPR019797;

3.40.1160.10;

A0A0S2UWC9

MAENGAAVQENQNVIRHQEVGHKSLLQSDALYQYILETSVYPREPESMKELRELTAKHPWNLMTTSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALAIPHDGKILAMDINRENYEIGLPVIEKAGVAHKIDFREGPALPVLDQLVEDKNNHGTYDFIFVDADKDNYINYHKRIIDLVKVGGLIGYDNTLWNGSLVAPADTPMRKYVRYYRDFILELNKALAADPRIEICMLPVGDGITLGRRIS

Petunia hybrida (Petunia)

FUNCTION: Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:26620524). Methylates caffeoyl-CoA to feruloyl-CoA, also able to methylate 5-hydroxyferuloyl-CoA (PubMed:26620524). {ECO:0000269|PubMed:26620524}.

2.1.1.-; 2.1.1.104

CATALYTIC ACTIVITY: Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16925, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104; Evidence={ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:26620524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16926; Evidence={ECO:0000269|PubMed:26620524}; CATALYTIC ACTIVITY: Reaction=(E)-5-hydroxyferuloyl-CoA + S-adenosyl-L-methionine = (E)-sinapoyl-CoA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:64860, ChEBI:CHEBI:15378, ChEBI:CHEBI:57393, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156249; Evidence={ECO:0000269|PubMed:26620524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64861; Evidence={ECO:0000269|PubMed:26620524};

COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q40313}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000250|UniProtKB:Q40313};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=5.8 pmol/sec/mg enzyme with (E)-caffeoyl-CoA as substrate {ECO:0000269|PubMed:26620524};

PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26620524}.

Cytoplasm;Lignin biosynthesis;Metal-binding;Methyltransferase;S-adenosyl-L-methionine;Transferase

circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; lignin biosynthetic process [GO:0009809]; methylation [GO:0032259]; phenylpropanoid metabolic process [GO:0009698]

cytosol [GO:0005829]

caffeoyl CoA:S-adenosyl-L-methionine O-methyltransferase activity [GO:0080076]; caffeoyl-CoA O-methyltransferase activity [GO:0042409]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26620524}.

IPR029063;IPR002935;

3.40.50.150;

A0A0S2Z366

MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN

Homo sapiens (Human)

1.3.8.7

CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61526; Evidence={ECO:0000256|ARBA:ARBA00001337}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449; Evidence={ECO:0000256|ARBA:ARBA00001337}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; Evidence={ECO:0000256|ARBA:ARBA00001483}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465; Evidence={ECO:0000256|ARBA:ARBA00001483}; CATALYTIC ACTIVITY: Reaction=H(+) + octanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48180, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62242; Evidence={ECO:0000256|ARBA:ARBA00001547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181; Evidence={ECO:0000256|ARBA:ARBA00001547}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentanoyl-CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43456, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57389, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:86160; Evidence={ECO:0000256|ARBA:ARBA00023695}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457; Evidence={ECO:0000256|ARBA:ARBA00023695}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61405; Evidence={ECO:0000256|ARBA:ARBA00001236}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317; Evidence={ECO:0000256|ARBA:ARBA00001236}; CATALYTIC ACTIVITY: Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723, ChEBI:CHEBI:83726; EC=1.3.8.7; Evidence={ECO:0000256|ARBA:ARBA00034058}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14478; Evidence={ECO:0000256|ARBA:ARBA00034058}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61406, ChEBI:CHEBI:61430; Evidence={ECO:0000256|ARBA:ARBA00000121}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177; Evidence={ECO:0000256|ARBA:ARBA00000121}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; Evidence={ECO:0000256|ARBA:ARBA00001486}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297; Evidence={ECO:0000256|ARBA:ARBA00001486};

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974, ECO:0000256|PIRSR:PIRSR634180-3, ECO:0000256|RuleBase:RU362125};

PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000256|ARBA:ARBA00005198}.

Acetylation;FAD;Flavoprotein;Oxidoreductase;Transit peptide

cardiac muscle cell differentiation [GO:0055007]; carnitine metabolic process, CoA-linked [GO:0019254]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; glycogen biosynthetic process [GO:0005978]; liver development [GO:0001889]; medium-chain fatty acid catabolic process [GO:0051793]; post-embryonic development [GO:0009791]; regulation of gluconeogenesis [GO:0006111]; response to cold [GO:0009409]; response to starvation [GO:0042594]

mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]

flavin adenine dinucleotide binding [GO:0050660]; medium-chain fatty acyl-CoA dehydrogenase activity [GO:0070991]

SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.

IPR006089;IPR006091;IPR046373;IPR036250;IPR009075;IPR013786;IPR037069;IPR009100;IPR034180;

1.10.540.10;2.40.110.10;1.20.140.10;

A0A0S2Z381

MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDFLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAIDLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGYHTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFKSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAGQNL

Homo sapiens (Human)

3.5.4.4

CATALYTIC ACTIVITY: Reaction=2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+); Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4; Evidence={ECO:0000256|ARBA:ARBA00034443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191; Evidence={ECO:0000256|ARBA:ARBA00034443}; CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000256|ARBA:ARBA00001600}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; Evidence={ECO:0000256|ARBA:ARBA00001600};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947};

Hydrolase;Nucleotide metabolism

adenosine catabolic process [GO:0006154]; allantoin metabolic process [GO:0000255]; alpha-beta T cell differentiation [GO:0046632]; amide catabolic process [GO:0043605]; AMP catabolic process [GO:0006196]; AMP salvage [GO:0044209]; B cell proliferation [GO:0042100]; calcium-mediated signaling [GO:0019722]; dAMP catabolic process [GO:0046059]; dATP catabolic process [GO:0046061]; deoxyadenosine catabolic process [GO:0006157]; embryonic digestive tract development [GO:0048566]; germinal center B cell differentiation [GO:0002314]; germinal center formation [GO:0002467]; GMP salvage [GO:0032263]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; leukocyte migration [GO:0050900]; liver development [GO:0001889]; lung alveolus development [GO:0048286]; mature B cell apoptotic process [GO:0002901]; mucus secretion [GO:0070254]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; negative regulation of inflammatory response [GO:0050728]; negative regulation of leukocyte migration [GO:0002686]; negative regulation of mature B cell apoptotic process [GO:0002906]; negative regulation of mucus secretion [GO:0070256]; negative regulation of penile erection [GO:0060407]; negative regulation of thymocyte apoptotic process [GO:0070244]; penile erection [GO:0043084]; Peyer's patch development [GO:0048541]; placenta development [GO:0001890]; positive regulation of alpha-beta T cell differentiation [GO:0046638]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of germinal center formation [GO:0002636]; positive regulation of heart rate [GO:0010460]; positive regulation of smooth muscle contraction [GO:0045987]; positive regulation of T cell differentiation in thymus [GO:0033089]; positive regulation of T cell receptor signaling pathway [GO:0050862]; response to inorganic substance [GO:0010035]; smooth muscle contraction [GO:0006939]; T cell differentiation in thymus [GO:0033077]; T cell receptor signaling pathway [GO:0050852]; thymocyte apoptotic process [GO:0070242]; trophectodermal cell differentiation [GO:0001829]; xanthine biosynthetic process [GO:0046111]

anchoring junction [GO:0070161]; cytoplasmic vesicle lumen [GO:0060205]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]

2'-deoxyadenosine deaminase activity [GO:0046936]; adenosine deaminase activity [GO:0004000]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cell membrane {ECO:0000256|ARBA:ARBA00004296}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004296}; Extracellular side {ECO:0000256|ARBA:ARBA00004296}. Cytoplasmic vesicle lumen {ECO:0000256|ARBA:ARBA00004321}.

IPR006650;IPR028893;IPR001365;IPR006330;IPR032466;

3.20.20.140;

A0A0S2Z3W3

MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT

Homo sapiens (Human)

3.2.1.52

CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-beta-D-6-sulfogalactosaminyl-(1->4)-alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine = alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine + N-acetyl-D-6-sulfogalactosamine; Xref=Rhea:RHEA:64384, ChEBI:CHEBI:15377, ChEBI:CHEBI:152567, ChEBI:CHEBI:152568, ChEBI:CHEBI:153064; Evidence={ECO:0000256|ARBA:ARBA00023541}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64385; Evidence={ECO:0000256|ARBA:ARBA00023541}; CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = a beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:48276, ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:90163, ChEBI:CHEBI:90164; Evidence={ECO:0000256|ARBA:ARBA00023953}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48277; Evidence={ECO:0000256|ARBA:ARBA00023953}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; Evidence={ECO:0000256|ARBA:ARBA00001231}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM2 (d18:1(4E)) + H2O = a ganglioside GM3 (d18:1(4E)) + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:47940, ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:60065, ChEBI:CHEBI:71502; Evidence={ECO:0000256|ARBA:ARBA00043767}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47941; Evidence={ECO:0000256|ARBA:ARBA00043767}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM2 + H2O = a ganglioside GM3 + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:47968, ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:79210, ChEBI:CHEBI:79218; Evidence={ECO:0000256|ARBA:ARBA00043827}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47969; Evidence={ECO:0000256|ARBA:ARBA00043827}; CATALYTIC ACTIVITY: Reaction=beta-D-GalNAc-(1->4)-alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + H2O = alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + N-acetyl-D-galactosamine; Xref=Rhea:RHEA:64372, ChEBI:CHEBI:15377, ChEBI:CHEBI:28037, ChEBI:CHEBI:152565, ChEBI:CHEBI:152566; Evidence={ECO:0000256|ARBA:ARBA00023505}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64373; Evidence={ECO:0000256|ARBA:ARBA00023505};

Disulfide bond;Glycosidase;Hydrolase;Lysosome;Signal;Zymogen

adult walking behavior [GO:0007628]; carbohydrate metabolic process [GO:0005975]; cell morphogenesis involved in neuron differentiation [GO:0048667]; dermatan sulfate catabolic process [GO:0030209]; ganglioside catabolic process [GO:0006689]; hyaluronan catabolic process [GO:0030214]; lipid storage [GO:0019915]; lysosome organization [GO:0007040]; maintenance of location in cell [GO:0051651]; myelination [GO:0042552]; neuromuscular process controlling balance [GO:0050885]; neuromuscular process controlling posture [GO:0050884]; sensory perception of sound [GO:0007605]; sexual reproduction [GO:0019953]; skeletal system development [GO:0001501]

cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; membrane [GO:0016020]

beta-N-acetylhexosaminidase activity [GO:0004563]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148]

SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.

IPR025705;IPR015883;IPR017853;IPR029018;IPR029019;

3.30.379.10;3.20.20.80;

A0A0S2Z4D1

MEVVDPQQLGMFTEGELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHKNVIQLVDVLYNEEKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFCQLIDGLEYLHSQGIVHKDIKPGNLLLTTGGTLKISDLGVAEALHPFAADDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWSAGVTLYNITTGLYPFEGDNIYKLFENIGKGSYAIPGDCGPPLSDLLKGMLEYEPAKRFSIRQIRQHSWFRKKHPPAEAPVPIPPSPDTKDRWRSMTVVPYLEDLHGADEDEDLFDIEDDIIYTQDFTVPGQVPEEEASHNGQRRGLPKAVCMNGTEAAQLSTKSRAEGRAPNPARKACSASSKIRRLSACKQQ

Homo sapiens (Human)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936};

ATP-binding;Cell cycle;Cytoplasm;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Nucleus;Phosphoprotein;Serine/threonine-protein kinase;Transferase

axonogenesis [GO:0007409]; cell cycle [GO:0007049]; cellular response to UV-B [GO:0071493]; dendrite extension [GO:0097484]; DNA damage response [GO:0006974]; epithelial cell proliferation involved in prostate gland development [GO:0060767]; establishment of cell polarity [GO:0030010]; glucose homeostasis [GO:0042593]; Golgi localization [GO:0051645]; negative regulation of cell growth [GO:0030308]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of epithelial cell proliferation involved in prostate gland development [GO:0060770]; phosphorylation [GO:0016310]; positive regulation of axonogenesis [GO:0050772]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of vesicle transport along microtubule [GO:1901610]; positive thymic T cell selection [GO:0045059]; protein localization to nucleus [GO:0034504]; regulation of dendrite morphogenesis [GO:0048814]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; regulation of Wnt signaling pathway [GO:0030111]; response to activity [GO:0014823]; response to glucagon [GO:0033762]; response to ionizing radiation [GO:0010212]; response to lipid [GO:0033993]; response to thyroid hormone [GO:0097066]; T cell receptor signaling pathway [GO:0050852]; tissue homeostasis [GO:0001894]; vasculature development [GO:0001944]

cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; protein-containing complex [GO:0032991]; Z disc [GO:0030018]

ATP binding [GO:0005524]; LRR domain binding [GO:0030275]; metal ion binding [GO:0046872]; protein kinase activator activity [GO:0030295]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR011009;IPR039154;IPR000719;IPR017441;IPR008271;

1.10.510.10;

A0A0S2Z4D2

MTELPAPLSYFQNAQMSEDNHLSNTNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI

Homo sapiens (Human)

FUNCTION: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. {ECO:0000256|RuleBase:RU361148}.

3.4.23.-

Apoptosis;Cell adhesion;Cell membrane;Cell projection;Endoplasmic reticulum;Golgi apparatus;Hydrolase;Membrane;Notch signaling pathway;Phosphoprotein;Protease;Synapse;Transmembrane;Transmembrane helix

amyloid precursor protein catabolic process [GO:0042987]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; intracellular signal transduction [GO:0035556]; Notch signaling pathway [GO:0007219]; protein processing [GO:0016485]; smooth endoplasmic reticulum calcium ion homeostasis [GO:0051563]

axon [GO:0030424]; cell junction [GO:0030054]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; synapse [GO:0045202]

aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]

SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, neuron projection {ECO:0000256|ARBA:ARBA00004487}. Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Synapse {ECO:0000256|ARBA:ARBA00034103}.

DOMAIN: The PAL motif is required for normal active site conformation. {ECO:0000256|RuleBase:RU361148}.

IPR002031;IPR001108;IPR006639;IPR042524;

1.10.472.100;

A0A0U1RPR8

MAGLQQGCHFEGQNWTAPHWKTCLPCQGPWRLTVSHLKTVSSISVLSVVFWSVLLWADSLSLLAWARETFTLGVLGPWDCDPIFAQALPSIATQLAVDQVNQDASLLPGSQLDFKVLPTGCDTPHALATFVAHKNIVAAFVGPVNPGFCSAAALLAQGWGKSLFSWACEAPEGGGDLVPTLPSAADVLLSVMRHFGWARWAIVSSHQDIWVTTAQQLATAFRTHGLPIGLVTSLGPGEKGATEVCKQLHSVHGLKIVVLCMHSALLGGLEQTTLLHCAWEEGLTDGRLVFLPYDTLLFALPYGNRSYLVLDDHGPLQEAYDAVLTVSLESSPESHAFTATEMSGGATANLEPEQVSPLFGTIYDAVILLAHALNRSETHGAGLSGAHLGDHVRALDVAGFSQRIRTDGKGRRLAQYVILDTDGEGSQLVPTHILDTSTWQVQPLGKPIHFPGGSPPAHDASCWFDPNTLCIRGVQPLGSLLTLTIACVLALVGGFLAYFIRLGLQQLRLLRGPHRILLTSQELTFLQRTPSRRRPHVDSGSESRSVVDGGSPRSVTQGSARSLPAFLEHTNVALYQGEWVWLKKFEAGVAPDLRPSSLSFLRKLREMRHENVTAFLGLFVGPGVSAMVLEHCARGSLEDLLQNENLRLDWTFKASLLLDLIRGLRYLHHRRFPHGRLKSRNCVVDTRFVLKITDHGYAEFLESHCSSRPQPAPEELLWTAPELLRGPGKATFKGDVFSLAIILQEVLTRDPPYCSWGLSAEEIIRKVASPPPLCRPLVSPDQGPLECIQLMQLCWEEAPDDRPSLDQIYTQFKSINQGKKTSVVDSMLRMLEKYSESLEDLVQERTEELELERRKTERLLSQMLPPSVAHALKMGTTVEPEYFDQVTIYFSDIVGFTTISALSEPIEVVGFLNDLYTLFDAVLDSHDVYKVETIGDAYMVASGLPRRNGNRHAAEIANLALDILSYAGNFRMRHAPDVPIRVRAGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVSQSTVQALLSLDEGYKIDVRGQTELKGKGLEETYWLTGKVGFCRPLPTPLSIKPGDPWQDRINQEIRTGFAKARQGLAEPRKSGEAGPGP

Mus musculus (Mouse)

FUNCTION: Functions as an olfactory receptor activated by urine odorants, uroguanylin and guanylin and as well by the volatile semiochemicals carbon disulfide (CS2) and carbon dioxide (CO2) (PubMed:17702944, PubMed:17724338, PubMed:20637621). Has guanylate cyclase activity upon binding of the ligand (By similarity). Activation of GUCY2D neurons leads to the cGMP-dependent activation of the CNGA3 channels, membrane depolarization and an increase in action potential frequency (PubMed:17724338, PubMed:20637621). Signaling pathways activated by GUCY2D may trigger social behaviors such as acquisition of food preference (PubMed:20637621). {ECO:0000250|UniProtKB:P51839, ECO:0000269|PubMed:17702944, ECO:0000269|PubMed:17724338, ECO:0000269|PubMed:20637621}.

4.6.1.2

CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:P51839};

Cell membrane;Cell projection;cGMP biosynthesis;Disulfide bond;Lyase;Membrane;Nucleotide-binding;Reference proteome;Signal;Transmembrane;Transmembrane helix

cGMP biosynthetic process [GO:0006182]; detection of carbon dioxide [GO:0003031]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; intracellular signal transduction [GO:0035556]; olfactory behavior [GO:0042048]; olfactory learning [GO:0008355]; positive regulation of cGMP-mediated signaling [GO:0010753]; receptor guanylyl cyclase signaling pathway [GO:0007168]; sensory perception of smell [GO:0007608]

ciliary membrane [GO:0060170]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886]

adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; guanylate cyclase activity [GO:0004383]; natriuretic peptide receptor activity [GO:0016941]; odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672]

SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:9096404}; Single-pass type I membrane protein.

DOMAIN: The protein kinase domain is predicted to be catalytically inactive. {ECO:0000305}.

IPR001054;IPR018297;IPR001828;IPR011009;IPR029787;IPR028082;IPR000719;IPR001245;

3.40.50.2300;6.10.250.780;3.30.70.1230;1.10.510.10;

A0A0U1RQF0

MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARRVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEAQWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSLAWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLARALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQWDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRLLWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVVSRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVAALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESLFSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRPVWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPGAQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEEPEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG

Homo sapiens (Human)

FUNCTION: Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000256|ARBA:ARBA00023442}.

1.1.1.100; 1.3.1.39; 2.3.1.38; 2.3.1.39; 2.3.1.41; 2.3.1.85; 3.1.2.14; 4.2.1.59

CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78453, ChEBI:CHEBI:78454; Evidence={ECO:0000256|ARBA:ARBA00023357}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813; Evidence={ECO:0000256|ARBA:ARBA00023357}; CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] + H(+) + NADPH = decanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78467, ChEBI:CHEBI:78468; Evidence={ECO:0000256|ARBA:ARBA00023387}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865; Evidence={ECO:0000256|ARBA:ARBA00023387}; CATALYTIC ACTIVITY: Reaction=(2E)-dodecenoyl-[ACP] + H(+) + NADPH = dodecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65264, ChEBI:CHEBI:78472; Evidence={ECO:0000256|ARBA:ARBA00023385}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881; Evidence={ECO:0000256|ARBA:ARBA00023385}; CATALYTIC ACTIVITY: Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADPH = hexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78481, ChEBI:CHEBI:78483; Evidence={ECO:0000256|ARBA:ARBA00023345}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913; Evidence={ECO:0000256|ARBA:ARBA00023345}; CATALYTIC ACTIVITY: Reaction=(2E)-hexenoyl-[ACP] + H(+) + NADPH = hexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78458, ChEBI:CHEBI:78459; Evidence={ECO:0000256|ARBA:ARBA00023359}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833; Evidence={ECO:0000256|ARBA:ARBA00023359}; CATALYTIC ACTIVITY: Reaction=(2E)-octadecenoyl-[ACP] + H(+) + NADPH = NADP(+) + octadecanoyl-[ACP]; Xref=Rhea:RHEA:41928, Rhea:RHEA-COMP:9655, Rhea:RHEA-COMP:9656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78489, ChEBI:CHEBI:78495; Evidence={ECO:0000256|ARBA:ARBA00023376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929; Evidence={ECO:0000256|ARBA:ARBA00023376}; CATALYTIC ACTIVITY: Reaction=(2E)-octenoyl-[ACP] + H(+) + NADPH = NADP(+) + octanoyl-[ACP]; Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78462, ChEBI:CHEBI:78463; Evidence={ECO:0000256|ARBA:ARBA00023420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849; Evidence={ECO:0000256|ARBA:ARBA00023420}; CATALYTIC ACTIVITY: Reaction=(2E)-tetradecenoyl-[ACP] + H(+) + NADPH = NADP(+) + tetradecanoyl-[ACP]; Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647, Rhea:RHEA-COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78475, ChEBI:CHEBI:78477; Evidence={ECO:0000256|ARBA:ARBA00023368}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897; Evidence={ECO:0000256|ARBA:ARBA00023368}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627, ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453; Evidence={ECO:0000256|ARBA:ARBA00023402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809; Evidence={ECO:0000256|ARBA:ARBA00023402}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|ARBA:ARBA00023388}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861; Evidence={ECO:0000256|ARBA:ARBA00023388}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643, ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472; Evidence={ECO:0000256|ARBA:ARBA00023351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877; Evidence={ECO:0000256|ARBA:ARBA00023351}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651, ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481; Evidence={ECO:0000256|ARBA:ARBA00023401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909; Evidence={ECO:0000256|ARBA:ARBA00023401}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631, ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458; Evidence={ECO:0000256|ARBA:ARBA00023373}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829; Evidence={ECO:0000256|ARBA:ARBA00023373}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41924, Rhea:RHEA-COMP:9654, Rhea:RHEA-COMP:9655, ChEBI:CHEBI:15377, ChEBI:CHEBI:78488, ChEBI:CHEBI:78489; Evidence={ECO:0000256|ARBA:ARBA00023399}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925; Evidence={ECO:0000256|ARBA:ARBA00023399}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635, ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462; Evidence={ECO:0000256|ARBA:ARBA00023332}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845; Evidence={ECO:0000256|ARBA:ARBA00023332}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647, ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475; Evidence={ECO:0000256|ARBA:ARBA00023398}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893; Evidence={ECO:0000256|ARBA:ARBA00023398}; CATALYTIC ACTIVITY: Reaction=3-oxobutanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxybutanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451; Evidence={ECO:0000256|ARBA:ARBA00023413}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805; Evidence={ECO:0000256|ARBA:ARBA00023413}; CATALYTIC ACTIVITY: Reaction=3-oxodecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466; Evidence={ECO:0000256|ARBA:ARBA00023418}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857; Evidence={ECO:0000256|ARBA:ARBA00023418}; CATALYTIC ACTIVITY: Reaction=3-oxododecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydodecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41872, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9642, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78469, ChEBI:CHEBI:78470; Evidence={ECO:0000256|ARBA:ARBA00023416}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873; Evidence={ECO:0000256|ARBA:ARBA00023416}; CATALYTIC ACTIVITY: Reaction=3-oxohexadecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480; Evidence={ECO:0000256|ARBA:ARBA00023390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905; Evidence={ECO:0000256|ARBA:ARBA00023390}; CATALYTIC ACTIVITY: Reaction=3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457; Evidence={ECO:0000256|ARBA:ARBA00023346}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825; Evidence={ECO:0000256|ARBA:ARBA00023346}; CATALYTIC ACTIVITY: Reaction=3-oxooctadecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41920, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9654, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78487, ChEBI:CHEBI:78488; Evidence={ECO:0000256|ARBA:ARBA00023419}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921; Evidence={ECO:0000256|ARBA:ARBA00023419}; CATALYTIC ACTIVITY: Reaction=3-oxooctanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461; Evidence={ECO:0000256|ARBA:ARBA00023364}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841; Evidence={ECO:0000256|ARBA:ARBA00023364}; CATALYTIC ACTIVITY: Reaction=3-oxotetradecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxytetradecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41888, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9646, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78473, ChEBI:CHEBI:78474; Evidence={ECO:0000256|ARBA:ARBA00023367}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889; Evidence={ECO:0000256|ARBA:ARBA00023367}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-[ACP] + malonyl-[ACP] = 3-oxooctadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487; Evidence={ECO:0000256|ARBA:ARBA00023365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917; Evidence={ECO:0000256|ARBA:ARBA00023365}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460; Evidence={ECO:0000256|ARBA:ARBA00023361}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837; Evidence={ECO:0000256|ARBA:ARBA00023361}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464; Evidence={ECO:0000256|ARBA:ARBA00023414}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853; Evidence={ECO:0000256|ARBA:ARBA00023414}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477, ChEBI:CHEBI:78478; Evidence={ECO:0000256|ARBA:ARBA00023341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901; Evidence={ECO:0000256|ARBA:ARBA00023341}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP]; Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; EC=3.1.2.14; Evidence={ECO:0000256|ARBA:ARBA00023378}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933; Evidence={ECO:0000256|ARBA:ARBA00023378}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] + tetradecanoate; Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=3.1.2.14; Evidence={ECO:0000256|ARBA:ARBA00023410}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124; Evidence={ECO:0000256|ARBA:ARBA00023410}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; Evidence={ECO:0000256|ARBA:ARBA00023333}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399; Evidence={ECO:0000256|ARBA:ARBA00023333}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|ARBA:ARBA00023394}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098; Evidence={ECO:0000256|ARBA:ARBA00023394}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39; Evidence={ECO:0000256|ARBA:ARBA00023381}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566; Evidence={ECO:0000256|ARBA:ARBA00023381}; CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00023389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837; Evidence={ECO:0000256|ARBA:ARBA00023389}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.85; Evidence={ECO:0000256|ARBA:ARBA00023370}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14994; Evidence={ECO:0000256|ARBA:ARBA00023370}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; Evidence={ECO:0000256|ARBA:ARBA00023397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789; Evidence={ECO:0000256|ARBA:ARBA00023397}; CATALYTIC ACTIVITY: Reaction=acetyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41800, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; Evidence={ECO:0000256|ARBA:ARBA00023352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801; Evidence={ECO:0000256|ARBA:ARBA00023352}; CATALYTIC ACTIVITY: Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456; Evidence={ECO:0000256|ARBA:ARBA00023403}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821; Evidence={ECO:0000256|ARBA:ARBA00023403}; CATALYTIC ACTIVITY: Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469; Evidence={ECO:0000256|ARBA:ARBA00023396}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869; Evidence={ECO:0000256|ARBA:ARBA00023396}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473; Evidence={ECO:0000256|ARBA:ARBA00023348}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885; Evidence={ECO:0000256|ARBA:ARBA00023348}; CATALYTIC ACTIVITY: Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP]; Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449; EC=2.3.1.39; Evidence={ECO:0000256|ARBA:ARBA00023404}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793; Evidence={ECO:0000256|ARBA:ARBA00023404};

PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|ARBA:ARBA00005194}.

