Datasets:

lhallee

/

exp_new_unprocessed

like 0

A0A0B4LFK8

MEDVEIKPRGYQLRLVDHLTKSNGIVYLPTGSGKTFVAILVLKRFSQDFDKPIESGGKRALFMCNTVELARQQAMAVRRCTNFKVGFYVGEQGVDDWTRGMWSDEIKKNQVLVGTAQVFLDMVTQTYVALSSLSVVIIDECHHGTGHHPFREFMRLFTIANQTKLPRVVGLTGVLIKGNEITNVATKLKELEITYRGNIITVSDTKEMENVMLYATKPTEVMVSFPHQEQVLTVTRLISAEIEKFYVSLDLMNIGVQPIRRSKSLQCLRDPSKKSFVKQLFNDFLYQMKEYGIYAASIAIISLIVEFDIKRRQAETLSVKLMHRTALTLCEKIRHLLVQKLQDMTYDDDDDNVNTEEVIMNFSTPKVQRFLMSLKVSFADKDPKDICCLVFVERRYTCKCIYGLLLNYIQSTPELRNVLTPQFMVGRNNISPDFESVLERKWQKSAIQQFRDGNANLMICSSVLEEGIDVQACNHVFILDPVKTFNMYVQSKGRARTTEAKFVLFTADKEREKTIQQIYQYRKAHNDIAEYLKDRVLEKTEPELYEIKGHFQDDIDPFTNENGAVLLPNNALAILHRYCQTIPTDAFGFVIPWFHVLQEDERDRIFGVSAKGKHVISINMPVNCMLRDTIYSDPMDNVKTAKISAAFKACKVLYSLGELNERFVPKTLKERVASIADVHFEHWNKYGDMTATVNKADKSKDRTYKTECPLEFYDALPRVGEICYAYEIFLEPQFESCEYTEHMYLNLQTPRNYAILLRNKLPRLAEMPLFSNQGKLHVRVANAPLEVIIQNSEQLELLHQFHGMVFRDILKIWHPFFVLDRRSKENSYLVVPLILGAGEQKCFDWELMTNFRRLPQSHGSNVQQREQQPAPRPEDFEGKIVTQWYANYDKPMLVTKVHRELTPLSYMEKNQQDKTYYEFTMSKYGNRIGDVVHKDKFMIEVRDLTEQLTFYVHNRGKFNAKSKAKMKVILIPELCFNFNFPGDLWLKLIFLPSILNRMYFLLHAEALRKRFNTYLNLHLLPFNGTDYMPRPLEIDYSLKRNVDPLGNVIPTEDIEEPKSLLEPMPTKSIEASVANLEITEFENPWQKYMEPVDLSRNLLSTYPVELDYYYHFSVGNVCEMNEMDFEDKEYWAKNQFHMPTGNIYGNRTPAKTNANVPALMPSKPTVRGKVKPLLILQKTVSKEHITPAEQGEFLAAITASSAADVFDMERLEILGDSFLKLSATLYLASKYSDWNEGTLTEVKSKLVSNRNLLFCLIDADIPKTLNTIQFTPRYTWLPPGISLPHNVLALWRENPEFAKIIGPHNLRDLALGDEESLVKGNCSDINYNRFVEGCRANGQSFYAGADFSSEVNFCVGLVTIPNKVIADTLEALLGVIVKNYGLQHAFKMLEYFKICRADIDKPLTQLLNLELGGKKMRANVNTTEIDGFLINHYYLEKNLGYTFKDRRYLLQALTHPSYPTNRITGSYQELEFIGDAILDFLISAYIFENNTKMNPGALTDLRSALVNNTTLACICVRHRLHFFILAENAKLSEIISKFVNFQESQGHRVTNYVRILLEEADVQPTPLDLDDELDMTELPHANKCISQEAEKGVPPKGEFNMSTNVDVPKALGDVLEALIAAVYLDCRDLQRTWEVIFNLFEPELQEFTRKVPINHIRQLVEHKHAKPVFSSPIVEGETVMVSCQFTCMEKTIKVYGFGSNKDQAKLSAAKHALQQLSKCDA

Drosophila melanogaster (Fruit fly)

3.1.26.3

CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; Evidence={ECO:0000256|ARBA:ARBA00000109};

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

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

apoptotic DNA fragmentation [GO:0006309]; cellular response to virus [GO:0098586]; defense response to virus [GO:0051607]; detection of virus [GO:0009597]; dosage compensation by hyperactivation of X chromosome [GO:0009047]; dsRNA transport [GO:0033227]; global gene silencing by mRNA cleavage [GO:0098795]; locomotory behavior [GO:0007626]; positive regulation of defense response to virus by host [GO:0002230]; regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194]; RISC complex assembly [GO:0070922]; siRNA processing [GO:0030422]

cytoplasm [GO:0005737]; nucleus [GO:0005634]; RISC complex [GO:0016442]

ATP binding [GO:0005524]; deoxyribonuclease I activity [GO:0004530]; helicase activity [GO:0004386]; ribonuclease III activity [GO:0004525]; siRNA binding [GO:0035197]

IPR011545;IPR038248;IPR005034;IPR048512;IPR014720;IPR014001;IPR001650;IPR027417;IPR003100;IPR000999;IPR036389;

3.30.160.20;3.30.160.380;3.40.50.300;2.170.260.10;1.10.1520.10;

A0A0B4LFQ3

MAAAHSHHNANMLSSDISRRNPQDEYELIQKIGSGTYGDVYKAKRIQSNELAAIKVIKLEPSDDIQIIQQEIIMMRDCRHPNIIAYYGSYLRRDKLWICMEFCGGGSLQDIYQVTGPLTEVQIAYMCRETLKGLEYLHSMGKMHRDIKGANILLTEYGDVKLADFGVSAQITATINKRKSFIGTPYWMAPEVAAVERKGGYNQLCDIWACGITAIELAELQPPMFDLHPMRALFLMSKSGFKPPTLNNKDKWSPTFHNFIKTALTKNPKKRPTAERLLQHPFVQCEMSLRVAKELLQKYQSPNPQFYYYLDGDEESVAGVPQRIASKMTSRTNGVPAQNHTLKTGMTTNSTWNERSSSPETLPSDIGDAVVGGNGGGSSNISSSGGASSGTNGLLDKHELDALPQAATKSAGDGFSHSNSPTANSGAGATGSRDNDGPSSSNSSHLYQNLLRSSSGETPAGSSSAGNNCDYRHENNQNGLEDSPRRHSSMDQLIGLLENMGKSPRTRSLSDGGTQDDDEAEKEAQPDLLNNTPPVPPKRSHKRRHTPPRPISNGLPPTPKVHMGACFSKIFNGCPLRVHCTASWIHPETRDQHLLIGAEEGIYNLNMNELHDAAIDQLFPRRTTWLYVIKDVLMSLSGKSCQLYRHDLVALHSKQTVRFSLHMNKIPERLVPRKFALTTKVPDTKCCTQCCVTRNPYNGYKYLCGATPSGIFLMQWYDPLNKFMLLKQCEWPAISIQGGGHGCVQNGHTPVFEMIITPELEYPIVCTGVRKAMNGCLKLELINMNSASWFHSEDLEYDAMATMVPRRDLLKVVRVHQVEKDAILVCYGNLIQVVTLQGNPKQHKKMVSQLNFDFNVDSIVCLPDSVLAFHKHGMQGKSLRNGEVTQEIKDMSRTYRLLGSDKVVALESQLLRTGSLGSEEGHDLYILAGHEASY

Drosophila melanogaster (Fruit fly)

FUNCTION: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. {ECO:0000256|PIRNR:PIRNR038172}.

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, ECO:0000256|PIRNR:PIRNR038172}; 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, ECO:0000256|PIRNR:PIRNR038172};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR038172};

ATP-binding;Kinase;Nucleotide-binding;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase

apoptotic process [GO:0006915]; Golgi organization [GO:0007030]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; positive regulation of TOR signaling [GO:0032008]; protein phosphorylation [GO:0006468]; regulation of cell size [GO:0008361]; regulation of growth rate [GO:0040009]; triglyceride homeostasis [GO:0070328]

cytoplasm [GO:0005737]

ATP binding [GO:0005524]; MAP kinase kinase kinase kinase activity [GO:0008349]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]

IPR001180;IPR011009;IPR021160;IPR000719;IPR017441;

1.10.510.10;

A0A0B4LFV0

MAAAHSHHNANMLSSDISRRNPQDEYELIQKIGSGTYGDVYKAKRIQSNELAAIKVIKLEPSDDIQIIQQEIIMMRDCRHPNIIAYYGSYLRRDKLWICMEFCGGGSLQDIYQVTGPLTEVQIAYMCRETLKGLEYLHSMGKMHRDIKGANILLTEYGDVKLADFGVSAQITATINKRKSFIGTPYWMAPEVAAVERKGGYNQLCDIWACGITAIELAELQPPMFDLHPMRALFLMSKSGFKPPTLNNKDKWSPTFHNFIKTALTKNPKKRPTAERLLQHPFVQCEMSLRVAKELLQKYQSPNPQFYYYLDGDEESVAGVPQRIASKMTSRTNGVPAQNHTLKTGMTTNSTWNERSSSPETLPSDIATLPLNNDTKDPLGAECSCSSHNGGAAGGGGGGGVGVGAGGAAANGSSSSSGGATVGTTHHQHQQHHQHHHHPNHLHQHQSHQLPQQQQQQSHQAAQQEHHHHHPMTSSISSGLVTANANNISSSASLASMPGLSAYLGMRSHVVGHMGMGFGMGLGMSNLRTTSIDADDDELVAADVAMNNAAAAVPGNGSGAGNGSGSGCSASAAHYLRYSSNYRSAAAAQASQAAHPHVNSNSNSNNGHGHAPITSSISSSASSASFYNRLLLLDNSSGDAVVGGNGGGSSNISSSGGASSGTNGLLDKHELDALPQAATKSAGDGFSHSNSPTANSGAGATGSRDNDGPSSSNSSHLYQNLLRSSSGETPAGSSSAGNNCDYRHENNQNGLEDSPRRHSSMDQLIGLLENMGKSPRTRSLSDGGTQDDDEAEKEAQPDLLNNTPPVPPKRSHKRRHTPPRPISNGLPPTPKVHMGACFSKIFNGCPLRVHCTASWIHPETRDQHLLIGAEEGIYNLNMNELHDAAIDQLFPRRTTWLYVIKDVLMSLSGKSCQLYRHDLVALHSKQTVRFSLHMNKIPERLVPRKFALTTKVPDTKCCTQCCVTRNPYNGYKYLCGATPSGIFLMQWYDPLNKFMLLKQCEWPAISIQGGGHGCVQNGHTPVFEMIITPELEYPIVCTGVRKAMNGCLKLELINMNSASWFHSEDLEYDAMATMVPRRDLLKVVRVHQVEKDAILVCYGNLIQVVTLQGNPKQHKKMVSQLNFDFNVDSIVCLPDSVLAFHKHGMQGKSLRNGEVTQEIKDMSRTYRLLGSDKVVALESQLLRTGSLGSEEGHDLYILAGHEASY

Drosophila melanogaster (Fruit fly)

FUNCTION: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. {ECO:0000256|PIRNR:PIRNR038172}.

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, ECO:0000256|PIRNR:PIRNR038172}; 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, ECO:0000256|PIRNR:PIRNR038172};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR038172};

ATP-binding;Kinase;Nucleotide-binding;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase

apoptotic process [GO:0006915]; Golgi organization [GO:0007030]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; positive regulation of TOR signaling [GO:0032008]; protein phosphorylation [GO:0006468]; regulation of cell size [GO:0008361]; regulation of growth rate [GO:0040009]; triglyceride homeostasis [GO:0070328]

cytoplasm [GO:0005737]

ATP binding [GO:0005524]; MAP kinase kinase kinase kinase activity [GO:0008349]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]

IPR001180;IPR011009;IPR021160;IPR000719;IPR017441;

1.10.510.10;

A0A0B4LGF5

MLRIYQNTYRRTARKAVVYSTKVACCNHSTLCGITSHPRRAQDSGSSSSNGRHRGHEEFLLAGNPARGWQMPPPSRGYGMLVVRILRGALKLRYIVLGGAIGGGVSLSKKYEEWKDGLPNFKWLEDAMPQGERWSQFSRNLIEVGSLVKNAIEVDPKLKQLGEDKLSEWRNWFDSRLDDAIEAADYQGVQIVETKDDLKAKTTVAALGITSDESRKKYEKLQSQVETLQTEIMNVQIKYQKELEKMEKENRELRQQYLILKTNKKTTAKKIKKSLIDMYSEVLDELSGYDTGYTMADHLPRVVVVGDQSSGKTSVLESIAKARIFPRGSGEMMTRAPVKVTLAEGPYHVAQFRDSDREYDLTKESDLQDLRRDVEFRMKASVRGGKTVSNEVIAMTVKGPGLQRMVLVDLPGIISTMTVDMASDTKDSIHQMTKHYMSNPNAIILCIQDGSVDAERSNVTDLVMQCDPLGRRTIFVLTKVDLAEELADPDRIRKILSGKLFPMKALGYYAVVTGRGRKDDSIDAIRQYEEDFFKNSKLFHRRGVIMPHQVTSRNLSLAVSDRFWKMVRETIEQQADAFKATRFNLETEWKNNFPRLRESGRDELFDKAKGEILDEVVTLSQISAKKWDDALSTKLWEKLSNYVFESIYLPAAQSDSFNTMVDIKLRQWAEQALPAKSVEAGWEALQQEFISLMERSKKAQDHDGIFDQLKSAVVDEAIRRHSWEDKAIDMLRVIQLNTLEDRFVHDKQEWDSAVKFLESSVNAKLVQTEETLAQMFGPGQMRRITHWQYLTQDQQKRRSVKNELDKILKNDTKHLPTLTHDELTTVRKNLQRDNVDVDTDYIRQTWFPVYRKHFLQQALQRAKDCRKAYYLYTQQGAECEISCSDVVLFWRIQQVIKITGNALRQQVINREARRLDKEIKAVLDEFSDDEEKKGYLLTGKRVLLAEELIKVRQIQEKLEEFINSLNQEK

Drosophila melanogaster (Fruit fly)

3.6.5.5

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; EC=3.6.5.5; Evidence={ECO:0000256|ARBA:ARBA00001837};

Apoptosis;Coiled coil;Lipid-binding;Membrane;Mitochondrion;Mitochondrion inner membrane;Proteomics identification;Reference proteome;Transit peptide;Transmembrane;Transmembrane helix

apoptotic process [GO:0006915]; compound eye morphogenesis [GO:0001745]; mitochondrial fusion [GO:0008053]; mitochondrion organization [GO:0007005]; positive regulation of mitochondrial fusion [GO:0010636]

cytoplasm [GO:0005737]; microtubule [GO:0005874]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]

GTP binding [GO:0005525]; GTPase activity [GO:0003924]; lipid binding [GO:0008289]; microtubule binding [GO:0008017]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.

IPR022812;IPR001401;IPR045063;IPR030381;IPR045817;IPR027417;

3.40.50.300;

A0A0B4LGK5

MASDKIKVAVRVRPFNRREIELDTKCIVEMEKQQTILQNPPPLEKIERKQPKTFAFDHCFYSLNPEDENFASQETVFDCVGRGILDNAFQGYNACIFAYGQTGSGKSYTMMGTQESKGIIPRLCDQLFSAIANKSTPELMYKVEVSYMEIYNEKVHDLLDPKPNKQSLKVREHNVMGPYVDGLSQLAVTSYQDIDNLMTEGNKSRTVAATNMNAESSRSHAVFSVVLTQILTDQATGVSGEKVSRMSLVDLAGSERAVKTGAVGDRLKEGSNINKSLTTLGLVISKLADQSNGKKSGNDKFVPYRDSVLTWLLKDNLGGNSRTVMVATISPSADNYEETLSTLRYADRAKRIVNHAVVNEDPNARIIRELRHEVETLRSMLKHATGSPVGDVQDKLAESENLMKQISQTWEEKLVKTERIQNERQQALEKMGISVQASGIKVEKNKYYLVNLNADPSLNELLVYYLKDRTLIGGRTISGQQPDIQLSGLGIQPEHCVITIEDSGLYMEPVQGARCFVNGSAAVEKTPLQNGDRILWGNHHFFRVNSPKSNNTSMCASEPQTPAQLIDYNFARDEIMQNELSNDPIQTAIARLERQHEEDKQVALEKQRQEYERQFQQLRNILSPSTPYAPYAPYDPLRMGKITPNTPTSQMRVEKWAQERDEMFRRSLGQLKTDIMRANSLVQEANFLAEEMEKKTKFSVTLQIPPANLSPNRRRGAFVSEPAILVKRTNSGSQIWTMEKLENKLIDMREMYQEHKERVLNGLPLIEPFSEDEFDDKDEDNAKPQDPFYESQENHNLIGVANIFLEVLFHDVKLDYHTPIISQQGEVAGRLQVEIERIAGQMPQDRMCESVSESSGDSRDEYDDPVDPTSNQITCRVTIKCASGLPLSLSNFVFCQYTFWGHQEMVVPVINAESTAHDQNMVFKFEHTQDFTVTINEEFLEHCIEGALSIEVWGHRSAGFSKTKGWEVEQQQAKARSLVDRWAELSRKIELWVEIHELNDNGEYSPVEVTNRNEVLTGGIYQLRQGQQRRVNVRVKPVQNSGTLPIICQSIVNVAIGSVTVRSRLQRPLDSYQEEDLTVLREKWSEALGRRRQYLDQQIQMLIKKEEKNEQERERELSLVHQWVSLTEERNAVLVPAPGSGIPGAPASWEPPSGMEPHVPVLFLNLNGDDLSAQNTNDELSVAGINSILSKEHGHKFYTLQILQHLDKDVCCVASWDSSMHDSQALNRVTEANERVYLILRTTVRLSHPAPMDLVLRKRLSINIKKGQTLTDRLKKFRLVRGENAIWQSGVTYEVVSNIPKASEELEDRESLAQLAASGDDCSASDGETYIEKYTRGVSAVESILTLDRLRQNVAVKELETAHGQPLSMRKTVSVPNFSQIMRFDASMESLLNVGRSESFADLNNSALGNKFTPAGHSPAGAGGVIRSRHSFGGKGSSDDSPGKAFGIASPATSKLLGMRMTTLHEEPLGGHRSLDEEPEDSYSDSEYAAEYEQERQQNKSMATRSRLTASKTMDSFMDVSSHSNQSYLSYTSSANANMKHLTGLATLSMSSSTSSGYGSQAVSCNNLSNEDIASMRSMSIDETPDFDRVNSNSPPNRQARVNPFLKDMPKAKIQEQPEQQAKKLQEAFTHPLEQLESSQNAQSDDDECAQLPKNNNNNLDLVNEPKPLSSQTDLEESMSQPKSKTEFATDNQNGNRSSDELSHSSEDLLEGDGIVREELPAGKVVRRKKSNTQPPSNGNSINNNNNGTTQAPRINHRASVAKMEGLAAYLDSSIMTSSTEVDEESKDVELVLPEWIVVGESVLIRPYNTSGVIRFVGTTEFQPGAWIGVELDTPTGKNDGSVKGVQYFQCKPKHGMFVRSDKLMLDKRGKAMRAYKAAEKSNSISKEMSTSMTGSMTRSKSRGDSLNLSARK

Drosophila melanogaster (Fruit fly)

3.6.1.3

ATP-binding;Coiled coil;Cytoplasm;Cytoskeleton;Hydrolase;Microtubule;Motor protein;Nucleotide-binding;Proteomics identification;Reference proteome

cytoskeleton-dependent intracellular transport [GO:0030705]; establishment of spindle orientation [GO:0051294]; microtubule-based movement [GO:0007018]

early endosome [GO:0005769]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule plus-end [GO:0035371]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; protein homodimerization activity [GO:0042803]

IPR036859;IPR000938;IPR000253;IPR022164;IPR022140;IPR032405;IPR019821;IPR001752;IPR036961;IPR027417;IPR008984;

2.60.200.20;6.10.250.2520;2.30.30.190;3.40.850.10;

A0A0B4LGY8

MAAAHSHHNANMLSSDISRRNPQDEYELIQKIGSGTYGDVYKAKRIQSNELAAIKVIKLEPSDDIQIIQQEIIMMRDCRHPNIIAYYGSYLRRDKLWICMEFCGGGSLQDIYQVTGPLTEVQIAYMCRETLKGLEYLHSMGKMHRDIKGANILLTEYGDVKLADFGVSAQITATINKRKSFIGTPYWMAPEVAAVERKGGYNQLCDIWACGITAIELAELQPPMFDLHPMRALFLMSKSGFKPPTLNNKDKWSPTFHNFIKTALTKNPKKRPTAERLLQHPFVQCEMSLRVAKELLQKYQSPNPQFYYYLDGDEESVAGVPQRIASKMTSRTNGVPAQNHTLKTGMTTNSTWNERSSSPETLPSDIPSAERSKPKLSGTLIMNMSLRSLLQYIDEELKLSGDAVVGGNGGGSSNISSSGGASSGTNGLLDKHELDALPQAATKSAGDGFSHSNSPTANSGAGATGSRDNDGPSSSNSSHLYQNLLRSSSGETPAGSSSAGNNCDYRHENNQNGLEDSPRRHSSMDQLIGLLENMGKSPRTRSLSDGGTQDDDEAEKEAQPDLLNNTPPVPPKRSHKRRHTPPRPISNGLPPTPKVHMGACFSKIFNGCPLRVHCTASWIHPETRDQHLLIGAEEGIYNLNMNELHDAAIDQLFPRRTTWLYVIKDVLMSLSGKSCQLYRHDLVALHSKQTVRFSLHMNKIPERLVPRKFALTTKVPDTKCCTQCCVTRNPYNGYKYLCGATPSGIFLMQWYDPLNKFMLLKQCEWPAISIQGGGHGCVQNGHTPVFEMIITPELEYPIVCTGVRKAMNGCLKLELINMNSASWFHSEDLEYDAMATMVPRRDLLKVVRVHQVEKDAILVCYGNLIQVVTLQGNPKQHKKMVSQLNFDFNVDSIVCLPDSVLAFHKHGMQGKSLRNGEVTQEIKDMSRTYRLLGSDKVVALESQLLRTGSLGSEEGHDLYILAGHEASY

Drosophila melanogaster (Fruit fly)

FUNCTION: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. {ECO:0000256|PIRNR:PIRNR038172}.