Acetylation;Fatty acid biosynthesis;Fatty acid metabolism;Hydrolase;Lipid biosynthesis;Lipid metabolism;Lyase;Multifunctional enzyme;NAD;NADP;Phosphopantetheine;Phosphoprotein;Proteomics identification;Pyridoxal phosphate;Reference proteome;S-nitrosylation;Transferase

fatty acid biosynthetic process [GO:0006633]

cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]

(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity [GO:0047117]; fatty acid synthase activity [GO:0004312]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; phosphopantetheine binding [GO:0031177]

IPR029058;IPR001227;IPR036736;IPR014043;IPR016035;IPR013149;IPR049391;IPR011032;IPR018201;IPR014031;IPR014030;IPR016036;IPR013217;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049552;IPR020843;IPR013968;IPR049900;IPR020806;IPR009081;IPR006162;IPR029063;IPR001031;IPR016039;

3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;3.40.50.150;

A0A0U1ZFN5

MAGNVKKSSGAGGSGSGGSGAGGLIGLMKDAFQPHHHHHHHLSPHPPCTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTVLSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQVERPSSPFSMAPQASLPPVPPRLDLLQQRAPVPASTSVLGTASKASSSSLHKDKPLPIPPTLRDLPPPPPPDRPYSVGTETRPQRRPLPCTPGDCPSRDKLPPVPSSRPGDSWLSRPIPKVPVATPNPGDPWNGRELTNRHSLPFSLPSQMEPRADVPRLGSTFSLDTSTTMNSSPVAGPESEHPKIKPSSSANAIYSLAARPLPVPKLPPGEQGDSEEDTEYMTPTSRPVGVQKPEPKRPAETAQSSRACDCDQQIDSCTYEAMYNIQSQALSVAENSACGEGNLATAHTSTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGEPTNFNEGSQVPERPPKPFPRRINSERKASSYQQGGGAMANPAAAAPSPQLSSEIERLMSQGYSYQDIQKALVIAHNNIEMAKNILREFVSISSPAHVAT

Rattus norvegicus (Rat)

FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. {ECO:0000256|RuleBase:RU367001}.

2.3.2.27

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900, ECO:0000256|RuleBase:RU367001};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367001}.

Calcium;Metal-binding;Proteomics identification;Reference proteome;Repeat;Transferase;Ubl conjugation pathway;Zinc;Zinc-finger

cell surface receptor signaling pathway [GO:0007166]; cellular response to hypoxia [GO:0071456]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; DNA damage response [GO:0006974]; male gonad development [GO:0008584]; mast cell degranulation [GO:0043303]; negative regulation of apoptotic process [GO:0043066]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of receptor-mediated endocytosis [GO:0048260]; protein autoubiquitination [GO:0051865]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of platelet-derived growth factor receptor-alpha signaling pathway [GO:2000583]; regulation of Rap protein signal transduction [GO:0032487]; response to activity [GO:0014823]; response to ethanol [GO:0045471]; response to gamma radiation [GO:0010332]; response to starvation [GO:0042594]; response to testosterone [GO:0033574]; signal transduction [GO:0007165]; ubiquitin-dependent endocytosis [GO:0070086]; ubiquitin-dependent protein catabolic process [GO:0006511]

axon [GO:0030424]; cilium [GO:0005929]; flotillin complex [GO:0016600]; Golgi apparatus [GO:0005794]; growth cone [GO:0030426]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]

calcium ion binding [GO:0005509]; ephrin receptor binding [GO:0046875]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; phosphotyrosine residue binding [GO:0001784]; protein kinase binding [GO:0019901]; protein tyrosine kinase binding [GO:1990782]; receptor tyrosine kinase binding [GO:0030971]; SH3 domain binding [GO:0017124]; ubiquitin protein ligase activity [GO:0061630]

DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. {ECO:0000256|RuleBase:RU367001}.

IPR024162;IPR014741;IPR036537;IPR003153;IPR014742;IPR024159;IPR011992;IPR036860;IPR015940;IPR009060;IPR018957;IPR001841;IPR013083;IPR017907;

1.20.930.20;1.10.8.10;1.10.238.10;3.30.505.10;3.30.40.10;

A0A0U3BRC5

MSHCTIFLYKYFPGKPRYQHCSFLHPLNHKLKSLFLPITGSRFLSNSTFSVSDSAHSHQAKPHVRNAQFDFKAYMLEKITAVNQALDAALPVREPVKIHEAMRYSLLLGGKRICPIVCLAACHLVGGDESTAMPSAAALEMIHAMSLMHDDLPCMDNDDLRRGRPSNHVVFGEGATVLAGYALIARAFEHIATATQGVGPGKILRVIGELAQLIGAEGVVGGQVVDLRCGGEGQMAIGLEQLEYIHLHKTAASVEASAVAGAVLGGASEEEIERLRKYSRSAGLLFQVVDDILDVTKSSEELGKTAGKDLAAGKTTYPKLLGMEKSREMAEKLKREAQEQLLGFDPIKAAPLIALVDFIAYRDK

Leucosceptrum canum (Hairy white-wand) (Clerodendron leucosceptrum)

FUNCTION: Involved in the biosynthesis of leucosceptrane sesterterpenoids natural products, which are playing defensive roles toward herbivorus insects (e.g. Spodoptera exigua) (PubMed:26941091). Catalyzes the condensation of isopentenyl pyrophosphate (IDP) with the allylic pyrophosphates to yield geranylfarnesyl diphosphate (GFDP), the C(25) prenyl diphosphate precursor to all sesterterpenoids (PubMed:26941091). Geranylgeranyl diphosphate (GGPP) is the preferred substrate, however dimethylallyl diphosphate (DMADP), farnesyl diphosphate (FDP) and geranyl diphosphate (GDP) can also be used as allylic substrate (PubMed:26941091). {ECO:0000269|PubMed:26941091}.

2.5.1.81

CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769; EC=2.5.1.81; Evidence={ECO:0000269|PubMed:26941091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695; Evidence={ECO:0000269|PubMed:26941091}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + 2 isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 2 diphosphate; Xref=Rhea:RHEA:66852, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:26941091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66853; Evidence={ECO:0000269|PubMed:26941091}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + 3 isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 3 diphosphate; Xref=Rhea:RHEA:66856, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; Evidence={ECO:0000269|PubMed:26941091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66857; Evidence={ECO:0000269|PubMed:26941091}; CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + 4 isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 4 diphosphate; Xref=Rhea:RHEA:66860, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57907, ChEBI:CHEBI:128769; Evidence={ECO:0000269|PubMed:26941091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66861; Evidence={ECO:0000269|PubMed:26941091};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P14324}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34.89 uM for dimethylallyl diphosphate (in the presence of isopentenyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=3.04 uM for isopentenyl diphosphate (in the presence of geranylgeranyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=6.28 uM for geranyl diphosphate (in the presence of isopentenyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=4.1 uM for farnesyl diphosphate (in the presence of isopentenyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=1.65 uM for geranylgeranyl diphosphate (in the presence of isopentenyl diphosphate) {ECO:0000269|PubMed:26941091}; Note=kcat is 16.9x10(-6) sec(-1) with dimethylallyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 8.2x10(-6) sec(-1) with isopentenyl diphosphate as substrate (in the presence of geranylgeranyl diphosphate) (PubMed:26941091). kcat is 6.16x10(-6) sec(-1) with geranyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 7.19x10(-6) sec(-1) with farnesyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 5.17x10(-6) sec(-1) with geranylgeranyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). {ECO:0000269|PubMed:26941091};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30468448}.; PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:26941091}.

Chloroplast;Isoprene biosynthesis;Magnesium;Metal-binding;Plastid;Transferase;Transit peptide

response to herbivore [GO:0080027]; response to insect [GO:0009625]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; terpenoid biosynthetic process [GO:0016114]

chloroplast [GO:0009507]

farnesyltranstransferase activity [GO:0004311]; geranylfarnesyl diphosphate synthase activity [GO:0044687]; metal ion binding [GO:0046872]; transferase activity [GO:0016740]

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:26941091}.

IPR008949;IPR000092;IPR033749;

1.10.600.10;

A0A125QXJ1

MVTVGNYCEAEGPLGPAWAQNGLSPCFFFTLVPSTLMALGALALVLVLPCRRRDVPSGTEELFWAADSRVAPYALQLFLATLQVALPLAGLAGRVGTARGVRLPGYLLLASMLGSLASACGLWLLVAERRQARQSLAMGVWMKFRHSSGLLLLWTVAFAAENLALVSWNSPQWWWARADLGQQVQFGLWVLRYVISGGLFILGLWAPGLRPQSYTLRVHEADQDVERNQAQSTDRTSTWRDLGRKLRLLSSYLWPRGSPALQFIVLICLGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVLRVVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLFLTIVVTEWRAKFRRAMNTQENITRARAVDSLLNFETVKYYNAEGYEVERYREAIIKYQGLEWKSSASLVVLNQTQNLVIGLGLLAGSLLCAYFVSEQKLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGQIEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRIAAGDSEVEAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVSADQILVIKDGCIIERGRHEALLSQGGVYAEMWQLQQKGQETVSEDSKPQDIA

Mesocricetus auratus (Golden hamster)

FUNCTION: ATP-dependent transporter that catalyzes the transport of a broad-spectrum of porphyrins from the cytoplasm to the extracellular space through the plasma membrane or into the vesicle lumen. May also function as an ATP-dependent importer of porphyrins from the cytoplasm into the mitochondria, in turn may participate in the de novo heme biosynthesis regulation and in the coordination of heme and iron homeostasis during phenylhydrazine stress. May also play a key role in the early steps of melanogenesis producing PMEL amyloid fibrils. In vitro, it confers to cells a resistance to toxic metal such as arsenic and cadmium and against chemotherapeutics agent such as 5-fluorouracil, SN-38 and vincristin (By similarity). In addition may play a role in the transition metal homeostasis (By similarity). {ECO:0000250|UniProtKB:O70595, ECO:0000250|UniProtKB:Q9NP58}.

7.6.2.5

CATALYTIC ACTIVITY: Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate; Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344, ChEBI:CHEBI:456216; EC=7.6.2.5; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19262; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + coproporphyrin III(in) + H2O = ADP + coproporphyrin III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66664, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:131725, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66665; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58687, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + coproporphyrinogen III(in) + H2O = ADP + coproporphyrinogen III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57309, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66681; Evidence={ECO:0000250|UniProtKB:Q9DC29}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + protoporphyrin IX(in) = ADP + H(+) + phosphate + protoporphyrin IX(out); Xref=Rhea:RHEA:61336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57306, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61337; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + coproporphyrin I(in) + H2O = ADP + coproporphyrin I(out) + H(+) + phosphate; Xref=Rhea:RHEA:66768, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167478, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66769; Evidence={ECO:0000250|UniProtKB:Q9DC29}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + uroporphyrin I(in) = ADP + H(+) + phosphate + uroporphyrin I(out); Xref=Rhea:RHEA:66772, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167480, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66773; Evidence={ECO:0000250|UniProtKB:Q9DC29}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + uroporphyrin III(in) = ADP + H(+) + phosphate + uroporphyrin III(out); Xref=Rhea:RHEA:66776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167479, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66777; Evidence={ECO:0000250|UniProtKB:Q9DC29};

ATP-binding;Cell membrane;Disulfide bond;Endoplasmic reticulum;Endosome;Glycoprotein;Golgi apparatus;Lysosome;Membrane;Mitochondrion;Mitochondrion outer membrane;Nucleotide-binding;Reference proteome;Secreted;Translocase;Transmembrane;Transmembrane helix;Transport

cellular detoxification of cadmium ion [GO:0098849]; heme metabolic process [GO:0042168]; heme transmembrane transport [GO:0035351]; porphyrin-containing compound metabolic process [GO:0006778]

early endosome membrane [GO:0031901]; endolysosome membrane [GO:0036020]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; melanosome membrane [GO:0033162]; mitochondrial outer membrane [GO:0005741]; multivesicular body membrane [GO:0032585]; plasma membrane [GO:0005886]

ABC-type heme transporter activity [GO:0015439]; ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; heme binding [GO:0020037]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NP58}. Late endosome membrane {ECO:0000250|UniProtKB:O70595}. Early endosome membrane {ECO:0000250|UniProtKB:O70595}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q9NP58}. Mitochondrion {ECO:0000250|UniProtKB:Q9NP58}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q9NP58}. Melanosome membrane {ECO:0000250|UniProtKB:Q9NP58}. Note=Present in the membrane of mature erythrocytes and in exosomes released from reticulocytes during the final steps of erythroid maturation. Traffics from endoplasmic reticulum to Golgi during its glycans's maturation, therefrom is first targeted to the plasma membrane, and is rapidly internalized through endocytosis to be distributed to the limiting membrane of multivesicular bodies and lysosomes. Localized on the limiting membrane of early melanosomes of pigment cells (By similarity). Targeted to the endolysosomal compartment (By similarity). {ECO:0000250|UniProtKB:O70595, ECO:0000250|UniProtKB:Q9NP58}.

PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NP58}.

DOMAIN: Contains two independently folding units, the N-terminal transmembrane domain (residues 1-205) and the ABC-core domain (206-842) are respectively responsible for the lysosomal targeting and the ATPase activity. {ECO:0000250|UniProtKB:Q9NP58}.

IPR003593;IPR011527;IPR036640;IPR003439;IPR017871;IPR032410;IPR027417;IPR039421;

1.20.1560.10;3.40.50.300;

A0A126GUP6

MEPHFFFTVLWMLLMGTSSTYAQEIFGYCRTPDENSGTCINLRECGYLFELLQSEEVTEQDRRFLQASQCGYRNGQVLEKHFCFTNVQICCANSRMRNQQPQWGNHPQPTQTTKPTKRSGTKLLPMAPNCGENFGDRVVGGNETTKREFPWMALIEYTKPGNVKGHHCGGSLINHRYVLTAAHCVSAIPSDWELTGVRLGEWDASTNPDCTVGKNGRRDCNEPYVDYPVEERIPHPQYPGNSRDQLNDIALLRLRDEVQYSDFILPVCLPTLASQHNNIFLGRKVVVAGWGRTETNFTSNIKLKAELDTVPTSECNQRYATQRRTVTTKQMCAGGVEGVDSCRGDSGGPLLLEDYSNGNSNYYIAGVVSYGPTPCGLKGWPGVYTRVEAYLNWIENNVRA

Drosophila melanogaster (Fruit fly)

FUNCTION: Serine protease which plays an essential role in the melanization immune response by acting downstream of sp7 to activate prophenoloxidase (PPO1) (PubMed:16861233). May function in diverse Hayan-dependent PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A in the hemolymph and Spn77BA in the trachea (PubMed:16861233, PubMed:18854145). Regulation of melanization and PPO1 activation appears to be largely independent of the Toll signaling pathway (PubMed:16861233). {ECO:0000269|PubMed:16861233, ECO:0000269|PubMed:18854145}.

3.4.21.-

Alternative splicing;Calcium;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Serine protease;Signal;Zymogen

melanization defense response [GO:0035006]; proteolysis [GO:0006508]; response to fungus [GO:0009620]; Toll receptor ligand protein activation cascade [GO:0160032]

endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; serine hydrolase activity [GO:0017171]; serine-type endopeptidase activity [GO:0004252]

DOMAIN: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure. {ECO:0000255|PROSITE-ProRule:PRU01236}.

IPR022700;IPR038565;IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;IPR033116;

3.30.1640.30;2.40.10.10;

A0A126GV13

MAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLASGRKLTIGSKRPVNLAVANKSQTLPRNLGSKTSVGAVQRQPAKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGPSGSGASTPVVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEALRRLAKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDITI

Drosophila melanogaster (Fruit fly)

FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000256|HAMAP-Rule:MF_03021}.

5.6.1.1

CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000256|ARBA:ARBA00036378, ECO:0000256|HAMAP-Rule:MF_03021};

ATP-binding;Cell cycle;Cell division;Chromosome;Cytoplasm;Cytoskeleton;Developmental protein;Differentiation;Hydrolase;Isomerase;Lipid droplet;Membrane;Microtubule;Mitosis;Neurogenesis;Nucleotide-binding;Reference proteome

adult locomotory behavior [GO:0008344]; cell differentiation [GO:0030154]; cell division [GO:0051301]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; nervous system development [GO:0007399]; positive regulation of microtubule depolymerization [GO:0031117]; protein hexamerization [GO:0034214]; regulation of synapse structure or activity [GO:0050803]

centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; spindle [GO:0005819]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000256|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000256|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000256|HAMAP-Rule:MF_03021}.

IPR003593;IPR041569;IPR003959;IPR003960;IPR007330;IPR036181;IPR027417;IPR015415;IPR017179;

1.10.8.60;3.40.50.300;1.20.58.80;

A0A139WFS2

MVIAKKITINNRFDGMPKPSDFKTIEEELPPLKPGEFLAEAVFLSVDPYMRAYAHNIPLGATMVGSQVAKIIESRNDKYPVGKHVVGKFDWRSHTISSGLPTVIQGAGNAPAPYLVPDLGNLPMSYLLGVLGMPGSTAYFGFLDICKPKNGEVVAVSGAAGAVGSIVGQIAKIEGCKVVGITGSEDKGRFLVDGLGFDGFVNYKTDDVAKKLDQLVPEGIDCYFDNVAGEISSTVIGHMRDYGFVGPFRPTTMMWKTRPENYLYQERSGEAFQQILKWLQAGRMKYHETITKGFDNMVAAFIEMLQGKNLGKAIVKVAKSSLQSRLTLYSPITTNGINKHQMPSSPIKRAISGGVNMVKARRYIFEKQFEGLPKSTDLRLVEEELPPIKDGEFLAEAVYLSVDPYMRAYAPRLSLGRTFIGSQVAKIIESKNDKFPVGKYVVGEFGWRTHSISDGRPLEVGRPGAWLAPELEGLPLSYTLGILGMPGNTAYFGFLELCKPKSGETVAVTGAAGAVGSIVGQIAKIKGCTVIGIAGSDEKGKWLVNELKFDHFINYKDPDFEKKLAQAAPKGIDCYFDNVGGQISTTIMNKMNLFGRVAVCGAISGYNDKSAARADPVQFPLVFSQLKMEGFVVHRWADRWFEGILQNKKWIKEGKLRYKETVTEGFENMFKAFVDMLQGGNTGKAIVKV

Tribolium castaneum (Red flour beetle)

1.3.1.48; 1.3.1.74

CATALYTIC ACTIVITY: Reaction=(5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51212, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133974, ChEBI:CHEBI:133975; Evidence={ECO:0000256|ARBA:ARBA00023498}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51213; Evidence={ECO:0000256|ARBA:ARBA00023498}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374, ChEBI:CHEBI:133409; Evidence={ECO:0000256|ARBA:ARBA00023548}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590; Evidence={ECO:0000256|ARBA:ARBA00023548}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584, ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133408; Evidence={ECO:0000256|ARBA:ARBA00023544}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586; Evidence={ECO:0000256|ARBA:ARBA00023544}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15-oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:79072, ChEBI:CHEBI:133411; Evidence={ECO:0000256|ARBA:ARBA00023543}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594; Evidence={ECO:0000256|ARBA:ARBA00023543}; CATALYTIC ACTIVITY: Reaction=20-hydroxy-leukotriene B4 + NADP(+) = 12-oxo-20-hydroxy-leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:51208, ChEBI:CHEBI:15378, ChEBI:CHEBI:57460, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133346; Evidence={ECO:0000256|ARBA:ARBA00023517}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51209; Evidence={ECO:0000256|ARBA:ARBA00023517}; CATALYTIC ACTIVITY: Reaction=4-hydroxynonanal + NADP(+) = (E)-4-hydroxynon-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:64736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58968, ChEBI:CHEBI:156112; Evidence={ECO:0000256|ARBA:ARBA00023553}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64738; Evidence={ECO:0000256|ARBA:ARBA00023553}; CATALYTIC ACTIVITY: Reaction=6-trans-leukotriene B4 + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51204, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:90723, ChEBI:CHEBI:133974; Evidence={ECO:0000256|ARBA:ARBA00023496}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51205; Evidence={ECO:0000256|ARBA:ARBA00023496}; CATALYTIC ACTIVITY: Reaction=NADP(+) + nonan-2-one = (3E)-nonen-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77927, ChEBI:CHEBI:133457; Evidence={ECO:0000256|ARBA:ARBA00023696}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50618; Evidence={ECO:0000256|ARBA:ARBA00023696}; CATALYTIC ACTIVITY: Reaction=NADP(+) + octanal = (2E)-octenal + H(+) + NADPH; Xref=Rhea:RHEA:50780, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61748; Evidence={ECO:0000256|ARBA:ARBA00023504}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50782; Evidence={ECO:0000256|ARBA:ARBA00023504}; CATALYTIC ACTIVITY: Reaction=NADP(+) + pentan-2-one = (E)-pent-3-en-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50788, ChEBI:CHEBI:15378, ChEBI:CHEBI:16472, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145276; Evidence={ECO:0000256|ARBA:ARBA00024160}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50790; Evidence={ECO:0000256|ARBA:ARBA00024160}; CATALYTIC ACTIVITY: Reaction=an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:13737, ChEBI:CHEBI:12834, ChEBI:CHEBI:13757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.74; Evidence={ECO:0000256|ARBA:ARBA00023507}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13739; Evidence={ECO:0000256|ARBA:ARBA00023507}; CATALYTIC ACTIVITY: Reaction=decanal + NADP(+) = (2E)-decenal + H(+) + NADPH; Xref=Rhea:RHEA:50612, ChEBI:CHEBI:15378, ChEBI:CHEBI:31457, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133455; Evidence={ECO:0000256|ARBA:ARBA00023691}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50614; Evidence={ECO:0000256|ARBA:ARBA00023691}; CATALYTIC ACTIVITY: Reaction=dodecanal + NADP(+) = (2E)-dodecenal + H(+) + NADPH; Xref=Rhea:RHEA:50784, ChEBI:CHEBI:15378, ChEBI:CHEBI:27836, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133741; Evidence={ECO:0000256|ARBA:ARBA00023530}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50786; Evidence={ECO:0000256|ARBA:ARBA00023530}; CATALYTIC ACTIVITY: Reaction=hexanal + NADP(+) = (E)-hex-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:50776, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:88528; Evidence={ECO:0000256|ARBA:ARBA00034052}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50778; Evidence={ECO:0000256|ARBA:ARBA00034052}; CATALYTIC ACTIVITY: Reaction=leukotriene B4 + NADP(+) = 12-oxo-leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:50608, ChEBI:CHEBI:15378, ChEBI:CHEBI:57461, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133309; Evidence={ECO:0000256|ARBA:ARBA00023545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50609; Evidence={ECO:0000256|ARBA:ARBA00023545};

Fatty acid metabolism;Hydroxylation;Lipid metabolism;Oxidoreductase;Prostaglandin metabolism;Reference proteome

prostaglandin metabolic process [GO:0006693]

cytoplasm [GO:0005737]

13-prostaglandin reductase activity [GO:0036132]; 15-oxoprostaglandin 13-oxidase activity [GO:0047522]; 2-alkenal reductase [NAD(P)+] activity [GO:0032440]

IPR013149;IPR041694;IPR011032;IPR045010;IPR036291;IPR020843;IPR014190;

3.90.180.10;3.40.50.720;

A0A140LIF8

MEEAVESPEVKEFEYFSDAVFIPKDGNTLSVGVIKRIETAVKEGEVVKVVSIVKEIIQNVSRNKIKIAVTGDSGNGMSSFINALRLIGHEEKDSAPTGVVRTTQKPTCYFSSHFPYVELWDLPGLGATAQSVESYLEEMQISIYDLIIIVASEQFSLNHVKLAITMQRMRKRFYVVWTKLDRDLSTSTFPEPQLLQSIQRNIRDSLQKEKVKEHPMFLVSVFKPESHDFPKLRETLQKDLPVIKYHGLVETLYQVCEKTVNERVESIKKSIDEDNLHTEFGISDPGNAIEIRKAFQKTFGLDDISLHLVALEMKNKHFNTSMESQETQRYQQDDWVLARLYRTGTRVGSIGFDYMKCCFTSHHSRCKQQKDILDETAAKAKEVLLKILRLSIPHP

Mus musculus (Mouse)

FUNCTION: Immunity-related GTPase that plays important roles in innate immunity and inflammatory response (PubMed:17641048, PubMed:33124745, PubMed:33124769, PubMed:34078740, PubMed:34338548). Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes (By similarity). Required for clearance of acute protozoan and bacterial infections (PubMed:17641048, PubMed:34078740, PubMed:34338548). Acts by participating to Tgtp1/Irgb6 and Gbp1-mediated parasite killing by promoting their accumulation on the T.gondii parasitophorous vacuole membranes (PubMed:34078740). Also required for prolonged loading of ubiquitin and p62/Sqstm1 to parasitophorous vacuole membranes (PubMed:34078740). Also acts as a key negative regulator of the inflammatory response by inhibiting the non-canonical inflammasome, thereby protecting against Casp11-driven septic shock during endotoxemia (PubMed:33124745, PubMed:33124769). {ECO:0000250|UniProtKB:Q60766, ECO:0000269|PubMed:17641048, ECO:0000269|PubMed:33124745, ECO:0000269|PubMed:33124769, ECO:0000269|PubMed:34078740, ECO:0000269|PubMed:34338548}.