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, ECO:0000256|PIRNR:PIRNR038172}; 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, ECO:0000256|PIRNR:PIRNR038172};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR038172};

ATP-binding;Kinase;Nucleotide-binding;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase

apoptotic process [GO:0006915]; Golgi organization [GO:0007030]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; positive regulation of TOR signaling [GO:0032008]; protein phosphorylation [GO:0006468]; regulation of cell size [GO:0008361]; regulation of growth rate [GO:0040009]; triglyceride homeostasis [GO:0070328]

cytoplasm [GO:0005737]

ATP binding [GO:0005524]; MAP kinase kinase kinase kinase activity [GO:0008349]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]

IPR001180;IPR011009;IPR021160;IPR000719;IPR017441;

1.10.510.10;

A0A0B4LHX7

MNGGGRTPALTRSCSSPAVYDIETHPASPVFPHLLLGNGRDADDPSSVGANCVLNVTCQSPNESHLQGLKYMQIPASDTPHQNIKQYFQEAYDFIEDARKTGSRVLLHCHAGISRSATIAIAYVMRYKSLSLLEAYKLVKVARPIISPNLNFMGQLLELEQNLRKSGVLAPATPHLNSPSNPSSSSVGLSTQSSQLVEQPEEEEKREQRERGKSKSDSEAMDEDGFDYDDVDSGSGSLAGSNCSSRLTSPPITPDDEAPSTSAAASSVSELDSPSSTSSSSGICSLLQSTSSSVSPRAISKPNLLSPTRQLALFKRNSPAKLRLDLESSYAPASPIPNTMPWLSVPSTPVCEEAPDSRINHVASNLTRD

Drosophila melanogaster (Fruit fly)

3.1.3.16; 3.1.3.48

Hydrolase;Protein phosphatase;Reference proteome

actin cytoskeleton organization [GO:0030036]; cellular response to oxidative stress [GO:0034599]; chitin-based embryonic cuticle biosynthetic process [GO:0008362]; chorion micropyle formation [GO:0046844]; compound eye development [GO:0048749]; determination of adult lifespan [GO:0008340]; determination of digestive tract left/right asymmetry [GO:0071907]; dorsal appendage formation [GO:0046843]; dorsal closure [GO:0007391]; embryonic anterior midgut (ectodermal) morphogenesis [GO:0048615]; epidermis development [GO:0008544]; follicle cell of egg chamber development [GO:0030707]; imaginal disc eversion [GO:0007561]; imaginal disc fusion [GO:0046528]; imaginal disc fusion, thorax closure [GO:0046529]; JNK cascade [GO:0007254]; negative regulation of apoptotic process [GO:0043066]; negative regulation of MAPK cascade [GO:0043409]; positive regulation of border follicle cell migration [GO:1903688]; positive regulation of immune response [GO:0050778]; protein dephosphorylation [GO:0006470]; protein secretion [GO:0009306]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; response to oxidative stress [GO:0006979]; wound healing [GO:0042060]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]

JUN kinase phosphatase activity [GO:0008579]; MAP kinase tyrosine phosphatase activity [GO:0033550]; MAP kinase tyrosine/serine/threonine phosphatase activity [GO:0017017]; myosin phosphatase activity [GO:0017018]; phosphoprotein phosphatase activity [GO:0004721]; protein tyrosine/threonine phosphatase activity [GO:0008330]

IPR000340;IPR029021;IPR016130;IPR000387;IPR020422;

3.90.190.10;

A0A0B4U9L8

MLQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPQKLTALLKGAIQQPEQKYEDAMQYEFKVNGKPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGHIQNDAHLTASISACNGLKGHFQLRGETYLIEPLKIPDSEAHAVYKYENVEKEDEGPKKCGVTQTNWKSDEPIKASQFILTPEQRAYMNANKYIKLAIVVDNVMFRKYTGNFTAIRTRIYEIVNTLNLIYTILNIHIALVFLEIWSKGDSINVQSVVDVTLNSFGEWRERDLLNRKRHDNAQLLTGINFNGDTIGFGFVGSMCIPKKSVGIVQDHSKTHLLVATTMAHELGHNLGINHDGDSCTCQANSCIMAAKLSHQPSYQFSDCSINELWMYLISHTPRCILNEPLTTDVVSPAVCGNYVVEEGEECDCGSLWYCRNPCCDAATCKLKPGAECGDGVCCYQCRFVTAGTVCRPARSECDIPEYCSGQSVECPMDHIQKNGKPCLMNHGYCYNGRCPIMIHQCIALWGPGTTVSSDVCFQRNESGQGYSYCRRENNQNIPCAPQDVKCGRLYCKFHNVNTLPCNFKYSDFAPDYGLVDHGTKCGDGKVCNSNRQCVDVNTAY

Vipera ammodytes ammodytes (Western sand viper)

FUNCTION: Zinc metalloprotease that has fibrinogenolytic activity. Does not have hemorrhagic activity in rats. Cleaves insulin B chain at '38-Ala-|-Leu-39' and '40-Tyr-|-Leu-41' bonds. Hydrolyzes only partially and weakly isolated extracellular matrix (ECM) bovine fibronectin and basal membrane (BM) protein human collagen IV in vitro. Murine laminin is not hydrolyzed, neither isolated nor in a solubilized BM preparation. Nidogen is hydrolyzed at '350-Ser-|-Phe-351' bond in a solubilized BM preparation. Hydrolyzes plasma proteins involved in blood coagulation in vitro. Has alpha-fibrinogenase activity cleaving human fibrinogen alpha chain at '432-Lys-|-Leu-433' bond, but does not cleave beta or gamma chains. Does not cleave fibrin. Hydrolyzes only partially bovine prothrombin at '200-Ser-|-Gly-201' bond, factor X (FX) heavy chain, and very slowly, FX light chain and plasminogen in vitro, without activating any of them. Has no effect in plasma thrombin generation. Does not inhibit platelet aggregation induced by collagen in vitro. May have a delayed pathological action as an anticoagulant in envenomed patients after they received serotherapy as it is not recognized by the venom antiserum. {ECO:0000269|PubMed:25549999}.

3.4.24.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9DGB9}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9DGB9};

Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen

envenomation resulting in modulation of blood coagulation in another organism [GO:0044468]; envenomation resulting in modulation of process in another organism [GO:0035738]; proteolysis [GO:0006508]

extracellular region [GO:0005576]; extraorganismal space [GO:0043245]; plasma membrane [GO:0005886]

metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25549999}.

PTM: N-glycosylated. {ECO:0000269|PubMed:25549999}.; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:25549999}.

IPR006586;IPR018358;IPR001762;IPR036436;IPR024079;IPR001590;IPR002870;IPR034027;

3.40.390.10;4.10.70.10;

A0A0B5CYA5

MNLWELEDHKSCRETPRPAQEPTAEEVMTTELQMKVDFFRKLGYSSAEIHSVLQKLGVQADTNTVLGELVKHGSAAERECQVSPDPCPQLPLVPRGGGTPKAPTVEPSPSEEDKEGGDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDAPITDQHILRDLEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAFESDGIMVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLSAEHRKQPCPYGRKCTYGIKCRFFHPERPSRPQRSVADELRANALLSPPRPPSKDKNGRRPSPPQPGSLPTEHEQCSLEGKKLGVQATPGTPREGLTQPFAQAGRSLPPSGGSGGSFGPSDWFPQTLDSLPYTSQDCLDSGIGSLESQMSELWGVRGGGPGEPGPSRGPYTGYSPYGAKLPATQAFSAFGRPVGAGHFSVPADYAPPPSAFPPREYWSEPYQLPPPAPVLQEPRVPGPGADRGPWGGGSSLAKERASVYTKLCGVFPPHLVEAVMERFPQLLDPQQLAAEILSYKSQQLNE

Sus scrofa (Pig)

3.1.-.-

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

Endonuclease;Hydrolase;Magnesium;Metal-binding;Nuclease;Reference proteome;Zinc;Zinc-finger

3'-UTR-mediated mRNA destabilization [GO:0061158]; cellular response to chemokine [GO:1990869]; cellular response to glucose starvation [GO:0042149]; cellular response to ionomycin [GO:1904637]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to oxidative stress [GO:0034599]; cellular response to sodium arsenite [GO:1903936]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to virus [GO:0098586]; DNA damage response [GO:0006974]; miRNA catabolic process [GO:0010587]; mRNA catabolic process [GO:0006402]; negative regulation by host of viral genome replication [GO:0044828]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of cardiac muscle contraction [GO:0055118]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of muscle cell apoptotic process [GO:0010656]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of type II interferon production [GO:0032689]; positive regulation of angiogenesis [GO:0045766]; positive regulation of autophagy [GO:0010508]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of execution phase of apoptosis [GO:1900119]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of gene expression [GO:0010628]; positive regulation of lipid storage [GO:0010884]; positive regulation of miRNA catabolic process [GO:2000627]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of protein deubiquitination [GO:1903003]; 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]; protein complex oligomerization [GO:0051259]; T cell receptor signaling pathway [GO:0050852]

cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-body [GO:0000932]; protein-containing complex [GO:0032991]; rough endoplasmic reticulum membrane [GO:0030867]

chromatin binding [GO:0003682]; cysteine-type deubiquitinase activity [GO:0004843]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; miRNA binding [GO:0035198]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA binding [GO:0003729]; ribosome binding [GO:0043022]; RNA endonuclease activity [GO:0004521]; RNA exonuclease activity [GO:0004532]; RNA stem-loop binding [GO:0035613]

IPR040546;IPR040757;IPR021869;

3.40.50.11980;

A0A0B5KYT4

MESLSLTWITAIAVVLYLVQRYVRSYWRLKDIPGPVLAKLTDLQRVWWVKTGRAHEFHRDMHAMYGPIVRFGPNMVSVSDPRVIPTIYPSRPGFPKGDFYRTQKPYTRNKGAMPAVFNTQDEDLHKQLRSPIASLYSMTNVVRLEPLVDETLTVLSKQLDERFVGTNDKPFDLGDWLQYFAFDSMGTLTFSRRYGFLEQGRDMHGILQEIWNFMTRVAVMGQIPWFDEIWNKNSFITLFKRPTGFGVLKVVDNFISQRVSSRENDEKADEKDMLSQFLNIQASNPHSIMPWAPRAWTFSNVMAGSDSTANVMRTMMYNLLVDRDTLKSLRAELLEAESSNGLSRSLPSWDGVRSLPYLDACVLEALRLHPPFCLPFERVVPEGGITVCETYLPAGTVVGISPYLANRDKQTFGDDADKWRPSRWLDLSREDRVKLENSILTFGAGRRTCLGKNIAILEIKKLFPMLLLNYEIEIVNPENYQTTNAWFFRQWGLHAVIRKLPAPERDDTIEQKASIPPALNIPPSSSTVDVRIIDSGTLLDLRPDLFWTPDLPGLLKVTAPTYCFLISNGSRHVLFDLAVRQDWENLPPSIVAMIKSQTVIQEPRNISDVLDSDESSLGIRSKDIEAIIWSHAHFDHIGDPSTFPPSTELVVGPGIRDTHWPGFPTNPDAINLNTDIQGRNVREISFEKTQKGATKIGSFDAMDYFGDGSFYLLDAAGHSVGHIGALARVTTSPDSFVFMGGDSCHHAGVLRPTKYLPCPLDSGDTSLPCKSDSVFTLSPALPTDYTAALRTVENIKELDACEDVFVVLAHDATLKGKVDFYPSKINDWKAKEYGKKTKWLFYKDIENAIEGQK

Penicillium brevicompactum

FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:31209052). MpaDE' is an endoplasmic reticulum-bound enzyme that catalyzes the conversion of 5-methylorsellinic acid (5MOA) into the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) (PubMed:31209052). MpaDE' first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB), and then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP (PubMed:31209052). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable) (PubMed:31209052). {ECO:0000269|PubMed:31209052, ECO:0000305|PubMed:31209052}.

1.-.-.-

CATALYTIC ACTIVITY: Reaction=5-methylorsellinate + O2 + reduced [NADPH--hemoprotein reductase] = 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:66668, 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:146172, ChEBI:CHEBI:167385; Evidence={ECO:0000269|PubMed:31209052}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66669; Evidence={ECO:0000269|PubMed:31209052}; CATALYTIC ACTIVITY: Reaction=4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoate + H(+) = 5,7-dihydroxy-4-methylphthalide + H2O; Xref=Rhea:RHEA:66672, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:68194, ChEBI:CHEBI:167385; Evidence={ECO:0000269|PubMed:31209052}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66673; Evidence={ECO:0000269|PubMed:31209052};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31209052}.

Endoplasmic reticulum;Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Transmembrane;Transmembrane helix

mycophenolic acid biosynthetic process [GO:0140722]; terpenoid biosynthetic process [GO:0016114]

endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31209052}; Single-pass membrane protein {ECO:0000255}.

IPR001128;IPR017972;IPR002403;IPR036396;IPR001279;IPR036866;

1.10.630.10;3.60.15.10;

A0A0B5LB55

MSTEKFTITEHLVPGSHIREYPGSTVNQEDVLKIHVKQYTPKREGPVPDDAITFIATHGVGLPKELYEPLWDELLDQASGFHIRAIWMADVASMNQSGIHNEDKLSMDCSWMDHARDLLLMINHFRDQMPRPLVGIGHSFGGNIITNLAYLHPRLFTTLLLLDPLIQLSPPSLGFGTDAPSAINYTLWRDDVWPSREVAIRANRAIMQGMDPRCLDRMTKHFFRDLPTPLYPDVEAIKALFGTTADSTTTPVTLTTPKYHELVAQIRQNFNARDPKTGRIEVPRDTHADMDPLVAYIPLYRPEPRSTFRRLETLRPSCLWVIAGATFLNIDEIREGVKICGSGIGGSGGVPDGRVREVVLPGFGHLMPFQEVKTVAETCIVWLQQEMDRFRQTERQWKEDRDGKSHLAVEENWYKVLKPIPSGRKKRNDKGKL

Penicillium brevicompactum

FUNCTION: Type I acyl-CoA thioesterase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:31209052, PubMed:33843134). MpaH' acts as a peroxisomal acyl-CoA hydrolase that converts MPA-CoA into the final product MPA (PubMed:31209052, PubMed:33843134). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable) (PubMed:31209052). {ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134, ECO:0000305|PubMed:31209052}.

3.1.1.-

CATALYTIC ACTIVITY: Reaction=H2O + mycophenolyl-CoA = CoA + H(+) + mycophenolate; Xref=Rhea:RHEA:66704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:62932, ChEBI:CHEBI:167447; Evidence={ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66705; Evidence={ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=722.3 uM for acetyl-CoA {ECO:0000269|PubMed:31209052}; KM=351.5 uM for propionyl-CoA {ECO:0000269|PubMed:31209052}; KM=76.37 uM for malonyl-CoA {ECO:0000269|PubMed:31209052}; KM=201.9 uM for isobutyryl-CoA {ECO:0000269|PubMed:31209052}; KM=780.83 uM for isovaleryl-CoA {ECO:0000269|PubMed:31209052}; KM=217.9 uM for benzoyl-CoA {ECO:0000269|PubMed:31209052}; KM=143 uM for N-decanoyl-CoA {ECO:0000269|PubMed:31209052}; KM=260.2 uM for lauroyl-CoA {ECO:0000269|PubMed:31209052}; KM=577 uM for palmitoyl-CoA {ECO:0000269|PubMed:31209052}; KM=316.6 uM for arachidonoyl-CoA {ECO:0000269|PubMed:31209052}; KM=382.6 uM for DMMPA-CoA {ECO:0000269|PubMed:31209052}; KM=117.5 uM for MPA-CoA {ECO:0000269|PubMed:31209052}; Note=The kcat values are 54.98 min(-1) for acetyl-CoA, 24.58 min(-1) for propionyl-CoA, 12.94 min(-1) for malonyl-CoA, 7.688 min(-1) for isobutyryl-CoA, 5.718 min(-1) for isovaleryl-CoA, 3.891 min(-1) for benzoyl-CoA, 136.5 min(-1) for N-decanoyl-CoA, 99.11 min(-1) for lauroyl-CoA, 23.19 min(-1) for palmitoyl-CoA, 47.35 min(-1) for arachidonoyl-CoA, 4438 min(-1) for DMMPA-CoA and 9578 min(-1) for MPA-CoA. {ECO:0000269|PubMed:31209052};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134}.

3D-structure;Hydrolase;Peroxisome

mycophenolic acid biosynthetic process [GO:0140722]; terpenoid biosynthetic process [GO:0016114]

peroxisomal matrix [GO:0005782]

fatty acyl-CoA hydrolase activity [GO:0047617]; hydrolase activity [GO:0016787]; polyketide synthase activity [GO:0016218]

SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:31209052}. Note=The mpaH' location in peroxisomes is required for the unique cooperation between biosynthetic and beta-oxidation catabolism machineries to produce final MPA. {ECO:0000269|PubMed:31209052}.

IPR029058;IPR000073;

3.40.50.1820;

A0A0C3VJP4

MEKVSLYACLILNLSLLVIFPYSKASQADKLNEFILSRKSQNPPKTLSWEEGDALKTLFSSAAYVAPPQEELRLADKIVTLPGQPYGVNFDQYSGYVTVDPETGRELFYYFVESPCNSSTKPLVLWLNGGPGCSSLGYGAFQELGPFRVNSDGKTLYRNPYAWNEVANVLFLESPAGIGFSYSNTTSDYDKSGDKSTAKDSYVFLINWLERFPQYKTRDFYISGESYAGHYVPQLASTILHNNKLYKNTIINLKGISLGNAWIDDATSLKGLYDNLWTHALNSDQTHELIEKYCDFTKQNYSAICTNAMNMSMIEKGKIDSFNIYAPLCHDSTLKNGSTGYVSNDLDPCSDYYGTAYLNRPEVQKALHAKPTNWSHCSDSINLNWKDSPITILPTIKYLIDNGIKLWIYSGDTDAVGVTISRYPINTLKLPIDSTWRPWYSGKEIGGYVVGYKGLTFVTVRGAGHLVPSWQPERALTLISSFLYGILPASVSPSN

Medicago truncatula (Barrel medic) (Medicago tribuloides)

FUNCTION: Carboxypeptidase that, together with KPI106, controls mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis). {ECO:0000269|PubMed:23662629}.

3.4.16.-

Apoplast;Carboxypeptidase;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal

arbuscular mycorrhizal association [GO:0036377]; proteolysis [GO:0006508]; response to symbiotic fungus [GO:0009610]

apoplast [GO:0048046]; extracellular space [GO:0005615]; vacuole [GO:0005773]

serine-type carboxypeptidase activity [GO:0004185]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23662629}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:23662629}.