3.6.5.-

CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:34078740}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:34078740};

Cytoplasm;Cytoplasmic vesicle;Golgi apparatus;GTP-binding;Hydrolase;Immunity;Innate immunity;Membrane;Nucleotide-binding;Reference proteome;Ubl conjugation

cellular response to interferon-beta [GO:0035458]; defense response [GO:0006952]; defense response to protozoan [GO:0042832]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640]; negative regulation of non-canonical inflammasome complex assembly [GO:0160076]; protein targeting to vacuolar membrane [GO:0044395]; response to bacterium [GO:0009617]

cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; vacuolar membrane [GO:0005774]

GTP binding [GO:0005525]; GTPase activity [GO:0003924]

SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:34078740}. Golgi apparatus membrane {ECO:0000269|PubMed:34078740}. Cytoplasm, cytosol {ECO:0000269|PubMed:34078740}. Note=Localizes to parasitophorous vacuole membranes. {ECO:0000269|PubMed:34078740}.

PTM: Ubiquitinated; polyubiquitinated in the cytosol, promoting Gbp1 recruitment to the T.gondii parasitophorous vacuole membranes. {ECO:0000269|PubMed:34078740}.

IPR030385;IPR007743;IPR027417;

3.40.50.300;

A0A140T892

MLVLERCDLELEANGRDHHTADLCRERLVVRRGQPFWLTLHFEGRNYEASVDSLTFCAVTGPDPSEEAGTKALFRLSDATEEGAWAAVAADQRDSTLSLHLSTPANAPVGHYRLSLEASTGYQGSSFMLGQFTLLFNSWCPADAVYLDSDEERQEYVLTQQGFIYQGSAKFIKNIPWNFGQFEEGILDICLMLLDVNPKFLRNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGRWDNNYADGISPMSWIGSVDILRRWKRDGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEFGEIQSDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNADVVDWIRQDDGSLHKSINHSLVVGLKISTKCVGRDDREDITHSYKYPEGSPEEREAFTRANHLNKLVNKEETGVAMRIRVGEGMNRGCDFDVFAHITNSTPEEHTGRLLLCARTVSYNGILGPECGTKDLLSLSLEPYSEKSIPLRILYEKYCDCLTESNLIKVRGLLIEPAANSYLLAERDIYLENPEIKIRILGEPKQNRKLVAEISLQNPLTVALSGCTFTVEGAGLIEEQKTVDIPDPVEAGEEVKVRVDLLPLYVGRHKLVVNFESDRLKAVKGFRNVIVGPS

Bos taurus (Bovine)

2.3.2.13; 3.5.1.44

CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline + L-glutaminyl-[protein] = 5-(R)-noradrenalinyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66560, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17054, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011, ChEBI:CHEBI:72587, ChEBI:CHEBI:167178; Evidence={ECO:0000256|ARBA:ARBA00036051}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66561; Evidence={ECO:0000256|ARBA:ARBA00036051}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973, ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000256|ARBA:ARBA00036025}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16442; Evidence={ECO:0000256|ARBA:ARBA00036025}; CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000256|ARBA:ARBA00036876}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54817; Evidence={ECO:0000256|ARBA:ARBA00036876}; CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[protein] + serotonin = 5-serotonyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66552, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17052, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011, ChEBI:CHEBI:167174, ChEBI:CHEBI:350546; Evidence={ECO:0000256|ARBA:ARBA00036377}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66553; Evidence={ECO:0000256|ARBA:ARBA00036377}; CATALYTIC ACTIVITY: Reaction=dopamine + L-glutaminyl-[protein] = 5-dopaminyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66556, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17053, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011, ChEBI:CHEBI:59905, ChEBI:CHEBI:167175; Evidence={ECO:0000256|ARBA:ARBA00036119}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66557; Evidence={ECO:0000256|ARBA:ARBA00036119}; CATALYTIC ACTIVITY: Reaction=histamine + L-glutaminyl-[protein] = 5-histaminyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66564, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17056, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011, ChEBI:CHEBI:58432, ChEBI:CHEBI:167179; Evidence={ECO:0000256|ARBA:ARBA00036107}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66565; Evidence={ECO:0000256|ARBA:ARBA00036107};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR000459-2}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000459-2};

Acyltransferase;Calcium;Cell membrane;Chromosome;Extracellular matrix;GTP-binding;Hydrolase;Membrane;Metal-binding;Mitochondrion;Nucleotide-binding;Nucleus;Protease;Proteomics identification;Reference proteome;Secreted;Transferase

proteolysis [GO:0006508]

chromosome [GO:0005694]; collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]

GTP binding [GO:0005525]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; protein-glutamine gamma-glutamyltransferase activity [GO:0003810]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Chromosome {ECO:0000256|ARBA:ARBA00004286}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.

IPR013783;IPR014756;IPR038765;IPR002931;IPR036985;IPR023608;IPR013808;IPR008958;IPR036238;IPR001102;

2.60.40.10;3.90.260.10;

A0A140T8D4

MIWEVTVLLSLVLGTGAVPLEDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIVHRNGIPDEQIIVMMYDDIANSEDNPTPGIVINRPNGSDVYQGVLKDYTGEDVTPKNFLAVLRGDAEAVKGVGSGKVLKSGPRDHVFVYFTDHGATGILVFPNEDLHVKDLNETIRYMYEHKMYQKMVFYIEACESGSMMNHLPPDINVYATTAANPRESSYACYYDEQRSTFLGDWYSVNWMEDSDVEDLTKETLHKQYQLVKSHTNTSHVMQYGNKSISAMKLMQFQGLKHQASSPISLPAVSRLDLTPSPEVPLSIMKRKLMSTNDLQESRRLVQKIDRHLEARNIIEKSVRKIVTLVSGSAAEVDRLLSQRAPLTEHACYQTAVSHFRSHCFNWHNPTYEYALRHLYVLVNLCENPYPIDRIKLSMNKVCHGYY

Bos taurus (Bovine)

3.4.22.34

CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.; EC=3.4.22.34; Evidence={ECO:0000256|ARBA:ARBA00000810};

Hydrolase;Protease;Reference proteome;Signal;Thiol protease;Zymogen

antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; associative learning [GO:0008306]; cellular response to amyloid-beta [GO:1904646]; cellular response to calcium ion [GO:0071277]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; dendritic spine organization [GO:0097061]; memory [GO:0007613]; negative regulation of ERBB signaling pathway [GO:1901185]; negative regulation of gene expression [GO:0010629]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell chemotaxis [GO:2001028]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of monocyte chemotaxis [GO:0090026]; proteolysis involved in protein catabolic process [GO:0051603]; receptor catabolic process [GO:0032801]; renal system process [GO:0003014]; response to acidic pH [GO:0010447]; self proteolysis [GO:0097264]; vacuolar protein processing [GO:0006624]

apical part of cell [GO:0045177]; extracellular region [GO:0005576]; late endosome [GO:0005770]; lysosomal lumen [GO:0043202]; perinuclear region of cytoplasm [GO:0048471]

cysteine-type endopeptidase activity [GO:0004197]; endopeptidase activator activity [GO:0061133]

IPR043577;IPR048501;IPR046427;IPR001096;

1.10.132.130;3.40.50.1460;

A0A140TAB8

MKSGSGGGSPTSLWGLVFLSAALSLWPTSGEICGPGIDIRNDYQQLKRLENCTVIEGFLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTIDWSLILDAVSNNYIVGNKPPKECGDLCPGTLEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSVCGKRACTENNECCHPECLGSCHTPDDNTTCVACRHYYYKGVCVPACPPGTYRFEGWRCVDRDFCANIPNAESSDSDGFVIHDGECMQECPSGFIRNSTQSMYCIPCEGPCPKVCGDEEKKTKTIDSVTSAQMLQGCTILKGNLLINIRRGNNIASELENFMGLIEVVTGYVKIRHSHALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWNHRNLTVRSGKMYFAFNPKLCVSEIYRMEEVTGTKGRQSKGDINTRNNGERASCESDVLRFTSTTTWKNRIIITWHRYRPPDYRDLISFTVYYKEAPFKNVTEYDGQDACGSNSWNMVDVDLPPNKEGEPGILLHGLKPWTQYAVYVKAVTLTMVENDHIRGAKSEILYIRTNASVPSIPLDVLSASNSSSQLIVKWNPPTLPNGNLSYYIVRWQRQPQDGYLFRHNYCSKDKIPIRKYADGTIDVEEVTENPKTEVCGGDKGPCCACPKTEAEKQAEKEEAEYRKVFENFLHNSIFVPRPERRRRDVLQVANTTMSSRSRNTTVADTYNITDPEEFETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVPAKTTYENFMHLIIALPVAILLIVGGLVIMLYVFHRKRVSGPAEGSSWKGPFPSCLFLVYVPDEWEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEVENNLVLIPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKDEMEPSFQEVSFYYSEENKPPEPEELEMELELEPENMESVPLDPSASSASLPLPERHSGHKAENGPGVLVLRASFDERQPYAHMNGGRANERALPLPQSSTC

Rattus norvegicus (Rat)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171, ECO:0000256|RuleBase:RU000312};

ATP-binding;Cleavage on pair of basic residues;Glycoprotein;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

amyloid-beta clearance [GO:0097242]; cellular response to amyloid-beta [GO:1904646]; cellular response to glucose stimulus [GO:0071333]; immune response [GO:0006955]; negative regulation of apoptotic process [GO:0043066]; negative regulation of MAPK cascade [GO:0043409]; phosphorylation [GO:0016310]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; regulation of JNK cascade [GO:0046328]; transcytosis [GO:0045056]

alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; axon [GO:0030424]; insulin receptor complex [GO:0005899]; intracellular membrane-bounded organelle [GO:0043231]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; insulin binding [GO:0043559]; insulin receptor activity [GO:0005009]; insulin receptor binding [GO:0005158]; insulin receptor substrate binding [GO:0043560]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor receptor activity [GO:0005010]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein transporter activity [GO:0140318]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR003961;IPR036116;IPR006211;IPR006212;IPR009030;IPR013783;IPR011009;IPR000719;IPR017441;IPR000494;IPR036941;IPR001245;IPR008266;IPR020635;IPR016246;IPR002011;

2.60.40.10;3.80.20.20;1.10.510.10;

A0A140TAU9

MWELLAFLLLAIAYFFRPKVKCPGAKYPKSLPYLPLVGSLPFLPRHGHPHVNFFKLQKKYGPIYSLRMGTKTTVMVGHYQLAKEVLIKKGKEFSGRPQVATLNILSDNQKGVAFADHGAPWQLHRKLVRAAFALFKDGNQKLEKIICHETSLLCDLLATQNGQTIDLSSPLFLAVTNVICWICFNSSYMKGDPALETMQNYHKGILETLEKDNVVDIFPALKIFPNKSLEKMRHCVNIRNELLSKIFEKHKENFNSDSITSMLDLLIQAKKNSDNNNTGPDQDSKLLSDKHILATIGDIFGAGVETTTSVVKWIVAFLLHDPQLKKKIQEEIDQNVGFSRTPTLSDRNRLLLLEATIREVLRIRPVAPMLIPHKALVDSSIGEFAVDEGTNVIINLWALHHNEKEWHQPDRFMPERFLDPTGSQLISPSLSYLPFGAGPRSCIGELLARQELFLFTAWLLQRFNLEGGPG

Equus caballus (Horse)

1.14.14.19; 1.14.14.32

CATALYTIC ACTIVITY: Reaction=16alpha,17alpha-dihydroxypregnenolone + O2 + reduced [NADPH--hemoprotein reductase] = 3beta,16alpha-dihydroxy-androst-5-en-17-one + acetate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53224, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:27771, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137049; Evidence={ECO:0000256|ARBA:ARBA00043677}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53225; Evidence={ECO:0000256|ARBA:ARBA00043677}; CATALYTIC ACTIVITY: Reaction=16alpha,17alpha-dihydroxyprogesterone + O2 + reduced [NADPH--hemoprotein reductase] = 6beta,16alpha,17alpha-trihydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53220, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:763, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137046; Evidence={ECO:0000256|ARBA:ARBA00043765}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53221; Evidence={ECO:0000256|ARBA:ARBA00043765}; CATALYTIC ACTIVITY: Reaction=17alpha-hydroxypregnenolone + O2 + reduced [NADPH--hemoprotein reductase] = 3beta-hydroxyandrost-5-en-17-one + acetate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50244, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28689, ChEBI:CHEBI:28750, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.32; Evidence={ECO:0000256|ARBA:ARBA00043778}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50245; Evidence={ECO:0000256|ARBA:ARBA00043778}; CATALYTIC ACTIVITY: Reaction=17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein reductase] = 16alpha,17alpha-dihydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53216, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:763, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17252, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000256|ARBA:ARBA00043807}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53217; Evidence={ECO:0000256|ARBA:ARBA00043807}; CATALYTIC ACTIVITY: Reaction=17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein reductase] = acetate + androst-4-ene-3,17-dione + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:14753, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16422, ChEBI:CHEBI:17252, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.32; Evidence={ECO:0000256|ARBA:ARBA00043692}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14754; Evidence={ECO:0000256|ARBA:ARBA00043692}; CATALYTIC ACTIVITY: Reaction=3beta-hydroxyandrost-5-en-17-one + O2 + reduced [NADPH--hemoprotein reductase] = 3beta,16alpha-dihydroxy-androst-5-en-17-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47220, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:27771, ChEBI:CHEBI:28689, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000256|ARBA:ARBA00043660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47221; Evidence={ECO:0000256|ARBA:ARBA00043660}; CATALYTIC ACTIVITY: Reaction=O2 + pregnenolone + reduced [NADPH--hemoprotein reductase] = 17alpha-hydroxypregnenolone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50236, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16581, ChEBI:CHEBI:28750, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.19; Evidence={ECO:0000256|ARBA:ARBA00043658}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50237; Evidence={ECO:0000256|ARBA:ARBA00043658}; CATALYTIC ACTIVITY: Reaction=O2 + progesterone + reduced [NADPH--hemoprotein reductase] = 17alpha-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46308, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17026, ChEBI:CHEBI:17252, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.19; Evidence={ECO:0000256|ARBA:ARBA00043730}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46309; Evidence={ECO:0000256|ARBA:ARBA00043730}; CATALYTIC ACTIVITY: Reaction=a C21-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 17alpha-hydroxy-C21-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:65760, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61313, ChEBI:CHEBI:138141; EC=1.14.14.19; Evidence={ECO:0000256|ARBA:ARBA00043780}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65761; Evidence={ECO:0000256|ARBA:ARBA00043780}; CATALYTIC ACTIVITY: Reaction=androst-4-ene-3,17-dione + O2 + reduced [NADPH--hemoprotein reductase] = 16alpha-hydroxyandrost-4-ene-3,17-dione + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53228, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16422, ChEBI:CHEBI:27582, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000256|ARBA:ARBA00043728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53229; Evidence={ECO:0000256|ARBA:ARBA00043728};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000256|ARBA:ARBA00001971, ECO:0000256|PIRSR:PIRSR602401-1};

PATHWAY: Hormone biosynthesis. {ECO:0000256|ARBA:ARBA00004972}.; PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis. {ECO:0000256|ARBA:ARBA00043954}.; PATHWAY: Steroid hormone biosynthesis. {ECO:0000256|ARBA:ARBA00025710}.

Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Signal;Steroidogenesis

hormone biosynthetic process [GO:0042446]; progesterone metabolic process [GO:0042448]; steroid biosynthetic process [GO:0006694]

endoplasmic reticulum membrane [GO:0005789]

17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid 17-alpha-monooxygenase activity [GO:0004508]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}. Membrane {ECO:0000256|ARBA:ARBA00004370}. Microsome membrane {ECO:0000256|ARBA:ARBA00004524}.

IPR001128;IPR017972;IPR002401;IPR036396;

1.10.630.10;

A0A140VJG8

MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP

Homo sapiens (Human)

FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. {ECO:0000256|ARBA:ARBA00003256}.

2.1.1.6

CATALYTIC ACTIVITY: Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53092, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:89268; Evidence={ECO:0000256|ARBA:ARBA00001894}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53093; Evidence={ECO:0000256|ARBA:ARBA00001894}; CATALYTIC ACTIVITY: Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53088, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:28955, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000256|ARBA:ARBA00001409}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53089; Evidence={ECO:0000256|ARBA:ARBA00001409}; CATALYTIC ACTIVITY: Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-estrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53108, ChEBI:CHEBI:1156, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136980; Evidence={ECO:0000256|ARBA:ARBA00000467}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53109; Evidence={ECO:0000256|ARBA:ARBA00000467}; CATALYTIC ACTIVITY: Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-methoxyestrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53100, ChEBI:CHEBI:1156, ChEBI:CHEBI:1189, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000256|ARBA:ARBA00000037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53101; Evidence={ECO:0000256|ARBA:ARBA00000037}; CATALYTIC ACTIVITY: Reaction=4-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 4-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53096, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:62845, ChEBI:CHEBI:136975; Evidence={ECO:0000256|ARBA:ARBA00001627}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53097; Evidence={ECO:0000256|ARBA:ARBA00001627}; CATALYTIC ACTIVITY: Reaction=4-hydroxyestrone + S-adenosyl-L-methionine = 4-methoxyestrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53104, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87602, ChEBI:CHEBI:136972; Evidence={ECO:0000256|ARBA:ARBA00000580}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53105; Evidence={ECO:0000256|ARBA:ARBA00000580}; CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000256|ARBA:ARBA00001722}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17878; Evidence={ECO:0000256|ARBA:ARBA00001722};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRNR:PIRNR037177, ECO:0000256|PIRSR:PIRSR037177-3}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRNR:PIRNR037177, ECO:0000256|PIRSR:PIRSR037177-3};

Catecholamine metabolism;Magnesium;Metal-binding;Methyltransferase;Neurotransmitter degradation;S-adenosyl-L-methionine;Transferase

artery development [GO:0060840]; behavioral fear response [GO:0001662]; cellular response to cocaine [GO:0071314]; cellular response to phosphate starvation [GO:0016036]; cerebellar cortex morphogenesis [GO:0021696]; cholesterol efflux [GO:0033344]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; dopamine catabolic process [GO:0042420]; dopamine secretion [GO:0014046]; exploration behavior [GO:0035640]; gene expression [GO:0010467]; glomerulus development [GO:0032835]; glycogen metabolic process [GO:0005977]; habituation [GO:0046959]; mastication [GO:0071626]; memory [GO:0007613]; methylation [GO:0032259]; multicellular organism growth [GO:0035264]; norepinephrine metabolic process [GO:0042415]; norepinephrine secretion [GO:0048243]; prostaglandin metabolic process [GO:0006693]; renal albumin absorption [GO:0097018]; renal filtration [GO:0097205]; renal sodium excretion [GO:0035812]; renin secretion into blood stream [GO:0002001]; response to amphetamine [GO:0001975]; response to angiotensin [GO:1990776]; response to corticosterone [GO:0051412]; response to cytokine [GO:0034097]; response to dopamine [GO:1903350]; response to food [GO:0032094]; response to hypoxia [GO:0001666]; response to inorganic substance [GO:0010035]; response to oxidative stress [GO:0006979]; response to salt [GO:1902074]; response to toxic substance [GO:0009636]; response to wounding [GO:0009611]; response to xenobiotic stimulus [GO:0009410]; startle response [GO:0001964]; synaptic transmission, dopaminergic [GO:0001963]; visual learning [GO:0008542]

axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; synapse [GO:0045202]; vesicle [GO:0031982]

catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; magnesium ion binding [GO:0000287]; orcinol O-methyltransferase activity [GO:0102938]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004228}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004228}; Extracellular side {ECO:0000256|ARBA:ARBA00004228}.

IPR017128;IPR029063;IPR002935;

3.40.50.150;

A0A140VJL2

MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALEVYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLPWDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYDFYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIFHTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKASQDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPGDTNSLFPGTWYLERVDEQHRRKYARRPV

Homo sapiens (Human)

FUNCTION: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. {ECO:0000256|RuleBase:RU364071}.; FUNCTION: Catalyzes the first irreversible step in ketogenesis, condensing acetyl-CoA to acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate. {ECO:0000256|ARBA:ARBA00037714}.

2.3.3.10

CATALYTIC ACTIVITY: Reaction=acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+); Xref=Rhea:RHEA:10188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43074, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.10; Evidence={ECO:0000256|ARBA:ARBA00001222}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10189; Evidence={ECO:0000256|ARBA:ARBA00001222};

PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3. {ECO:0000256|ARBA:ARBA00005218, ECO:0000256|RuleBase:RU364071}.

Acetylation;Cholesterol biosynthesis;Cholesterol metabolism;Lipid biosynthesis;Lipid metabolism;Mitochondrion;Phosphoprotein;Steroid biosynthesis;Steroid metabolism;Sterol biosynthesis;Sterol metabolism;Transferase;Transit peptide

acetyl-CoA metabolic process [GO:0006084]; adipose tissue development [GO:0060612]; cellular response to amino acid stimulus [GO:0071230]; cellular response to fatty acid [GO:0071398]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to insulin stimulus [GO:0032869]; cellular response to lipopolysaccharide [GO:0071222]; cholesterol biosynthetic process [GO:0006695]; farnesyl diphosphate biosynthetic process, mevalonate pathway [GO:0010142]; ketone body biosynthetic process [GO:0046951]; kidney development [GO:0001822]; liver development [GO:0001889]; lung development [GO:0030324]; midgut development [GO:0007494]; multicellular organismal response to stress [GO:0033555]; response to cAMP [GO:0051591]; response to ethanol [GO:0045471]; response to glucagon [GO:0033762]; response to growth hormone [GO:0060416]; response to linoleic acid [GO:0070543]; response to metal ion [GO:0010038]; response to monosaccharide [GO:0034284]; response to nutrient [GO:0007584]; response to prostaglandin F [GO:0034696]; response to starvation [GO:0042594]; response to temperature stimulus [GO:0009266]; response to testosterone [GO:0033574]; response to triglyceride [GO:0034014]; response to xenobiotic stimulus [GO:0009410]

mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]

hydroxymethylglutaryl-CoA synthase activity [GO:0004421]

SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.

IPR000590;IPR013746;IPR013528;IPR010122;IPR016039;

3.40.47.10;

A0A140VJL3

MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA

Homo sapiens (Human)

FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway. {ECO:0000256|ARBA:ARBA00025301}.

2.4.2.8

CATALYTIC ACTIVITY: Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8; Evidence={ECO:0000256|RuleBase:RU364099};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|RuleBase:RU364099};

PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1. {ECO:0000256|ARBA:ARBA00004669, ECO:0000256|RuleBase:RU364099}.

Cytoplasm;Glycosyltransferase;Magnesium;Metal-binding;Nucleotide-binding;Purine salvage;Transferase

adenine metabolic process [GO:0046083]; AMP salvage [GO:0044209]; central nervous system neuron development [GO:0021954]; cerebral cortex neuron differentiation [GO:0021895]; dendrite morphogenesis [GO:0048813]; dopamine metabolic process [GO:0042417]; dopaminergic neuron differentiation [GO:0071542]; GMP salvage [GO:0032263]; grooming behavior [GO:0007625]; guanine salvage [GO:0006178]; hypoxanthine metabolic process [GO:0046100]; IMP salvage [GO:0032264]; locomotory behavior [GO:0007626]; lymphocyte proliferation [GO:0046651]; purine ribonucleoside salvage [GO:0006166]; response to amphetamine [GO:0001975]; striatum development [GO:0021756]; T cell mediated cytotoxicity [GO:0001913]

cytosol [GO:0005829]

guanine phosphoribosyltransferase activity [GO:0052657]; hypoxanthine phosphoribosyltransferase activity [GO:0004422]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364099}.

IPR005904;IPR000836;IPR029057;

3.40.50.2020;

A0A140VK13

MVPRLLLRAWPRGPAVGPGAPSRPLSAGSGPGQYLQRSIVPTMHYQDSLPRLPIPKLEDTIRRYLSAQKPLLNDGQFRKTEQFCKSFENGIGKELHEQLVALDKQNKHTSYISGPWFDMYLSARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNMTVSAIRFLKTLRAGLLEPEVFHLNPAKSDTITFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPKPSRDELFTDDKARHLLVLRKGNFYIFDVLDQDGNIVSPSEIQAHLKYILSDSSPAPEFPLAYLTSENRDIWAELRQKLMSSGNEESLRKVDSAVFCLCLDDFPIKDLVHLSHNMLHGDGTNRWFDKSFNLIIAKDGSTAVHFEHSWGDGVAVLRFFNEVFKDSTQTPAVTPQSQPATTDSTVTVQKLNFELTDALKTGITAAKEKFDATMKTLTIDCVQFQRGGKEFLKKQKLSPDAVAQLAFQMAFLRQYGQTVATYESCSTAAFKHGRTETIRPASVYTKRCSEAFVREPSRHSAGELQQMMVECSKYHGQLTKEAAMGQGFDRHLFALRHLAAAKGIILPELYLDPAYGQINHNVLSTSTLSSPAVNLGGFAPVVSDGFGVGYAVHDNWIGCNVSSYPGRNAREFLQCVEKALEDMFDALEGKSIKS

Homo sapiens (Human)

2.3.1.21

CATALYTIC ACTIVITY: Reaction=(5Z)-tetradecenoyl-CoA + (R)-carnitine = CoA + O-(5Z)-tetradecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44852, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:84649, ChEBI:CHEBI:84650; Evidence={ECO:0000256|ARBA:ARBA00035780}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + (R)-carnitine = CoA + O-(9Z)-octadecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44856, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:84651; Evidence={ECO:0000256|ARBA:ARBA00036699}; CATALYTIC ACTIVITY: Reaction=(9Z)-tetradecenoyl-CoA + (R)-carnitine = CoA + O-(9Z)-tetradecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44848, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:65060, ChEBI:CHEBI:84647; Evidence={ECO:0000256|ARBA:ARBA00036256}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-dimethylnonanoyl-(R)-carnitine; Xref=Rhea:RHEA:44860, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061, ChEBI:CHEBI:84654; Evidence={ECO:0000256|ARBA:ARBA00024283}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine + decanoyl-CoA = CoA + O-decanoyl-(R)-carnitine; Xref=Rhea:RHEA:44828, ChEBI:CHEBI:16347, ChEBI:CHEBI:28717, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000256|ARBA:ARBA00036573}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine + dodecanoyl-CoA = CoA + O-dodecanoyl-R-carnitine; Xref=Rhea:RHEA:40279, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:77086; Evidence={ECO:0000256|ARBA:ARBA00036709}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine + eicosanoyl-CoA = CoA + O-eicosanoyl-(R)-carnitine; Xref=Rhea:RHEA:44844, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:84645; Evidence={ECO:0000256|ARBA:ARBA00035828}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine; Xref=Rhea:RHEA:12661, ChEBI:CHEBI:16347, ChEBI:CHEBI:17490, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=2.3.1.21; Evidence={ECO:0000256|ARBA:ARBA00036506}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12663; Evidence={ECO:0000256|ARBA:ARBA00036506}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine + octadecanoyl-CoA = CoA + O-octadecanoyl-(R)-carnitine; Xref=Rhea:RHEA:44840, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:84644; Evidence={ECO:0000256|ARBA:ARBA00036389}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine + octanoyl-CoA = CoA + O-octanoyl-(R)-carnitine; Xref=Rhea:RHEA:17177, ChEBI:CHEBI:16347, ChEBI:CHEBI:18102, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; Evidence={ECO:0000256|ARBA:ARBA00035841}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine + tetradecanoyl-CoA = CoA + O-tetradecanoyl-(R)-carnitine; Xref=Rhea:RHEA:44832, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:84634; Evidence={ECO:0000256|ARBA:ARBA00036375};

PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000256|ARBA:ARBA00005005}.

Acyltransferase;Fatty acid metabolism;Lipid metabolism;Membrane;Mitochondrion;Mitochondrion inner membrane;Transferase;Transport

fatty acid beta-oxidation [GO:0006635]; in utero embryonic development [GO:0001701]; positive regulation of cold-induced thermogenesis [GO:0120162]

mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]

carnitine O-palmitoyltransferase activity [GO:0004095]

SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.

IPR000542;IPR042572;IPR023213;IPR039551;IPR042231;

1.20.1280.180;3.30.559.10;1.10.275.20;3.30.559.70;

A0A142ZC57

MKYTDFLAHPDEIIPTIRMMYADYRLKNMEIKDPSVRFCYNMLNRVSRSFAMVIQQLPVELRDATCVFYLILRALDTVEDDMAIPKEVKIPMLRTFHEHLSDRSWKIKCGYGPYVDLMDNYPLVTDVYLRFDEGTKAVIKDITRRMGNGMADFIDLDEVLTIPQYDLYCHYVAGLCGIGMCKLFVDSGLEKEDLVAEEDLANQMGLFLQKNNIVRDYLEDINELPAPRMFWPKEIWGNYAKQLDEFKDPKNLDKAMLCLNHMVTDALRHCEVGLRSLSLLHNPNILRAVLIPQVMGVRTLTLVYNNPEVFRGVVKMRRGETAKIFVTTTSKLSFFRTYLQFANEMEQKCLTEAKNDPMVALTLKRVQGVQAACRAAIVKAEIAEGAKGPSTAMVLAGALLIAALAYFAYVYSAGGTSLKALPLFGVVIILAIGLFGRNLALKTV

Botryococcus braunii (Green alga)

FUNCTION: Converts the C20 geranylgeranyl diphosphate (GGPP) to the C40 lycopaoctaene, the first committed intermediate in the production of lycopadiene (PubMed:27050299, PubMed:28813599). Converts farnesyl diphosphate (FPP) into squalene, a precursor for sterol biosynthesis in eukaryotes (PubMed:27050299, PubMed:28813599). Converts with low efficiency the C20 phytyl diphosphate (PPP) to the C40 lycopadiene in vitro. This reaction may not have biological significance in vivo (PubMed:27050299). {ECO:0000269|PubMed:27050299, ECO:0000269|PubMed:28813599}.

2.5.1.148; 2.5.1.21

CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000269|PubMed:27050299}; CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000269|PubMed:27050299}; CATALYTIC ACTIVITY: Reaction=2 (2E,6E,10E)-geranylgeranyl diphosphate + H(+) + NADPH = all-trans-lycopaoctaene + 2 diphosphate + NADP(+); Xref=Rhea:RHEA:58176, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58756, ChEBI:CHEBI:142538; EC=2.5.1.148; Evidence={ECO:0000269|PubMed:27050299};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P37268};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.07 mM for geranylgeranyl diphosphate {ECO:0000269|PubMed:27050299}; KM=0.13 mM for farnesyl diphosphate {ECO:0000269|PubMed:27050299}; KM=0.11 mM for phytil diphosphate {ECO:0000269|PubMed:27050299};

Magnesium;Membrane;Metal-binding;NAD;NADP;Transferase;Transmembrane;Transmembrane helix

cholesterol biosynthetic process [GO:0006695]; ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate metabolic process [GO:0045338]; sterol biosynthetic process [GO:0016126]

endoplasmic reticulum membrane [GO:0005789]

farnesyl-diphosphate farnesyltransferase activity [GO:0004310]; farnesyltranstransferase activity [GO:0004311]; metal ion binding [GO:0046872]; squalene synthase activity [GO:0051996]

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

IPR008949;IPR002060;IPR006449;IPR019845;IPR044844;IPR033904;

1.10.600.10;

A0A143RHU3

MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVEQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKRQEEEMMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFPEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMLCGRLPFYNQDHEKLFELILMEELRFPRTLSPEAKSLLSGLLKKDPKQRLGGGAEDAKEIMQHRFFASIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQGDSVEGEDSERRPHFPQFSYSASGTA

Felis catus (Cat) (Felis silvestris catus)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};

ATP-binding;Carbohydrate metabolism;Glucose metabolism;Glycogen biosynthesis;Kinase;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Sugar transport;Transferase;Transport

activation-induced cell death of T cells [GO:0006924]; apoptotic mitochondrial changes [GO:0008637]; behavioral response to pain [GO:0048266]; canonical NF-kappaB signal transduction [GO:0007249]; cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to cadmium ion [GO:0071276]; cellular response to decreased oxygen levels [GO:0036294]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to oxidised low-density lipoprotein particle stimulus [GO:0140052]; cellular response to prostaglandin E stimulus [GO:0071380]; cellular response to reactive oxygen species [GO:0034614]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; epidermal growth factor receptor signaling pathway [GO:0007173]; establishment of protein localization to mitochondrion [GO:0072655]; execution phase of apoptosis [GO:0097194]; gene expression [GO:0010467]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; glycogen cell differentiation involved in embryonic placenta development [GO:0060709]; inflammatory response [GO:0006954]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; interleukin-18-mediated signaling pathway [GO:0035655]; intracellular signal transduction [GO:0035556]; labyrinthine layer blood vessel development [GO:0060716]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; maintenance of protein location in mitochondrion [GO:0072656]; mammalian oogenesis stage [GO:0022605]; maternal placenta development [GO:0001893]; negative regulation of autophagy [GO:0010507]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; negative regulation of cilium assembly [GO:1902018]; negative regulation of fatty acid beta-oxidation [GO:0031999]; negative regulation of gene expression [GO:0010629]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of leukocyte cell-cell adhesion [GO:1903038]; negative regulation of long-chain fatty acid import across plasma membrane [GO:0010748]; negative regulation of lymphocyte migration [GO:2000402]; negative regulation of protein localization to lysosome [GO:0150033]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of proteolysis [GO:0045861]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; non-canonical NF-kappaB signal transduction [GO:0038061]; osteoblast differentiation [GO:0001649]; peripheral nervous system myelin maintenance [GO:0032287]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphorylation [GO:0016310]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell growth [GO:0030307]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of I-kappaB phosphorylation [GO:1903721]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of organ growth [GO:0046622]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of protein localization to endoplasmic reticulum [GO:1905552]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of sodium ion transport [GO:0010765]; positive regulation of TORC1 signaling [GO:1904263]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein import into nucleus [GO:0006606]; protein ubiquitination [GO:0016567]; regulation of myelination [GO:0031641]; regulation of neuron projection development [GO:0010975]; regulation of postsynapse organization [GO:0099175]; regulation of tRNA methylation [GO:0110002]; response to fluid shear stress [GO:0034405]; response to food [GO:0032094]; response to heat [GO:0009408]; response to UV-A [GO:0070141]; sphingosine-1-phosphate receptor signaling pathway [GO:0003376]; striated muscle cell differentiation [GO:0051146]

cell-cell junction [GO:0005911]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; spindle [GO:0005819]; vesicle [GO:0031982]

14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; nitric-oxide synthase regulator activity [GO:0030235]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; potassium channel activator activity [GO:0099104]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]

IPR000961;IPR034676;IPR011009;IPR011993;IPR001849;IPR039026;IPR017892;IPR000719;IPR017441;IPR008271;

2.30.29.30;1.10.510.10;

A0A143ZZK9

MSSQNNNKQGGQDINNKKDSDDIKPSVSKEDLINSLKNDELNKNTTMDQNDMKKNENMNIKKNEVLNNSNNVEDGDNENSKFMNKSKEGLNNINGEKNDDNNSIVKVEESPKSIGYNYYASESIENLCKEFGLESINTGLNSEQVKINRDKYGENFIEKDEVVPVWLIFLSQYCSPVVLLLLVAAVASLALNEVVEGVAIISIVTLNACLATYMEKSSGDAIGKLAEMASPQCTVLRNGQKVVIPSREVVVGDVVLINTGDSISADLRLFDVIELKTNESLLTGESEDIKKTIVADNLSTPFATNLCFATTSVTSGSGKGIVISTGLDTQVGKIASQLKKSSKGSKLTPLQVALNKLGGLIGLIAIIVLVVIISLAVIIKYRDPAHADKDPTFVIIIIGVGFAVSSIPEGLPMVVTITLSAGAKDMVKKNANVRKLPAVETLGCCSVICSDKTGTLTEGKMTAINAVTICKNSSLSDENNKLTKTFDFYPTKGFEPCGGLFDSNELTSEKKKEIVIAKNQNTSYDKVLYNYGNPSNKSVIVDKTRSLMFAAYLNSYDTTLSRDPKTLKWGIHGNMSEGPIVVAAAKVGYSFINNPNHKSYLDNFQRLDDLEVTFNSSRKMKITFYKLKTVNVFENVYLDKPGKVYTHVALIKGAPDRLLDRSTHLLEETSMKKVQVSWNSTITQEERNVLIKKNLELSQKALRVLSICIKPLTDQNIEELKKLEDADERLKYVNYDENGGFIPMGYVASFDPPRPGVKEAIQTCREAQVKVIMITGDQKPTAVAIGKLIGLIEEKSEQVEDINSLAIECSELHINKNPNEPILPNDQLDEFTDKILIYSRAQPEDKITIVQSLKRKGYLVAMTGDGVNDAPALKAADIGVAMGINGTEVAKGASEMILIDDNFCTVVSAIDVGRTIFSNIQKFVCFLLGTNIGEIIYLSVAIVAQMPFPLEALQILFLNLMTDGCPAVALSREPPNDDNMKTPPRPKKQPIMTKRWWFYGILPHTIFEALCVLLSLAFSLYICTGFYNLNGIHNLCKTVNLVDVNDANVYHEYKYFCSSYEYRISTDYVGWVTNVSFWDPQNNEAVNFWGAAKGKVENINPLSDIVHPELRLRMQDGCSGDLTLDENGWCRPKDNKTSDGYNDELEGILKKGFEDVTAKGSKRGRTMAFISAVWCEMLRAYTVRSWEPFYKVFNRNMWMHLACSISATLTFLSTCIPGITSILNTTCLLWWQYLLAIFWALLNLFLDEIVPKVIYRRKYMTIKN

Plasmodium falciparum (isolate 3D7)

FUNCTION: Sodium-exporting ATPase (PubMed:23414762, PubMed:29986883, PubMed:31311978, PubMed:36180431). Required for the extrusion of Na(+) from the intraerythrocytic parasites to maintain a low cytosolic concentration of Na(+) (PubMed:23414762, PubMed:25322084, PubMed:25453091, PubMed:29555632, PubMed:36180431). {ECO:0000269|PubMed:23414762, ECO:0000269|PubMed:25322084, ECO:0000269|PubMed:25453091, ECO:0000269|PubMed:29555632, ECO:0000269|PubMed:29986883, ECO:0000269|PubMed:31311978, ECO:0000269|PubMed:36180431}.

7.2.2.3

CATALYTIC ACTIVITY: Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.3; Evidence={ECO:0000269|PubMed:23414762, ECO:0000269|PubMed:29986883, ECO:0000269|PubMed:31311978, ECO:0000269|PubMed:36180431}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634; Evidence={ECO:0000305};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for ATP (in the presence of 150-153 mM of Na(+)) {ECO:0000269|PubMed:29986883}; KM=16.1 mM for Na(+) {ECO:0000269|PubMed:29986883};

ATP-binding;Cell membrane;Hydrolase;Ion transport;Membrane;Nucleotide-binding;Reference proteome;Sodium;Sodium transport;Translocase;Transmembrane;Transmembrane helix;Transport

calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; manganese ion transport [GO:0006828]

endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]

ABC-type sodium transporter activity [GO:0140679]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type calcium transporter activity [GO:0005388]; P-type sodium transporter activity [GO:0008554]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20813948, ECO:0000269|PubMed:23414762, ECO:0000269|PubMed:29986883, ECO:0000269|PubMed:8813672}; Multi-pass membrane protein {ECO:0000255}.

IPR006068;IPR004014;IPR023299;IPR018303;IPR023298;IPR008250;IPR036412;IPR023214;IPR001757;IPR044492;

3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;

A0A144A134

MKNLDINTFDNIEDIPLGSSEQDPYDFFTLSDRNVMNSDMKKNIVQWNSRYSYNQLKNKDSLIMFLVEIFRSLFVSNCIDKNIDNVLLSIEEMFIDHYYNPQHSRLKYLIDDVGIFFTKLPITKAFHTYNKKYRITKRLYAPPTFNEVRHILNLAQILSLEEGLDLLTFDADETLYPDGHDFNDEVLASYISCLLKKMNIAIVTAASYNNDAEKYQKRLENLLKYFSKHNIKDGSYKNFYVMGGESNYLFKCNEEATLYSVPENEWRHYKKFVDYDTVQEILNISEKCLEKVIKDFGLCAQIQRKEKSIGLVPNKIPSLNIKNEQKNYMIKYEVLEEAVIRIKKEIIKNKITAPYCAFNGGQDLWVDVGNKAEGLLILQKLLKIQKKKCCHIGDQFLHSGNDFPTRFCSLTLWVSNPQETKACLKSIMHLNIKSFIPEVLYENQ

Plasmodium falciparum (isolate 3D7)

FUNCTION: Specifically, catalyzes the dephosphorylation of inosine monophosphate (IMP) into inosine (PubMed:32591529). By dephosphorylating IMP, plays a role in the purine salvage pathway (PubMed:32591529). Does not have phosphotransferase activity with IMP as phosphate donor and adenosine as phosphate acceptor (PubMed:32591529). {ECO:0000269|PubMed:32591529}.

3.1.3.99

CATALYTIC ACTIVITY: Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence={ECO:0000269|PubMed:32591529};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32591529};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 mM for IMP (at pH 5, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=66 mM for IMP (at pH 8, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=6.8 mM for IMP (at pH 8, 25 degrees Celsius and in the presence of ATP) {ECO:0000269|PubMed:32591529}; KM=105.5 mM for AMP (at pH 5, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=72.2 mM for AMP (at pH 8, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=71.7 mM for AMP (at pH 8, 25 degrees Celsius and in presence of ATP) {ECO:0000269|PubMed:32591529}; Note=kcat is 10.3 sec(-1) with IMP as substrate (at pH 5, 25 degrees Celsius and in the absence of ATP) (PubMed:32591529). kcat is 13.5 sec(-1) with IMP as substrate (at pH 8, 25 degrees Celsius and in the absence of ATP) (PubMed:32591529). kcat is 21 sec(-1) with IMP as substrate (at pH 8, 25 degrees Celsius and in the presence of ATP) (PubMed:32591529). kcat is 23.2 sec(-1) with AMP as substrate (at pH 5, 25 degrees Celsius and in the absence of ATP) (PubMed:32591529). kcat is 12.5 sec(-1) with AMP as substrate (at pH 8, 25 degrees Celsius and in the absence of ATP) (PubMed:32591529). kcat is 19.4 sec(-1) with AMP as substrate (at pH 8, 25 degrees Celsius and in the presence of ATP) (PubMed:32591529). {ECO:0000269|PubMed:32591529};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-5. {ECO:0000269|PubMed:32591529};

3D-structure;Allosteric enzyme;ATP-binding;Cytoplasm;Hydrolase;Magnesium;Metal-binding;Nucleotide metabolism;Nucleotide-binding;Reference proteome

IMP catabolic process [GO:0006204]; inosine salvage [GO:0006190]; nicotinamide riboside biosynthetic process [GO:0071590]; nicotinic acid riboside biosynthetic process [GO:0071592]

cytoplasm [GO:0005737]

ATP binding [GO:0005524]; IMP 5'-nucleotidase activity [GO:0050483]; magnesium ion binding [GO:0000287]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32591529}.

IPR036412;IPR023214;IPR009453;

3.40.50.1000;

A0A144A2H0

MQLNFLLFVFIFLMVFHLNIFNKGKRQNLVSAYLNHFKKSYFSGVTSGSDCVNKSEVSSDNNNNNNNNNNKIAHNFFSKKYQRNFENNNLSENQENNKNIIYSGSNIFKNIYNTEMMSNNNTVDVNMMDNNPAARLEELRTIMKKNKIDVYILINSDEHNSEIINEKDKKIVKITNYSGADGILIVTKDKPILYVNALYELQAMNELDQNLFTLRISRIDNRDEIFETISSLEFNTIAFDGKNTSVVFYEKLRKALLNAYPKKKIVEKIIYNNNFDDVNKKDDENVLNFLVLEKSLVEIKDYPVNNKTLYIHDRKYNGACAGEKIDKLKQSLMYDIKNVDNLLLSELDEIAYLLNLRGYDYQYSPLFYSYLLFQFDREEQDFSKIVFFTTVKNLPADVKNLLEINKVIVKEYEEIVPYLRDVVIPSIPKHNDDNPDFKKYDISLSPYINLMIYKLFDRKNVLLQNSPVVKMKAVKNDVEIDNMKQAHILDGLALLQFFHWCEQKRKTKELFNETEMSLRHKVDYFRSTKKNFIFPSFSTISASGPNAAVIHYECTDKTNATIKPAIYLLDSGGQYLHGTTDVTRTTHFGEPTAEEKRIYTLVLKGHLRLRKVIFASYTNSSALDFIARENLFNNFMDYNHGTGHGVGLTLNVHEGGCSIGPVGGAPLKKNMVLSNEPGYYMKDKFGVRIENMQYVISKEITDTTEYLSFDDLTMYPYEKKLLDFSLLTNQEIKELNEYHTTIRNTLLPLVKQSPQEYGESVEKYLIEITEPIAIHNN

Plasmodium falciparum (isolate 3D7)

FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides (PubMed:17895246, PubMed:19574214, PubMed:27462122). In the food vacuole, involved in the final step of host hemoglobin catabolism, by cleaving hemoglobin-derived oligopeptides (PubMed:17895246, PubMed:19574214). In the cytoplasm, may be involved in the last steps of the turnover of ubiquitinated proteins (Probable). {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214, ECO:0000269|PubMed:27462122, ECO:0000305|PubMed:19574214}.

3.4.11.9

CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214, ECO:0000269|PubMed:27462122};

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19574214}; Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000269|PubMed:27462122};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.51 mM for human hemoglobin peptide HbPep1 (FPHFD) (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; KM=0.86 mM for human hemoglobin peptide HbPep1 (FPHFD) (at pH 5.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; KM=1.4 mM for human hemoglobin peptide HbPep2 (YPWTQ) (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; KM=1.8 mM for human hemoglobin peptide HbPep2 (YPWTQ) (at pH 5.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; Note=kcat is 8.6 sec(-1) with for human hemoglobin peptide HbPep1 (FPHFD) as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:19574214). kcat is 5.4 sec(-1) with for human hemoglobin peptide HbPep1 (FPHFD) as substrate (at pH 5.5 and 37 degrees Celsius) (PubMed:19574214). kcat is 1500 sec(-1) with for human hemoglobin peptide HbPep2 (YPWTQ) as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:19574214). kcat is 12 sec(-1) with for human hemoglobin peptide HbPep2 (YPWTQ) as substrate (at pH 5.5 and 37 degrees Celsius) (PubMed:19574214). {ECO:0000269|PubMed:19574214};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 (PubMed:19574214). Active at pH 5.5-7.5 (PubMed:19574214). {ECO:0000269|PubMed:19574214};

3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome;Signal;Vacuole

hemoglobin catabolic process [GO:0042540]; proteolysis [GO:0006508]

cytoplasm [GO:0005737]; food vacuole [GO:0020020]; vacuolar lumen [GO:0005775]

manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]

SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}. Cytoplasm {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}. Note=Localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}.

PTM: The N-terminus may be proteolytically cleaved to generate a 73-kDa mature form. {ECO:0000269|PubMed:19574214}.

IPR029149;IPR036005;IPR000587;IPR000994;IPR033740;IPR032416;IPR001131;

3.90.230.10;3.40.350.10;

A0A163UT06

MNIKHNYISYFQMNGIQIPGISNPEAIIPITGEKKSYKLVLDFNDGAISIIEARYLDSKLHREIQDLSDNDVTILGTEISDGAYDENLDIHCDKCNKFYRPYCRLHPLFKIPDRVLKRDESSNLSFSQQTLPILFRIEESKLPNAGLGVIAEVFIPVGMVFGPYKGRRCQKKTDFYKDGYAWLIKSGDKRFYIDGSDAERSNWLRYINSPRFEDEQNMLAFQTNGKIFYRVIKPIRINQELLVWYGSSYGNEFVESENGNKYKKPAKNPFICVGAQR

Caenorhabditis elegans

FUNCTION: Histone methyltransferase that specifically mono- and di-methylates 'Lys-4' of histone H3 in vitro (PubMed:24685137). Does not tri-methylate 'Lys-4' of histone H3 in vitro (PubMed:24685137). Promotes spermatid development and fertility by positively regulating the transcription of spermatocyte-specific genes in primary spermatocytes (PubMed:29702639). Together with spr-5, required for transgenerational fertility (PubMed:24685137). {ECO:0000269|PubMed:24685137, ECO:0000269|PubMed:29702639}.

2.1.1.-; 2.1.1.364

CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:24685137}; CATALYTIC ACTIVITY: Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364; Evidence={ECO:0000269|PubMed:24685137};

Alternative splicing;Methyltransferase;Nucleus;Reference proteome;S-adenosyl-L-methionine;Transferase

methylation [GO:0032259]; oligodendrocyte development [GO:0014003]; regulation of DNA-templated transcription [GO:0006355]

nucleus [GO:0005634]

histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 monomethyltransferase activity [GO:0140945]

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29702639}. Note=In males and hermaphrodites, localizes to foci in the nucleus of spermatocytes, which express the mono- and di-methyl states of 'Lys-4' of histone H3 (PubMed:29702639). These foci are stable nuclear structures with slow diffusion and liquid-like properties (PubMed:29702639). In turn, these foci co-localize with the transcription start sites for major sperm proteins (PubMed:29702639). {ECO:0000269|PubMed:29702639}.

IPR044417;IPR001214;IPR046341;

2.170.270.10;

A0A166U5H3

MAGMKTSPSQDEEACVLAIQLATSTVLPMILKSAIELDILNTISKAGPGNYLSPSDLASKLLMSNPHAPIMLERILRVLATYKVLGCKPSELSDGEVEWLYCWTPVCKFLSNNEDGASIAPLLLVHQDQVPMKSWYHLTDAILDGGTAFNKAYGMNIFDYASQDPQFNKVFNRSMAGHSTITMKKILETYNGFEGLKSIVDVGGGSGATLNMIISKYPTIKGINFDLPHVVGDSPIHPGVEHVGGDMFASVPKGDAIFLKWIFHSWSDEDCLRILKNCYEALADNKKVIVAEFIIPEVPGGSDDATKSVVHLDAVMLAYVPGGKERTEKEFEALATSAGFKSFRKVCCAFNTWIMEFSK

Kitagawia praeruptora (Peucedanum praeruptorum)

FUNCTION: O-methyltransferase involved in the biosynthesis of furocoumarins natural products such as bergapten, a photosensitizer used for medical purpose such as treating psoriasis and vitiligo or facilitating resistance to microbial infection and other stresses (PubMed:27252733, PubMed:30934718, PubMed:31666994). Catalyzes specifically the methylation of bergaptol (PubMed:27252733, PubMed:30934718, PubMed:31666994). Not active on xanthotol, isoscopoletin, scopoletin and esculetin (PubMed:27252733, PubMed:30934718). {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.

2.1.1.69

CATALYTIC ACTIVITY: Reaction=bergaptol + S-adenosyl-L-methionine = bergapten + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11808, ChEBI:CHEBI:18293, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77728; EC=2.1.1.69; Evidence={ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11809; Evidence={ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994};

PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.; PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.

3D-structure;Cytoplasm;Methyltransferase;S-adenosyl-L-methionine;Transferase

aromatic compound biosynthetic process [GO:0019438]; coumarin biosynthetic process [GO:0009805]; methylation [GO:0032259]; response to jasmonic acid [GO:0009753]

cytoplasm [GO:0005737]

5-hydroxyfuranocoumarin 5-O-methyltransferase activity [GO:0030752]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27252733}.

IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;

3.40.50.150;1.10.10.10;

A0A172J1V3

MTENNRAGAVPLSSILLQMITGYWVTQSLYVAAKLGIADLVADAPKPIEELAAKTGAKAPLLKRVLRTIASIGVFTETEPGIFGITPLAALLRSGTPDSMRPQAIMHGEEQYRAWADVLHNVQTGETAFEKEFGTSYFGYLAKHPEADRVFNEAQAGYTKQVAHAVVDAYDFSPFKTVIDIGAGYGPLLSAILRSQPEARGILFDQPHVAQAAGKRLAEAGVGDRCGTVGGDFFVEVPADGDVYILSLLLHDWDDQRSIEILRNCRRAMPAHGKLLIVELVLPEGEEPFFGKWLDLHMLVLLGAQERTADEFKTLFAASGFALERVLPTASGLSIVEARPI

Lysobacter antibioticus

FUNCTION: Involved in the biosynthesis of phenazine natural products including myxin, an N(5),N(10)-dioxide phenazine antiobiotic, which has antimicrobial activity. O-methyltransferase, which converts iodinin (1,6-dihydroxyphenazine N(5),N(10)-dioxide) to myxin (1-hydroxy-6-methoxyphenazine N(5),N(10)-dioxide). Catalyzes both monomethoxy and dimethoxy formation of phenazine natural compounds. Acts on a wide variety of substrates, catalyzing O-methylation of phenazines with non-, mono- or di-N-oxide. Highest activity with 1,6-dihydroxyphenazine (DHP) as substrate. Less active with monohydroxy-containing and monohydroxy-monomethoxy-containing phenazines. Least active with non-phenazine substrates, such as 8-hydroxyquinoline and 6-hydroxyquinoline. Is not able to convert 1-hydroxyphenazine to 1-hydroxy-N5-methylphenazine (pyocyanine), hence does not function as an N-methyltransferase. {ECO:0000269|PubMed:29510028}.