IPR029058;IPR001563;IPR033124;IPR018202;

3.40.50.11320;6.10.250.940;3.40.50.1820;

A0A0C5CJR8

MSKAKDKAIVSAAQASTAYSQIDSFSHLYDRGGNLTINGKPSYTVDQAATQLLRDGAAYRDFDGNGKIDLTYTFLTSASSSTMNKHGISGFSQFNAQQKAQAALAMQSWSDVANVTFTEKASGGDGHMTFGNYSSGQDGAAAFAYLPGTGAGYDGTSWYLTNNSYTPNKTPDLNNYGRQTLTHEIGHTLGLAHPGDYNAGEGAPTYNDATYGQDTRGYSLMSYWSESNTNQNFSKGGVEAYASGPLIDDIAAIQKLYGANYNTRAGDTTYGFNSNTGRDFLSATSNADKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGLVGNVSIAKGVTIENAFGGAGNDLIIGNNAANVIKGGAGNDLIYGAGGADQLWGGAGNDTFVFGASSDSKPGAADKIFDFTSGSDKIDLSGITKGAGLTFVNAFTGHAGDAVLTYAAGTNLGTLAVDFSGHGVADFLVTTVGQAAVSDIVA

Pseudomonas marginalis (Pseudomonas panacis)

FUNCTION: Peptidase able to cleave azocasein and the milk substrates beta-casein and Na-caseinate. Can withstand UHT processing of milk, and is able to spoil UHT milk over the storage period. {ECO:0000269|Ref.1}.

3.4.24.-

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q03023}; Note=Binds 8 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:Q03023}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q03023}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q03023};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|Ref.1};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. At higher temperatures, the activity decreases rapidly. Shows high enzyme activity with casein as a substrate under the storage conditions of UHT milk. Is highly thermostable. Withstands general ultra-high temperature (UHT) processing (138 degrees Celsius for 18 seconds) in skim milk, with 88% of the initial enzyme activity remaining after heating. The milk matrix has a protective effect on the enzyme activity during the thermal process. {ECO:0000269|Ref.1};

Calcium;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Signal;Zinc

collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]

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

calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.

IPR018511;IPR001343;IPR024079;IPR001818;IPR016294;IPR013858;IPR006026;IPR034033;IPR011049;

3.40.390.10;2.150.10.10;

A0A0C5Q4Y6

MDSFPLLAALFFILAATWFISFRRPRNLPPGPFPYPIVGNMLQLGTQPHETFAKLSKKYGPLMSIHLGSLYTVIVSSPEMAKEIMHKYGQVFSGRTVAQAVHACGHDKISMGFLPVGGEWRDMRKICKEQMFSHQSMEDSQWLRKQKLQQLLEYAQKCSERGRAIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLAIIEGFLNERVESRRTNPNAPKKDDFLETLVDTLQTNDNKLKTDHLTHLMLDLFVGGSETSTTEIEWIMWELLANPEKMAKMKAELKSVMGEEKVVDESQMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGAQVLINAWAIGRDHSIWKNPDSFEPERFLDQKIDFKGTDYELIPFGSGRRVCPGMPLANRILHTVTATLVHNFDWKLERPEASDAHRGVLFGFAVRRAVPLKIVPFKV

Rosmarinus officinalis (Rosemary) (Salvia rosmarinus)

FUNCTION: Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of abietatriene to produce ferruginol (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol (PubMed:27703160). Ferruginol and 11-hydroxyferruginol are intermediates in the biosynthesis of carnosate, a potent antioxidant (PubMed:26020634, PubMed:27703160). May also convert miltiradiene into 11-oxomiltiradiene (By similarity). {ECO:0000250|UniProtKB:A0A0S1TP26, ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}.

1.14.14.-; 1.14.14.175; 1.14.14.60

CATALYTIC ACTIVITY: Reaction=abieta-8,11,13-triene + O2 + reduced [NADPH--hemoprotein reductase] = ferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48080, 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:78274, ChEBI:CHEBI:86062; EC=1.14.14.175; Evidence={ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48081; Evidence={ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}; CATALYTIC ACTIVITY: Reaction=ferruginol + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxyferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55428, 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:78274, ChEBI:CHEBI:138942; EC=1.14.14.60; Evidence={ECO:0000269|PubMed:27703160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55429; Evidence={ECO:0000269|PubMed:27703160}; CATALYTIC ACTIVITY: Reaction=miltiradiene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 11-oxomiltiradiene + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:66796, 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:65037, ChEBI:CHEBI:167496; Evidence={ECO:0000250|UniProtKB:A0A0S1TP26}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66797; Evidence={ECO:0000250|UniProtKB:A0A0S1TP26};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q94IP1};

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

Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Transmembrane;Transmembrane helix

diterpenoid biosynthetic process [GO:0016102]

membrane [GO:0016020]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]

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

IPR001128;IPR017972;IPR002401;IPR036396;

1.10.630.10;

A0A0C5QRZ2

MDPFPLVAAALFIAATWFITFKRRRNLPPGPFPYPIVGNMLQLGSQPHETFAKLSKKYGPLMSIHLGSLYTVIISSPEMAKEIMHKYGQVFSGRTIAQAVHACDHDKISMGFLPVGAEWRDMRKICKEQMFSHQSMEDSQNLRKQKLQQLLEYAQKCSEEGRGIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLGLIEGYLNERIEFRKANPNAPKKDDFLETLVDALDAKDYKLKTEHLTHLMLDLFVGGSETSTTEIEWIMWELLASPEKMAKVKAELKSVMGGEKVVDESMMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGAQVLINAWAMGRDPSLWKNPDSFEPERFLDQKIDFKGTDYELIPFGSGRRVCPGMPLANRILHTVTATLVHNFDWKLERPEASDAHKGVLFGFAVRRAVPLKIVPIKA

Salvia fruticosa (Greek sage)

FUNCTION: Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of abietatriene to produce ferruginol (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol (PubMed:27703160). Ferruginol and 11-hydroxyferruginol are intermediates in the biosynthesis of carnosate, a potent antioxidant (PubMed:26020634, PubMed:27703160). May also convert miltiradiene into 11-oxomiltiradiene (By similarity). {ECO:0000250|UniProtKB:A0A0S1TP26, ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}.

1.14.14.-; 1.14.14.175; 1.14.14.60

CATALYTIC ACTIVITY: Reaction=abieta-8,11,13-triene + O2 + reduced [NADPH--hemoprotein reductase] = ferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48080, 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:78274, ChEBI:CHEBI:86062; EC=1.14.14.175; Evidence={ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48081; Evidence={ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}; CATALYTIC ACTIVITY: Reaction=ferruginol + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxyferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55428, 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:78274, ChEBI:CHEBI:138942; EC=1.14.14.60; Evidence={ECO:0000269|PubMed:27703160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55429; Evidence={ECO:0000269|PubMed:27703160}; CATALYTIC ACTIVITY: Reaction=miltiradiene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 11-oxomiltiradiene + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:66796, 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:65037, ChEBI:CHEBI:167496; Evidence={ECO:0000250|UniProtKB:A0A0S1TP26}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66797; Evidence={ECO:0000250|UniProtKB:A0A0S1TP26};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q94IP1};

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

Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Transmembrane;Transmembrane helix

diterpenoid biosynthetic process [GO:0016102]

membrane [GO:0016020]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]

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

IPR001128;IPR017972;IPR002401;IPR036396;

1.10.630.10;

A0A0D1DWQ2

MKLSVSIFVLLAVSAFGGGSAAAVSGKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGGRAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTRPLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPTNMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVLLGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLTDHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRLFQAYLIPITTQIEAAAILDHANKCT

Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)

FUNCTION: Secreted chorismate mutase that is one component of a cocktail of effectors shaping the host metabolome and acting as virulence factors. The enzyme is taken up by plant cells, can spread to neighboring cells where it affects the biosynthesis of the plant immune signal salicylic acid by channelling chorismate into the phenylpropanoid pathway (PubMed:21976020, PubMed:30651637). Interferes with the activity of host cytosolic chorismate mutase CM2 through heterodimerization (PubMed:21976020). {ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:30651637}.

5.4.99.5

CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:30651637}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898; Evidence={ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:30651637};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 mM for chorismate {ECO:0000269|PubMed:30651637}; Vmax=40.8 umol/min/mg enzyme {ECO:0000269|PubMed:30651637}; Vmax=21.1 umol/min/mg enzyme (when bound to host KWL1) {ECO:0000269|PubMed:30651637};

3D-structure;Allosteric enzyme;Glycoprotein;Host cytoplasm;Isomerase;Reference proteome;Secreted;Signal;Virulence

aromatic amino acid family biosynthetic process [GO:0009073]; chorismate metabolic process [GO:0046417]; effector-mediated suppression of host salicylic acid-mediated innate immune signaling [GO:0140502]

extracellular region [GO:0005576]; host apoplast [GO:0140593]; host cell cytosol [GO:0044164]

chorismate mutase activity [GO:0004106]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21976020}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:21976020}. Note=Is translocated to host plant cells and spreads to neighboring tissue. The spreading is likely to occur through plasmodesmata. {ECO:0000269|PubMed:21976020}.

DOMAIN: The extensive loop region (ELR) is specific for fungal secreted chorismate mutases and is required for the interaction with the host defense kiwellin KWL1. {ECO:0000269|PubMed:30651637}.

IPR036263;IPR037039;

1.10.590.10;

A0A0D1DXX6

MATPSLGAGPMASAANGHTALFPPATSPPLGQEDSTEMVLELADGTAYRGISFGAEGKSVSGECVFQTGMVGYVESITDPSYEGQILVLTFPLAGNYGVPSREEATQSIQKLLASPFESSRIHVAGLVVSYYSHEFSHYLAQTGLSEWLKESGVPAIYGIDTRALTKKIRNQGSMLGKLLMPQPGASIADAAAAGDWRMAVVDLPFADPNAQNLVARVSCKKPQLYTPANTASGESLGKFEAPLLHPSGRPIRILALDVGMKYNQIRCFTSRGVELKVVPWDYDFLAESEAFDGLFISNGPGDPVSCGPTIARIAELLKLKGANKIPVFGICFPCTDQISGRCYIPFQNHGYAVNADTLPAGWKPLFSNANDDTNEGIYCTEGPFFSVQFHPESTPGPRDTEFLFDVFIRSVVDCAAVKAAPGATPATILPPVGFTGGLLADNAAATPRVRVRKVLVLGSGGLSIGQAGEFDYSGSQAIKALKEEGIYTVLINPNIATIQTSSGLADKVYFLPVTPEFVLKVIEHERPDGIYCTFGGQTALNVGIKIKDHLPKLGVRVLGTPIETIITTEDRDLFARAMEEIGEKCAPSAAANNWDEALEAAQSIGFPVIVRAAFALGGLGSGFANNVDELRKLCAAAFANSPQVLVEKSMKGWKEVEYEVVRDCRNNCITVCNMENFDPLGVHTGDSIVIAPSQTLSDDDYNMLRTTAVNVIRHLGVVGECNIQYALNPHKREYCIIEVNARLSRSSALASKATGYPLAFIAAKLGLNIPLNEIRNSVTRETSACFEPSLDYVVTKFPRWDLRKFVRVSSKLGSSMKSVGEVMSIGRTFEESIQKAIRSVDYAHDGFSQNDIVDDEDIDEELANPTDRRMFAIANAMAKGYSVDKIHQLSNIDRWFLSKLMRIMNASKVFATHNAADFPPAMLRQAKQLGFSDKQLAKALNSTELAVRKMRQEHAIMPFVKQIDTVAAEFPAYTNYLYTTYNAVEHDISFGDKGVMVLGSGVYRIGSSVEFDWCAVRAIRTLRQRGFKTIMVNYNPETVSTDYDEADRLYFENISLETVLDIYDTEQSAGVIMSMGGQTPNNIALPLYRQNVKVLGTSPEMIDMAENRYKFSRMLDKIGVDQPMWKELTSFEEAQSACARFGYPVLVRPSYVLSGAAMNVVYSPEDLNSYLSQASAINREHPVVITKYLEGAKEIEMDAVAKDGRLMMHYISEHVENAGVHSGDATLILPPQDLDPETVRRIEVATAKIAASLHITGPMNIQFIAKNNDIKVIECNVRASRSFPFVSKVTGVDAIQMATDLMLDLPVEAYPKVDLPRNYVGVKVPQFSFSRLAGADPILGVEMASTGEVACFGRDKYEAYLKAMIASGIRLPTKNVLLSIGSYSEKQELLPAVRTLHQLGFTLYGSSGSADFYSEQGIPVVHLEALPEDDESKFEDTAKASYSLLTHLTQGLSSLFISLPSKNKYRRPVSFTSMGYRARRLAIDRSIPLITNVKNAKLFVEALARHRKANSNFDISPVDFKTSHTAFTLPGLINVNAFVPSIADGKVSADELAAVTRASIAGGFTTVQVMPAGVSSSIIDAASLANAESKIAGGAHCDVSLGVSATADNHESIDQLADSARSLLVSFNGLGSNVSKAAAIASHFASWPAERPIVTDARNTDLASVLLLASLNNRSIHVTNVLSRDDIHLIALAKAKGLQVTCDVAVYALFFTTEMYPQATCLPSADDQKALWEKLDDIDMFSIGSTPYQLAKEIGEVAAPQSGIEETLLLLLDAVNEHRLTLDDILLRLYTKPMEIFGVQAQANTQVEIEIDRPTAFVRRDYWSPLESRATVGSINRVTFKGKTVFVDGEVLSDSTLGSNVSSIAKVAKQAKSTGRRVSFSAVTAATGSSVVSAQDAPMSPPPLSLGLKSPVLGSSEPAHPRSGSGSGSLMAAFANDSTALTIAPPAPSIGSVLYHPTFARRHILSVKNFSRDDLHALFSVATEMRVMVERQGSVDLLRGRVLATLFYEESTRTSCSFEAAMLRLGGQVVKVQPDKSSVQKGESIPDTIRTLGCYADAVVMRHPAAGSVHLAAKHSAVPVISGGESSIEHPTQALLDTFAIREEMGTVAGLTITMVGDLKYGRTVHSLVQLLCLYGVTVNYVSPESLKMPEDVKQAVARKGIKQYESSVLTDDILARTDVLYVTRVQKERFPDMASYEAVKDTYIVDNATLSKCKPTTIVLHPLPKNNELADDLEYDPRAAWWRQVKYGLYLRMALLAMVLHHRA

Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)

2.1.3.2; 3.5.1.2; 6.3.4.16; 6.3.5.5

CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000256|ARBA:ARBA00001777}; CATALYTIC ACTIVITY: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000256|ARBA:ARBA00043687}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000256|ARBA:ARBA00001062}; CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|ARBA:ARBA00001363};

PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|ARBA:ARBA00004812}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000256|ARBA:ARBA00004852}.

ATP-binding;Glutamine amidotransferase;Hydrolase;Ligase;Multifunctional enzyme;Nucleotide-binding;Pyrimidine biosynthesis;Reference proteome;Repeat;Transferase

'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; UTP biosynthetic process [GO:0006228]

carbamoyl-phosphate synthase complex [GO:0005951]; cytoplasm [GO:0005737]; cytosol [GO:0005829]

amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; metal ion binding [GO:0046872]

IPR006132;IPR006130;IPR036901;IPR002082;IPR006131;IPR011761;IPR013815;IPR006275;IPR005480;IPR036897;IPR002474;IPR036480;IPR005479;IPR005483;IPR029062;IPR035686;IPR017926;IPR032466;IPR011607;IPR036914;IPR016185;

3.40.50.20;3.40.50.880;3.40.50.1370;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.20.20.140;3.40.50.1380;

A0A0D1E894

MESQLANLHLDGGSTADLKQGSRPSHAQASHGNRHVHPTNSSLRPLAPSSSIASNMGINMGVNMQHFNRLAASSTGLTNPNSIAQGMSRAAQQPLNGSRPSTQQQPTQAHIKSRPPSVAGGLNAAAGPSYRPAAPAAQSTKQPASAGSAVASVDLGRYDGGLERDEARGRRGTMQFDPLTLSSADAGKQHPPTRVWSLKDFEMGRPLGKGKFGRVYMVRTRAAPNKGYIIALKCMYKNELVENKVEKQLRREIEIQMNLRHPHILRLHGYFHDEGRVFLMIEFAGRGELYKLMNKLHDRRFEEKVAATYIAQMADALSYLHSKHVIHRDIKPENLLLGIKGDLKIGDFGWSVHAPGNRRQTLCGTLDYLPPEMVNGEQHDKAVDLWALGVLCYEFLEGVPPFEELENAPAGTYKRINNIDFKIPRHFSPEAADLVKALLKKKPDDRLPLTKVLRHPWIMKYDPDACRRASRGKIQ

Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)

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, ECO:0000256|RuleBase:RU367134}; 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, ECO:0000256|RuleBase:RU367134};

ATP-binding;Kinase;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Transferase

attachment of meiotic spindle microtubules to kinetochore [GO:0051316]; interphase mitotic telomere clustering [GO:0120110]; meiotic spindle assembly checkpoint signaling [GO:0033316]; mitotic sister chromatid biorientation [GO:1990758]; mitotic spindle assembly checkpoint signaling [GO:0007094]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of mitotic chromosome condensation [GO:1903380]; positive regulation of mitotic sister chromatid arm separation [GO:1905824]; positive regulation of mitotic sister chromatid biorientation [GO:0140429]; protein localization to kinetochore [GO:0034501]; regulation of cytokinesis [GO:0032465]; regulation of mitotic cytokinesis [GO:1902412]; regulation of spindle attachment to meiosis I kinetochore [GO:1904967]

chromosome passenger complex [GO:0032133]; chromosome, telomeric region [GO:0000781]; inner kinetochore [GO:0000939]; kinetochore [GO:0000776]; meiotic spindle midzone [GO:1990385]; mitotic spindle midzone [GO:1990023]; nucleolar peripheral inclusion body [GO:0140602]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]

ATP binding [GO:0005524]; histone H3S10 kinase activity [GO:0035175]

IPR030616;IPR011009;IPR000719;IPR017441;IPR008271;

1.10.510.10;

A0A0D1EDG8

MVNPRAPGSLSRKIRITVVAADGLAKRDVFRLPDPFAIVTVDGEQTHSTSVIKKTLNPYWNDSFDVNVTDSSVIAVQIFDQKKFKKRDQGFLGVINIRVADVLDLELGGKRLLNKELKKSNDNLVVHGKLIIDLNTNVSTPINNNSTAGPTNLLVPGTSNASSASLATPSSSSVTRSDAPPNTSGSGAIAAAATAASTASTNGDTSSRPASTIDTASSSASVTVPSSAATTPSAGVNNEARSSAAPTSTASRPNPSQDTRSDEYGPLPAGWERRTDHLGRTYYVDHNTRSTTWTRPSTNPSANDAAAASSSAADRQRHSNRALADDFLGVNDGDTSRSSATGSTATSPGAAAASANPLPASSSTTAGNGPLPAGWEQRHTPEGRPYFVDHNTRTTTWVDPRRQQILRIMGPNGSNLTVQPQSVSQLGPLPSGWEMRLTSTARVYFVDHNTKTTTWDDPRLPSSLDQNVPQYKRDFRRKLIYFRSQPALRPIPGQCHIKVRRTHIFEDSYAEIMRQQPNDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGINPEHLNYFKFIGRVLGLAIFHRRFLDAYFIVSFYKMILKKKITLSDLESVDADYHRSLQWMLDNSIEGIVEETFTAVEDKFGEMVTVELKKGGEEVEVTDENKKEYVDLMTEWRISKRVEEQFKAFISGFTELIPQDLINVFDERELELLIGGMSEIDVDDWKKFTDYRGFTEQDQVVQWFWQCVRAWPTEKKSRLLQFATGTSRIPVNGFKDLQGSDGPRRFTIEKSGDVNQLPKSHTCFNRIDLPPYPSFETLESKLALAIEEGMGFGNE

Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)

2.3.2.26

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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885, ECO:0000256|PIRNR:PIRNR001569};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.