2.1.1.-

CATALYTIC ACTIVITY: Reaction=1,6-dihydroxyphenazine + S-adenosyl-L-methionine = 1-hydroxy-6-methoxyphenazine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72523, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192365, ChEBI:CHEBI:192366; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72524; Evidence={ECO:0000269|PubMed:29510028}; CATALYTIC ACTIVITY: Reaction=1-hydroxy-6-methoxyphenazine + S-adenosyl-L-methionine = 1,6-dimethoxyphenazine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72527, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192366, ChEBI:CHEBI:192367; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72528; Evidence={ECO:0000269|PubMed:29510028}; CATALYTIC ACTIVITY: Reaction=1-hydroxy-6-methoxyphenazine N(10)-oxide + S-adenosyl-L-methionine = 1,6-dimethoxyphenazine N(5)-oxide + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72635, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192368, ChEBI:CHEBI:192369; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72636; Evidence={ECO:0000269|PubMed:29510028}; CATALYTIC ACTIVITY: Reaction=1,6-dihydroxyphenazine N(5),N(10)-dioxide + S-adenosyl-L-methionine = 1-hydroxy-6-methoxyphenazine N(5),N(10)-dioxide + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72639, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192372, ChEBI:CHEBI:192373; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72640; Evidence={ECO:0000269|PubMed:29510028}; CATALYTIC ACTIVITY: Reaction=1-hydroxy-6-methoxyphenazine N(5),N(10)-dioxide + S-adenosyl-L-methionine = 1,6-dimethoxyphenazine N(5),N(10)-dioxide + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72643, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192373, ChEBI:CHEBI:192374; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72644; Evidence={ECO:0000269|PubMed:29510028};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33.6 uM for 6-hydroxy-1-methoxyphenazine N(5)-oxide (at pH 7.8 and at room temperature) {ECO:0000269|PubMed:29510028}; Vmax=2.9 umol/min/mg enzyme with 6-hydroxy-1-methoxyphenazine N(5)-oxide as substrate (at pH 7.8 and at room temperature) {ECO:0000269|PubMed:29510028}; Note=kcat is 0.6 min(-1) with 6-hydroxy-1-methoxyphenazine N(5)-oxide as substrate. {ECO:0000269|PubMed:29510028};

3D-structure;Methyltransferase;S-adenosyl-L-methionine;Transferase

methylation [GO:0032259]; phenazine biosynthetic process [GO:0002047]

identical protein binding [GO:0042802]; O-methyltransferase activity [GO:0008171]; protein homodimerization activity [GO:0042803]; S-adenosyl-L-methionine binding [GO:1904047]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

DOMAIN: Contains an N-terminal dimerization domain. The C-terminal region contains the S-adenosyl-L-methionine binding site. {ECO:0000305|PubMed:29510028}.

IPR031725;IPR016461;IPR001077;IPR029063;IPR036388;IPR036390;

3.40.50.150;1.10.10.10;

A0A193AU77

MGSESLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNIGEEPSPIGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKEVIPRMIKKNEEQNRPVSCLINNPFIPWVSDVAESLGLPSAMLWVQSCACFAAYYHYYHGLVPFPSESAMEIDVQLPCMPLLKHDEVPSFLYPTTPYPFLRRAIMGQYKNLDKPFCVLMDTFQELEHEIIEYMSKICPIKTVGPLFKNPKAPNANVRGDFMKADDCISWLDSKPPASVVYVSFGSVVYLKQDQWDEIAFGLLNSGLNFLWVMKPPHKDSGYQLLTLPEGFLEKAGDKGKVVQWSPQEQVLAHPSVACFVTHCGWNSSMEALSSGMPVVAFPQWGDQVTDAKYLVDVFKVGVRMCRGEAENKLIMRDVVEKCLLEATVGPKAAEVKENALKWKAAAEAAVAEGGSSDRNIQAFVDEVKRRSIAIQSNKSEPKPVVQNAAVADHFGAKATTNGVAADLAGSNADGKVELVA

Punica granatum (Pomegranate)

FUNCTION: Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinnamic acid, sinapic acid, coumaric acid, caffeic acid and ferulic acid in vitro. Gallic acid is the predicted native substrate of the enzyme, which thus catalyzes the formation of 1-O-galloyl-beta-D-glucose, the first committed step of hydrolyzable tannins (HTs) biosynthesis, with punicalagin isomers being the major HTs of pomegranate. Catalyzes the formation of flavonoid glucosides with genistein, apigenin and luteolin in vitro. Has low activity with benzoic acid, 2-hydroxybenzoic acid, 3-hydroxybenzoic acid, 2,4-dihydroxybenzoic acid, naringenin and quercetin. No activity with catechol, resveratrol, chlorogenic acid, catechin and epicatechin (building blocks of proanthocyanidins) or cyanidin, delphinidin and pelargonidin (the three anthocyanidins). {ECO:0000269|PubMed:27227328}.

2.4.1.120; 2.4.1.136; 2.4.1.170; 2.4.1.177; 2.4.1.194; 2.4.1.81

CATALYTIC ACTIVITY: Reaction=3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-beta-D-glucose + UDP; Xref=Rhea:RHEA:15249, ChEBI:CHEBI:15834, ChEBI:CHEBI:16918, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=3,4-dihydroxybenzoate + UDP-alpha-D-glucose = 1-O-(3,4-dihydroxy-benzoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:52844, ChEBI:CHEBI:36241, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:136876; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=4-hydroxybenzoate + UDP-alpha-D-glucose = 4-(beta-D-glucosyloxy)benzoate + H(+) + UDP; Xref=Rhea:RHEA:15153, ChEBI:CHEBI:11935, ChEBI:CHEBI:15378, ChEBI:CHEBI:17879, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.194; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamate + UDP-alpha-D-glucose = 1-O-(trans-cinnamoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:13437, ChEBI:CHEBI:15669, ChEBI:CHEBI:16279, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.177; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-sinapate + UDP-alpha-D-glucose = 1-O-(trans-sinapoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:13305, ChEBI:CHEBI:16546, ChEBI:CHEBI:30023, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.120; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + UDP-alpha-D-glucose = 1-O-(trans-4-coumaroyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:57472, ChEBI:CHEBI:12876, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:71498; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-caffeate + UDP-alpha-D-glucose = 1-O-[(E)-caffeoyl]-beta-D-glucose + UDP; Xref=Rhea:RHEA:57464, ChEBI:CHEBI:614, ChEBI:CHEBI:57770, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-ferulate + UDP-alpha-D-glucose = 1-O-[(E)-feruloyl]-beta-D-glucose + UDP; Xref=Rhea:RHEA:57468, ChEBI:CHEBI:29749, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:81321; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=genistein + UDP-alpha-D-glucose = genistein 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:56056, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:74224, ChEBI:CHEBI:140305; EC=2.4.1.170; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=apigenin + UDP-alpha-D-glucose = apigenin 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:59760, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58470, ChEBI:CHEBI:58885, ChEBI:CHEBI:77722; EC=2.4.1.81; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=luteolin + UDP-alpha-D-glucose = H(+) + luteolin 7-O-beta-D-glucoside + UDP; Xref=Rhea:RHEA:19577, ChEBI:CHEBI:15378, ChEBI:CHEBI:57545, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:77791; EC=2.4.1.81; Evidence={ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.98 mM for gallic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.17 mM for 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=4.44 mM for 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.77 mM for caffeic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=0.86 mM for cinnamic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.06 mM for coumaric acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.32 mM for ferulic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=0.78 mM for sinapic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; Vmax=0.39 uM/sec/mg enzyme with gallic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.43 uM/sec/mg enzyme with 4-hydroxybenzoic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.96 uM/sec/mg enzyme with 3,4-dihydroxybenzoic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.63 uM/sec/mg enzyme with caffeic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.32 uM/sec/mg enzyme with cinnamic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.31 uM/sec/mg enzyme with coumaric acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.47 uM/sec/mg enzyme with ferulic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.31 uM/sec/mg enzyme with sinapic acid as substrate (at pH 5.0 and 30 degrees Celsius); Note=kcat is 0.55 sec(-1) with gallic acid as substrate. kcat is 0.6 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 1.35 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.89 sec(-1) with caffeic acid as substrate. kcat is 0.45 sec(-1) with cinnamic acid as substrate. kcat is 0.44 sec(-1) with coumaric acid as substrate. kcat is 0.66 sec(-1) with ferulic acid as substrate. kcat is 0.44 sec(-1) with sinapic acid as substrate. {ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity remains fairly constant between 20-55 degrees Celsius. Active even at 0 degrees Celsius. {ECO:0000269|PubMed:27227328};

Cytoplasm;Glycosyltransferase;Reference proteome;Transferase

3,4-dihydroxybenzoate metabolic process [GO:0046278]; cinnamic acid ester metabolic process [GO:0009801]; ferulate metabolic process [GO:0033494]

cytoplasm [GO:0005737]

4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity [GO:0047250]; cinnamate beta-D-glucosyltransferase activity [GO:0050412]; flavone 7-O-beta-glucosyltransferase activity [GO:0047891]; gallate 1-beta-glucosyltransferase activity [GO:0047913]; isoflavone 7-O-glucosyltransferase activity [GO:0050004]; quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044]; sinapate 1-glucosyltransferase activity [GO:0050284]; UDP-glucosyltransferase activity [GO:0035251]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27227328}.

IPR002213;IPR035595;

3.40.50.2000;

A0A193AUF6

MGSESSLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNISDQPAPVGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKVLIPQMIQKNAEQGRPVSCLINNPFIPWVSDVAETLGLPSAMLWVQSCACFLAYYHYYHGLVPFPSENAMEIDVQLPSMPLLKHDEVPSFLYPTTPYPFLRRAILGQYKNLEKPFCILMDTFQELEHEIIEYTSKICPIKTVGPLFKNPKAPNTTVKGDFMKADDCIGWLDSKPASSVVYVSFGSVVYLKQDQWDEIAYGLLNSGVNFLWVMKPPHKDSGYTVLTLPEGFLEKAGDRGKVVQWSPQEQVLAHPATACFVTHCGWNSSMEALTSGMPVVAFPQWGDQVTDAKYLVDEFKVGVRMCRGEAEDKLITRDVVEQCLREATQGPKAAEMKKNALKWKAAAEASFVEGGSSDRNLQAFVDEVKRRSIEITASKPAVKAAPNGVVAAAESVVETKANGKVELAA

Punica granatum (Pomegranate)

FUNCTION: Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinnamic acid, sinapic acid, coumaric acid, caffeic acid and ferulic acid in vitro. Gallic acid is the predicted native substrate of the enzyme, which thus catalyzes the formation of 1-O-galloyl-beta-D-glucose, the first committed step of hydrolyzable tannins (HTs) biosynthesis, with punicalagin isomers being the major HTs of pomegranate. Catalyzes the formation of flavonoid glucosides with genistein, apigenin and luteolin in vitro. Has low activity with benzoic acid, 2-hydroxybenzoic acid, 3-hydroxybenzoic acid, 2,4-dihydroxybenzoic acid, naringenin and quercetin. No activity with catechol, resveratrol, chlorogenic acid, catechin and epicatechin (building blocks of proanthocyanidins) or cyanidin, delphinidin and pelargonidin (the three anthocyanidins). {ECO:0000269|PubMed:27227328}.

2.4.1.120; 2.4.1.136; 2.4.1.170; 2.4.1.177; 2.4.1.194; 2.4.1.81

CATALYTIC ACTIVITY: Reaction=3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-beta-D-glucose + UDP; Xref=Rhea:RHEA:15249, ChEBI:CHEBI:15834, ChEBI:CHEBI:16918, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=3,4-dihydroxybenzoate + UDP-alpha-D-glucose = 1-O-(3,4-dihydroxy-benzoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:52844, ChEBI:CHEBI:36241, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:136876; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=4-hydroxybenzoate + UDP-alpha-D-glucose = 4-(beta-D-glucosyloxy)benzoate + H(+) + UDP; Xref=Rhea:RHEA:15153, ChEBI:CHEBI:11935, ChEBI:CHEBI:15378, ChEBI:CHEBI:17879, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.194; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamate + UDP-alpha-D-glucose = 1-O-(trans-cinnamoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:13437, ChEBI:CHEBI:15669, ChEBI:CHEBI:16279, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.177; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-sinapate + UDP-alpha-D-glucose = 1-O-(trans-sinapoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:13305, ChEBI:CHEBI:16546, ChEBI:CHEBI:30023, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.120; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + UDP-alpha-D-glucose = 1-O-(trans-4-coumaroyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:57472, ChEBI:CHEBI:12876, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:71498; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-caffeate + UDP-alpha-D-glucose = 1-O-[(E)-caffeoyl]-beta-D-glucose + UDP; Xref=Rhea:RHEA:57464, ChEBI:CHEBI:614, ChEBI:CHEBI:57770, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-ferulate + UDP-alpha-D-glucose = 1-O-[(E)-feruloyl]-beta-D-glucose + UDP; Xref=Rhea:RHEA:57468, ChEBI:CHEBI:29749, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:81321; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=genistein + UDP-alpha-D-glucose = genistein 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:56056, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:74224, ChEBI:CHEBI:140305; EC=2.4.1.170; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=apigenin + UDP-alpha-D-glucose = apigenin 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:59760, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58470, ChEBI:CHEBI:58885, ChEBI:CHEBI:77722; EC=2.4.1.81; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=luteolin + UDP-alpha-D-glucose = H(+) + luteolin 7-O-beta-D-glucoside + UDP; Xref=Rhea:RHEA:19577, ChEBI:CHEBI:15378, ChEBI:CHEBI:57545, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:77791; EC=2.4.1.81; Evidence={ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.89 mM for gallic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.19 mM for 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=2.46 mM for 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.06 mM for caffeic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.12 mM for cinnamic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=0.94 mM for coumaric acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.58 mM for ferulic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=0.86 mM for sinapic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; Vmax=0.37 uM/sec/mg enzyme with gallic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.43 uM/sec/mg enzyme with 4-hydroxybenzoic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.54 uM/sec/mg enzyme with 3,4-dihydroxybenzoic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.45 uM/sec/mg enzyme with caffeic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.4 uM/sec/mg enzyme with cinnamic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.37 uM/sec/mg enzyme with coumaric acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.52 uM/sec/mg enzyme with ferulic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.35 uM/sec/mg enzyme with sinapic acid as substrate (at pH 5.0 and 30 degrees Celsius); Note=kcat is 0.52 sec(-1) with gallic acid as substrate. kcat is 0.61 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 0.76 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.64 sec(-1) with caffeic acid as substrate. kcat is 0.56 sec(-1) with cinnamic acid as substrate. kcat is 0.52 sec(-1) with coumaric acid as substrate. kcat is 0.72 sec(-1) with ferulic acid as substrate. kcat is 0.5 sec(-1) with sinapic acid as substrate. {ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity remains fairly constant between 20-55 degrees Celsius. Active even at 0 degrees Celsius. {ECO:0000269|PubMed:27227328};

Cytoplasm;Glycosyltransferase;Reference proteome;Transferase

3,4-dihydroxybenzoate metabolic process [GO:0046278]; cinnamic acid ester metabolic process [GO:0009801]; ferulate metabolic process [GO:0033494]

cytoplasm [GO:0005737]

4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity [GO:0047250]; cinnamate beta-D-glucosyltransferase activity [GO:0050412]; flavone 7-O-beta-glucosyltransferase activity [GO:0047891]; gallate 1-beta-glucosyltransferase activity [GO:0047913]; isoflavone 7-O-glucosyltransferase activity [GO:0050004]; quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044]; sinapate 1-glucosyltransferase activity [GO:0050284]; UDP-glucosyltransferase activity [GO:0035251]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27227328}.

IPR002213;IPR035595;

3.40.50.2000;

A0A193KX02

MVSPAIALAFLPLLLTLIIRYRYYFVLLYRAVLTRWVRDCLSGISREERAFQYILTHATPGDSQSILDTFDTWCSKVEFISNIGPKKGKILDRLLQENCPITVLELGTHCGYSTVRMARSLPIGARIYSVEMDQRNAQVAEKIIRLAGFDDDMVELIQRPSDEVIPRLREDLGVERLDLVLMDHWKRCYLPDLHLLEDSGLIGQGSIILADNVIFPGAPNFLRYARRCGLYEVRVHRATLEYMRGIPDGMAELTYIGIK

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (By similarity). Required for auditory function. Component of the hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity (PubMed:28534737). {ECO:0000250|UniProtKB:P21964, ECO:0000269|PubMed:28534737}.

2.1.1.6

CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000250|UniProtKB:P21964};

Catecholamine metabolism;Cell membrane;Deafness;Endoplasmic reticulum;Golgi apparatus;Hearing;Membrane;Methyltransferase;Neurotransmitter degradation;Reference proteome;S-adenosyl-L-methionine;Transferase

auditory behavior [GO:0031223]; catecholamine catabolic process [GO:0042424]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; developmental process [GO:0032502]; dopamine metabolic process [GO:0042417]; endocytosis [GO:0006897]; hair cell differentiation [GO:0035315]; inner ear receptor cell stereocilium organization [GO:0060122]; methylation [GO:0032259]; neuromast development [GO:0048884]; sensory perception of sound [GO:0007605]

basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]

catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; orcinol O-methyltransferase activity [GO:0102938]

SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:28534737}. Golgi apparatus {ECO:0000269|PubMed:28534737}. Basolateral cell membrane {ECO:0000269|PubMed:28534737}. Note=Enriched in an apical membrane compartment above the nucleus in the hair cells. Not detectable in the hair bundle. May be present at lower levels in the endoplasmic reticulum and the basolateral membrane. {ECO:0000269|PubMed:28534737}.

IPR029063;IPR002935;

3.40.50.150;

A0A1B0GTW7

MLLLLLLLLLLPPLVLRVAASRCLHDETQKSVSLLRPPFSQLPSKSRSSSLTLPSSRDPQPLRIQSCYLGDHISDGAWDPEGEGMRGGSRALAAVREATQRIQAVLAVQGPLLLSRDPAQYCHAVWGDPDSPNYHRCSLLNPGYKGESCLGAKIPDTHLRGYALWPEQGPPQLVQPDGPGVQNTDFLLYVRVAHTSKCHQETVSLCCPGWSTAAQSQLTAALTSWAQRRGFVMLPRLCLKLLGSSNLPTLASQSIRITGPSVIAYAACCQLDSEDRPLAGTIVYCAQHLTSPSLSHSDIVMATLHELLHALGFSGQLFKKWRDCPSGFSVRENCSTRQLVTRQDEWGQLLLTTPAVSLSLAKHLGVSGASLGVPLEEEEGLLSSHWEARLLQGSLMTATFDGAQRTRLDPITLAAFKDSGWYQVNHSAAEELLWGQGSGPEFGLVTTCGTGSSDFFCTGSGLGCHYLHLDKGSCSSDPMLEGCRMYKPLANGSECWKKENGFPAGVDNPHGEIYHPQSRCFFANLTSQLLPGDKPRHPSLTPHLKEAELMGRCYLHQCTGRGAYKVQVEGSPWVPCLPGKVIQIPGYYGLLFCPRGRLCQTNEDINAVTSPPVSLSTPDPLFQLSLELAGPPGHSLGKEQQEGLAEAVLEALASKGGTGRCYFHGPSITTSLVFTVHMWKSPGCQGPSVATLHKALTLTLQKKPLEVYHGGANFTTQPSKLLVTSDHNPSMTHLRLSMGLCLMLLILVGVMGTTAYQKRATLPVRPSASYHSPELHSTRVPVRGIREV

Homo sapiens (Human)

FUNCTION: Putative metalloproteinase that plays a role in left-right patterning process. {ECO:0000250|UniProtKB:A0A1D5NSK0}.

3.4.24.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08148}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148};

Alternative splicing;Disease variant;Glycoprotein;Heterotaxy;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc

cell adhesion [GO:0007155]; establishment of left/right asymmetry [GO:0061966]; proteolysis [GO:0006508]

cytoplasm [GO:0005737]; membrane [GO:0016020]

metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.

IPR001577;

3.10.170.20;3.90.132.10;

A0A1B0GWR2

MTATTRGSPVGGNDNQGQAPDGQSQPPLQQNQTSSPDSSNENSPATPPDEQGQGDAPPQIEDEEPAFPHTDLAKLDDMINRPRWVVPVLPKGELEVLLEAAIDLSKKGLDVKSEACQRFFRDGLTISFTKILTDEAVSGWKFEIHRCIINNTHRLVELCVAKLAQDWFPLLELLAMALNPHCKFHIYNGTRPCESVSSSVQLPEDELFARSPDPRSPKGWLVDLLNKFGTLNGFQILHDRFINGSALNVQIIAALIKPFGQCYEFLTLHTVKKYFLPIIEMVPQFLENLTDEELKKEAKNEAKNDALSMIIKSLKSLASRVPGQEETVKNLEIFRLKMILRLLQISSFNGKMNALNEVNKVISSVSYYTHRHGSSEEEEWLTAERMAEWIQQNNILSIVLRDSLHQPQYVEKLEKILRFVIKEKALTLQDLDNIWAAQAGKHEAIVKNVHDLLAKLAWDFSPEQLDHLFDCFKASWTNASKKQREKLLELIRRLAEDDKDGVMAHKVLNLLWNLAHSDDVPVDIMDLALSAHIKILDYSCSQDRDTQKIQWIDRFIEELRTNDKWVIPALKQIREICSLFGEAPQNLSQTQRSPHVFYRHDLINQLQHNHALVTLVAENLATYMESMRLYGRDNEDYDPQTVRVGSRYSHVQEVQERLNFLRFLLKDGQLWLCAPQAKQIWKCLAENAVYLCDREACFKWYSKLMGDEPDLDPDINKDFFESNVLQLDPSLLTENGMKCFERFFKAVNCREGKLVAKRRAYMMDDLELIGLDYLWRVVIQSNDDIASRAIDLLKEIYTNLGPRLQVNQVVIHEDFIQSCFDRLKASYDTLCVLDGDKDSINCARQEAVRMVRVLTVLREYINECDSDYHEERTILPMSRAFRGKHLSFIVRFPNQGRQVDDLEVWSHTNDTIGSVRRCILNRIKANVAHTKIELFVGGELIDPGDDRKLIGQLNLKDKSVITGAKYGDKILGRPFLKPRSNFSANYLFADLGSSLNMPPLRDGARVLMKLMPPDSTTIEKLRAICLDHAKLGESSLSPSLDSLFFGPSASQVLYLTEVVYALLMPAGAPLADDSSDFQFHFLKSGGLPLVLSMLTRNNFLPNADMETRRGAYLNALKIAKLLLTAIGYGHVRAVAEACQPGVEGVNPMTSVNQVTHDQAVVLQSALQSIPNPSSECMLRNVSVRLAQQISDEASRYMPDICVIRAIQKIIWTSGCGGLQLVFSPNEEVTKIYEKTNAGNEPDLEDEQVCCEALEVMTLCFALIPTALDALSKEKAWQTFIIDLLLHCHSKTVRQVAQEQFFLMCTRCCMGHRPLLFFITLLFTVLGSTARERAKHSGDYFTLLRHLLNYAYNSNINVPNAEVLLNNEIDWLKRIRDDVKRTGETGVEETILEGHLGVTKELLAFQTPEKKFHIGCEKGGANLIKELIDDFIFPASNVYLQYMRNGELPAEQAIPVCGSPATINAGFELLVALAVGCVRNLKQIVDSLTEMYYIGTALTEWEYLPPVGPRPPKGFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDEKQDNESNVDPRDDVFGYPQQFEDKPPLSKTEDRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVNPESQLIQQNEQSESEKAGSTKYRLVGVLVHSGQASGGHYYSYIIQRNGGDGEKNRWYKFDDGDVTECKMDDDEEMKNQCFGGEYMGEVFDHMMKRMSYRRQKRWWNAYILFYERMDTIDHDDEVIRYISEIAITTRPHQIVMPSAIERSVRKQNVQFMHNRMQYSLEYFQFMKKLLTCNGVYLNPPPGQDHLSPEAEEITMISIQLAARFLFTTGFHTKKIVRGSASDWYDALCILLRHSKNVRFWFAHNVLFNVSNRFSEYLLECPSAEVRGAFAKLIVFIAHFSLQDGPCPSPFASPGPSSQAYDNLSLSDHLLRAVLNLLRREVSEHGRHLQQYFNLFVMYANLGVAEKTQLLKLSVPATFMLVSLDEGPGPPIKYQYAELGKLYSVVSQLIRCCNVSSRMQSSINGNPSLPNPFGDPNLSQPIMPIQQNVVDILFVRTSYVKKIIEDCSNSDETVKLLRFCCWENPQFSSTVLSELLWQVAYSYTYELRPYLDLLLQILLIEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIKCMVALFSSCPVAYQILQGNGDLKRKWTWAVEWLGDELERRPYTGNPQYTYNNWSPPVQSNETSNGYFLERSHSARMTLAKACELCPEEEPDDQDAPDEHESPPPEDAPLYPHSPGSQYQQVNRSQMVGLTSTVALNLKPATL

Rattus norvegicus (Rat)

3.4.19.12

CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};

Hydrolase;Protease;Proteomics identification;Reference proteome;Thiol protease;Ubl conjugation pathway

axon extension [GO:0048675]; BMP signaling pathway [GO:0030509]; cell migration [GO:0016477]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cerebellar cortex structural organization [GO:0021698]; cilium assembly [GO:0060271]; cytosolic ciliogenesis [GO:0061824]; hippocampus development [GO:0021766]; in utero embryonic development [GO:0001701]; monoubiquitinated protein deubiquitination [GO:0035520]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; neuron migration [GO:0001764]; neuron projection extension [GO:1990138]; positive regulation of DNA demethylation [GO:1901537]; positive regulation of TORC2 signaling [GO:1904515]; post-embryonic development [GO:0009791]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]; regulation of circadian rhythm [GO:0042752]; transforming growth factor beta receptor signaling pathway [GO:0007179]

apical part of cell [GO:0045177]; centrosome [GO:0005813]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; growth cone [GO:0030426]; nucleus [GO:0005634]

co-SMAD binding [GO:0070410]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; deubiquitinase activity [GO:0101005]; K11-linked deubiquitinase activity [GO:0180017]; K48-linked deubiquitinase activity [GO:1990380]; K63-linked deubiquitinase activity [GO:0061578]; molecular sequestering activity [GO:0140313]; ubiquitin protein ligase binding [GO:0031625]

IPR016024;IPR021905;IPR038765;IPR001394;IPR018200;IPR028889;

3.90.70.10;

A0A1B1FHP3

MAGKSAEEEHPIKAYGWAVKDRTTGILSPFKFSRRATGDDDVRIKILYCGICHTDLASIKNEYEFLSYPLVPGMEIVGIATEVGKDVTKVKVGEKVALSAYLGCCGKCYSCVNELENYCPEVIIGYGTPYHDGTICYGGLSNETVANQSFVLRFPERLSPAGGAPLLSAGITSFSAMRNSGIDKPGLHVGVVGLGGLGHLAVKFAKAFGLKVTVISTTPSKKDDAINGLGADGFLLSRDDEQMKAAIGTLDAIIDTLAVVHPIAPLLDLLRSQGKFLLLGAPSQSLELPPIPLLSGGKSIIGSAAGNVKQTQEMLDFAAEHDITANVEIIPIEYINTAMERLDKGDVRYRFVVDIENTLTPPSEL

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Converts precondylocarpine acetate to dihydroprecondylocarpine acetate. {ECO:0000269|PubMed:29724909}.