Reference proteome;Transferase;Ubl conjugation pathway

chromatin organization [GO:0006325]; late endosome to vacuole transport via multivesicular body sorting pathway [GO:0032511]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; mitochondrion organization [GO:0007005]; nonfunctional rRNA decay [GO:0070651]; poly(A)+ mRNA export from nucleus [GO:0016973]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of dolichol biosynthetic process [GO:0010794]; regulation of ergosterol biosynthetic process [GO:0032443]; regulation of mRNA export from nucleus [GO:0010793]; regulation of multivesicular body size [GO:0010796]; regulation of nitrogen utilization [GO:0006808]; regulation of phosphate metabolic process [GO:0019220]; regulation of protein localization [GO:0032880]; regulation of ribosomal large subunit export from nucleus [GO:2000203]; regulation of rRNA processing [GO:2000232]; regulation of tRNA export from nucleus [GO:2000238]; regulation of tRNA processing [GO:2000235]; regulation of ubiquinone biosynthetic process [GO:0010795]; ribophagy [GO:0034517]; ubiquitin-dependent endocytosis [GO:0070086]; ubiquitin-dependent protein catabolic process [GO:0006511]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]

cellular bud tip [GO:0005934]; cytoplasm [GO:0005737]; cytosolic ribosome [GO:0022626]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; RSP5-BUL ubiquitin ligase complex [GO:1990306]; ubiquitin ligase complex [GO:0000151]

phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]

IPR000008;IPR035892;IPR024928;IPR000569;IPR035983;IPR001202;IPR036020;

2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10;

A0A0D2Y5A7

MLSAALRRRVLAPTHSALRTGFAAHVVRHYASFPEHQVIKMPALSPTMQAGNIGAWQKKPGDSIAPGDVLVEIETDKAQMDFEFQEEGVIAKILKDAGEKDIPVGSPIAVLVEEGTDISAFEKFSIEDAGGDAAKPAAPKKEEKSESKSESASAPEPTPEPQQYQSQGRLQTALDRLPNISASAKRLAREKGISIDGLKGTGKNGQITEEDVKKAISSPAASSAPSATYEDIPISGMRKTIANRLVESTQTNPHFYVTSSISVSKLLKLRQALNSSADGKYKLSVNDFLIKAIAVASRKVPQVNSSWRDGNIRQFNNVDVSVAVSTPTGLITPIVTGVEGRGLEAISSQVKSLAKKARDGKLKPEEYQGGTISISNMGMNPAVDHFTAVINPPQAAILAVGTTKKVAIPAENEAGVEFDDQITLTASFDHKVVDGAVGAEWLKELKQVLENPLELLL

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

FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2) (PubMed:34927582). High pyruvate dehydrogenase complex activity is required for sufficient energy production during germination of conidia (PubMed:34927582). {ECO:0000269|PubMed:34927582}.

2.3.1.12

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:0000255|RuleBase:RU361137};

COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000255|PROSITE-ProRule:PRU01066}; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000255|PROSITE-ProRule:PRU01066};

Acyltransferase;Lipoyl;Mitochondrion;Pyruvate;Reference proteome;Transferase;Transit peptide

acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; aerobic respiration [GO:0009060]

mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]

dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742]

SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:34927582}.

PTM: Decrotonylated at 'Lys-148' by SIR5, which inhibits the activity of the pyruvate dehydrogenase complex (PDC). {ECO:0000269|PubMed:34927582}.

IPR003016;IPR001078;IPR000089;IPR023213;IPR045257;IPR036625;IPR006257;IPR004167;IPR011053;

2.40.50.100;3.30.559.10;4.10.320.10;

A0A0D5W690

MYELEKENLRRLSSYITAIIRPSLIKTFMTTYLKKETVERIMSTEQSSPSAAAQMLLDCMCDLEEDGWFQAFLDFLLTAEYSGLHDAIKNWNFLEYEELHEHRKLLERIEPSITKHLKPRELLMHMNCCLNQRESEEIQAVEAQRGPIAASEKLVDCLLRSDKSNWFKVLKMALDTCELYEALDLLETDGAGKSVQDSDCMMAESSTVCFEYREEMETENMAAPESCSHMSITETPAGVTGDSGRSGKRKLREYQRELMTAAVNGQNTIICAPTGCGKTIVALGICEEHLKLLRGRAKIAFLATKVDVYEQQYKLFQEHFSSKDPNIRVTGMCGDMALSVRMLIETHDIVVLTAQILVNALQSGEMENLQLLTLILLDECHNTTGKHPYNNIMTRYLDSKLTGNGSPLPQIVGLTASVGIGSFKNQMEAENNVTQLCANMDTRVITTVSKHLDELRSYVHTPEKEFFHVFQSPSDPFIRIIQNIMSNIEQMAKKTYNIESLSNISNREYGSQKYEQWIVSVQKSCRVLQMQNADGERRICRELCNYTEHLRKYNDALIINEDARTIDALDYLDVFFQQVRNAGFQTTERKLTALYDTQRPQLQCLATEGQQNPKLEELRFILEEEYHNNQETRTVMFVRTRALADAMKKWIDDTDTLKFLKPGVLIGKGRKSNFTGSGMTPSNQRGVLDTFKSSDQSKMLIATSVADEGIDIPQCNLVLMYEYVGNVVKMVQVRGRGRAQGSRCFLISSSAERIEKEKMNMMKERLVEAAIVALQSRPADLSFKVDILQKEDKARRDFLSASPDKPKTQDSFKLLCAKCKMFACQSDDLRVVQESHHIVVDRSIFSRCSRVPHRKPINFCGFSKKEKMLCVECKHDWGLVVSYLTIQDLPLLKIESFVVQNLVTGEQHYFRKWCKVTFAIREFDMTEITPETWALVN

Danio rerio (Zebrafish) (Brachydanio rerio)

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:ARBA00029316}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000256|ARBA:ARBA00029316};

ATP-binding;Cytoplasm;Helicase;Hydrolase;Immunity;Innate immunity;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Repeat;RNA-binding;Zinc

antiviral innate immune response [GO:0140374]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; primitive hemopoiesis [GO:0060215]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468]; RIG-I signaling pathway [GO:0039529]; type I interferon-mediated signaling pathway [GO:0060337]; type II interferon-mediated signaling pathway [GO:0060333]

cytosol [GO:0005829]; nucleus [GO:0005634]

ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; hydrolase activity [GO:0016787]; RNA helicase activity [GO:0003724]; single-stranded RNA binding [GO:0003727]; zinc ion binding [GO:0008270]

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

IPR031964;IPR042145;IPR011545;IPR011029;IPR014001;IPR001650;IPR027417;IPR041204;IPR038557;IPR021673;

1.20.1320.30;1.10.533.10;3.40.50.300;2.170.150.30;

A0A0D9R447

MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKDSSGTGHFTSGVRVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST

Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus)

2.7.11.26

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; Evidence={ECO:0000256|ARBA:ARBA00023955}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.26; Evidence={ECO:0000256|ARBA:ARBA00023915};

ATP-binding;Carbohydrate metabolism;Cell membrane;Cytoplasm;Glycogen metabolism;Kinase;Membrane;Nucleotide-binding;Nucleus;Reference proteome;Serine/threonine-protein kinase;Signal transduction inhibitor;Transferase;Wnt signaling pathway

beta-catenin destruction complex disassembly [GO:1904886]; cellular response to retinoic acid [GO:0071300]; epithelial to mesenchymal transition [GO:0001837]; ER overload response [GO:0006983]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; glycogen metabolic process [GO:0005977]; hippocampus development [GO:0021766]; insulin receptor signaling pathway [GO:0008286]; intracellular signal transduction [GO:0035556]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of gene expression [GO:0010629]; negative regulation of mesenchymal stem cell differentiation [GO:2000740]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of protein-containing complex assembly [GO:0031333]; neuron projection development [GO:0031175]; phosphorylation [GO:0016310]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of gene expression [GO:0010628]; positive regulation of mitochondrion organization [GO:0010822]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein localization to centrosome [GO:1904781]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of protein-containing complex assembly [GO:0031334]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of microtubule anchoring at centrosome [GO:0150101]; regulation of neuron projection development [GO:0010975]; regulation of protein binding [GO:0043393]; superior temporal gyrus development [GO:0071109]

axon [GO:0030424]; beta-catenin destruction complex [GO:0030877]; centrosome [GO:0005813]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; presynapse [GO:0098793]

ATP binding [GO:0005524]; beta-catenin binding [GO:0008013]; dynactin binding [GO:0034452]; NF-kappaB binding [GO:0051059]; p53 binding [GO:0002039]; protease binding [GO:0002020]; protein kinase A catalytic subunit binding [GO:0034236]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321]; ubiquitin protein ligase binding [GO:0031625]

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

IPR011009;IPR000719;IPR017441;IPR008271;IPR039192;

1.10.510.10;

A0A0E3JXD9

MTEQMLDYFIVGAGLGGVAFAEVALQHQKSIFVFAGDKPPSSVAAAGVYNAVILKRFTLVSQAQEQINLLKVFYPEIEKRIQKNIIFDLPTYRRLASVEEQNNFIVASDRPLFQLFLSPKIISDKFKAVISPFGFGLMKQTGYVDTKLLLQSYRNYLQQNGCISAETFNYAELIIHPDFVEYKGQKAKQIIFAEGFQMKHNPFFKDLPLEGAKGELLVIRSENLDVNVLLKAGVFVLPIGNDLYKVGATYNWTDKTNKPTQSAKDELISELKELISCDFEVVEHLAGIRPTVKDRKPLVGRHPFHKNIYLLNGLGTRGVMLAPYLSYKLFDFIESDLPLDSSISIERYYNSITSSNK

Unknown prokaryotic organism

FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. {ECO:0000269|PubMed:25900453}.

1.4.3.3

CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:25900453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21817; Evidence={ECO:0000269|PubMed:25900453}; CATALYTIC ACTIVITY: Reaction=D-phenylalanine + H2O + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:57981; Evidence={ECO:0000269|PubMed:25900453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70964; Evidence={ECO:0000269|PubMed:25900453}; CATALYTIC ACTIVITY: Reaction=D-lysine + H2O + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:37583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32557, ChEBI:CHEBI:58183; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:25900453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37584; Evidence={ECO:0000269|PubMed:25900453}; CATALYTIC ACTIVITY: Reaction=D-methionine + H2O + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57932; Evidence={ECO:0000269|PubMed:25900453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78208; Evidence={ECO:0000269|PubMed:25900453}; CATALYTIC ACTIVITY: Reaction=D-arginine + H2O + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32689, ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:25900453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78220; Evidence={ECO:0000269|PubMed:25900453}; CATALYTIC ACTIVITY: Reaction=D-ornithine + H2O + O2 = 5-amino-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78255, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57668, ChEBI:CHEBI:58802; Evidence={ECO:0000269|PubMed:25900453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78256; Evidence={ECO:0000269|PubMed:25900453}; CATALYTIC ACTIVITY: Reaction=D-leucine + H2O + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:143079; Evidence={ECO:0000269|PubMed:25900453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78212; Evidence={ECO:0000269|PubMed:25900453}; CATALYTIC ACTIVITY: Reaction=D-histidine + H2O + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:78227, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58133, ChEBI:CHEBI:142967; Evidence={ECO:0000269|PubMed:25900453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78228; Evidence={ECO:0000269|PubMed:25900453};

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q1AYM8};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.96 mM for D-methionine (at 37 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:25900453}; Note=kcat is 10.9 sec(-1) with D-methionine as substrate (at 37 degrees Celsius and at pH 8.0). {ECO:0000269|PubMed:25900453};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:25900453};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:25900453};

Cell wall;Cytoplasm;FAD;Flavoprotein;Oxidoreductase;Secreted

amino acid catabolic process [GO:0009063]

cytoplasm [GO:0005737]; peptidoglycan-based cell wall [GO:0009274]

D-amino-acid oxidase activity [GO:0003884]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A5U3S4}. Secreted, cell wall {ECO:0000250|UniProtKB:A5U3S4}.

IPR006076;IPR036188;

3.30.9.10;3.50.50.60;

A0A0E3KBH3

MAGLKVEWNDWCPGCGNFGILSAEQQAIQELGLDPKKVVLVSGIGCSGKIPHFIRLPASGVHTLHGRALTFAIGIKLANPSLEVIVNGGDGDQLGIGVGHFVSAGRRNVDLTVIVHNNGVYGLTKGQASPTLKLGVKTKSLPKPNINSDINPIALAISSGYTFVARGYAYDVKHLKEIIKKAIKHKGLAMIDVLQPCPTYNDIHTKEYYDKRVYKLDEDPSWDPIVKKPEEMDDKMSKAILKSMEWGDRTPIGIFYQNELVSTYEQRIAERSPSYLDNPPAHDVIEFEGKPTTDVEDILKERRVT

Saccharolobus solfataricus (Sulfolobus solfataricus)

FUNCTION: Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-oxobutyrate to form their CoA derivatives. {ECO:0000269|PubMed:16466637}.

1.2.7.11

CATALYTIC ACTIVITY: Reaction=a 2-oxocarboxylate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = an acyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:42316, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:35179, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; EC=1.2.7.11; Evidence={ECO:0000269|PubMed:16466637};

COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q96XT4}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:Q96XT4}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:Q96XT4}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250|UniProtKB:Q96XT4}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q96XT4}; Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:Q96XT4};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=163 uM for 2-oxoglutarate {ECO:0000269|PubMed:16466637}; KM=275 uM for pyruvate {ECO:0000269|PubMed:16466637}; KM=516 uM for 2-oxobutyrate {ECO:0000269|PubMed:16466637}; Note=kcat is 452 min(-1) for 2-oxoglutarate as substrate. kcat is 144 min(-1) for pyruvate as substrate. kcat is 93 min(-1) for 2-oxobutyrate as substrate.;

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7-8. {ECO:0000269|PubMed:16466637};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:16466637};

Iron;Iron-sulfur;Magnesium;Metal-binding;Oxidoreductase;Thiamine pyrophosphate

2-oxobutyrate synthase activity [GO:0018491]; 2-oxoglutarate synthase activity [GO:0047553]; 4 iron, 4 sulfur cluster binding [GO:0051539]; magnesium ion binding [GO:0000287]; pyruvate synthase activity [GO:0019164]; thiamine pyrophosphate binding [GO:0030976]

IPR011896;IPR032686;IPR029061;IPR011766;

3.40.50.970;

A0A0E3T3B5

MAIQIPSRQLFIDGEWREPVLKKRIPIINPATEQIIGDIPAATAEDVEIAVEAARKALARNKGRDWALAPGAVRAKYLRAIAAKIAERKSEIAKLEAIDCGKPLDEAAWDIDDVSGCFEYYADLAEGLDAQQKTPISLPMEQFKSHVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCAAILKPSELASVTCLELADVCREVGLPPGVLNILTGLGHEAGAPLASHPHVDKIAFTGSTMTGSKIMTAAAQLVKPVSLELGGKSPIVVFDDVDIDKAAEWTAFGIFWTNGQICSATSRLIIHENIAAKFLDRLVQWCKNIKIADPLEEGCRLGPVVSGGQYEKILKFIATAKSEGARVLSGGARPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSSEDEALELANDSHYGLGAAVISKDLERCERVSKALQAGIVWINCSQPCFCQAPWGGNKRSGFGRELGKWGLDNYLTVKQVTEYVSDDPWGWYKSPSKL

Malus domestica (Apple) (Pyrus malus)

FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:26296314). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (PubMed:26296314). {ECO:0000269|PubMed:26296314, ECO:0000305}.

1.2.1.-; 1.2.1.19

CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000269|PubMed:26296314}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106; Evidence={ECO:0000269|PubMed:26296314}; CATALYTIC ACTIVITY: Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH; Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966, ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:26296314}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696; Evidence={ECO:0000269|PubMed:26296314};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=160 uM for 4-aminobutanal {ECO:0000269|PubMed:26296314}; KM=8.2 uM for 3-aminopropanal {ECO:0000269|PubMed:26296314}; KM=82.8 uM for NAD(+) with 3-aminopropanal as substrate {ECO:0000269|PubMed:26296314}; Vmax=1.9 umol/min/mg enzyme with 4-aminobutanal as substrate {ECO:0000269|PubMed:26296314}; Vmax=11.2 umol/min/mg enzyme with 3-aminopropanal as substrate {ECO:0000269|PubMed:26296314}; Vmax=20.9 umol/min/mg enzyme toward NAD(+) in presence of 3-aminopropanal {ECO:0000269|PubMed:26296314};

PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000305}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.75 with 4-aminobutanal as substrate. {ECO:0000269|PubMed:26296314};

Metal-binding;NAD;Oxidoreductase;Peroxisome;Sodium

cellular detoxification of aldehyde [GO:0110095]; glycine betaine biosynthetic process from choline [GO:0019285]

peroxisome [GO:0005777]

1-pyrroline dehydrogenase activity [GO:0033737]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:26296314}.

IPR016161;IPR016163;IPR016160;IPR029510;IPR016162;IPR015590;

A0A0E3T552

MAIQIPSRLLFIDGEWREPVLKKRIPIINPATEEIIGHIPAATAEDVELAVEAARRALSRNKGRDWASAPGAVRAKYLRAIAAKIGERKPEIAKLEAIDCGKPLDEAAWDIDDVSGCFEYYAELAEGLDAQQKAPISLPMEQFKSHVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCAAILKPSELASVTCLELADVCREVGLPPGVLNILTGLGHEAGAPLVSHPHVDKIAFTGSTMTGSKIMTAAAQLVKPVSLELGGKSPIVVFDDVDIDKAAEWTAFGCFWTNGQICSATSRLILHENIATEFLDRLLKWCKNIKIADPLEEGCRLGPVVSGGQYEKILKSIETAKSEGARVLSGGDRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSSEDEALELANDTHYGLGAAVISKDLERCDRFSKGLQAGIVWINCSQPCFCQAPWGGNKRSGFGRELGKWGLDNYLTVKQVTEYVSDDPWGWYTSPSKL

Malus domestica (Apple) (Pyrus malus)

FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:26296314). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (PubMed:26296314). {ECO:0000269|PubMed:26296314, ECO:0000305}.

1.2.1.-; 1.2.1.19

CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000269|PubMed:26296314}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106; Evidence={ECO:0000269|PubMed:26296314}; CATALYTIC ACTIVITY: Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH; Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966, ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:26296314}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696; Evidence={ECO:0000269|PubMed:26296314};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=84.8 uM for 4-aminobutanal {ECO:0000269|PubMed:26296314}; KM=16 uM for 3-aminopropanal {ECO:0000269|PubMed:26296314}; KM=33.8 uM for NAD(+) with 3-aminopropanal as substrate {ECO:0000269|PubMed:26296314}; Vmax=1.2 umol/min/mg enzyme with 4-aminobutanal as substrate {ECO:0000269|PubMed:26296314}; Vmax=11.3 umol/min/mg enzyme with 3-aminopropanal as substrate {ECO:0000269|PubMed:26296314}; Vmax=5.4 umol/min/mg enzyme toward NAD(+) in presence of 3-aminopropanal {ECO:0000269|PubMed:26296314};

PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000305}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.75 with 4-aminobutanal as substrate. {ECO:0000269|PubMed:26296314};

Cytoplasm;Metal-binding;NAD;Oxidoreductase;Sodium

cellular detoxification of aldehyde [GO:0110095]; glycine betaine biosynthetic process from choline [GO:0019285]

cytosol [GO:0005829]

1-pyrroline dehydrogenase activity [GO:0033737]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26296314}.

IPR016161;IPR016163;IPR016160;IPR029510;IPR016162;IPR015590;

A0A0F5HNH9

MKEELDAFHQIFTTTKEAIERFMAMLTPVIENAEDDHERLYYHHIYEEEEQRLSRLDVLIPLIEKFQDETDEGLFSPSNNAFNRLLQELNLEKFGLHNFIEHVDLALFSFTDEERQTLLKELRKDAYEGYQYVKEKLAEINARFDHDYADPHAHHDEHRDHLADMPSAGSSHEEVQPVAHKKKGFTVGSLIQ

Bacillus thermotolerans (Quasibacillus thermotolerans)

FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like iron-binding protein probably involved in iron mineralization in the encapsulin nanocompartment. Has ferroxidase activity even when encapsulated, the rate is probably controlled by the rate of Fe flux across the nanocompartment pores (PubMed:31282860). Part of the iron-mineralizing encapsulin-associated Firmicute (IMEF) system. 2 different cargo proteins have been identified (IMEF and Fer); when both are expressed in E.coli with the shell protein only IMEF is detected within the nanocompartment. E.coli expressing all 3 genes stores the largest amount of iron and is protected from Fe/H2O2-induced oxidative stress (PubMed:28263314). {ECO:0000269|PubMed:28263314, ECO:0000269|PubMed:31282860}.

1.16.3.1

CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000269|PubMed:31282860, ECO:0000305|PubMed:31194509}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149; Evidence={ECO:0000269|PubMed:31282860};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: The empty encapsulin nanocompartment is stable until 86.6 degrees Celsius, when loaded with cargo protein is stable until 88.9 degrees Celsius and when grown in high-iron conditions is stable until 91.8 degrees Celsius. {ECO:0000269|PubMed:31282860};

3D-structure;Encapsulin nanocompartment;Iron;Iron storage;Oxidoreductase;Reference proteome

intracellular iron ion homeostasis [GO:0006879]

encapsulin nanocompartment [GO:0140737]

ferroxidase activity [GO:0004322]

SUBCELLULAR LOCATION: Encapsulin nanocompartment {ECO:0000269|PubMed:31194509, ECO:0000269|PubMed:31282860}.

DOMAIN: The C-terminus (targeting peptide) is probably responsible for targeting to the encapsulin nanocompartment; it is separated from the rest of the protein by a flexible 37-residue linker. {ECO:0000305|PubMed:28263314, ECO:0000305|PubMed:31282860}.

IPR030909;

A0A0G2JDV3

MTQPQMAPICLVENHNEQLSVNQEAIEILDKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMITINHQALEQLQYVTELTELIRAKSSPNPAGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQLDPKFQEVTKAFVSYIFTYAKIKTLKEGIKVTGNRLGILVTTYVNAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENISTFFVPCGHKLYMDKREKIEHDYWQVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGEKAIAEERAQKVAAEKEQELLRQKQKEQQEYMEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEGFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKEALLNGFSTVLFHYLVRYLKHL

Mus musculus (Mouse)

FUNCTION: Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens, such as bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii (PubMed:18025219, PubMed:21551061). Confers protection to several pathogens, including the bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii (PubMed:18025219, PubMed:21551061). {ECO:0000269|PubMed:18025219, ECO:0000269|PubMed:21551061}.

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:0000250|UniProtKB:P32455};

Antimicrobial;Cytoplasmic vesicle;GTP-binding;Hydrolase;Immunity;Innate immunity;Nucleotide-binding;Reference proteome

adhesion of symbiont to host [GO:0044406]; cellular response to interferon-beta [GO:0035458]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to type II interferon [GO:0071346]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832]; response to bacterium [GO:0009617]

cytoplasmic vesicle [GO:0031410]; symbiont-containing vacuole membrane [GO:0020005]

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

SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:18025219}.

IPR030386;IPR037684;IPR003191;IPR036543;IPR015894;IPR027417;

1.20.1000.10;3.40.50.300;

A0A0G2JGI9

MEHSKQIRILLLNEMEKLEKTLFRLEQGFELQFRLGPTLQGKAVTVYTNYPLPGEAFNREKFRSLDWENPTEREDDSDKYCKLHLQQSGSFQYYFLQGNEKSGGGYIVVDPILRIGVDNHVLPLDCVTLQTFLAKCLGPFDEWESRLRVAKESGYNMIHFTPLQTLGLSRSCYSLADQLELNPDFSRPSKRYTWSDVGQLVEKLKREWNILCITDVVYNHTATNSKWILEHPESAYNLVNSPHLKPAWVLDRALWHFSCDVADGKYREKGVPALIENDQHMNCIRKIIWEDIFPRIQLWEFFQVDVHKAVEQFRRLLSQENRRVTKSEPKEHLKIIQDPEYRRRGCAVDMDTALATFIPHDNGPAAIEECCNWFRKRLEELNSEKHHLTSCHQEQAVNCLLGNVFYERLAGHGPKLGPVTRKYPLVTRYFTFPFGEMALSAEEALIHLPDKACFLMAHNGWVMGDDPLRNFAEPGSDVYLRRELICWGDSVKLRYGNKPEDCPYLWAHMKKYTEITATHFQGVRLDNCHSTPLHVAEYMLDAARKLQPNLYVVAELFTGSEELDNIFVTRLGISSLIREAMSAYNSHEEGRLVYRYGGEPVGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSAYDALPSTTVVSMACCASGSTRGYDELVPHQISVVAEERFYTKWNPGASPADTGDVNVHSGIIAARCAINRLHQELGAKGFIQVYVDQVDEDIVAVTRHSPSIHQSVVAVSRTAFRNPKTSFYSKEVPQMCIPGKIEEVVLEARTIERNTKPYKKDENSINGMPNMTVELREHIQLHESKIVRQAGVATKGPNEYIQEIEFENLSPGSVIIFRVSLDPHAQVAVGILRNHLTQFSSHFKSGSLAVDNADPILKIPFASIASKLTLAELNQVLYRCESEEQEDGGGCYDIPNWSSLKYAGLQGLMSVLAEIRPKNDLGHPFCENLRSGDWMIDYVSGRLISRSGSIAEVGKWLQAMFFYLKQIPRYLIPCYFDAILIGAYTTLLDVAWKQMSSFVQNGSTFVKHLSLGSVQMCGVGKCPCLPLLSPSLLDVPCRLNEITKEKEQCCASLAAGLPHFSSGLFRCWGRDTFIALRGMLLVTGRYLEARNIILAFASTLRHGLIPNLLGEGTYARYNCRDAVWWWLQCIQDYCRTVPNGLDILKCPVSRMYPTDDSAPLPAGTLDQPLFEVIQEAMQRHMQGIQFRERNAGPQIDRNMKDEGFNITAGIDEETGFVYGGNRFNCGTWMDKMGESDRARNRGIPATPR

Mus musculus (Mouse)

FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. {ECO:0000256|ARBA:ARBA00003530}.

2.4.1.25; 3.2.1.33

CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin.; EC=3.2.1.33; Evidence={ECO:0000256|ARBA:ARBA00000927}; CATALYTIC ACTIVITY: Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439};

Cytoplasm;Glycogen biosynthesis;Glycosidase;Glycosyltransferase;Hydrolase;Multifunctional enzyme;Proteomics identification;Reference proteome;Transferase

glycogen biosynthetic process [GO:0005978]; glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; response to glucocorticoid [GO:0051384]; response to hormone [GO:0009725]; response to nutrient [GO:0007584]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; inclusion body [GO:0016234]; nucleus [GO:0005634]; sarcoplasmic reticulum [GO:0016529]

4-alpha-glucanotransferase activity [GO:0004134]; amylo-alpha-1,6-glucosidase activity [GO:0004135]; beta-maltose 4-alpha-glucanotransferase activity [GO:0102500]; carbohydrate binding [GO:0030246]; glycogen debranching enzyme activity [GO:0004133]; polysaccharide binding [GO:0030247]; polyubiquitin modification-dependent protein binding [GO:0031593]

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

IPR008928;IPR010401;IPR032788;IPR029436;IPR032792;IPR032790;IPR006421;IPR017853;

3.20.20.80;

A0A0G2JTH7

MKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGASNNSEIKMNKKEEFKEVDYLTEEKVYEIYEFCREREDYSPLIRVIGRIFSSAEALVQSFRKVKQHTKEELKSLQEKDEDKDEDEKEKAACSAAAMEEDSEASSSRMGDSSQGDNNVQKLGPDDVTVDIDAIRRVYSSLLSDEKIETAFLNALVYLSPNVECDLTYHNVYTRDPNYLNLFIIVMENRNLHSPEYLEMALPLFCKAMSKLPLAAQGKLIRLWSKYSADQIRRMMETFQQLITYKVISNEFNSRNLVNDDDAIVAASKCLKMVYYANVVGGDVDTNHNEEDDEEPIPESSELTLQELLGEERRNKKGPRVDPLETEIGVKTLDCRKPLISFEEFINEPLNDVLEMDKDYTFFKVETENKFSFMTCPFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATRLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFCDLGDSHPILYQSLKDLLEYEGNVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVSLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRESVVIR

Rattus norvegicus (Rat)

2.3.2.26

Proteomics identification;Reference proteome;Ubl conjugation pathway

androgen receptor signaling pathway [GO:0030521]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; locomotory exploration behavior [GO:0035641]; modulation of chemical synaptic transmission [GO:0050804]; motor learning [GO:0061743]; negative regulation of dendritic spine morphogenesis [GO:0061002]; negative regulation of TORC1 signaling [GO:1904262]; ovarian follicle development [GO:0001541]; positive regulation of Golgi lumen acidification [GO:1905528]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of transcription by RNA polymerase II [GO:0045944]; progesterone receptor signaling pathway [GO:0050847]; prostate gland growth [GO:0060736]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of circadian rhythm [GO:0042752]; regulation of synaptic plasticity [GO:0048167]; regulation of ubiquitin-dependent protein catabolic process [GO:2000058]; response to cocaine [GO:0042220]; response to hydrogen peroxide [GO:0042542]; response to progesterone [GO:0032570]; sperm entry [GO:0035037]; ubiquitin-dependent protein catabolic process [GO:0006511]

cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]

transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]

IPR032353;IPR042556;IPR044611;IPR000569;IPR035983;

3.30.2160.10;3.90.1750.10;6.10.130.10;

A0A0G2JTL4

PLCKPHHKDRPPSLGTSQPSASPGEPSPPSIQPAQSELIVEAGDTIRLTCTDPAFVKWTFEILDVRIENKQSEWIREKAEATHTGKYTCVSGSGLRSSIYVFVRDPAVLFLVGLPLFGKEDNDALVRCPLTDPQVSNYSLIECDGKSLPTDLKFVPNPKAGITIKNVKRAYHRLCIRCAAQREGKWMRSDKFTLKVRAAIKAIPVVSVPETSHLLKEGDTFTVICTIKDVSTSVDSMWIKLNPQPQSKAQVKRNSWHQGDFNYERQETLTISSARVNDSGVFMCYANNTFGSANVTTTLKVVEKGFINIFPVKNTTVFVTDGENVDLVVEFEAYPKPEHQQWIYMNRTPTNRGEDYVKSDNQSNIRYVNELRLTRLKGTEGGTYTFLVSNSDVSASVTFDVYVNTKPEILTYDRLMNGRLQCVAAGFPEPTIDWYFCTGAEQRCTVPVPPVDVQIQNASVSPFGKLVVQSSIDSSVFRHNGTVECKASNAVGKSSAFFNFAFKGNSKEQIQPHTLFTPLLIGFVVTAGLMGIIVMVLAYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSFIFSKQEEQADAALYKNLLHSKESSCDSSNEYMDMKPGVSYVVPTKTDKRRSARIDSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAAMYEVMKTCWDADPLKRPTFKQVVQLIEKQISDSSKHIYSNLANCNPNPENPVVVDHSVRVNSVGSSTSSTQPLLVHEDA

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|PIRNR:PIRNR500951};

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

actin cytoskeleton organization [GO:0030036]; B cell differentiation [GO:0030183]; cell chemotaxis [GO:0060326]; cell population proliferation [GO:0008283]; cytokine-mediated signaling pathway [GO:0019221]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; developmental pigmentation [GO:0048066]; digestive tract development [GO:0048565]; ectopic germ cell programmed cell death [GO:0035234]; embryonic hemopoiesis [GO:0035162]; epithelial cell proliferation [GO:0050673]; erythrocyte differentiation [GO:0030218]; erythropoietin-mediated signaling pathway [GO:0038162]; Fc receptor signaling pathway [GO:0038093]; germ cell migration [GO:0008354]; glycosphingolipid metabolic process [GO:0006687]; hematopoietic progenitor cell differentiation [GO:0002244]; hematopoietic stem cell migration [GO:0035701]; hemopoiesis [GO:0030097]; immature B cell differentiation [GO:0002327]; inflammatory response [GO:0006954]; intracellular signal transduction [GO:0035556]; Kit signaling pathway [GO:0038109]; lamellipodium assembly [GO:0030032]; lymphoid progenitor cell differentiation [GO:0002320]; male gonad development [GO:0008584]; mast cell chemotaxis [GO:0002551]; mast cell degranulation [GO:0043303]; mast cell differentiation [GO:0060374]; mast cell proliferation [GO:0070662]; megakaryocyte development [GO:0035855]; melanocyte adhesion [GO:0097326]; melanocyte differentiation [GO:0030318]; melanocyte migration [GO:0097324]; myeloid progenitor cell differentiation [GO:0002318]; negative regulation of developmental process [GO:0051093]; negative regulation of programmed cell death [GO:0043069]; negative regulation of reproductive process [GO:2000242]; ovarian follicle development [GO:0001541]; phosphorylation [GO:0016310]; pigmentation [GO:0043473]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of colon smooth muscle contraction [GO:1904343]; positive regulation of dendritic cell cytokine production [GO:0002732]; positive regulation of gene expression [GO:0010628]; positive regulation of long-term neuronal synaptic plasticity [GO:0048170]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mast cell cytokine production [GO:0032765]; positive regulation of mast cell proliferation [GO:0070668]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of pseudopodium assembly [GO:0031274]; positive regulation of pyloric antrum smooth muscle contraction [GO:0120072]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of small intestine smooth muscle contraction [GO:1904349]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vascular associated smooth muscle cell differentiation [GO:1905065]; programmed cell death [GO:0012501]; regulation of bile acid metabolic process [GO:1904251]; regulation of cell shape [GO:0008360]; response to cadmium ion [GO:0046686]; response to radiation [GO:0009314]; somatic stem cell population maintenance [GO:0035019]; spermatid development [GO:0007286]; spermatogenesis [GO:0007283]; stem cell differentiation [GO:0048863]; T cell differentiation [GO:0030217]; tongue development [GO:0043586]; visual learning [GO:0008542]

acrosomal vesicle [GO:0001669]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; protein tyrosine kinase activity [GO:0004713]; SH2 domain binding [GO:0042169]; stem cell factor receptor activity [GO:0005020]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. 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;IPR000719;IPR017441;IPR027263;IPR001245;IPR008266;IPR020635;IPR001824;

2.60.40.10;1.10.510.10;

A0A0G2JTW1

MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDLESEREVSSNEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSACNIQ

Rattus norvegicus (Rat)

FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. {ECO:0000256|RuleBase:RU367057}.

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; EC=3.6.5.2; Evidence={ECO:0000256|ARBA:ARBA00023421};

Endosome;GTP-binding;Lipoprotein;Membrane;Methylation;Nucleotide-binding;Palmitate;Prenylation;Reference proteome

actin cytoskeleton organization [GO:0030036]; cellular response to xenobiotic stimulus [GO:0071466]; establishment of protein localization [GO:0045184]; microvillus assembly [GO:0030033]; negative regulation of cell migration [GO:0030336]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of protein phosphorylation [GO:0001934]; protein localization [GO:0008104]; protein localization to plasma membrane [GO:0072659]; Rap protein signal transduction [GO:0032486]; regulation of dendrite morphogenesis [GO:0048814]; regulation of JNK cascade [GO:0046328]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; regulation of synapse assembly [GO:0051963]

cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic membrane [GO:0097060]

G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]

SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|ARBA:ARBA00004238}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004238}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004238}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004523, ECO:0000256|RuleBase:RU367057}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004523, ECO:0000256|RuleBase:RU367057}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004523, ECO:0000256|RuleBase:RU367057}.

PTM: Palmitoylated. {ECO:0000256|RuleBase:RU367057}.

IPR027417;IPR041840;IPR005225;IPR001806;IPR020849;

3.40.50.300;

A0A0G2JU12

MAGDSSLLAAVSLLSACQQSYFALQVGRVRLKYKIAPPAVTGSLEFERIFRAQQNSLEFYSVFIISLWMAGWYFNQEFPMMDLNEADCLEEKVLGFCNLSGSPVHIRPSQVFLGLCRSR

Rattus norvegicus (Rat)

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;Transferase;Transmembrane;Transmembrane helix

glutathione biosynthetic process [GO:0006750]; leukotriene biosynthetic process [GO:0019370]; lipid metabolic process [GO:0006629]; membrane lipid catabolic process [GO:0046466]; response to lipopolysaccharide [GO:0032496]; response to organonitrogen compound [GO:0010243]

endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; 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;

A0A0G2JUK0

MQPEVRRVCCAVGSCVRSACAAAWAMGRRARGRRFQQPPQPEGEEDGSDGSRKRGQEGWEGGYPEIIKENKLFEHYYQELKIVPEGEWDQFMGSLREPLPATLRITGYKSHAKEILHCLKNKYFKELEDLEVDGQKVEVPQPLSWYPEELAWHTNLSRKILRKSPLLAKFHQFLVSETESGNISRQEAVSMIPPLLLNVEPHHKILDMCAAPGSKTTQLIEMLHADMSVPFPEGFVIANDVDNKRCYLLVHQAKRLSSPCIMVVNHDASSIPRLTVDVDGRKEILFYDRILCDVPCCSGTVCCVNLRSTLSLQLRIATRGAEQLAEGGRMVYSTCSLNPVEDEAVIAALLEKSEGALELADVSAELPGLKWMPGVSQWKVMTRDGQWFADWQEVPQGRHTQIRPTMFPPKDLDKLQAMHLERCLRILPHHQNTGGFFVAVLVKKAPMPWNKRQPKVQSKSAQARDPKASNTVAATKGNPSDQSELESQMITGAGDSEAAQTTENTESNEKKDGVCGPPPSKKMKLFGFKEDPFVFIPEDDPLFPPIEKFYALDPSFPRMNLLTRTTEGKKRQLYMVSKELRNVLLNNSEKMKVINTGIKVWCRNNSGEEFDCAFRLAQEGIYTLYPFINSRIITVSMEDVKTLLTQENPFFRKLSSEAYSQVKDLTKGSVVLKYEPDSANPDTLRCPIVLCGWRGKASIRTFVPKNERLHYLRMMGLEVLGEKKKEGVILTNESVASPEQPEEEDAKQTAQDPCNPDSVPGCDPGAAEPSR

Rattus norvegicus (Rat)

2.1.1.203

CATALYTIC ACTIVITY: Reaction=a cytidine in mRNA + S-adenosyl-L-methionine = a 5-methylcytidine in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61464, Rhea:RHEA-COMP:15145, Rhea:RHEA-COMP:15826, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000256|ARBA:ARBA00000377}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61465; Evidence={ECO:0000256|ARBA:ARBA00000377}; CATALYTIC ACTIVITY: Reaction=cytidine(34) in tRNA precursor + S-adenosyl-L-methionine = 5-methylcytidine(34) in tRNA precursor + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42940, Rhea:RHEA-COMP:10291, Rhea:RHEA-COMP:10295, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.203; Evidence={ECO:0000256|ARBA:ARBA00001128}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42941; Evidence={ECO:0000256|ARBA:ARBA00001128}; CATALYTIC ACTIVITY: Reaction=cytidine(48) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(48) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42948, Rhea:RHEA-COMP:10293, Rhea:RHEA-COMP:10297, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000256|ARBA:ARBA00001405}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42949; Evidence={ECO:0000256|ARBA:ARBA00001405}; CATALYTIC ACTIVITY: Reaction=cytidine(49) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(49) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42952, Rhea:RHEA-COMP:10294, Rhea:RHEA-COMP:10385, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000256|ARBA:ARBA00000276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42953; Evidence={ECO:0000256|ARBA:ARBA00000276}; CATALYTIC ACTIVITY: Reaction=cytidine(50) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(50) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61488, Rhea:RHEA-COMP:15838, Rhea:RHEA-COMP:15839, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000256|ARBA:ARBA00001828}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61489; Evidence={ECO:0000256|ARBA:ARBA00001828};

Methyltransferase;Nucleus;Phosphoprotein;Proteomics identification;Reference proteome;RNA-binding;S-adenosyl-L-methionine;Transferase;tRNA processing;tRNA-binding

hair follicle maturation [GO:0048820]; in utero embryonic development [GO:0001701]; meiotic cell cycle checkpoint signaling [GO:0033313]; mRNA methylation [GO:0080009]; regulation of mRNA export from nucleus [GO:0010793]; regulation of stem cell differentiation [GO:2000736]; spermatid development [GO:0007286]; tRNA methylation [GO:0030488]; tRNA stabilization [GO:0036416]

chromatoid body [GO:0033391]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]

mRNA (cytidine-5-)-methyltransferase activity [GO:0062152]; tRNA (cytidine-5-)-methyltransferase activity [GO:0016428]; tRNA binding [GO:0000049]

SUBCELLULAR LOCATION: Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.