1.1.1.-

CATALYTIC ACTIVITY: Reaction=dihydroprecondylocarpine acetate + NADP(+) = H(+) + NADPH + precondylocarpine acetate; Xref=Rhea:RHEA:58576, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142769, ChEBI:CHEBI:142770; Evidence={ECO:0000269|PubMed:29724909}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58578; Evidence={ECO:0000269|PubMed:29724909};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00327}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P00327};

PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29724909}.

3D-structure;Alkaloid metabolism;Cytoplasm;Glycoprotein;Metal-binding;NAD;Oxidoreductase;Zinc

alcohol metabolic process [GO:0006066]; alkaloid biosynthetic process [GO:0009821]; lignin biosynthetic process [GO:0009809]

cytosol [GO:0005829]

alcohol dehydrogenase (NADP+) activity [GO:0008106]; cinnamyl-alcohol dehydrogenase activity [GO:0045551]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}.

IPR013149;IPR013154;IPR047109;IPR011032;IPR036291;IPR020843;

3.90.180.10;3.40.50.720;

A0A1B1J8Z2

MIIKLLVALIHYLHETMAVQSIITTPLLVILMSLRSYAFTEPSLHRQQPPSKGGVRAAYWPAWSDFSTSSIDTNYFTHIYYAFVQPAPESFNLEITESYKKWAPKYDGIHNIRPRVTTLLSIGGGGNNATLFSEMASSKQNRASFINSTIHVARKHEFNGLDLDWEWPGDEKDMSNLALLLKEWYKALVVEANTSRKSRLLLTSAVYFNSTISLIGNGPRSYPVRAIRKYLDWASPMCFDYNGAWANETGFNAALYDPNSNISTKYGIGSWIGSGVPAEKLVMGLPLYGRAWELKDPNDHGVGAKAVGPAVDTDGSMDYDEILVFNKDTGAKVVYDEVAVSFYSYSGTTWIGYDDGPSITKKVQFARSMGLKGYFFWAIGKDKDWTISKQASNAWGY

Lotus japonicus (Lotus corniculatus var. japonicus)

FUNCTION: Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5 (PubMed:27383628). Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules (PubMed:27383628). Has the capacity to inhibit hyphal growth of the fungus Trichoderma viride in an agar-plate bioassay (PubMed:27383628). Involved in symbiotic signaling (PubMed:30284535). Required for root hair infection threads (ITs) elongation and nodule development (PubMed:30284535). Possesses Nod factor (NF) hydrolase activity (PubMed:30284535). NFs are lipo-chitooligosaccharide signaling molecules produced by nitrogen-fixing rhizobia to initiate nodulation (symbiosis) on the roots of legumes (PubMed:30284535). Modulates NF levels and signaling to complete transition of infected nodules to functional nitrogen-fixing organs (PubMed:30284535). {ECO:0000269|PubMed:27383628, ECO:0000269|PubMed:30284535}.

3.2.1.14

CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000269|PubMed:27383628};

PATHWAY: Glycan degradation; chitin degradation. {ECO:0000305}.

Carbohydrate metabolism;Chitin degradation;Glycoprotein;Glycosidase;Hydrolase;Nodulation;Plant defense;Polysaccharide degradation;Signal

chitin catabolic process [GO:0006032]; defense response to fungus [GO:0050832]; nodulation [GO:0009877]; polysaccharide catabolic process [GO:0000272]

extracellular region [GO:0005576]

chitin binding [GO:0008061]; chitinase activity [GO:0004568]

IPR011583;IPR029070;IPR001223;IPR001579;IPR017853;

3.10.50.10;3.20.20.80;

A0A1C7D1B7

MKKLSRTISGVTPVAVMTKPLPCPGKCIYCPTFAATPQSYTPESPAVLRAKSCEYQAYKQVALRLRIIQDMGHPTDKVELIIMGGTFLSADITYQYGFIKDCYDALNGVVAGSLEEAKTINETAQHRCVGLCIETRPDICGKAEIQRMIDFGTTRVELGVQMLDDDIYKLVERGHRVSDVAEATCLLREYGLKVHYHWMPGLPGSSPEKDLALSRMVFEDPRFCPDGLKLYPTMVVEGTILEQWWKEGRYTPYPNGTMTGLIADIKALVPPYVRISRVLRDIPAVFISAGLKDSLRDGVRQILESRHQKCRCIRCREYGHRQRKGQTSGEPTLRRLDYPASGGKEIFLSFEDASDTLYGLLRLRIPCASLPVLGQKYGAKTGLVRELHVYGTELSLGEQGDQSAQHRGLGRKLLAEAECLARDEFGLDSLAILSGVGAREYYRSLGYELVAGYMCKHLD

Dehalococcoides mccartyi (strain CBDB1)

FUNCTION: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:27455459). The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not show protein lysine acetyltransferase activity (By similarity). {ECO:0000250|UniProtKB:D5VRB9, ECO:0000269|PubMed:27455459}.

2.3.1.311

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407, Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74882; EC=2.3.1.311; Evidence={ECO:0000269|PubMed:27455459}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021; Evidence={ECO:0000269|PubMed:27455459};

COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:27455459}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q02908};

PATHWAY: tRNA modification. {ECO:0000269|PubMed:27455459}.

3D-structure;4Fe-4S;Acyltransferase;Iron;Iron-sulfur;Metal-binding;RNA-binding;S-adenosyl-L-methionine;Transferase;tRNA processing;tRNA-binding;Zinc

tRNA acetylation [GO:0051391]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble uridine modification [GO:0002098]

cytoplasm [GO:0005737]; elongator holoenzyme complex [GO:0033588]

4 iron, 4 sulfur cluster binding [GO:0051539]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; S-adenosyl-L-methionine binding [GO:1904047]; tRNA binding [GO:0000049]; tRNA uridine(34) acetyltransferase activity [GO:0106261]

IPR016181;IPR039661;IPR034687;IPR006638;IPR032432;IPR007197;

3.40.630.30;

A0A1D5NSK0

MSFLLCIGILLLPWFPCVCGKCIFDQIQRSVNVVSPPTAQYASAYRFKTQRSKRHIMPMDNLQPIRIKIWIPSESPALSDWEREKLMSAVGEAVSEVSSLLSVKRVKDRLLLNRDVNKYCKFIWRNSSTLNHMKCGRAHENYRFESCLGVIIPDEHLDGCSVYPNPEHPVPTVLRPRGPGVPDADFLLYVFTHNTEKCRAESSVLAYTAHCQTGSDGRPLAGTMVICRETLKKERYTYQHFVKVTTVIHELFHVLGFSKELLSNWKDFGVDCWSHGQVTSTDQTGQVRLYSPTVIRAMQKHFNSTHTDLGAPLENKDAALDGLSSHWEARVLQGSIMAASLVEASLVRIDAITLAALQDTGWYSVNHSRAQSLVWGEGEGSDFGSVSACHNSSAFFCTGSGLGCHFLHLNKGECVTDQYLDGCHIFKPLANASECWIEDNARSGMNEGGGEIFGSDSRCFISNITRLNNVTAYTPVSGHCYRHRCTGINKYHIQVKDSDWMDCPAGTSIEVSGYQGFIFCPENRLCKYSDLAPPTSTQRTESLFSDTTAQSDLGMMEKDAAVQPSFTSLFLVSEAKISLAAVLSLMAVFALLSAAVLLYRKNLSVRVHAASYRTPLPHILYRN

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: Plays an essential role for patterning the left-right axis. Requires solely on the left side, downstream of the leftward flow, but upstream of dand5, a nodal inhibitor involved in left-right patterning. {ECO:0000269|PubMed:34903892}.

3.4.24.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08148}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148};

Developmental protein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc

cell adhesion [GO:0007155]; determination of heart left/right asymmetry [GO:0061371]; establishment of left/right asymmetry [GO:0061966]; proteolysis [GO:0006508]

cytoplasm [GO:0005737]; membrane [GO:0016020]

metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.

IPR001577;

3.10.170.20;3.90.132.10;2.30.34.10;

A0A1D5NSP9

MVKAKVWILKKHFEGFPKESNFELKEVDLPELQDGDVLVEAIYFSLDPYMRSLSKMFLKEGDVQYGTQLAKVLKSKDPEFPEGCYVVADCGWRTHTVTKAKGPRGPILTRIVSEWPTDIPMSLALGSLGMPGLTALYGLEEVCKIQPGQTVLVSAAAGTVGTVVGQICKIKGCKVVGSAGGDDKVAYLKELGFDQAFNYKTVPSLEEALKNASPEGYDCYFESVGGPMFTAALKNMKPGGRIAVCGAIATYNDTTPQMCPYPHHEIIVRSLTIQGFMVTNYKEKDEESVKRLLTWMKEGKLKTKEMVTVGFDKLPIAFMKMLKGDGLGKAIVKV

Danio rerio (Zebrafish) (Brachydanio rerio)

1.3.1.48; 1.3.1.74

CATALYTIC ACTIVITY: Reaction=(5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51212, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133974, ChEBI:CHEBI:133975; Evidence={ECO:0000256|ARBA:ARBA00023498}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51213; Evidence={ECO:0000256|ARBA:ARBA00023498}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374, ChEBI:CHEBI:133409; Evidence={ECO:0000256|ARBA:ARBA00023548}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590; Evidence={ECO:0000256|ARBA:ARBA00023548}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584, ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133408; Evidence={ECO:0000256|ARBA:ARBA00023544}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586; Evidence={ECO:0000256|ARBA:ARBA00023544}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15-oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:79072, ChEBI:CHEBI:133411; Evidence={ECO:0000256|ARBA:ARBA00023543}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594; Evidence={ECO:0000256|ARBA:ARBA00023543}; CATALYTIC ACTIVITY: Reaction=20-hydroxy-leukotriene B4 + NADP(+) = 12-oxo-20-hydroxy-leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:51208, ChEBI:CHEBI:15378, ChEBI:CHEBI:57460, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133346; Evidence={ECO:0000256|ARBA:ARBA00023517}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51209; Evidence={ECO:0000256|ARBA:ARBA00023517}; CATALYTIC ACTIVITY: Reaction=4-hydroxynonanal + NADP(+) = (E)-4-hydroxynon-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:64736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58968, ChEBI:CHEBI:156112; Evidence={ECO:0000256|ARBA:ARBA00023553}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64738; Evidence={ECO:0000256|ARBA:ARBA00023553}; CATALYTIC ACTIVITY: Reaction=6-trans-leukotriene B4 + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51204, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:90723, ChEBI:CHEBI:133974; Evidence={ECO:0000256|ARBA:ARBA00023496}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51205; Evidence={ECO:0000256|ARBA:ARBA00023496}; CATALYTIC ACTIVITY: Reaction=NADP(+) + nonan-2-one = (3E)-nonen-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77927, ChEBI:CHEBI:133457; Evidence={ECO:0000256|ARBA:ARBA00023696}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50618; Evidence={ECO:0000256|ARBA:ARBA00023696}; CATALYTIC ACTIVITY: Reaction=NADP(+) + octanal = (2E)-octenal + H(+) + NADPH; Xref=Rhea:RHEA:50780, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61748; Evidence={ECO:0000256|ARBA:ARBA00023504}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50782; Evidence={ECO:0000256|ARBA:ARBA00023504}; CATALYTIC ACTIVITY: Reaction=NADP(+) + pentan-2-one = (E)-pent-3-en-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50788, ChEBI:CHEBI:15378, ChEBI:CHEBI:16472, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145276; Evidence={ECO:0000256|ARBA:ARBA00024160}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50790; Evidence={ECO:0000256|ARBA:ARBA00024160}; CATALYTIC ACTIVITY: Reaction=an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:13737, ChEBI:CHEBI:12834, ChEBI:CHEBI:13757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.74; Evidence={ECO:0000256|ARBA:ARBA00023507}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13739; Evidence={ECO:0000256|ARBA:ARBA00023507}; CATALYTIC ACTIVITY: Reaction=decanal + NADP(+) = (2E)-decenal + H(+) + NADPH; Xref=Rhea:RHEA:50612, ChEBI:CHEBI:15378, ChEBI:CHEBI:31457, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133455; Evidence={ECO:0000256|ARBA:ARBA00023691}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50614; Evidence={ECO:0000256|ARBA:ARBA00023691}; CATALYTIC ACTIVITY: Reaction=dodecanal + NADP(+) = (2E)-dodecenal + H(+) + NADPH; Xref=Rhea:RHEA:50784, ChEBI:CHEBI:15378, ChEBI:CHEBI:27836, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133741; Evidence={ECO:0000256|ARBA:ARBA00023530}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50786; Evidence={ECO:0000256|ARBA:ARBA00023530}; CATALYTIC ACTIVITY: Reaction=hexanal + NADP(+) = (E)-hex-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:50776, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:88528; Evidence={ECO:0000256|ARBA:ARBA00034052}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50778; Evidence={ECO:0000256|ARBA:ARBA00034052}; CATALYTIC ACTIVITY: Reaction=leukotriene B4 + NADP(+) = 12-oxo-leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:50608, ChEBI:CHEBI:15378, ChEBI:CHEBI:57461, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133309; Evidence={ECO:0000256|ARBA:ARBA00023545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50609; Evidence={ECO:0000256|ARBA:ARBA00023545};

Fatty acid metabolism;Hydroxylation;Lipid metabolism;Oxidoreductase;Prostaglandin metabolism;Reference proteome

prostaglandin metabolic process [GO:0006693]

cytoplasm [GO:0005737]

13-prostaglandin reductase activity [GO:0036132]; 15-oxoprostaglandin 13-oxidase activity [GO:0047522]; 2-alkenal reductase [NAD(P)+] activity [GO:0032440]

IPR013149;IPR041694;IPR011032;IPR045010;IPR036291;IPR020843;IPR014190;

3.90.180.10;3.40.50.720;

A0A1D5NZL7

MAGAQPGVHALQLKPVCVSDTLKKGIKFVKWDDDSTVVTPIILRTDPQGFFFYWTDQNKETELLDISLVKDARCGKHARAPKDPKLRELLDAGNVGSRLENRMITVVYGPDLVNISYLNLVAFQEDIAKEWSDEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACNLPSSRNDSIPQDDFTPDVYRVFLNNLCPRPEIDHIFSEFGAKSKPYLTVDQMMEFINLKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSNLAKKGQISVDGFMRYLSGEENGVVPPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMDPLEKYPLEPGVPLPSPMDLMYKILVKNKKKSHKSADGSAKKKLSEQASNTCSDTSSMFEPSSPGAGEAEIESDDDDDYDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEVSKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQVFWNAGCQMVALNFQTVDLSMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTESIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKALKTKTSQGNAVNPVWEEETIVFKKVVLPTLACLRLAVYEEGGKFIGHRILPVSAIRPGYHYICLRNERNQPLTLPALFVYIEVKDYVPDTFADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEVDHGDAPSEANSEPRPTPAENGVNHTASLTSKPTTQVVHSQPTPGLVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTAKYNEIQNDYLRRRAVLEKTAKRDSKKRSETGSPDHGSSTIEQELASLDSEMTQKLVELKEKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNSQLKKLKETCEKEKKELKKKMDKKRQEKITEAKSKDKNQMEEEKTEMIRSYIQEVVQYIKRLEDAQSKRQEKLIEKHKEIRQQILDEKPKLQVELDQEYQDKFKRLPLEILEFVQEAMKGKISEDGDHSSAPSSLASDSGKSNHKPLQSEEELEEDNSEKVFDTTF

Gallus gallus (Chicken)

FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. {ECO:0000256|PIRNR:PIRNR000956}.

3.1.4.11

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433; Evidence={ECO:0000256|ARBA:ARBA00023726}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485; Evidence={ECO:0000256|ARBA:ARBA00023726}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={ECO:0000256|ARBA:ARBA00023674}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; Evidence={ECO:0000256|ARBA:ARBA00023674};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR000956-2}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000956-2};

Calcium;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Phosphoprotein;Proteomics identification;Reference proteome;Transducer

activation of meiosis involved in egg activation [GO:0060466]; cerebral cortex development [GO:0021987]; fat cell differentiation [GO:0045444]; G protein-coupled receptor signaling pathway [GO:0007186]; G2/M transition of mitotic cell cycle [GO:0000086]; glutamate receptor signaling pathway [GO:0007215]; insulin-like growth factor receptor signaling pathway [GO:0048009]; interleukin-1-mediated signaling pathway [GO:0070498]; interleukin-12-mediated signaling pathway [GO:0035722]; interleukin-15-mediated signaling pathway [GO:0035723]; ion channel modulating, G protein-coupled receptor signaling pathway [GO:0099105]; ligand-gated ion channel signaling pathway [GO:1990806]; lipid catabolic process [GO:0016042]; memory [GO:0007613]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of monocyte extravasation [GO:2000438]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway [GO:0007207]; positive regulation of acrosome reaction [GO:2000344]; positive regulation of CD24 production [GO:2000560]; positive regulation of developmental growth [GO:0048639]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of embryonic development [GO:0040019]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of insulin secretion [GO:0032024]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of JNK cascade [GO:0046330]; positive regulation of myoblast differentiation [GO:0045663]; postsynaptic modulation of chemical synaptic transmission [GO:0099170]; regulation of establishment of endothelial barrier [GO:1903140]; regulation of fertilization [GO:0080154]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of retrograde trans-synaptic signaling by endocanabinoid [GO:0099178]; release of sequestered calcium ion into cytosol [GO:0051209]

chromatin [GO:0000785]; cytoplasm [GO:0005737]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; nuclear speck [GO:0016607]; postsynaptic cytosol [GO:0099524]

calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; GTPase activator activity [GO:0005096]; lamin binding [GO:0005521]; phosphatidylinositol phospholipase C activity [GO:0004435]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]

IPR000008;IPR035892;IPR011992;IPR001192;IPR016280;IPR028400;IPR014815;IPR042531;IPR009535;IPR037862;IPR017946;IPR015359;IPR000909;IPR001711;

2.30.29.240;2.60.40.150;1.10.238.10;3.20.20.190;1.20.1230.10;

A0A1D5NZW4

MFDRTRLPFVALDVVCVVLAGLPLGVLNLAKIKPYQRGFFCNDDSIKYPFHDSTITSTVLYTVGFTLPILSIILGETLSVFYNHLHSNSFVRNNYIATIYKAIGTFIFGAAASQSLTDIAKYSIGRLRPHFLAVCQPDWTQINCSLGYIENIPCQGDKAKINEGRLSFYSGHSSFSMYCMLFLALYLQARMKGDWARLVRPTIQFGLIAASIYVGLSRVSDYKHHWSDVLTGLIQGALVAILIVVYVSDFFKVRGCTFQPKEDSHTTLHETPTNGNHFGSNHQP

Gallus gallus (Chicken)

3.1.3.106; 3.1.3.4; 3.6.1.75

CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937, ChEBI:CHEBI:84973; Evidence={ECO:0000256|ARBA:ARBA00000974}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885; Evidence={ECO:0000256|ARBA:ARBA00000974}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546; Evidence={ECO:0000256|ARBA:ARBA00000980}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245; Evidence={ECO:0000256|ARBA:ARBA00000980}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859, ChEBI:CHEBI:82929; Evidence={ECO:0000256|ARBA:ARBA00001611}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237; Evidence={ECO:0000256|ARBA:ARBA00001611}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544, ChEBI:CHEBI:75757; Evidence={ECO:0000256|ARBA:ARBA00000235}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836; Evidence={ECO:0000256|ARBA:ARBA00000235}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:64839, ChEBI:CHEBI:75466; Evidence={ECO:0000256|ARBA:ARBA00023681}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256; Evidence={ECO:0000256|ARBA:ARBA00023681}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466, ChEBI:CHEBI:145465; Evidence={ECO:0000256|ARBA:ARBA00001542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161; Evidence={ECO:0000256|ARBA:ARBA00001542}; CATALYTIC ACTIVITY: Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815, ChEBI:CHEBI:85376; Evidence={ECO:0000256|ARBA:ARBA00001710}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041; Evidence={ECO:0000256|ARBA:ARBA00001710}; CATALYTIC ACTIVITY: Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377, ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589; Evidence={ECO:0000256|ARBA:ARBA00001476}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737; Evidence={ECO:0000256|ARBA:ARBA00001476}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine; Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57756, ChEBI:CHEBI:60119; Evidence={ECO:0000256|ARBA:ARBA00001716}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519; Evidence={ECO:0000256|ARBA:ARBA00001716}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000256|ARBA:ARBA00001180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430; Evidence={ECO:0000256|ARBA:ARBA00001180}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.6.1.75; Evidence={ECO:0000256|ARBA:ARBA00035886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450; Evidence={ECO:0000256|ARBA:ARBA00035886}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683; EC=3.1.3.106; Evidence={ECO:0000256|ARBA:ARBA00001472}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156; Evidence={ECO:0000256|ARBA:ARBA00001472}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674; Evidence={ECO:0000256|ARBA:ARBA00023977}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744; Evidence={ECO:0000256|ARBA:ARBA00023977};

PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000256|ARBA:ARBA00005074}.; PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.

Cell membrane;Hydrolase;Lipid metabolism;Membrane;Reference proteome

phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]

apical plasma membrane [GO:0016324]; caveola [GO:0005901]; plasma membrane [GO:0005886]

lysophosphatidic acid phosphatase activity [GO:0052642]; phosphatidate phosphatase activity [GO:0008195]

SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane raft {ECO:0000256|ARBA:ARBA00004314}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004314}. Membrane, caveola {ECO:0000256|ARBA:ARBA00004189}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004189}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR036938;IPR000326;IPR043216;

1.20.144.10;

A0A1D5PHB6

MSYEQRRDWGRGRGRGGDGGSSAASSGGGGHGGRGGGRGRHPSHLKGREIGLWYARKQGQKSKETDRQQRAVVRMDERREEQIVQLLNAVQPRAEKEQEAMSWWSGDEEGHVPEQPPKVKPGAEKAEKAPVKRRPILQKTFLDQDVEYLFEKNDQDADLDEQLKEDLRKKKSDPRYIEMQRFREKLPSYGMRQELVNLINNNRVTVISGETGCGKTTQVTQFILDDYIERGKGSTCRIVCTQPRRISAISVAERVAAERAEACGNGKSTGYQIRLQSRLPRKQGSILYCTTGIVLQWLQSDKHLSSISHVVLDEIHERNLQSDVLMSIIKDLLNVRLDLKVILMSATLNAEKFSEYFDNCPMIHIPGFTFPVVEYLLEDVIEKLRYTPENTDRRPRWKKGFMQGHISRPEKEEKEEIYRERWPEYLRQLRGRYSAGTIDALEMMDDDKVDLDLIAALIRHIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDRFIIIPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVFVIDGGKIKETHFDTQNNISTMAAEWVSKANAKQRKGRAGRVQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQIKILKLGGIAYFLSKLMDPPSRDAVMLAINHLMELNALDRQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKVADARRKELSKNTKSDHLTVVNAFTGWEETRRRGFRTEKDYCWEYFLSPNTLQMLHNMKGQFAEHLLAAGFVNSRDPKDPKSNTNSDNEKLLKAVICAGLYPKVAKIRPSFSKKRKMVKVCTKTDGTVNIHPKSVNVEETEFHYNWLVYHLKMRTSSIYLYDCTEVSPYCLLFFGGDISIQKDKDQDTIAVDEWIVFQSPARIAHLVKNLRQELDDLLQEKIENPHPVDWNDTKSRDTAVLTAIIDLITTQENESARNYAPRFQSERCS

Gallus gallus (Chicken)

3.6.4.13

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000256|ARBA:ARBA00001556};

ATP-binding;Helicase;Hydrolase;Nucleotide-binding;Proteomics identification;Reference proteome;RNA-binding

3'-UTR-mediated mRNA destabilization [GO:0061158]; cellular response to arsenite ion [GO:1903843]; cellular response to heat [GO:0034605]; cellular response to UV [GO:0034644]; G-quadruplex DNA unwinding [GO:0044806]; negative regulation of translation [GO:0017148]; ossification [GO:0001503]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cardioblast differentiation [GO:0051891]; positive regulation of cytoplasmic translation [GO:2000767]; positive regulation of hematopoietic progenitor cell differentiation [GO:1901534]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of mRNA 3'-end processing [GO:0031442]; positive regulation of myeloid dendritic cell cytokine production [GO:0002735]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regulation of telomere maintenance via telomere lengthening [GO:1904358]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; regulation of embryonic development [GO:0045995]; regulation of transcription by RNA polymerase III [GO:0006359]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; RNA secondary structure unwinding [GO:0010501]; spermatogenesis [GO:0007283]; telomerase RNA stabilization [GO:0090669]

chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]

ATP binding [GO:0005524]; DNA helicase activity [GO:0003678]; double-stranded RNA binding [GO:0003725]; G-quadruplex DNA binding [GO:0051880]; G-quadruplex RNA binding [GO:0002151]; histone deacetylase binding [GO:0042826]; hydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 5'-UTR binding [GO:0048027]; RNA helicase activity [GO:0003724]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; single-stranded DNA binding [GO:0003697]; telomerase RNA binding [GO:0070034]