IPR049560;IPR001678;IPR023267;IPR023270;IPR029063;

3.40.50.150;

A0A0G2JUP3

MDHSFSGAPRFLTRPKAFVVSVGKDATLSCQIVGNPTPHVSWEKDRQPVEAGARFRLAQDGDVYRLTILDLALGDSGQYVCRARNAIGEAFAAVGLRVDSEGTCAEQAPHFLLRPTSIRVREGADATFRCRVGGSPQPAVSWSKDGRRLGAPDAPHVRVEDRGEASALRIRSARPRDGGTYEVRAENPLGSASAAAALVVDSDAEAAGPPGTSVATLLAHLQQRREAMRAEGVPPSPPGAGTRTCTVTEGKHARLSCFVTGEPKPETVWKKDGQLVNEGRRHVVYEDEQENFVLKILFCKQSDRGLYTCTASNLVGQTYSSVLVVVREPAVPFKKRLQDLEVREKESATFQCEVAQPATEAAWFKEETRLWASAKYDIEEEGTERRLTVRNVSADDDAVYICETTEGSRTVAELSVKGNLTRKLPRKTAVRTGDTAIFWVELAVPEGPVQWLRNQEEMVAGGRIAITAEGTCHTLTIFQCTLEDMGEVAFVAGGCRTTTQFCVSAPRRPPLYPPADPVVKAKTESSVTLSWSPPPHGDRPVTIDGYVVEKRKLGAYAWSRCHEAEWLATTEFTIAGVAEEGDFQFRVSAINHFGHSPYLEFPGTMHLVPTLAVKTPLKAVEAMEGGEVTFSVDLTVASSGEWFLDGKALKESSTYVIRCDRTRHMLTIREVPASLHGAQLKFVANGIETSIQMVVRGALGLPSNKLPAVAAREVLAQLHEEAQLLAELSDQAAAVTWLKDGRELSLGPKYEMQVSAGKQALLVRDVAQDDAGLYECVSRGSRITYQLLVQEANLMFAKKQQARSEVKAEVGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQVGKADAGEYSCEAGGQKVSFRLDVTEPKVVFAKGQQSHSKVKAEAGANATLSCEVAQAQTEVTWFKDGKKLSSSSKVCVEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFCLDVAEPKVVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVSWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFRLDVTEPKVVFAKEQQARSEVKAEAGANATLSCEVAEAQTEVSWFKDGKKLSSSSKLRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFRLDVTEPKVVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFRLDVAEPKVVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFRLDVAEPKVVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVMWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFRLDVTEPKLVFAKEQQACSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFRLDVTEPKVVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVCVEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFRLDVAEPKLVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFRLDVTEPKVVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVSWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFRLDVAEPKVVFAKEQQACSEVKAEAGASATLSCEVAQAQTEVIWFKDGKKLSSSSKVRVEASGCSRRLVVQQVGKADAGEYSCEAGGQKVSFRLDVPDTKLMFAKEQQACSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKVSFRLDVAEPESQTPQRPSRREPLVIKEHETIVLSATIAAPSVAAVTWLKDGVEIRRSKRHETTSVGDTHTLTVRGAQVLDSAIYSCRVGKEGQDFPVQVEEVATKFSKPLEPVEGELGGTVTLVCELSPEQAEVVWRCGSTQLRAGKRFQMTAEGSRRTLTVSGLREDDAEEYVCESRDDRTSARLTVKVPRVVKFTSGLSAMAAEEGQEATFQCVVSPSDAAVMWYKDGTQLQPSEKFVMVQSGASRSLTILGLTLEDAGHVTVEAEGASSSAALRVREAPVLFKKKLEPQTVEERTPVTLEVELTRPWPEVKWTRNAAVLVPSENVEIHAEGARHRLVLRSVGFADRGFFGCETPDDKTQAKLNVEMRQVRLVRGLQEVEAKEQGTASMDVELSHADVEGSWTRDGLRLQPGPKCHLAVQGPVHILTLSALQPQDSGLVAFRAEGVHTSARLIVTELPVSFTRLLQDVVATQKEKVTLECELSRPVDVRWLKDGVELRAGKAIGIVAQGTCRSLVIYRCETGDQGVYVCDALDAQTSASLRVQGRTYTLIFRRVLAEDAGEIKFVAENAESRAHLRVKELPVTLLRPLRDKIAMEKHRGVLECQVSRASAQVRWFKGKVELQPGPKYEVVSDGLYRKLVINDVQPEDEDTYTCDAGDVKTSAQFFVEEQSITIVRGLKDMTVMEPAPAWFECETSIPSVRPPKWLLGKTVLQAGGNVGLEQDGTVHRLTLHKTCSTMTGPVHFTIGKSRSTAQLVVSDIPVVLTRPLEPKAGRELQSVVLSCDFRPAPKAVQWYKEDTPLSPSEKFKMVLEGQMAELRILRLTPADAGVYRCQAGSAQSSAEVTVEAREVTVIQPLQDVEAMEEGRVCFSCELSHKDEDIEWSLNGTPLYSDSFHEISHEGCLHTLVLKSVRQADTGTVCATSPKVSVSARLVVKAKPVVFLKALDDVSAEERGTLTLQCEVSDPEARVVWRKDGVELGPSDKYDFLHKAGVRSLTVHDMSHEDAGLYTCQVGSKETQSRVSVHDLHVGITKRLKTVEVLEGESCSFECVLSHESPSDPAVWTVGGKIVRSSDHFQAVRQGRKYTLTVKDAALSDAGEVVFSVLGLTSKASLIIREKPVDITKPLEDQHTTPGEDVMLSCELSRAGSSVRWLKDGKAIRKSQKYDLLIEGTQAVLVVRKASLKDSGEYTCETEASRSTARLCVEEKTNRFTEELADLQVEEKGRAVFTCKTEQPASIVTWRKGLLELRASGKHVPSQEGLTLTLTINALERTDSDTYTCDIGQARTQARLLVHGQKVRVIEDLEDTAVQEGSSAKFCCRISPADYGPVHWFLDKTPLHSNELNEITVQSGGYHVLTLRQLTLKDSGTVYFEAGDQRTSAALRVTEKPSIFSRPLTDVTVTEGEDLTLVCETTTPDSSVRWTKDGKTLRPSARCQLNREGCQAQLVITGTTLQDGGRYKCEVGGASSSSIVRVHARPVRFRESLKDMEVPEGKAATLRCVLSSVAAPVEWRHGDDVLKSSNKYSLRQEGAVLELVIRDLKPQDSGQYSCSFGDQTTSATLTVKTSSAQFIGKLRNKEATEGTMATLRCELTKEAPVEWKKGTETLRNGDKYSLKQDGAVCELQICNLLVADAGEYLCVCGQEKTSATLTVKGKEHTWLPPPPSLCTYLLMGSFLLLCCVRSRSLSWCDCVCVFLTSPALPAKFIESLKNEGATEGTTATLSCKLSKAVPVTWKRGTKTLRDGDKYGLRQDGAVCELQIRGLTTADAGEYSCVCGQEKTSAALTVKGLPAKFIEDLRSQEAMEGATAILRCELSKAAPVEWRKGSKILEDGDRYTLRQDGAVCELQIRGLAVVDTGTYSSLPAKFTEGLRNEESMEGTMVTLRCQMSKVTPVEWRKGSETLRDGGRYSLRQDGAVCELQIRGLILEDAGEYSCVCGQEKTSATLSVKALPPRFIEDLRSQEAMEGTMVTLRCQMNKAAPVEWRKGSETLRDGGRYSLRQDGAGCELQIHRLALEDAGEYSCVCGQEKTSATLSVKALPPRFIEDLRSQEATEGTMVTLRCQMNKAPSSTVEWRKGSESLRDGGRYSLRQDGAVCELQIRGLTLEDAGEYSCVFGQERTSATLSVKALPPRFIEDLGSQEAMEGTMVTLRCQMSKTAPVEWRKGSETLRDGGRYSLRQDGALCELQIHRLALEDAGEYSCVCGQEKTSATLSVKALPPRFIEDLRSQKATEGTMVTLRCQMSKVAPVEWRKGSESLRDGDRYSLRQDGAMCELQICGLAVEDSGEYSCVCGQERTSATLTVDALPPKFTEGLKKEEATEGNMATLRCQMSKAAPVEWRKGSETLRDGGRYSLRQDGAACELQIRGLALEDAGEYSCLCGQEKTSATLSVKALPPRFTEDLRSQKATEGTMVTLRCQMSKAAPVEWRKGSETLRDGGRYSLRQDGAVYELQIRGLALEDAGEYSCVCGQEKTSATLSVKGKDPLWPPEPGAWCLHVVSLLCLTSYVTQLLYSLWVYVLCTKSSSVTFSVTPWSFPALPARFIEDLRSQEVPESSTVTMRCELSKKAPVVWRKGSETLKNGARYSLRQDGAVCELEIRDLTVEDAGEYSCTCGKERTSATLSIMAPQVVFQKLLENLQAEEGSTASLRCELSVPNTAVVWSKGGLELQADTCRETRQQGCVAELLLRDVRREDAGEYSCTCGSQTTSATLMVTAAPVRFLQELQAQDVDEGTTARLRCELSREAASVEWRKGSLQLFPCAKYQMVQEGTTAELLVHGVEQEDAGEYTCDAGHMQSIARLSVRAPKPKFKTGLQSKEQEAGGTARLCCQLSEAESGTPVQWLKEGVELHVSSKYEMRCQGAMCELLIHKLEAKDTGEYACVVGGQKTLASLRVKEPEVTIVQGLVDMEVQADEDVEFTCKVSQAGATDVQWHLQGLPLQSNEVTEVAVLGDGCTHVLQLKGVTLDDAGTVSFHVGSHSSSAQLIVRVPEVTVLEPLKDVQLSEGQDAHFQCRLSRASGQEARWALGGVPLQCNEMNDITVEQGTLYSLTLHKVTLEDAGTITLQVGSCSSEAQLKVTAKNTVVRGLENVDALEGGEALFECQLSQPEVAAHTWLLDDEPVHTSANVEVVYFENGLRHLLLLKNLKPQDSCRVTFLAGDVVTSAFLTVRGWRLEVLEPPQDASVKAGTQVCFTCILSEALPVGEATWYINGAAIQPDDADWIVTADGSHHALTLSNAQPQHAGEVTFAARDAVASARLSVLALPGPPEDAEVVGRSDHSVTLSWVAPVSDGGGGLCGYRVEMKEASTGQWQLCHELVPGPECVVDGLVSGKTYRFRVAAVGPAGAGEPVHLPQMVKIAPTPTPAPAPAPAPAPATRRAVVGEDVCLELEVAADAGEVVWHKGTERIHPSGHFEVLSQGQRQMLVIKGFRTEDQGEYRCGPIQGLPSSGASTFNVVVTSGSEDEVPAQPSLPPEAAQEGDLHLLWEALARKRRMSREPTLDSISELPEEDSRVQHLRQEAEEAAPDLSEGYSTADELARTGEADLSHTSSDDESRAGTPSLITYLKKAGGPGISPLASKHEAQVATSVKPQKQQERVVPTCPLPGDLNAADLKDPSLDKAAVKIQAAFKGYKVRKEMKQQGGPVFSRTFGDTEAQVGDALRLECVVSTKADVRACWLKDGVELTDGRHYHIDQLKDGTCSLLVTGLGPTDSGRYTCQVSTKFGSVSHSACVMVSGTESEAESSSGGELDDAFRRAARRLHRLFRTKSPAELSEEELFLSADEGPMEPEEPADWQTYREDENFVCIRFESLAEAHRAVTCFRDMFATMGIGVEISLGEQGPRGVEMRIGKVAPTVIPAVPLAKTPGLQTSDAAPVFLTELQNQDVQDGYPMSFDCVVTGQPVPSVRWFKDGKLLEEDDHYMINEDQQGGHQLIITAVVPADMGVYRCLAENSMGVSSTKAELRVELTSTDYDTAADATETSSYFSAQGYLSSREQEGTESDEGQLPQVLEELKDLQVAPGTRLAKFQLKVKGEDVGVVMCYPPLTTSDHIRMTDKKTLHTLEIVSITREDSGQYAAYISNAVGAAYSSARLLVRGPSEPEEKPQPDVHERLVPPRILEKFTPKKVKRGSSITFSVKVEGHPAPSVHWLKEEAEKGVLWIGPDTPGYTMASSSKQHSLVLLDVGRQHQGTYTCIATNAAGQALCSASLHISGLAKEEEQERVKEALISSFLQGTSQAVSAQMSESASFADLVGQRKGESLVAEEAHSHLSLSEVGTEEFLQKLTSQITEMVSAKISQAKLQVPGGDSDEESKTPSASPRHGRSRPSSSVQESSSESEDGDSRGEIFDIYVVTADYLPLGAEQDAIILREGQYVEVLDSAHPLRWLVRTKPTKSSPSRQGWVSPAYLDKRLKLSPEWGPTEAPEFPGEAVSEDEYRTRLSSVIQELLSSEQAFVGELQFLESHHIKHLDRSPRVPAAVASQKTVIFRNVQDISHFHSSFLKELQSCGTDDDVAMCFIKNQEAFEKYLEFLVGRVQAESVVVSTPVQEFYKKYAEEMLSAKDPTQPPPPPLQHYLEQPVERVQKYQALLKELIRNKARNRQNCALLEQAYAVVSALPQRAENKLHVSLMENYPGTLEALGEPIRQGHFIVWEGAPGARMPWKGHNRHVFLFRNHLVICKPRRDSRTDTFSYVFRNMMKLNSIDLNDQVEGDDRAFEVWHEREDSVRKYLLQARTVIIKNSWVKEICGIQQRLAQPVWRPPEFEEELADCTAELGETVKLACRVTGTPKPIVSWYKDGKPVEVDPHHILIEDPDGSCTLILDNLTGIDSGQYMCFAASAAGNASTLGKILVQVPPRFVNKVRATPFVEGEDAQITCTVEGAPYPQIRWYKDGALLTLGNRYRMVNEPRSGMLVLVIQAASKEDLGHYECELVNRLGSTRCGGELYMQSPALRAWDQHHREQLVAAVEVTEQETKVPKKTVIIEETITTVVKSPRGRRQSPSKSPSRSPSRRSASPRRPGLLAPEMLYPPGTSPSRRLEVEQGRKAPVPALYVTEAEAHTPASQPQPKWLEVEETIEVRVKKTGSRGASPVREMTSHGEGILFTLPGGIPARDPNANNSNNKSVYQGARTWGPAVVHVGEPFVFQVDSVGNVDWAAAGPESEEVRASQEEENVEKEEGGSDGDENTFLMEEPQDTDSLQGRDPKILTHNGRVLTLADLEDYVPQEGETFGCGDPTPSAPDEPPCEVSVLQREIGELTVGQPVLLNVGRPPGPSATPSFFRPSSQVHSPESVSFLLREAWTGPASAAPWTSSFHTHVQSSVDGGHGSFKTEVSTQTVSFGAVGETVTLHIDPDGGEAPGPSQG

Rattus norvegicus (Rat)

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};

Coiled coil;Cytoplasm;Disulfide bond;Immunoglobulin domain;Kinase;Magnesium;Nucleotide-binding;Reference proteome;Repeat;Serine/threonine-protein kinase;SH3 domain;Transferase

negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; phosphorylation [GO:0016310]

cytosol [GO:0005829]; extracellular space [GO:0005615]; intercalated disc [GO:0014704]; M band [GO:0031430]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sarcomere [GO:0030017]; Z disc [GO:0030018]

ankyrin binding [GO:0030506]; ATP binding [GO:0005524]; cadherin binding [GO:0045296]; guanyl-nucleotide exchange factor activity [GO:0005085]; phosphatidylinositol bisphosphate binding [GO:1902936]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; titin binding [GO:0031432]

IPR035899;IPR000219;IPR003961;IPR036116;IPR007110;IPR036179;IPR013783;IPR013098;IPR003599;IPR003598;IPR013106;IPR000048;IPR035526;IPR011993;IPR001849;IPR036028;IPR001452;

1.20.900.10;2.60.40.10;2.30.29.30;2.30.30.40;

A0A0G2JUY1

SGHQTTLILFLDPYVKLSLYVADENRELALVQTKTIKKVGRPVNPSNHRLLFEVFDENRLTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSEQRDDMEHGWEVVDSNDSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRSTQWHRPSLMDVSSESDNNIRQINQEAAHRRFRSRRHISEDLEPEASEGGGEGPEPWETISEEVNMAGDSLSLALPPPPASPVSRTSPQELSEELSRRLQITPDSNGEQFSALIQREPSSRLRSCSVTDTVAEQAHLPPPSTPTRRARSSTVTGGEESTPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQLAEDGASGSATNSNNHLVEPQIRRPRSLSSPTVTLSAPLEGAKDSPIRRAVKDTLSNPQSPQPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKASLNPNDLGPLPVSILQRHEMVQKCVLILPKFMGSLCTCPSAPCPSAPCPSAVPYSREFKQKYDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD

Rattus norvegicus (Rat)

2.3.2.26

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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885, ECO:0000256|PIRNR:PIRNR001569};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.

Proteomics identification;Reference proteome;Transferase;Ubl conjugation pathway

establishment of localization in cell [GO:0051649]; negative regulation of potassium ion transmembrane transport [GO:1901380]; negative regulation of protein localization to cell surface [GO:2000009]; negative regulation of sodium ion transmembrane transport [GO:1902306]; negative regulation of sodium ion transport [GO:0010766]; negative regulation of systemic arterial blood pressure [GO:0003085]; positive regulation of dendrite extension [GO:1903861]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of sodium ion transport [GO:0010765]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; protein monoubiquitination [GO:0006513]; protein ubiquitination [GO:0016567]; regulation of bicellular tight junction assembly [GO:2000810]; regulation of dendrite morphogenesis [GO:0048814]; regulation of membrane depolarization [GO:0003254]; regulation of membrane potential [GO:0042391]; regulation of membrane repolarization [GO:0060306]; regulation of monoatomic ion transmembrane transport [GO:0034765]; regulation of protein stability [GO:0031647]; regulation of sodium ion transmembrane transport [GO:1902305]; regulation of sodium ion transport [GO:0002028]; response to salt stress [GO:0009651]; sodium ion transport [GO:0006814]; ubiquitin-dependent protein catabolic process [GO:0006511]

cytoplasm [GO:0005737]

potassium channel inhibitor activity [GO:0019870]; potassium channel regulator activity [GO:0015459]; sodium channel inhibitor activity [GO:0019871]; sodium channel regulator activity [GO:0017080]; transmembrane transporter binding [GO:0044325]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]

IPR035892;IPR024928;IPR000569;IPR035983;IPR001202;IPR036020;

2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10;

A0A0G2JVC1

MKEIIFYIGQYIMTKRLYDEKQQHIVYCSNDLLGDVFGVPSFSVKEHRKIYAMIYRNLVVVSQQDSGTSPSESRCQPEGGSDLKDPVQASQEEKPSSSDVVSRPSTSSRRRAISETEENTDELPGERQRKRHRALSFDESLGLCVLREICCERSSSSEATDTPSHQDLDDGVSDHSADCLDQDSVSDQFSVEFEVESLDSEDYSLSDEGHELSDEDDEVYRVTVYQAGESDADSFEGDPEISLADYWKCTSCNEMNPPLPSHCNRCWTLRENWLPDDKGKDKVEISEKAKLESSDQAEEGLDVPDGKKVTEDDAKESSAEDSEEKVAQMLLSQESDDYSQPSTSSSIVYSSQESGKELKEDTQDKEESMESSFSLNAIEPCVICQGRPKNGCIVHGKTGHLMSCFTCAKKLKKRNKPCPVCRQPIQMIVLTYFN

Rattus norvegicus (Rat)

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};

Cytoplasm;Metal-binding;Reference proteome;Transferase;Zinc;Zinc-finger

amyloid fibril formation [GO:1990000]; apoptotic process [GO:0006915]; atrial septum development [GO:0003283]; atrioventricular valve morphogenesis [GO:0003181]; blood vessel development [GO:0001568]; blood vessel remodeling [GO:0001974]; cardiac septum morphogenesis [GO:0060411]; cellular response to actinomycin D [GO:0072717]; cellular response to alkaloid [GO:0071312]; cellular response to antibiotic [GO:0071236]; cellular response to estrogen stimulus [GO:0071391]; cellular response to gamma radiation [GO:0071480]; cellular response to growth factor stimulus [GO:0071363]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to organic cyclic compound [GO:0071407]; cellular response to organic substance [GO:0071310]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to UV-C [GO:0071494]; cellular response to vitamin B1 [GO:0071301]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; endocardial cushion morphogenesis [GO:0003203]; establishment of protein localization [GO:0045184]; fibroblast activation [GO:0072537]; heart development [GO:0007507]; heart valve development [GO:0003170]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902254]; negative regulation of neuron projection development [GO:0010977]; negative regulation of protein processing [GO:0010955]; negative regulation of signal transduction by p53 class mediator [GO:1901797]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cell cycle [GO:0045787]; positive regulation of gene expression [GO:0010628]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of vascular associated smooth muscle cell migration [GO:1904754]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; protein autoubiquitination [GO:0051865]; protein destabilization [GO:0031648]; protein localization to nucleus [GO:0034504]; protein ubiquitination [GO:0016567]; protein-containing complex assembly [GO:0065003]; proteolysis involved in protein catabolic process [GO:0051603]; regulation of cell cycle [GO:0051726]; regulation of gene expression [GO:0010468]; regulation of heart rate [GO:0002027]; regulation of protein catabolic process [GO:0042176]; response to antibiotic [GO:0046677]; response to cocaine [GO:0042220]; response to ether [GO:0045472]; response to formaldehyde [GO:1904404]; response to iron ion [GO:0010039]; response to magnesium ion [GO:0032026]; response to steroid hormone [GO:0048545]; response to toxic substance [GO:0009636]; response to water-immersion restraint stress [GO:1990785]; response to xenobiotic stimulus [GO:0009410]; traversing start control point of mitotic cell cycle [GO:0007089]; ubiquitin-dependent protein catabolic process [GO:0006511]; ventricular septum development [GO:0003281]

cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription repressor complex [GO:0017053]

5S rRNA binding [GO:0008097]; disordered domain specific binding [GO:0097718]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; ligase activity [GO:0016874]; NEDD8 ligase activity [GO:0061663]; p53 binding [GO:0002039]; peroxisome proliferator activated receptor binding [GO:0042975]; protein domain specific binding [GO:0019904]; receptor serine/threonine kinase binding [GO:0033612]; ribonucleoprotein complex binding [GO:0043021]; SUMO transferase activity [GO:0019789]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.

IPR028340;IPR044080;IPR016495;IPR036885;IPR003121;IPR001876;IPR036443;IPR001841;IPR013083;

1.10.245.10;3.30.40.10;2.30.30.380;

A0A0G2JW03

MAEKDPVCSSKWEAPRDKSSLDSAWSWIPIMRDPGWIRNVWPSNINVQTMNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVVRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKLGDNGEAFFVQETDNDQEVIPMYLATSPILSEGASRMESQLKRNSVDRIRGLDPTTAAQGLPPSDTPSTGSLGKKRRKRRRKAHLDNLKRDDNVNTSEDEDMFPIEMSSDEDTALMDGSRALPNDVPPFQDDIPKENLPSISTYPQSASYPNSDREWSPSPSSLVDCQRTPPHLAEGVLSSSCPLQSCHFHASESPSGSRPSTPKSDSELVSKSADRLTPKNNLEMLWLWGELPQAAKSSSPHKMKDSSPLGGRKMADKIHFQTIHSESSDTFSDQSPTMARGLLIHQSKAQTEMQFVNEEDLEALGAAAPPLSVAEELKAPASSTAQTSSKSDSPSRKKDKRSRHLGADGVYLDDLTDMDPEVAALYFPKNGDPGGLPKQASDNGARSANQSPQSVGSSGIDSGVESTSDSLRDLPSIAISLCGGLSDHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKIGNKYYNWTTAAPLLLAMQAFQKPLPKATVESIMRDKMPKKGGRWWFSWRGRNATIKEESKPEQGLPGKGHNTGEQPAQLGLTTRIKHESSSSDEEHSATKPSSSSHLSLLSNVSYKKTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFPLLKRSHSCDFPCSDTFSNFTFWREPLPPFENQDVHSASA

Rattus norvegicus (Rat)

3.1.3.4

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};

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

Hydrolase;Reference proteome

actin cytoskeleton organization [GO:0030036]; animal organ regeneration [GO:0031100]; cellular lipid metabolic process [GO:0044255]; cellular response to insulin stimulus [GO:0032869]; fatty acid catabolic process [GO:0009062]; immune response [GO:0006955]; lipid metabolic process [GO:0006629]; mitochondrial fission [GO:0000266]; negative regulation of myelination [GO:0031642]; negative regulation of transcription by RNA polymerase II [GO:0000122]; phosphatidic acid biosynthetic process [GO:0006654]; phosphatidic acid metabolic process [GO:0046473]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of DNA replication [GO:0045740]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of fat cell differentiation [GO:0045598]; ruffle organization [GO:0031529]; triglyceride biosynthetic process [GO:0019432]; triglyceride mobilization [GO:0006642]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]

histone deacetylase binding [GO:0042826]; peroxisome proliferator activated receptor binding [GO:0042975]; phosphatidate phosphatase activity [GO:0008195]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713]

IPR036412;IPR026058;IPR031703;IPR007651;IPR013209;IPR031315;

A0A0G2JW59

MRALARRSDRLPLLVVLSVMILETVTNQDLPVIKCVLIIHKNNGSAAGKSSSHVMVPESPEDLRCAPKHRSEGVVYEAVTVEVAQSASFTLQVQLTTPGDVSCLWVFKHSSLGCQPHFDLQNRRIVSMTILNVTETQAGEYLLHIQSEATNHTVLFTVNVRDTQLYVLRRPSFRKMENQDALLCVSEGVPEPTVEWVVCSSHRDSCREEGSAVVKKEEKVLHELFETDIRCCARNALGRECTKLFTIDLNQAPQSTLPQLFLKVGEPLWIRCKAIHVNHGFGLTWELGNKVLEEGSYFEMSSYSTNRSMIRILLAFVSSVGRNNTGYYTCSSSKHPSQTALVTILEKGFINATSSQEEYEIDPYEKFCFSVRFKAYPQIRCKWTFSQTSFPCEQSGLEDGYSISKFCDHKNNPGEYIFHGENDDAQFTKMFILNIRRKPQVLANASASQASCFSDGYPLPNWTWKKCSDKSPNCTEEIPEGVWNKKANRKVFGQWVSSSTLNMSEAGRGFLVKCCAYNSMGTSCETILLNSPGPFLFIQDNISFYATIGLCPPFIVVLTVLICHKYKKQFRYESQLQMIQVTGPLDNEYFYIDFRDYEYDLKWEFPRENLEFGKVLGSGAFGRVMNATAYGISKTGVSIQVAVKMLKEKADRCEREALMAELKMMTHLGHHDNIVNLLGACTLSGPVYLIFEYCCHGDLLNYLRSKREKFHRTWTEIFKEHNFSFYPTFQSHSNSSMPGSREVQIYPPVDQVSGFNGNSIHSEDEIEYENQKRLEEEEEEDLNVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDILSDSSYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQSGFKMEQPFYATEEIYFVMQSCWAFDSRKRPSFPNLTSFLGCQLAEAEAAMYQNMGGDVPLEHPAIYQNRRPASREAGSEPPSPQVQEKTHRERS

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};

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

animal organ regeneration [GO:0031100]; antigen processing and presentation [GO:0019882]; B cell differentiation [GO:0030183]; cell population proliferation [GO:0008283]; cellular response to cytokine stimulus [GO:0071345]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to virus [GO:0098586]; common myeloid progenitor cell proliferation [GO:0035726]; cytokine-mediated signaling pathway [GO:0019221]; dendritic cell differentiation [GO:0097028]; dendritic cell homeostasis [GO:0036145]; hemopoiesis [GO:0030097]; homeostasis of number of cells within a tissue [GO:0048873]; leukocyte homeostasis [GO:0001776]; lymph node development [GO:0048535]; lymphocyte differentiation [GO:0030098]; lymphocyte proliferation [GO:0046651]; lymphoid progenitor cell differentiation [GO:0002320]; myeloid progenitor cell differentiation [GO:0002318]; negative regulation of B cell differentiation [GO:0045578]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of tumor necrosis factor production [GO:0032720]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of type II interferon production [GO:0032729]; post-embryonic development [GO:0009791]; pro-B cell differentiation [GO:0002328]; pro-T cell differentiation [GO:0002572]; response to organonitrogen compound [GO:0010243]; spleen development [GO:0048536]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]

cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; protein-containing complex [GO:0032991]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; cytokine receptor activity [GO:0004896]; growth factor binding [GO:0019838]; metal ion binding [GO:0046872]; nuclear glucocorticoid receptor binding [GO:0035259]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein self-association [GO:0043621]; protein tyrosine kinase activity [GO:0004713]; protein-containing complex binding [GO:0044877]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; ubiquitin protein ligase binding [GO:0031625]

SUBCELLULAR LOCATION: 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;IPR013151;IPR011009;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;IPR001824;

2.60.40.10;1.10.510.10;

A0A0G2JWT3

MLLFPRVAVKTEPMSSSEIASTAADGSLDSFSGSALGSSSFSPRPAHPFSPPQIYPSKPYPHILPTPSSQTMAAYGQTQFTTGMQQATAYATYPQPGQHYGISSYGALWAGIKTEGGLSQSQSPGQTGFLSYGTSFGTPQPGQAPYSYQMQGSSFTTSSGLYTGNNSLTNSSGFNSSQQDYPSYPGFGQGQYAQYYNSSPYPAHYMTSSNTSPTTPSTNATYQLQEPPSGVTSQAVTDPTAEYSTIHSPSTPIKESDSDRLRRGSDGKSRGRGRRNNNPSPPPDSDLERVFIWDLDETIIVFHSLLTGSYANRYGRDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYNFGTDGFPAAATSANLCLATGVRGGVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALSLIHSRANCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQRFGRKVVYVVIGDGVEEEQGAKKHAMPFWRVSSHSDLMALHHALELEYL

Rattus norvegicus (Rat)

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:0000256|ARBA:ARBA00001490, ECO:0000256|RuleBase:RU362036};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRSR:PIRSR628472-2, ECO:0000256|RuleBase:RU362036}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR628472-2, ECO:0000256|RuleBase:RU362036};

Activator;Hydrolase;Magnesium;Metal-binding;Nucleus;Protein phosphatase;Reference proteome;Transcription;Transcription regulation

animal organ morphogenesis [GO:0009887]; aorta morphogenesis [GO:0035909]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell fate commitment [GO:0045165]; cochlea morphogenesis [GO:0090103]; columnar/cuboidal epithelial cell differentiation [GO:0002065]; double-strand break repair [GO:0006302]; embryonic skeletal system morphogenesis [GO:0048704]; epithelial cell proliferation [GO:0050673]; establishment of mitotic spindle orientation [GO:0000132]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; inner ear morphogenesis [GO:0042472]; lung epithelial cell differentiation [GO:0060487]; mesodermal cell fate specification [GO:0007501]; metanephros development [GO:0001656]; middle ear morphogenesis [GO:0042474]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; neuron fate specification [GO:0048665]; otic vesicle development [GO:0071599]; otic vesicle morphogenesis [GO:0071600]; outer ear morphogenesis [GO:0042473]; outflow tract morphogenesis [GO:0003151]; pattern specification process [GO:0007389]; pharyngeal system development [GO:0060037]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of secondary heart field cardioblast proliferation [GO:0072513]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization [GO:0008104]; protein sumoylation [GO:0016925]; regulation of neuron differentiation [GO:0045664]; response to ionizing radiation [GO:0010212]; semicircular canal morphogenesis [GO:0048752]; striated muscle tissue development [GO:0014706]; ureteric bud development [GO:0001657]

cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; protein-DNA complex [GO:0032993]

histone H2AXY142 phosphatase activity [GO:0140793]; metal ion binding [GO:0046872]; protein tyrosine phosphatase activity [GO:0004725]; RNA binding [GO:0003723]

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

IPR006545;IPR042577;IPR038102;IPR028472;

3.40.50.12350;

A0A0G2JXT6

MEHIRTTKVEQVKLLDRFSTNNKSLTGTLYLTATHLLFIDAHQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRIVHFIVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDTERLNGWQLIDLAAEYERMGVPNANWQLSDANREYKVCETYPRELYVPRTASRPVIVGSSNFRSKGRLPVLSYCQQGTEAAICRCSQPLSGFSARCLEDEHLLQAISKANPGNRYMYVVDTRPKLRMQSWWDTQKDIGRIIVRISSKIWNDEKIRESDEKKRLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVNGSKGLSVNDFYSGLESSGWLRHIKAVLDAAIFLAKAIVVENASVLVHCSDGWDRTSQVCSLGSLLLDSYYRTMKGFMVLIEKDWISFGHKFSERCGHLDGDPKEVSPVFTQFLECVWHLTEQFPQAFEFNEAFLLQIHEHIHSCQFGNFLGNCQKEREELRLKEKTYSLWPFLLADKKKYLNPLYSSKSQRLTVLEPNTASFNFKFWRNMYHQFDRTLHPRQSVLNIIMNMNEQNKQLEEDVKDLEAKIKQCKSGILTKDLLHAVHPESPSLKTSLCLKEQSLLPVKDTLRAVEGSSPADNRYCDYTEEFSKSEPAVVSLEYGVARMTC

Rattus norvegicus (Rat)

FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate. Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), phosphatidic acid and phosphatidylserine (By similarity). Negatively regulates ER-Golgi protein transport (PubMed:23188820). Probably in association with MTMR9, plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3-phosphate in membrane ruffles. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4(+) T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3-phosphate. Negatively regulates proliferation of reactivated CD4(+) T-cells. In complex with MTMR9, negatively regulates DNA damage-induced apoptosis. The formation of the MTMR6-MTMR9 complex stabilizes both MTMR6 and MTMR9 protein levels (By similarity). {ECO:0000250|UniProtKB:Q9Y217, ECO:0000269|PubMed:23188820}.

3.1.3.64; 3.1.3.95

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795, ChEBI:CHEBI:57923; EC=3.1.3.95; Evidence={ECO:0000250|UniProtKB:Q9Y217}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; Evidence={ECO:0000250|UniProtKB:Q9Y217}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911, ChEBI:CHEBI:85342; Evidence={ECO:0000250|UniProtKB:Q9Y217}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934; Evidence={ECO:0000250|UniProtKB:Q9Y217};

Cell membrane;Cell projection;Coiled coil;Cytoplasm;Endocytosis;Endoplasmic reticulum;Hydrolase;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome

endocytosis [GO:0006897]; phosphatidylinositol dephosphorylation [GO:0046856]

cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; nuclear envelope [GO:0005635]; perinuclear region of cytoplasm [GO:0048471]; ruffle membrane [GO:0032587]

phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3,5-bisphosphate phosphatase activity [GO:0106018]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23188820}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y217}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q8VE11}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:23188820}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y217}. Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR9 to the perinuclear region (By similarity). Partially localizes to the endoplasmic reticulum (By similarity). Co-localizes with RAB1B to the endoplasmic reticulum-Golgi intermediate compartment and to the peri-Golgi region (PubMed:23188820). {ECO:0000250|UniProtKB:Q8VE11, ECO:0000250|UniProtKB:Q9Y217, ECO:0000269|PubMed:23188820}.

DOMAIN: The GRAM domain is required for cell membrane localization. {ECO:0000250|UniProtKB:Q8VE11}.; DOMAIN: The C-terminus domain (aa 540-655) mediates interaction with MTMR9. {ECO:0000250|UniProtKB:Q8VE11}.

IPR035998;IPR010569;IPR030564;IPR011993;IPR029021;IPR016130;IPR003595;

2.30.29.30;

A0A0G2JXZ9

MSPGKPGAGGAGTRRTGWRRRRRRRRLEAETRAPGFGHTAGRVPGTFQGAQGMKPAARETRTPPRSPGLRWALLPLLLLLRQGQVVCAGAAPSPVFDVEAVTSPTSVVLTWKHNDSATSEYKINEGNTLRYTVKNQTSFNITGLSPATSYKFSITLGTVNETSGKPTYKNITTEPWPVSDLQVAYIGVTQALLAWSNANGTASYRMQIVELTTNSSGGISDLKPGTHKSLAVQGSNETQHDLWVTEGVSDANGTEGSPVANISQLHKNSLASADPPSARDPSLTEVLLTELKPDTQYKVTIYSQAADGTEGQPGNKVFKTNPIQVSDIRAVNISDSNMTLTWKSNNNESHASFTYKIYVAGGSDSINETVNETQAVIRGLSSSTLYNITVLPFLGQTAGIPGFLQVYTSPRPVSDFRVTNVSLREIGLAWRSNDSESFEIFITQEGSEKRWNASTGDLSYIVENLKPGTSYQFEIFPRGPNGTEGPSQTVVGRTDCSAVTDIRVVSVSTTEIQLEWQNTDSASGYTYHLVLESENGSIKTNSSQKWITVGGLTPGTLYNVTIFPEVDQMEGNSSSITQYTRPSNVSYIEVNTNTTVAAIQWKNLDAASASYSYSVLILKAGDGSNVTSRVRDIPSVTIPGLIPGVSYEVKIFTKIRNTEVGNEVPGQKLFCMEPAQVDSLHCEVVPKEPALVLKWACPPGMNSGFELGVRSDAWDNMTHLENCTLDNDTECRTEVTYLNFSTSYNISIATLSCGKMALPTQSTCTTGITDPPPPDGSPNITSVSHNSVKVKFSGFEASHGPIKAYAVLLTTGEAGQPSTDVLKYTYEDFKKGASDTYVTYLIRIEEKGQSQGLSEALNYEIDVGNQSTTLGYYNGRLEPLGSYRACVAGFTNITYNLQNDGLINGDESYVSFSPYSEAVSLPQDPGVICGAVFGCIFGALAIVAVGGFIFWRKKRKDAKNNEVSFSQIKSKLIRVENFEAYFKKQQADSNCGFAEEYEDLKLIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIRAQKDSKVDLIYQNTTAMTIYENLEPVSMFGKTNGYIA

Rattus norvegicus (Rat)

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:0000256|ARBA:ARBA00001490};

Glycoprotein;Hydrolase;Membrane;Protein phosphatase;Reference proteome;Signal;Transmembrane

B cell differentiation [GO:0030183]; blood coagulation [GO:0007596]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; dephosphorylation [GO:0016311]; glucose homeostasis [GO:0042593]; heart development [GO:0007507]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of platelet-derived growth factor receptor signaling pathway [GO:0010642]; negative regulation of T cell receptor signaling pathway [GO:0050860]; negative regulation of vascular permeability [GO:0043116]; oligodendrocyte differentiation [GO:0048709]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive chemotaxis [GO:0050918]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of Fc receptor mediated stimulatory signaling pathway [GO:0060369]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of platelet activation [GO:0010572]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of cell adhesion [GO:0030155]; vasculogenesis [GO:0001570]

cell surface [GO:0009986]; cell-cell junction [GO:0005911]; immunological synapse [GO:0001772]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587]

beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; delta-catenin binding [GO:0070097]; gamma-catenin binding [GO:0045295]; mitogen-activated protein kinase binding [GO:0051019]; phosphatase activity [GO:0016791]; platelet-derived growth factor receptor binding [GO:0005161]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]

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}.