IPR011709;IPR011545;IPR002464;IPR048333;IPR007502;IPR014001;IPR001650;IPR027417;

1.20.120.1080;3.40.50.300;

A0A1D5PIQ5

MSQERPKFYRQELNKTVWEVPERYQNLSPVGSGAYGSVCSAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPAKSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGPELLKKISSESARNYIQSLSYMPKMNFENVFIGANPLAVDLLEKMLVLDTDKRITAAEALAHAYFAQYHDPDDEPVADPYDQSFESRELEIEEWKSLTYDEVISFVPPPLDQEEMES

Gallus gallus (Chicken)

2.7.11.24

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

Proteomics identification;Reference proteome;Stress response

angiogenesis [GO:0001525]; bone development [GO:0060348]; cartilage condensation [GO:0001502]; cell morphogenesis [GO:0000902]; cellular response to ionizing radiation [GO:0071479]; cellular response to lipoteichoic acid [GO:0071223]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to UV-B [GO:0071493]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; cellular response to virus [GO:0098586]; chondrocyte differentiation [GO:0002062]; DNA damage checkpoint signaling [GO:0000077]; fatty acid oxidation [GO:0019395]; glucose import [GO:0046323]; glucose metabolic process [GO:0006006]; intracellular signal transduction [GO:0035556]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of hippo signaling [GO:0035331]; osteoblast differentiation [GO:0001649]; osteoclast differentiation [GO:0030316]; p38MAPK cascade [GO:0038066]; positive regulation of brown fat cell differentiation [GO:0090336]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of glucose import [GO:0046326]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of myotube differentiation [GO:0010831]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cytokine production involved in inflammatory response [GO:1900015]; regulation of ossification [GO:0030278]; regulation of synaptic membrane adhesion [GO:0099179]; response to dietary excess [GO:0002021]; response to insulin [GO:0032868]; response to muramyl dipeptide [GO:0032495]; response to muscle stretch [GO:0035994]; skeletal muscle tissue development [GO:0007519]; stem cell differentiation [GO:0048863]; stress-activated MAPK cascade [GO:0051403]; stress-induced premature senescence [GO:0090400]; striated muscle cell differentiation [GO:0051146]; transcription by RNA polymerase II [GO:0006366]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle pole [GO:0000922]

ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; mitogen-activated protein kinase p38 binding [GO:0048273]; NFAT protein binding [GO:0051525]; protein phosphatase binding [GO:0019903]; protein serine/threonine kinase activity [GO:0004674]

IPR011009;IPR003527;IPR038784;IPR008352;IPR000719;IPR017441;

1.10.510.10;

A0A1D5PLJ8

MPSAINAAVAQQTAAGSVPSTTSTTTEGTGGGTGGIYSAIISRNQPIIKVKEKTYEELHKKCLEENILYEDPDFPPNETSLFYSQKVPIKFEWKRPREICENPRFIIGGANRTDICQGELGDCWFLAAIACLTLNKKLLCRVIPHDQSFIQNYAGIFHFQFWRYGDWVDVIIDDCLPTYNNQLVFTKSSQRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVTEFYEIKDAPKDIYKIMKHAIARGSLMASSIDDNLGFSYGAAPRSDIGELIARMVKNLENAQMTYSTVDYQGTDERPAWTIMPMQYETRMSCGLVKGHAYSVTAVEETTYKGEKMRLVRLRNPWGQVEWNGPWSDKSEEWNFIDEEEKTRLQHKIAEDGEFWISFEDFMRHFTKLEICNLTPDTLEADKLQTWTVSVNEGRWVRGCSAGGCRNYPDTFWTNPQYRLKLLEEDDDPEDEEVICSFLVALMQKNRRKERKLGANLYTIGFAIYEVPKEMHGTKHHLQKDFFLYNASKARSKTYINMREISERFRLPPSEYVIIPSTYEPHQEGEFILRVFSEKRSLSEEVENMIEADRPSKKKKGKPIIFVSDRANSNKELTTDEDAGKDGEKTHVDEKKRSSAKAREKSEEETQFRNIFRQIAGDDMEINAEELRNVLNNVVKKHKDLKTEGFELESCRSMIALMDTDGSGKINFDEFRHLWDKIKSWQKIFKHYDADHSGTINSYEMRNAVKDAGFRLNNQLYDIITMRYADKNMNIDFDSFICCFVRLDAMFRAFHAFDKDGDGIIKLNVLEWLQLTMYA

Gallus gallus (Chicken)

FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000256|RuleBase:RU367132}.

3.4.22.54

CATALYTIC ACTIVITY: Reaction=Broad endopeptidase activity.; EC=3.4.22.54; Evidence={ECO:0000256|ARBA:ARBA00023702, ECO:0000256|RuleBase:RU367132};

Calcium;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Protease;Reference proteome;Repeat;Thiol protease

calcium-dependent self proteolysis [GO:1990092]; cellular response to calcium ion [GO:0071277]; cellular response to salt stress [GO:0071472]; G1 to G0 transition involved in cell differentiation [GO:0070315]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of protein sumoylation [GO:0033234]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of proteolysis [GO:0045862]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of satellite cell activation involved in skeletal muscle regeneration [GO:0014718]; programmed cell death [GO:0012501]; protein catabolic process [GO:0030163]; protein destabilization [GO:0031648]; protein localization to membrane [GO:0072657]; protein-containing complex assembly [GO:0065003]; proteolysis [GO:0006508]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of myoblast differentiation [GO:0045661]; sarcomere organization [GO:0045214]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]

calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; ligase regulator activity [GO:0055103]; molecular adaptor activity [GO:0060090]; sodium ion binding [GO:0031402]; structural constituent of muscle [GO:0008307]; titin binding [GO:0031432]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU367132}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.

IPR033883;IPR022684;IPR022682;IPR022683;IPR036213;IPR029531;IPR011992;IPR018247;IPR002048;IPR038765;IPR000169;IPR001300;

2.60.120.380;3.90.70.10;1.10.238.10;

A0A1D5PNE8

MELSEVRCLSDSDELYTINRTPPGSSRPQRLLWQTAVRHITEQRFIQEHSSSSGGSSSVGGKGFSSEETCCPNHHPHHHHHHFRRQSAGRSLGSERHNNGGTKVFPERTSSNGDLGFLPLDCAPSNSDFFLNWGYTYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRKSEVVMNILDVLTKLTLLFLHLTLASAPMDPIKGILLGFFTGIEVVICALVVVRKDTTSYTYLQYSGVVTWVAMATQILAAGLGCGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLVTSVLQLIMQLVIPRLAVTSLNQIAAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEARLRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHKIYIHRYENVSILFADVKGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAHCCVEMGLSMIKTIRYVRSRTKHDIDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKLESGGIPGRIHISKATLDCLNGDYKVEEGHGKERNEFLRKHNIETYLIKQPEESLLTLPEDIVKEAVSSSDSRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHVQSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAFIVLVFITAIQSLLPSSRVIPMVIQFSILIMLHSALVLITTAEDYKCLPLMLRKTCCWINETYLARNVIIFASILINFLGAIINILWCDFDKPVPLKNQTFNSSASFSDICSYPEYFVFTGVLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETIYASLFLQYDHLNHNGETDFLGTKEASLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVARHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDELLGEERFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSIALNESIQEINKHSFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSDRIQVPEETYLILKDRGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPLILQPRKLTGQYSLAAVVLGLVQSLNRQKQKQILNENNNSGIIKGHYNRRTLLTPGGSEAAAQAEGADKTELP

Gallus gallus (Chicken)

FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. {ECO:0000256|PIRNR:PIRNR039050}.

4.6.1.1

CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000256|ARBA:ARBA00001593, ECO:0000256|PIRNR:PIRNR039050};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR039050}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936};

ATP-binding;cAMP biosynthesis;Lyase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Reference proteome

adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP biosynthetic process [GO:0006171]; cellular response to glucagon stimulus [GO:0071377]; cellular response to morphine [GO:0071315]; glucose mediated signaling pathway [GO:0010255]; intracellular signal transduction [GO:0035556]; locomotory behavior [GO:0007626]; long-term memory [GO:0007616]; neuroinflammatory response [GO:0150076]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of long-term synaptic depression [GO:1900454]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of synaptic plasticity [GO:0031915]; regulation of cellular response to stress [GO:0080135]; regulation of cytosolic calcium ion concentration [GO:0051480]

apical plasma membrane [GO:0016324]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body membrane [GO:0032809]; postsynaptic density [GO:0014069]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]

adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR001054;IPR018297;IPR032628;IPR030672;IPR009398;IPR029787;

3.30.70.1230;

A0A1D5PPP7

MSGAERRPAAGRVQLDSKPTPTTTADGNQNITEVDAFDKRQTFDPAVQYKMNHQRRGVALIFNHEHFFWHLRLPDRRGTLADRNNLKRSLTDLGFEVRIFDDLKAEDVLKKVFEASRDDYSNADCFVCVFLSHGENDHVYAYDAQIKIETITNMFRGDKCQSLVGKPKIFIIQACRGDKHDDPVLVQDSVDSKDETTVNQTEVDAAGVYTLPAGADFIMCYSVAQGYFSHRETVNGSWYIQDLCEALGKHGSSLEFTELLTVVNRKVSHRKVDICRDINAIGKKQIPCFASMLTKKLYFHPKSK

Gallus gallus (Chicken)

FUNCTION: Cysteine protease that plays essential roles in programmed cell death, development and innate immunity (PubMed:11953316). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein lamin-A/LMNA thereby inducing nuclear shrinkage and fragmentation (PubMed:11953316). Lamin-A/LMNA cleavage is required for chromatin condensation and nuclear disassembly during apoptotic execution (PubMed:11953316). Plays an essential role in defense against viruses by acting as a central mediator of the ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis), independently of its cysteine protease activity. PANoptosis is a unique inflammatory programmed cell death, which provides a molecular scaffold that allows the interactions and activation of machinery required for inflammasome/pyroptosis, apoptosis and necroptosis (By similarity). {ECO:0000250|UniProtKB:P55212, ECO:0000269|PubMed:11953316}.

3.4.22.59

CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59; Evidence={ECO:0000250|UniProtKB:P55212};

Apoptosis;Autocatalytic cleavage;Cytoplasm;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease;Zymogen

activation of innate immune response [GO:0002218]; apoptotic chromosome condensation [GO:0030263]; apoptotic DNA fragmentation [GO:0006309]; apoptotic nuclear changes [GO:0030262]; apoptotic process [GO:0006915]; hepatocyte apoptotic process [GO:0097284]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; lens fiber cell differentiation [GO:0070306]; positive regulation of apoptotic process [GO:0043065]; positive regulation of necroptotic process [GO:0060545]; positive regulation of neuron apoptotic process [GO:0043525]; protein autoprocessing [GO:0016540]; proteolysis [GO:0006508]; pyroptosis [GO:0070269]

cytoplasm [GO:0005737]; nucleus [GO:0005634]

cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type peptidase activity [GO:0008234]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}.

DOMAIN: The N-terminal disordered prodomain is required to prevent self-activation. {ECO:0000250|UniProtKB:P55212}.; DOMAIN: The Tri-arginine exosite is required to recruit substrates for hydrolysis. {ECO:0000250|UniProtKB:P55212}.; DOMAIN: Undergoes helix-strand structural transitions upon substrate-binding: the 130's region interconverts between an inactive helical state and the canonically active strand state. Other caspases rest constitutively in the strand conformation before and after substrate-binding. {ECO:0000250|UniProtKB:P55212}.

IPR029030;IPR033139;IPR011600;IPR002138;IPR001309;IPR015917;

3.40.50.1460;

A0A1D5PRR9

MSGGRQRTLPEAWRRAAGPALQAGRDADGNDDDDDELLAAAAAELDPDPNPNVDPNPGPGPEAAAGGFCAAAGALWIYPTNRPERPYQLRMARAALFANTLLCLPTGLGKTFVAAVVMYNFYRWFPSGKVLFLAPTKALVAQQMEACAQLMGIPGRDMAEMTGGTQALSRRELWASRRVFFLTPQIMVNDLSRGTCPAVEVKCLVVDEAHKALGNHAYCQVVKELSRYTTQFRVLALTATPGSDTKAVQQVVSNLLIAQIELCSEDSPEIQPYSHERQVEKIVVPLGEELGGIQRAYIHVLETFAGRLIKLGVLARRDVPSLTKYQIILARDQYRKNPSPQNVGMQPGIIEGDFALCISLYHGYELLQQMGVRSLFIYLCGIMDGSKGLTRTKNELGRNEDFMRLYQQLTDMFSDTCQTSANGNLHKSRTVSENKKEFIYSHPKLKKLEEIVIEHFKSRKMGCSDQTTSGGTCVDTRVMIFSSFRDSVQEIAEMLSRFSPVVRVMTFVGHSTGKSTKGFTQKEQLEVVKRFREGGYNTLVSTCVGEEGLDIGEVDLIICFDAQKSPIRLVQRMGRTGRQRQGRVVVILAEGREERTYNQSQSNRRSIQKAISGNKMLHFYQHSPRMIPEGINPELHRMFITAEKYKPNDSGRLPKGRPSSLHHKSALFSCVTDPKEMHCHENWSLSPEEFEIWDRLYRLKENDGVKEPILPHTRFETLENLDKTSKPEEEAAHKLSLSEWSIWQSRPFPTSMVDHSDRCYHFISVMELIEVMRQEQGDCSYELELQPHLRIEDIHVRRNKGHLSTTSSAFAQKTHSSKRDMARTKRPFVPDVNDNEREFFSIFKTTNTKTPRTAPGLDLEEPELPTDTNGSEPCSARRLTLVASTDQGSPKEEEIEKVTFDLNEFNDLCDDGESTVAHESAAVKDLRLLDKHCSSVGLNHTDLGYSSFTAEKSPASSDLFYLPESHVDSFVLVSSSAELAGLEGAFSCVKGLLAHSPPPVSKLEGIEELLRHEETLCPLPKVSCRSYSGQLPHGDFPSSLAVDQSLLPAESPELEVTIGLSAAVNTCVSKPASTPTAAGGAEERPPGGGSFHSLLGKEGFTANHTDNPPNKHFVQGDEEDSEMKRDVTIDGEKSIHLFEDEHTYKVNDEMPSVDVEPLLRLGSGGHTARPSAGPASQQPPSGDSPRGDTACGEGAARGEMAPGGAWGRGSAAEQALHNSELCDYSQELFSVNFDLGFSIEECEEEIFEGDTDAMNTPKLNSASRSRADVQLTANRKSLNDGCRVQTPPKWDCKGLKGRNISTPLPLQSGHVRDTAVPGGTAGGRTGRGSPGASPPSPATPTGRRVSSAEATRRIRKKVFSTVREETPEVCPTDKVNPNSQRNSFGSSASDALHTTGGRTENLEGTNLHTSRVFPAEGTSSESEEEIVFQRKNRRNNVLRSPDVGSDSDFGSPVCAVRKRRHPLTVSDVSSDDGVDFHKNPNRGTRGCSAAGSKAQLRGVKRQKVRSKVTCKNAARQFLDEEAELSQQDESCVSSDETEDTDKELSSSLAQFLNDDAEVTQVLNDSEMRGVYLKSVRSPALGSRYRMVHREFNSTEIFSQIPEQDEAYAEDSFCVAEGDEETCNKSESSEEEEVCVNFDLLNNESFGGGGGRYLTRRRKKLHGANMEQNCSAPVQKKPSRIIVLSDSSGEETNVSNEKGTAAHCSRAGRENAELLTSMPSVSSVPHKKSAGDVSAHQSAESKSGMLLGLKASVSEVLDFHPGPRSGSGKEALQAAAQHLQLESSVKNSAGNAPGATKASPALLDGDTALCVLVDSREISSGADVISSLKAVHGLKVQVCSLGSGDYVVSNRMAVERKFQSELLSSVNRTKVTQRLQRLQGMFERVCVIVEKDRTRPGETSRFSQRTQHYDATLAALLQAGIRVLFSSCQEETAVLLKELALLEQRKNAAICVPTEVEGHKQEMLNFYLSLPNISYLAALNMCHHFSSVRTMVNSSPSDIAAGARVSLQRAEETYRYLRYGFDTQMLPESLCAKGKSNTATRS

Gallus gallus (Chicken)

FUNCTION: DNA-dependent ATPase component of the Fanconi anemia (FA) core complex (By similarity). Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:16116434, PubMed:19465393). In complex with CENPS and CENPX, binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction substrates (By similarity). Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork (By similarity). This activity is strongly stimulated in the presence of CENPS and CENPX (By similarity). In complex with FAAP24, efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates (By similarity). In vitro, on its own, strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA (By similarity). {ECO:0000250|UniProtKB:Q8IYD8, ECO:0000269|PubMed:16116434, ECO:0000269|PubMed:19465393}.

3.6.4.13

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q8IYD8};

3D-structure;ATP-binding;DNA damage;DNA repair;DNA-binding;Helicase;Hydrolase;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome

double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; interstrand cross-link repair [GO:0036297]

nucleus [GO:0005634]

3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; four-way junction DNA binding [GO:0000400]; four-way junction helicase activity [GO:0009378]; nuclease activity [GO:0004518]; RNA helicase activity [GO:0003724]

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19465393}.

PTM: Phosphorylated; hyperphosphorylated in response to genotoxic stress. {ECO:0000269|PubMed:19465393}.

IPR011545;IPR006166;IPR031879;IPR039686;IPR044749;IPR014001;IPR001650;IPR027417;IPR011335;IPR010994;IPR047418;

3.40.50.10130;1.10.150.20;1.20.1320.20;3.40.50.300;

A0A1D5PUY5

MAEPPAAPGPEGEEGPVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIRADIEKDVLTVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIKCSLNPEWNETFRFQLKEADKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKSGVDGWFKLLSQEEGEYFNVPVPPEGEEGNEELRQKFERAKIGTGSKAADEKTTNAISKFDNNGSRDRMKLSDFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYQIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPAKRLGCGPEGERDIKEHAFFRYIDWDKLERKEIQPPFKPKACGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSFFNSEFFKPEAKS

Gallus gallus (Chicken)

2.7.11.13

CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|PIRNR:PIRNR000550};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR000550-4}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000256|PIRSR:PIRSR000550-4};

Adaptive immunity;ATP-binding;Calcium;Cytoplasm;Immunity;Kinase;Metal-binding;Nucleotide-binding;Nucleus;Phosphoprotein;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc;Zinc-finger

adaptive immune response [GO:0002250]; B cell activation [GO:0042113]; B cell receptor signaling pathway [GO:0050853]; calcium ion transport [GO:0006816]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to carbohydrate stimulus [GO:0071322]; intracellular calcium ion homeostasis [GO:0006874]; intracellular signal transduction [GO:0035556]; negative regulation of glucose transmembrane transport [GO:0010829]; phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway [GO:0007207]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of B cell receptor signaling pathway [GO:0050861]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of insulin secretion [GO:0032024]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; post-translational protein modification [GO:0043687]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of synaptic vesicle exocytosis [GO:2000300]; regulation of transcription by RNA polymerase II [GO:0006357]

nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; presynaptic cytosol [GO:0099523]; spectrin [GO:0008091]

ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone H3T6 kinase activity [GO:0035403]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; protein kinase C binding [GO:0005080]; protein serine/threonine kinase activity [GO:0004674]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR000961;IPR046349;IPR000008;IPR035892;IPR034664;IPR020454;IPR011009;IPR002219;IPR017892;IPR000719;IPR017441;IPR014375;IPR008271;

3.30.60.20;2.60.40.150;1.10.510.10;

A0A1D5PZB7

MLCPWQFAFKPHAVKNQSSEEKDINNNVEKDVKVHSFVKDDAKLHSLSKKQMKMSPIITSAEKHPQNGIKASNQISRCPRHVKVRNMENGSSLLDTLHLTAKEVINCRTRACQGALMTPKGLVRSTRDGPVPPAELLPQAVDFVKQYYSSFKELKIEEHLARLETVTKEIETTGTYHLTKDELIFAAKQAWRNAPRCIGRIQWSNLQVFDARDCKTAKEMFEYICRHIQYATNNGNIRSAITIFPQRTDGKHDFRVWNSQLIRYAGYQMPDGSVIGDPASVEFTKLCIELGWKPKYGRFDVVPLILQANGQDPEIFEYPPEIILEVPMEHPKYEWFKELDLKWYALPAVANMLLEVGGLEFTACPFNGWYMGTEIGVRDFCDVQRYNILKEVGRRMGLETNKLASLWKDRAVVEINVAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRVRGGCPADWVWIVPPMSGSITPVFHQEMLNYVLTPFFYYQVDAWKTHIWHDETRRPKKREIKLSILAKAVLFASLLLQKTMAARPKVTVIYATETGKSETLANSLCSLFSCAFNTKILCMDEYNISDLEKETLLLVVTSTFGNGDSPNNGKTLKNSLLTLKLLRKNIRYAVFGLGSTMYPEFCAFAHAIDQKLSQLGALQLTPVGEGDELNGQEEAFRTWAVTAFKTACDIFDIRGKNSIQLPEIYTSDDSWNPKKHRIVYDSQTMDLTKALSDIHGKNVIPMKLKFRQNLQSLKSSRVTILVKLSCETNQEVHYLPGEHIGISPGNQPELVHGLIARVKDAPPADQTIRLETCTEGGYWASEKKIPACTLSQALTYLLDITTPPTQQLLKKLSQLVTAEGDKQRLEVLCHSTEEYNKWKFYNSPNILEVLEEFPSAEVSTAFLLTQLPLLKPRYYSVSSSCDMTPREIHLTVAVVNYRTRDGQGPLHHGVCSTWLNKIALNETVPCFVRSADGFRLPKEPAKPCILIGPGTGIAPFRSFWQQRLYDLEKKGIKGGDMILLFGCRHPDMDHIYKEEVEEMKRKGVLKEVFTAYSRQPGQPKVYVQDILQNELETKVCNILHKEEGHLYVCGDVRMARDVAQTLKRMLVKKLNHTEQQAEEYFFQLKSQKRYHEDIFGAVFPHEVKRI

Gallus gallus (Chicken)

FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions. {ECO:0000256|PIRNR:PIRNR000333}.

1.14.13.39

CATALYTIC ACTIVITY: Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; Evidence={ECO:0000256|ARBA:ARBA00035595}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898; Evidence={ECO:0000256|ARBA:ARBA00035595};

COFACTOR: Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin; Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000256|ARBA:ARBA00001950}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|PIRNR:PIRNR000333}; Note=Binds 1 FAD. {ECO:0000256|PIRNR:PIRNR000333}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|PIRNR:PIRNR000333}; Note=Binds 1 FMN. {ECO:0000256|PIRNR:PIRNR000333}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|ARBA:ARBA00001970, ECO:0000256|PIRNR:PIRNR000333};

Calmodulin-binding;FAD;Flavoprotein;FMN;Heme;Iron;Metal-binding;NADP;Oxidoreductase;Reference proteome

arginine catabolic process [GO:0006527]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to type II interferon [GO:0071346]; cellular response to xenobiotic stimulus [GO:0071466]; circadian rhythm [GO:0007623]; defense response to bacterium [GO:0042742]; inflammatory response [GO:0006954]; negative regulation of blood pressure [GO:0045776]; negative regulation of gene expression [GO:0010629]; negative regulation of protein catabolic process [GO:0042177]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide mediated signal transduction [GO:0007263]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of killing of cells of another organism [GO:0051712]; prostaglandin secretion [GO:0032310]; regulation of cell population proliferation [GO:0042127]; regulation of cytokine production involved in inflammatory response [GO:1900015]; regulation of insulin secretion [GO:0050796]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]; response to lipopolysaccharide [GO:0032496]; superoxide metabolic process [GO:0006801]

cortical cytoskeleton [GO:0030863]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]

arginine binding [GO:0034618]; calmodulin binding [GO:0005516]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitric-oxide synthase activity [GO:0004517]; protein homodimerization activity [GO:0042803]; tetrahydrobiopterin binding [GO:0034617]

IPR003097;IPR017927;IPR001094;IPR008254;IPR001709;IPR029039;IPR039261;IPR023173;IPR044943;IPR044940;IPR044944;IPR012144;IPR004030;IPR036119;IPR001433;IPR017938;

3.40.50.360;6.10.250.410;3.90.440.10;3.40.50.80;2.40.30.10;

A0A1D5PZJ5

MRKKQKTAWKEILKWEKEVTGTKPKMSTTRKILLILGFLSTLAAIALITVAVTQNQPLPKNIKYGIVLDAGSSHTNLYVYEWPAEKENDTGVVQQVEVCKVEGPGISGYSQTTEKAGPSLVQCLRQAEGVIPLKQHQETPVYLGATAGMRLLRLENKDAAEKVLSSVEKTLRSAPFNFQGARIISGQEEGAYGWITINYLLGNFKQSGWKKFLHSLKSVSETSGALDLGGASTQITFVPDEISSESPQNLLYFRLYGKDYRVYTHSFLCYGKDQALQQKLARDLQSTENSSLFDPCFHQGYQRTISVSNFFKNPCTSVEKKQFPFSQLHIEGEGNYEKCRRNIQNLFNKTDCPYSSCSFNGIYLPPLQGDFGAFSAFYFVMNFLNLTSDDPFTLDEVASAIKKFCARPWHEVKLQYHQIKEKYLSEYCFSGAYILSLLENGYEFTTENWKRIHFLGKIGSSDAGWTLGYMLNLTNMIPAEEPPAPPLSYGSYVGLMVLCSLVLVSVILLAWLLFHKPKCLQKGVV

Gallus gallus (Chicken)

3.6.1.5

CATALYTIC ACTIVITY: Reaction=2 H2O + ITP = 2 H(+) + IMP + 2 phosphate; Xref=Rhea:RHEA:77735, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; Evidence={ECO:0000256|ARBA:ARBA00043682}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77736; Evidence={ECO:0000256|ARBA:ARBA00043682}; CATALYTIC ACTIVITY: Reaction=2 H2O + UTP = 2 H(+) + 2 phosphate + UMP; Xref=Rhea:RHEA:64896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; Evidence={ECO:0000256|ARBA:ARBA00043678}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64897; Evidence={ECO:0000256|ARBA:ARBA00043678}; CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437; Evidence={ECO:0000256|ARBA:ARBA00036139}; CATALYTIC ACTIVITY: Reaction=ATP + 2 H2O = AMP + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:20988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00043702}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20989; Evidence={ECO:0000256|ARBA:ARBA00043702}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034440}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000256|ARBA:ARBA00034440}; CATALYTIC ACTIVITY: Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00043676}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881; Evidence={ECO:0000256|ARBA:ARBA00043676}; CATALYTIC ACTIVITY: Reaction=CTP + 2 H2O = CMP + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:64908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00043680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64909; Evidence={ECO:0000256|ARBA:ARBA00043680}; CATALYTIC ACTIVITY: Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:58069; Evidence={ECO:0000256|ARBA:ARBA00043776}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388; Evidence={ECO:0000256|ARBA:ARBA00043776}; CATALYTIC ACTIVITY: Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; Evidence={ECO:0000256|ARBA:ARBA00043654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157; Evidence={ECO:0000256|ARBA:ARBA00043654}; CATALYTIC ACTIVITY: Reaction=GTP + 2 H2O = GMP + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:64904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00043766}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64905; Evidence={ECO:0000256|ARBA:ARBA00043766}; CATALYTIC ACTIVITY: Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; Evidence={ECO:0000256|ARBA:ARBA00043688}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208; Evidence={ECO:0000256|ARBA:ARBA00043688}; CATALYTIC ACTIVITY: Reaction=H2O + ITP = H(+) + IDP + phosphate; Xref=Rhea:RHEA:28330, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58280, ChEBI:CHEBI:61402; Evidence={ECO:0000256|ARBA:ARBA00043752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28331; Evidence={ECO:0000256|ARBA:ARBA00043752}; CATALYTIC ACTIVITY: Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; Evidence={ECO:0000256|ARBA:ARBA00043716}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877; Evidence={ECO:0000256|ARBA:ARBA00043716}; CATALYTIC ACTIVITY: Reaction=H2O + UTP = H(+) + phosphate + UDP; Xref=Rhea:RHEA:64900, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223; Evidence={ECO:0000256|ARBA:ARBA00043661}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64901; Evidence={ECO:0000256|ARBA:ARBA00043661}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; Evidence={ECO:0000256|ARBA:ARBA00043714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800; Evidence={ECO:0000256|ARBA:ARBA00043714}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5; Evidence={ECO:0000256|ARBA:ARBA00043753}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36796; Evidence={ECO:0000256|ARBA:ARBA00043753}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; Evidence={ECO:0000256|ARBA:ARBA00043686}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681; Evidence={ECO:0000256|ARBA:ARBA00043686};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00001913};

ATP-binding;Calcium;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Nucleotide-binding;Proteomics identification;Reference proteome;Transmembrane;Transmembrane helix

nucleoside diphosphate catabolic process [GO:0009134]

plasma membrane [GO:0005886]

GDP phosphatase activity [GO:0004382]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR000407;

3.30.420.40;3.30.420.150;

A0A1D5Q1K7

ADGATALQPGRESETLSQKKRKNEKDREERETEKRKRQSKAKKEEETAAFFPCDAFLCEIESREESLAVSPRLECSGAISAHCSLRLLGSSNSPASASRVAGITGAHCNFQSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEAILNKPGLKYKPAVNQIECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSNQDMTTLLSYNRNWRVCALLSCASHKDYPFHEEF

Macaca mulatta (Rhesus macaque)

1.1.1.21; 1.1.1.300

CATALYTIC ACTIVITY: Reaction=(E)-hex-2-en-1-ol + NADP(+) = (E)-hex-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:58424, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:141205; Evidence={ECO:0000256|ARBA:ARBA00035762}; CATALYTIC ACTIVITY: Reaction=(E,E)-2,4-hexadien-1-ol + NADP(+) = (E,E)-2,4-hexadienal + H(+) + NADPH; Xref=Rhea:RHEA:58428, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:82334, ChEBI:CHEBI:142625; Evidence={ECO:0000256|ARBA:ARBA00036840}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine + H(+) + NADPH = 1-hexadecanoyl-2-(5-hydroxypentanoyl)-sn-glycero-3-phosphocholine + NADP(+); Xref=Rhea:RHEA:58512, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77890, ChEBI:CHEBI:142747; Evidence={ECO:0000256|ARBA:ARBA00036458}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphoethanolamine + H(+) + NADPH = 1-hexadecanoyl-2-(5-hydroxypentanoyl)-sn-glycero-3-phosphoethanolamine + NADP(+); Xref=Rhea:RHEA:58756, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142750, ChEBI:CHEBI:142751; Evidence={ECO:0000256|ARBA:ARBA00036583}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(7-oxoheptanoyl)-sn-glycero-3-phosphocholine + H(+) + NADPH = 1-hexadecanoyl-2-(7-hydroxyheptanoyl)-sn-glycero-3-phosphocholine + NADP(+); Xref=Rhea:RHEA:58752, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:134601, ChEBI:CHEBI:142748; Evidence={ECO:0000256|ARBA:ARBA00036601}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + H(+) + NADPH = 1-hexadecanoyl-2-(9-hydroxynonanoyl)-sn-glycero-3-phosphocholine + NADP(+); Xref=Rhea:RHEA:58592, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61042, ChEBI:CHEBI:142749; Evidence={ECO:0000256|ARBA:ARBA00036167}; CATALYTIC ACTIVITY: Reaction=13-cis-retinol + NADP(+) = 13-cis-retinal + H(+) + NADPH; Xref=Rhea:RHEA:54920, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479, ChEBI:CHEBI:45487, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000256|ARBA:ARBA00036024}; CATALYTIC ACTIVITY: Reaction=9-cis-retinol + NADP(+) = 9-cis-retinal + H(+) + NADPH; Xref=Rhea:RHEA:54916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273; Evidence={ECO:0000256|ARBA:ARBA00036611}; CATALYTIC ACTIVITY: Reaction=NADP(+) + prenol = 3-methyl-2-butenal + H(+) + NADPH; Xref=Rhea:RHEA:58420, ChEBI:CHEBI:15378, ChEBI:CHEBI:15825, ChEBI:CHEBI:16019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000256|ARBA:ARBA00036263}; CATALYTIC ACTIVITY: Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin H2; Xref=Rhea:RHEA:45312, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404, ChEBI:CHEBI:57405, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000256|ARBA:ARBA00036352}; CATALYTIC ACTIVITY: Reaction=a 4-hydroxynonen-1-ol + NADP(+) = a 4-hydroxynonenal + H(+) + NADPH; Xref=Rhea:RHEA:58336, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142593, ChEBI:CHEBI:142606; Evidence={ECO:0000256|ARBA:ARBA00036873}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.300; Evidence={ECO:0000256|ARBA:ARBA00000975}; CATALYTIC ACTIVITY: Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH; Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555, ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21; Evidence={ECO:0000256|ARBA:ARBA00036731};

Acetylation;NADP;Reference proteome

cellular hyperosmotic salinity response [GO:0071475]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; epithelial cell maturation [GO:0002070]; fructose biosynthetic process [GO:0046370]; L-ascorbic acid biosynthetic process [GO:0019853]; metanephric collecting duct development [GO:0072205]; negative regulation of apoptotic process [GO:0043066]; regulation of urine volume [GO:0035809]; renal water homeostasis [GO:0003091]; retinoid metabolic process [GO:0001523]

cytosol [GO:0005829]; nucleoplasm [GO:0005654]

alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; glyceraldehyde oxidoreductase activity [GO:0043795]; L-glucuronate reductase activity [GO:0047939]; retinal dehydrogenase activity [GO:0001758]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.

IPR020471;IPR018170;IPR023210;IPR036812;

3.20.20.100;

A0A1D5Q1P0

MESALPAAGFLYWVGAGTVAYLALRISYSLFTALRVWGVGNEAGVGPGLGEWAVVTGGTDGIGKSYAEELAKRGMKVVLISRSQDKLDQVSSEIKEKFKVETRTIVVDFTLEDIYDKIKTGLAGLEIGILVNNVGMSYEYPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMFPVPLLTIYSATKTFVDFFSQCLHEEYRSKGIFVQSVLPYFVATKLAKIRKPTLDKPTPETFVKSAIKTVGLQSRTNGYLIHVLMGWIISNLPSWIYLKIAMNMNKATRAHYLKKIKKN

Macaca mulatta (Rhesus macaque)

FUNCTION: Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation. {ECO:0000256|ARBA:ARBA00037337}.

1.1.1.330; 1.1.1.62

CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + H(+) + NADPH = (3R)-hydroxy-(7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + NADP(+); Xref=Rhea:RHEA:39323, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73852, ChEBI:CHEBI:76415; Evidence={ECO:0000256|ARBA:ARBA00036946}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + H(+) + NADPH = (3R)-hydroxy-(7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + NADP(+); Xref=Rhea:RHEA:39459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73863, ChEBI:CHEBI:76460; Evidence={ECO:0000256|ARBA:ARBA00036361}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + H(+) + NADPH = (3R)-hydroxy-(8Z,11Z,14Z)-eicosatrienoyl-CoA + NADP(+); Xref=Rhea:RHEA:39311, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:71481, ChEBI:CHEBI:76411; Evidence={ECO:0000256|ARBA:ARBA00036851}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence={ECO:0000256|ARBA:ARBA00035946}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH; Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62; Evidence={ECO:0000256|ARBA:ARBA00036215}; CATALYTIC ACTIVITY: Reaction=3-oxooctadecanoyl-CoA + H(+) + NADPH = (3R)-hydroxyoctadecanoyl-CoA + NADP(+); Xref=Rhea:RHEA:39151, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:71407, ChEBI:CHEBI:76374; Evidence={ECO:0000256|ARBA:ARBA00035933}; CATALYTIC ACTIVITY: Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330; Evidence={ECO:0000256|ARBA:ARBA00036602};

PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|ARBA:ARBA00005194}.; PATHWAY: Steroid biosynthesis; estrogen biosynthesis. {ECO:0000256|ARBA:ARBA00037929}.

Lipid biosynthesis;Lipid metabolism;Membrane;Oxidoreductase;Reference proteome;Steroid biosynthesis;Transmembrane;Transmembrane helix

extracellular matrix organization [GO:0030198]; fatty acid elongation, saturated fatty acid [GO:0019367]; positive regulation of cell-substrate adhesion [GO:0010811]; steroid biosynthetic process [GO:0006694]

endoplasmic reticulum [GO:0005783]; extracellular matrix [GO:0031012]; fatty acid elongase complex [GO:0009923]

collagen binding [GO:0005518]; fibronectin binding [GO:0001968]; heparin binding [GO:0008201]; oxidoreductase activity [GO:0016491]; very-long-chain 3-oxoacyl-CoA reductase activity [GO:0141040]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR036291;IPR020904;IPR002347;

3.40.50.720;

A0A1D5Q1X3

MAKERGLISPSDFAQLQKYMESSSVALSSVLLRCAHDWEREEREMGRCARSRLSTHLRCTWTACSSSQRRGVKSDSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIYLEVDNVPRHLSLALFQSFKTDHCLNEANVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEWVRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNLSTSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRLFKDVPDGRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQNLAKILKDLETSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVLNIPSMHGGSNLWGDTRKPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLEGAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL

Macaca mulatta (Rhesus macaque)

2.7.1.107

CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023371}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000256|ARBA:ARBA00023371}; CATALYTIC ACTIVITY: Reaction=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378, ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023395}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429; Evidence={ECO:0000256|ARBA:ARBA00023395}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycerol + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:63324, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:72859, ChEBI:CHEBI:82929, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034632}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63325; Evidence={ECO:0000256|ARBA:ARBA00034632}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-2-acyl-sn-glycerol + ATP = 1-O-alkyl-2-acyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:44072, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52595, ChEBI:CHEBI:73332, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034642}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073; Evidence={ECO:0000256|ARBA:ARBA00034642}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-sn-glycerol + ATP = 1-O-alkyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:16937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15850, ChEBI:CHEBI:30616, ChEBI:CHEBI:58014, ChEBI:CHEBI:456216; EC=2.7.1.93; Evidence={ECO:0000256|ARBA:ARBA00043787}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16938; Evidence={ECO:0000256|ARBA:ARBA00043787}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40403, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77184, ChEBI:CHEBI:77186, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034624}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40404; Evidence={ECO:0000256|ARBA:ARBA00034624}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40407, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77185, ChEBI:CHEBI:77187, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034638}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40408; Evidence={ECO:0000256|ARBA:ARBA00034638}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + ATP = 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75936, ChEBI:CHEBI:78385, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034647}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677; Evidence={ECO:0000256|ARBA:ARBA00034647}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-sn-glycerol + ATP = 1-O-hexadecyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41672, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:34115, ChEBI:CHEBI:77580, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673; Evidence={ECO:0000256|ARBA:ARBA00034614}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43416, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:64839, ChEBI:CHEBI:75466, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43417; Evidence={ECO:0000256|ARBA:ARBA00034636}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023400}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; Evidence={ECO:0000256|ARBA:ARBA00023400}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + ATP = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:63328, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:73990, ChEBI:CHEBI:77593, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034613}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63329; Evidence={ECO:0000256|ARBA:ARBA00034613}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000256|RuleBase:RU361128};

PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000256|ARBA:ARBA00005175}.

Acetylation;ATP-binding;Calcium;Kinase;Lipid metabolism;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Repeat;Transferase;Zinc;Zinc-finger

diacylglycerol metabolic process [GO:0046339]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; phosphatidic acid biosynthetic process [GO:0006654]; platelet activation [GO:0030168]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]

cytosol [GO:0005829]; plasma membrane [GO:0005886]

alkylglycerol kinase activity [GO:0047649]; ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; calcium ion binding [GO:0005509]; phospholipid binding [GO:0005543]; protein kinase activity [GO:0004672]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.

IPR017438;IPR046349;IPR047469;IPR029477;IPR037607;IPR038199;IPR000756;IPR001206;IPR011992;IPR018247;IPR002048;IPR011009;IPR016064;IPR002219;IPR000719;IPR017441;IPR008271;

2.60.200.40;3.30.60.20;1.10.238.110;1.10.238.10;1.10.510.10;

A0A1D5Q2Y8

SLSPGGMEGVACKILLLLLPLLLLLEPQVSQGLVITPPGPELILNVSSTFVLTCSGSAPVVWERMSQELPQEMAKAQDNTFSSVLTLTNLTGLDTGEYFCTYNDSRGLEPDERKRLYIFVPDPTMGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDIALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWMYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLGEVGALQFAELHRSRTLQVVFEAYPPPTVLWFKDNRTLGDSSAGEIALSTRNVSETRYVSELTLVRVKVAEAGHYTMRAFHEDAEVQLSFQLQINVPVRVLELSESHPDSGEQTVRCRGRGMPQPNIIWSACRDLKRCPRELPPMLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRCTLRNAVGQDMQEVIVVPHSLPFKAVVISAILALVVLTIISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPMQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQHHSDKRRPPSAELYSNALPVGLPLPSHVSLTGESDGGYMDMSKDESVDYVPMLDMKGDVKYADIESSNYMAPYDNYVPSAPERTCRATLINESPVLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGFHGLRSPLDSSSVLYTAVQPNEGDNDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQEEPEPEPQLERQVEPEPELEQLPDSGCPAPRAEAEDSFL

Macaca mulatta (Rhesus macaque)

FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. {ECO:0000256|PIRNR:PIRNR500948}.

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171, ECO:0000256|PIRNR:PIRNR500948};

ATP-binding;Cell membrane;Chemotaxis;Cytoplasmic vesicle;Developmental protein;Disulfide bond;Glycoprotein;Immunoglobulin domain;Kinase;Lysosome;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

angiogenesis [GO:0001525]; cell chemotaxis [GO:0060326]; phosphorylation [GO:0016310]; positive regulation of phosphate metabolic process [GO:0045937]; positive regulation of protein modification process [GO:0031401]; positive regulation of response to stimulus [GO:0048584]; positive regulation of smooth muscle cell migration [GO:0014911]

cytoplasmic vesicle [GO:0031410]; lysosomal lumen [GO:0043202]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; metal ion binding [GO:0046872]; platelet-derived growth factor beta-receptor activity [GO:0005019]; platelet-derived growth factor binding [GO:0048407]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR500948}; Single-pass type I membrane protein {ECO:0000256|PIRNR:PIRNR500948}. Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR500948}. Lysosome lumen {ECO:0000256|PIRNR:PIRNR500948}. Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}.

IPR007110;IPR036179;IPR013783;IPR003599;IPR003598;IPR013151;IPR011009;IPR027288;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;IPR001824;

2.60.40.10;1.10.510.10;

A0A1D5Q330

MAWRCPRMGRVPLAWCLALCGWVCMAPRGTQAEESPFVGNPGNITGARGLTGTLRCQLQVQGEPPEVHWLRDGQILELADSTQTQVPLGEDEQDDWIVVSQLRIASLQLSDAGQYQCLVFLGHQNFVSQPGYVGLEGLPYFLEEPEDRTVAANTHFNLSCQAQGPPEPVDLLWLQDAVPLATAPGHGPQRNLHVPGLNKTSSFSCEAHNAKGVTTSRTATITVLPQQPRNLHLVSRQPTELEVAWTPGLSGIYPLTHCTLQAMLSDNEVGIQAGEPDPPEEPLTLQASVPPHQLRLGSLHPHTPYYIRVACTSSQGPSSWTHWLPVETPEGVPLGPPENISATRNGSQAFVHWQEPRAPLQGTLLGYRLAYQGQDTPEVLMDIGLRQEVTLELQGDGSVSNLTVCVAAYTAAGDGPWSLPVPLEAWRPGQAQPVHQLVKETSAPAFSWPWWYILLGAVVAAACVLILALFLVHRRKKETRYGEVFEPTVERGELVVRYRVRKSYSRRTTEATLNSLGISEELKEKLRDVMVDRHKVALGKTLGEGEFGAVMEGQLNQDDSILKVAVKTMKIAICTRSELEDFLSEAVCMKEFDHPNVMRLIGVCFQGSERESFPAPVVILPFMKHGDLHSFLLYSRLGDQPVYLPTQMLVKFMADIASGMEYLSTKRFIHRDLAARNCMLNENMSVCVADFGLSKKIYNGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQPADCLDGLYALMSRCWELNPQDRPSFTELREDLENTLKALPPAQEPDEILYVNMDEGGGYPEPPGAAGGADPPTQLDPKDSCSCLTSAEVHPAGRYVLCPSTAPSPAQPADRGSPAAPGQEDGA

Macaca mulatta (Rhesus macaque)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171};

ATP-binding;Disulfide bond;Glycoprotein;Immunoglobulin domain;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

blood vessel remodeling [GO:0001974]; cell maturation [GO:0048469]; cell migration [GO:0016477]; cellular response to extracellular stimulus [GO:0031668]; cellular response to interferon-alpha [GO:0035457]; cellular response to lipopolysaccharide [GO:0071222]; dendritic cell differentiation [GO:0097028]; erythrocyte homeostasis [GO:0034101]; establishment of localization in cell [GO:0051649]; forebrain cell migration [GO:0021885]; inflammatory response [GO:0006954]; natural killer cell differentiation [GO:0001779]; negative regulation of apoptotic process [GO:0043066]; negative regulation of dendritic cell apoptotic process [GO:2000669]; negative regulation of lymphocyte activation [GO:0051250]; negative regulation of macrophage cytokine production [GO:0010936]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of type II interferon production [GO:0032689]; nervous system development [GO:0007399]; neuron apoptotic process [GO:0051402]; neuron migration [GO:0001764]; neutrophil clearance [GO:0097350]; ovulation cycle [GO:0042698]; phagocytosis [GO:0006909]; platelet activation [GO:0030168]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; positive regulation of natural killer cell differentiation [GO:0032825]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of pinocytosis [GO:0048549]; positive regulation of viral life cycle [GO:1903902]; secretion by cell [GO:0032940]; spermatogenesis [GO:0007283]; substrate adhesion-dependent cell spreading [GO:0034446]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vagina development [GO:0060068]

actin cytoskeleton [GO:0015629]; cell surface [GO:0009986]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphatidylserine binding [GO:0001786]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; virus receptor activity [GO:0001618]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR003961;IPR036116;IPR007110;IPR036179;IPR013783;IPR003599;IPR011009;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;

2.60.40.10;1.10.510.10;

A0A1D5Q518

MGMWASLDALWEIPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSEIEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEERNSEEIKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHYSHPPLLERLQALKSMKQH

Macaca mulatta (Rhesus macaque)

FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated proteins. {ECO:0000256|RuleBase:RU366005}.

3.4.24.84

CATALYTIC ACTIVITY: Reaction=Hydrolyzes the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where P1' and P2' are amino acids with aliphatic side chains and P3' is any C-terminal residue.; EC=3.4.24.84; Evidence={ECO:0000256|ARBA:ARBA00044456, ECO:0000256|RuleBase:RU366005};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR627057-2, ECO:0000256|RuleBase:RU366005}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR627057-2, ECO:0000256|RuleBase:RU366005};

Endoplasmic reticulum;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc

adult walking behavior [GO:0007628]; bone mineralization [GO:0030282]; CAAX-box protein processing [GO:0071586]; calcium ion import into sarcoplasmic reticulum [GO:1990036]; CAMKK-AMPK signaling cascade [GO:0061762]; cardiac conduction [GO:0061337]; cardiac muscle cell development [GO:0055013]; cardiac ventricle development [GO:0003231]; cellular lipid metabolic process [GO:0044255]; cellular response to gamma radiation [GO:0071480]; determination of adult lifespan [GO:0008340]; DNA repair [GO:0006281]; growth plate cartilage development [GO:0003417]; hair follicle development [GO:0001942]; heart morphogenesis [GO:0003007]; inflammatory cell apoptotic process [GO:0006925]; kidney morphogenesis [GO:0060993]; liver development [GO:0001889]; maintenance of rDNA [GO:0043007]; multicellular organism growth [GO:0035264]; negative regulation of miRNA processing [GO:1903799]; neuromuscular process [GO:0050905]; nuclear envelope organization [GO:0006998]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; prenylated protein catabolic process [GO:0030327]; regulation of autophagy [GO:0010506]; regulation of bone mineralization [GO:0030500]; regulation of cell shape [GO:0008360]; regulation of cellular senescence [GO:2000772]; regulation of defense response to virus [GO:0050688]; regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043516]; regulation of fibroblast proliferation [GO:0048145]; regulation of glucose metabolic process [GO:0010906]; regulation of hormone metabolic process [GO:0032350]; regulation of lipid metabolic process [GO:0019216]; regulation of mitotic cell cycle DNA replication [GO:1903463]; regulation of multicellular organism growth [GO:0040014]; regulation of stress-activated protein kinase signaling cascade [GO:0070302]; regulation of termination of RNA polymerase I transcription [GO:2000730]; regulation of TOR signaling [GO:0032006]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]; response to DNA damage checkpoint signaling [GO:0072423]; thymus development [GO:0048538]; ventricular cardiac muscle tissue development [GO:0003229]

endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; protein-containing complex [GO:0032991]

double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU366005}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU366005}.

IPR027057;IPR001915;IPR032456;

3.30.2010.10;

A0A1D5Q874

MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSSSGSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASGSGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRKSEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHTYLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTSLLQVILQVVIPRLAVISINQVVAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEARLRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADVKGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAHCCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKLESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEDSLLSLPEDIVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHVQSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAFIVLLFITAIQSLLPSSRVMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINETYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTGVLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETIYAGLFLRYDNLNHSGEDFLGTKEASLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVARHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDELLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKHSFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLILKDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLVQSLNRQRQKQLLNENNNTGIIKGHYNRRTLLSPSGTEPGAQAEGTDKSDLP

Macaca mulatta (Rhesus macaque)

FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. {ECO:0000256|PIRNR:PIRNR039050}.

4.6.1.1

CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000256|ARBA:ARBA00001593, ECO:0000256|PIRNR:PIRNR039050};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR039050}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936};

ATP-binding;cAMP biosynthesis;Lyase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Reference proteome;Transmembrane;Transmembrane helix

adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP biosynthetic process [GO:0006171]; cellular response to glucagon stimulus [GO:0071377]; cellular response to morphine [GO:0071315]; glucose mediated signaling pathway [GO:0010255]; intracellular signal transduction [GO:0035556]; locomotory behavior [GO:0007626]; long-term memory [GO:0007616]; neuroinflammatory response [GO:0150076]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of long-term synaptic depression [GO:1900454]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of synaptic plasticity [GO:0031915]; regulation of cellular response to stress [GO:0080135]; regulation of cytosolic calcium ion concentration [GO:0051480]

apical plasma membrane [GO:0016324]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body membrane [GO:0032809]; postsynaptic density [GO:0014069]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]

adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR001054;IPR018297;IPR032628;IPR030672;IPR009398;IPR029787;

3.30.70.1230;

A0A1D5Q9I1

MGCGCSSHPEDDWMENIDVCENCHYPIVPLDGKGTLLIRNGSEVRDPLVTYEGSNPPASPLQGDPRQQGLKDKACRSLAVGFHLTPTYSLPGPAFLVPRPVTPGFLPIPARFSLMPLVFTDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTSSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMPCPENCPEELYQLMRLCWKERPEDRPTFDYLRSVLEDFFTATEGQYQPQP

Macaca mulatta (Rhesus macaque)

2.7.10.2

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000256|ARBA:ARBA00001149, ECO:0000256|RuleBase:RU362096};

ATP-binding;Cell membrane;Cytoplasm;Kinase;Lipoprotein;Membrane;Nucleotide-binding;Palmitate;Phosphoprotein;Reference proteome;SH2 domain;SH3 domain;Transferase;Tyrosine-protein kinase

B cell receptor signaling pathway [GO:0050853]; Fc-gamma receptor signaling pathway [GO:0038094]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; intracellular zinc ion homeostasis [GO:0006882]; phosphorylation [GO:0016310]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of T cell activation [GO:0050870]; response to xenobiotic stimulus [GO:0009410]; T cell differentiation [GO:0030217]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]

cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; immunological synapse [GO:0001772]; membrane raft [GO:0045121]; pericentriolar material [GO:0000242]

ATP binding [GO:0005524]; ATPase binding [GO:0051117]; CD4 receptor binding [GO:0042609]; CD8 receptor binding [GO:0042610]; identical protein binding [GO:0042802]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol 3-kinase binding [GO:0043548]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; phosphotyrosine residue binding [GO:0001784]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; protein serine/threonine phosphatase activity [GO:0004722]; SH2 domain binding [GO:0042169]; signaling receptor binding [GO:0005102]; T cell receptor binding [GO:0042608]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004423}.

IPR011009;IPR035850;IPR035749;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR036028;IPR001452;IPR008266;IPR020635;

3.30.505.10;2.30.30.40;1.10.510.10;