IPR003961;IPR036116;IPR013783;IPR029021;IPR000242;IPR041201;IPR016130;IPR003595;IPR000387;

2.60.40.10;3.90.190.10;

A0A0G2JY48

QMTSTLGCPLLTPSSWLDSGPELAKDWETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKFIRRRGAHRIHVEMKFSVRDCSSIPSVPGSCKETFNLYYYEADFDLATKTFPNWMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRNGFYLAFQDYGGCMSLIAVRVFYRKCPRVIQNGAIFQETLSGAESTSLVAARGSCIANAEEVDVPIKLYCNGDGEWLVPIGRCMCKAGFEAVENGTVCRGCPSGTFKANQGDEACTHCPINSRTTSEGATNCVCRNGYYRADLDPLDMPCTTIPSAPQAVISSVNETSLMLEWTPPRDSGGREDLVYNIICKSCGSGRGACTRCGDNVQYAPRQLGLTEPRIYISDLLAHTQYTFEIQAVNGVTDQSPFSPQFASVNITTNQAVNRVVALFNHLLCSQQELSEYNATAIKSPTNTVTVQGLKAGAIYVFQVRARTVAGYGRYSGKMYFQTMTEVASRGCPPSLPMAYCGSHLPGCLQVAPALCSCSRRRGFERADSEYTDKLQHYTSGHMTPGMKIYIDPFTYEDPNEAVREFAKEIDISCVKIEQVIGAGEFGEVCSGHLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNVIHLEGVVTKSTPVMIITEFMENGSLDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLADMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYTSALGGKIPIRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMTNQDVINAIEQDYRLPPPMDCPSALHQLMLDCWQKDRNHRPKFGQIVNTLDKMIRNPNSLKAMAPLSSGINLPLLDRTIPDYTSFNTVDEWLEAIKMGQYKESFTNAGFTSFDVVSQMMMEDILRVGVTLAGHQKKILNSIQVMRAQMNQIQSVEV

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};

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

angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; axonogenesis [GO:0007409]; B cell activation [GO:0042113]; camera-type eye morphogenesis [GO:0048593]; cell morphogenesis [GO:0000902]; cellular response to amyloid-beta [GO:1904646]; cellular response to lipopolysaccharide [GO:0071222]; central nervous system projection neuron axonogenesis [GO:0021952]; commissural neuron axon guidance [GO:0071679]; corpus callosum development [GO:0022038]; dendritic spine development [GO:0060996]; dendritic spine morphogenesis [GO:0060997]; ephrin receptor signaling pathway [GO:0048013]; hindbrain tangential cell migration [GO:0021934]; inner ear morphogenesis [GO:0042472]; learning [GO:0007612]; learning or memory [GO:0007611]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of Ras protein signal transduction [GO:0046580]; neuron projection retraction [GO:0106028]; optic nerve morphogenesis [GO:0021631]; phosphorylation [GO:0016310]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of cell migration [GO:0030335]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of gene expression [GO:0010628]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of long-term neuronal synaptic plasticity [GO:0048170]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic plasticity [GO:0031915]; positive regulation of tumor necrosis factor production [GO:0032760]; postsynaptic membrane assembly [GO:0097104]; regulation of autophagosome assembly [GO:2000785]; regulation of axonogenesis [GO:0050770]; regulation of behavioral fear response [GO:2000822]; regulation of blood coagulation [GO:0030193]; regulation of body fluid levels [GO:0050878]; regulation of filopodium assembly [GO:0051489]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation of receptor signaling pathway via JAK-STAT [GO:0046425]; regulation of synapse assembly [GO:0051963]; regulation of T-helper 17 type immune response [GO:2000316]; retinal ganglion cell axon guidance [GO:0031290]; roof of mouth development [GO:0060021]; tight junction assembly [GO:0120192]; trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission [GO:0099557]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; urogenital system development [GO:0001655]; vesicle-mediated intercellular transport [GO:0110077]

axon [GO:0030424]; cell surface [GO:0009986]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]

amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; axon guidance receptor activity [GO:0008046]; ephrin receptor activity [GO:0005003]; identical protein binding [GO:0042802]; protein tyrosine kinase activity [GO:0004713]; protein-containing complex binding [GO:0044877]; signaling receptor activity [GO:0038023]; signaling receptor binding [GO:0005102]; transmembrane-ephrin receptor activity [GO:0005005]

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}.

IPR027936;IPR034238;IPR001090;IPR003961;IPR036116;IPR008979;IPR009030;IPR013783;IPR011009;IPR000719;IPR017441;IPR001660;IPR013761;IPR001245;IPR011641;IPR008266;IPR020635;IPR016257;IPR001426;

2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;

A0A0G2JYR2

MKGDSRHLNEEEGASGYEDCIIVNGNCSDQSSDTKDAPSPPVLEAICTEPVCTPETRGRRSSSRLSKREVSSLLNYTQDVVGDGDGEADDGDGSDILMMPKLTRETKDARTPSESPAVRTRNSNSISSLERQRTSPRITRGRQGRYHVQEYPVEFPATKSRRRRASSSASTPWSSPASIELMEDVTPKSSSTPSVDLSQDGPQEGMDATQVDAESRDGDSTEYQDDKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMPGMRWVQWFGDGKFSEIAADKLVALGLFSQHFNLATFNKLVSYRKAMYHTLEKAMVRAGKTFPSRPGDSLEDQLKPMLEWAHGGFKPTGIEGLKPNNKQPEVHKSKVRRSGSRNLEARRRENKSRRRTTIDFAASEYSTPPKRLKTNSYGGKDRGEDEESRERMASDVTNNKGNLEDRCLSCGKKNPVSFHPLFEGGLCQSCRDRFLELFYMYDEDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGTGTAEDAKLQEPWSCYMCLPQRCHGVLRRRKDWNMRLQDFFTTDPDLEEFEPPKLYPAIPAAKRRPIRVLSLFDGIATGYLVLKDLGIKVEKYVASEVCAESIAVGTIKHEGQIKYVNDVRKITKKNIEEWGPFDLVIGGSPCNDLSNVNPARKGLYEGTGRLFFEFYHLLNYTRPKEGDNRPFFWMFENVVAMKVNDKKDISRFLACNPVMIDAIKVSAAHRARYFWGNLPGMNRIFGFPAHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE

Rattus norvegicus (Rat)

2.1.1.37

Metal-binding;Methyltransferase;Nucleus;Reference proteome;Repressor;S-adenosyl-L-methionine;Transferase;Zinc;Zinc-finger

autosome genomic imprinting [GO:0141068]; cellular response to amino acid stimulus [GO:0071230]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to hyperoxia [GO:0071455]; DNA methylation-dependent heterochromatin formation [GO:0006346]; methylation [GO:0032259]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of gene expression [GO:0010628]; post-fertilization epigenetic regulation of gene expression [GO:0043045]; protein-containing complex localization [GO:0031503]; response to activity [GO:0014823]; response to caffeine [GO:0031000]; response to cocaine [GO:0042220]; response to estradiol [GO:0032355]; response to hypoxia [GO:0001666]; response to ionizing radiation [GO:0010212]; response to toxic substance [GO:0009636]; response to vitamin A [GO:0033189]; response to xenobiotic stimulus [GO:0009410]; retrotransposon silencing by DNA methylation-dependent heterochromatin formation [GO:0141095]

catalytic complex [GO:1902494]; chromosome, centromeric region [GO:0000775]; heterochromatin [GO:0000792]; nucleus [GO:0005634]

chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates [GO:0051718]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; transcription corepressor activity [GO:0003714]

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

IPR025766;IPR018117;IPR001525;IPR040552;IPR049554;IPR030488;IPR000313;IPR029063;IPR011011;

2.30.30.140;1.10.720.50;3.40.50.150;

A0A0G2JYX9

MAGGPGPGEPVVPGAQHFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSEQRTASVLWPWINRNARVADLVHILTHLQLLRARDIITAWHPPASVLPPSTGAPRPSSISAGSETEDWSPRKLQSSASTFLSPAFPGSQTHSESELLQVPLSDSLGPPLQSSAPSSIKQPSPESPVSGLQRARPSPFCWPFCEISQGTCNFSEELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLIEDEAEEVGVTLKSTQPTLWMGVATDAWTAPIAAQIYKKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEGLQAVPPWKLEVAGHGSPSPQENSYMSTTGSAQSGDEPWQPLVVTTRAPAQAAQQLQRSPNQPVESDESVPGLSATLHSWHLTPDSHPSPVSFREASCTQGGTTRESSLRSGPGFQPTTMEGSSMGSSSLLSSEPPQIIINPARQKMVQKLALYEEGVLDSLQLLSSGFFPGLDLEPEKRKRPEESDEFQS

Rattus norvegicus (Rat)

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;Kinase;Nucleotide-binding;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase

canonical NF-kappaB signal transduction [GO:0007249]; cellular response to heat [GO:0034605]; cellular response to hypoxia [GO:0071456]; cellular response to lipopolysaccharide [GO:0071222]; cytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; interleukin-1-mediated signaling pathway [GO:0070498]; interleukin-33-mediated signaling pathway [GO:0038172]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; negative regulation of cholesterol efflux [GO:0090370]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of leukocyte adhesion to vascular endothelial cell [GO:1904996]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of type I interferon production [GO:0032481]; regulation of cytokine-mediated signaling pathway [GO:0001959]; response to interleukin-1 [GO:0070555]; response to lipopolysaccharide [GO:0032496]; response to peptidoglycan [GO:0032494]; Toll signaling pathway [GO:0008063]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 4 signaling pathway [GO:0034142]; type I interferon-mediated signaling pathway [GO:0060337]

cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; heat shock protein binding [GO:0031072]; identical protein binding [GO:0042802]; interleukin-1 receptor binding [GO:0005149]; kinase activity [GO:0016301]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]

IPR011029;IPR000488;IPR035533;IPR011009;IPR000719;IPR017441;IPR008271;

1.10.533.10;1.10.510.10;

A0A0G2JZ79

MIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDINTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRIIQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRTQKELVHLSELPPTPLHISEDSSSPERTVPQDSSVIATLVDQTIKNKVDDLEVSEPKSCVEEKSQEVQTYRNVESINVENPDFKAVGSSTGDKNERTSVAETVRKCWPNRLAKEQISKRLDGNQYLFVPPNRYIFHGAEVYSDSEDDALSSSSCGSNSDSGTCQSPSLEEPLEDESEIEEFYNGLEDDADRPECAGGSGADGGDQEAVNEAIAMKQELTDVNCTPDKSEHY

Rattus norvegicus (Rat)

FUNCTION: NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of H1-4. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A-mediated transcription. Required for the repression of ESRRG by CREBZF. Deacetylates NR1H3 AND NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteasomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates p300/EP300 and PRMT1. Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation. Involved in liver and muscle metabolism. Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Promotes DNA double-strand breaks by mediating deacetylation of SIRT6. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacetylates MECOM/EVI1. Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteasome. Protects cardiomyocytes against palmitate-induced apoptosis. Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity. Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis. Involved in the CCAR2-mediated regulation of PCK1 and NR1D1. Deacetylates CTNB1 at 'Lys-49'. In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling. In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating protein depropionylation and decrotonylation. Mediates depropionylation of Osterix (SP7). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase. Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity. Involved in the regulation of centrosome duplication. Deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly (By similarity). Deacetylates NDC80/HEC1 (By similarity). {ECO:0000250|UniProtKB:Q923E4, ECO:0000250|UniProtKB:Q96EB6}.

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:0000250|UniProtKB:Q96EB6, ECO:0000255|PROSITE-ProRule:PRU00236}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-propanoyl-L-lysyl-[protein] + NAD(+) = 3''-O-propanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:23500, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13758, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:138019, ChEBI:CHEBI:145015; Evidence={ECO:0000250|UniProtKB:Q923E4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23501; Evidence={ECO:0000250|UniProtKB:Q923E4}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] + NAD(+) = 2''-O-(2E)-but-2-enoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:69332, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:137954, ChEBI:CHEBI:183235; Evidence={ECO:0000250|UniProtKB:Q96EB6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69333; Evidence={ECO:0000250|UniProtKB:Q96EB6};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8IXJ6}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8IXJ6};

Acetylation;Apoptosis;Biological rhythms;Cytoplasm;Developmental protein;Differentiation;Metal-binding;Methylation;Myogenesis;NAD;Nucleus;Phosphoprotein;Reference proteome;S-nitrosylation;Transcription;Transcription regulation;Transferase;Ubl conjugation;Zinc

angiogenesis [GO:0001525]; behavioral response to starvation [GO:0042595]; cardiac muscle cell apoptotic process [GO:0010659]; cellular response to amyloid-beta [GO:1904646]; cellular response to antibiotic [GO:0071236]; cellular response to curcumin [GO:1904644]; cellular response to glucose starvation [GO:0042149]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to ionizing radiation [GO:0071479]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to organic cyclic compound [GO:0071407]; cellular response to resveratrol [GO:1904639]; cellular response to rotenone [GO:1904648]; cellular response to starvation [GO:0009267]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to vitamin B3 [GO:0071303]; cholesterol homeostasis [GO:0042632]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; DNA damage response [GO:0006974]; DNA repair-dependent chromatin remodeling [GO:0140861]; DNA synthesis involved in DNA repair [GO:0000731]; energy homeostasis [GO:0097009]; fatty acid homeostasis [GO:0055089]; heterochromatin formation [GO:0031507]; intracellular glucose homeostasis [GO:0001678]; intracellular triglyceride homeostasis [GO:0035356]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; leptin-mediated signaling pathway [GO:0033210]; macrophage differentiation [GO:0030225]; maintenance of nucleus location [GO:0051658]; muscle organ development [GO:0007517]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of cell cycle [GO:0045786]; negative regulation of cellular response to testosterone stimulus [GO:2000655]; negative regulation of cellular senescence [GO:2000773]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of fibroblast apoptotic process [GO:2000270]; negative regulation of gene expression [GO:0010629]; negative regulation of growth hormone secretion [GO:0060125]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of peptidyl-lysine acetylation [GO:2000757]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of phosphorylation [GO:0042326]; negative regulation of prostaglandin biosynthetic process [GO:0031393]; negative regulation of protein acetylation [GO:1901984]; negative regulation of protein localization to nucleus [GO:1900181]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; negative regulation of TOR signaling [GO:0032007]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of triglyceride biosynthetic process [GO:0010868]; negative regulation of tumor necrosis factor production [GO:0032720]; neuron apoptotic process [GO:0051402]; ovulation from ovarian follicle [GO:0001542]; positive regulation of adaptive immune response [GO:0002821]; positive regulation of adipose tissue development [GO:1904179]; positive regulation of angiogenesis [GO:0045766]; positive regulation of apoptotic process [GO:0043065]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell growth involved in cardiac muscle cell development [GO:0061051]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cellular senescence [GO:2000774]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of DNA repair [GO:0045739]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of heart rate [GO:0010460]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of macroautophagy [GO:0016239]; positive regulation of macrophage apoptotic process [GO:2000111]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of neuron projection development [GO:0010976]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein deacetylation [GO:0090312]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of skeletal muscle cell proliferation [GO:0014858]; positive regulation of smooth muscle cell differentiation [GO:0051152]; positive regulation of thyroid-stimulating hormone secretion [GO:2000614]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein depropionylation [GO:0106230]; protein destabilization [GO:0031648]; protein ubiquitination [GO:0016567]; pyrimidine dimer repair by nucleotide-excision repair [GO:0000720]; rDNA heterochromatin formation [GO:0000183]; regulation of apoptotic process [GO:0042981]; regulation of bile acid biosynthetic process [GO:0070857]; regulation of brown fat cell differentiation [GO:0090335]; regulation of cell population proliferation [GO:0042127]; regulation of centrosome duplication [GO:0010824]; regulation of glucose metabolic process [GO:0010906]; regulation of lipid storage [GO:0010883]; regulation of mitotic cell cycle [GO:0007346]; regulation of peroxisome proliferator activated receptor signaling pathway [GO:0035358]; regulation of smooth muscle cell apoptotic process [GO:0034391]; regulation of transcription by glucose [GO:0046015]; response to cocaine [GO:0042220]; response to ethanol [GO:0045471]; response to fluoride [GO:1902617]; response to hydrogen peroxide [GO:0042542]; response to insulin [GO:0032868]; response to kainic acid [GO:1904373]; response to leptin [GO:0044321]; response to mycotoxin [GO:0010046]; response to nutrient levels [GO:0031667]; response to oxidative stress [GO:0006979]; response to resveratrol [GO:1904638]; single strand break repair [GO:0000012]; spermatogenesis [GO:0007283]; stress-induced premature senescence [GO:0090400]; transforming growth factor beta receptor signaling pathway [GO:0007179]; triglyceride mobilization [GO:0006642]; UV-damage excision repair [GO:0070914]; vasodilation [GO:0042311]; white fat cell differentiation [GO:0050872]

axon [GO:0030424]; chromatin [GO:0000785]; chromatin silencing complex [GO:0005677]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; eNoSc complex [GO:0061773]; ESC/E(Z) complex [GO:0035098]; euchromatin [GO:0000791]; growth cone [GO:0030426]; heterochromatin [GO:0000792]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; protein-containing complex [GO:0032991]; rDNA heterochromatin [GO:0033553]

bHLH transcription factor binding [GO:0043425]; deacetylase activity [GO:0019213]; DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; histone binding [GO:0042393]; histone deacetylase activity [GO:0004407]; histone H3K deacetylase activity [GO:0141050]; histone H4K12 deacetylase activity [GO:0140937]; HLH domain binding [GO:0043398]; identical protein binding [GO:0042802]; keratin filament binding [GO:1990254]; lysine-acetylated histone binding [GO:0070577]; metal ion binding [GO:0046872]; mitogen-activated protein kinase binding [GO:0051019]; NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; NAD-dependent histone decrotonylase activity [GO:0160012]; NAD-dependent histone H3K14 deacetylase activity [GO:0032041]; NAD-dependent histone H3K9 deacetylase activity [GO:0046969]; NAD-dependent histone H4K16 deacetylase activity [GO:0046970]; NAD-dependent protein deacetylase activity [GO:0034979]; nuclear receptor binding [GO:0016922]; p53 binding [GO:0002039]; promoter-specific chromatin binding [GO:1990841]; protein domain specific binding [GO:0019904]; protein kinase B binding [GO:0043422]; protein lysine deacetylase activity [GO:0033558]; protein-propionyllysine depropionylase activity [GO:0106231]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]

SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250|UniProtKB:Q96EB6}. Cytoplasm {ECO:0000250|UniProtKB:Q96EB6}. Nucleus {ECO:0000250|UniProtKB:Q96EB6}. Note=Recruited to the nuclear bodies via its interaction with PML. Colocalized with APEX1 in the nucleus. May be found in nucleolus, nuclear euchromatin, heterochromatin and inner membrane (By similarity). Shuttles between nucleus and cytoplasm (By similarity). Colocalizes in the nucleus with XBP1 isoform 2 (By similarity). {ECO:0000250|UniProtKB:Q923E4, ECO:0000250|UniProtKB:Q96EB6}.

PTM: Methylated on multiple lysine residues; methylation is enhanced after DNA damage and is dispensable for deacetylase activity toward p53/TP53. {ECO:0000250|UniProtKB:Q96EB6}.; PTM: Phosphorylated. Phosphorylated by STK4/MST1, resulting in inhibition of SIRT1-mediated p53/TP53 deacetylation. Phosphorylation by MAPK8/JNK1 at Thr-338 leads to increased nuclear localization and enzymatic activity. Phosphorylation at Thr-338 by DYRK1A and DYRK3 activates deacetylase activity and promotes cell survival. Phosphorylated by CaMK2, leading to increased p53/TP53 and NF-kappa-B p65/RELA deacetylation activity (By similarity). {ECO:0000250|UniProtKB:Q923E4, ECO:0000250|UniProtKB:Q96EB6}.; PTM: S-nitrosylated by GAPDH, leading to inhibit the NAD-dependent protein deacetylase activity. {ECO:0000250|UniProtKB:Q923E4}.; PTM: Acetylated at various Lys residues. Deacetylated via an autocatalytic mechanism. Autodeacetylation at Lys-46 promotes its protein deacetylase activity. {ECO:0000250|UniProtKB:Q923E4}.; PTM: Ubiquitinated; leading to degradation. Deubiquitinated by USP22; leading to stabilization. {ECO:0000250|UniProtKB:Q96EB6}.

IPR029035;IPR003000;IPR026591;IPR026590;

3.30.1600.10;3.40.50.1220;

A0A0G2JZV3

MSKLKVVGEKSLTNSSRVVGLLAQLEKINTDSTESDTARHVTSKILHLAQSQEKTRREMTTKGSTGMEVLLSTLENTKDLQTVLNILSILIELVSSGGGRRASFLVAKGGSQILLQLLMNASKDSPPHEEVMVQTHSILAKIGPKDKKFGVKARVNGALNITLNLVKQHFQNYRLVLPCLQLLRVYSTNSVNSVSLGKNGVVELMFKIIGPFSKKNSGLMKVALDTLAALLKSKTNARRAVDRGYVQVLLTIYVDWHRHDNRHRNMLIRKGILQSLKSVTNIKLGRKAFIDANGMRILYNTSQECLAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSSFHFQLPIIPVTGPVAQLYNLPPEVDDVVDESDDNDDIDLEAENEVENEDDLDQSFKNDDIETDINKLRPQQVPGRTIEELKMYEHLFPELVDDFQDYELIAKEPKPFVFEGKVRGPIVVPTAGEEVPGNPGNVRKGAAVKEKASPKGEEVKEDAKGHDKTPPWQLGGQNRAAASAHSSNNDLVKALDRITLQSTPSQVAAGLTAGMRKDYGLPLTVLSCTKACPHVAKCTSALFEGRTVHLGKLCCTGVETEDDEDFESHSSAEQVSSVEASDGPPTLHDPDLYIEIVKNTKSVPEYSEVAYPDYFGHIPPPFKEPILERPYGVQRTKIAQDIERLIHQNDIIDRVVYDLDNPNYTTPEEGDILKFNSKFESGNLRKVIQIRKSEYDLILNSDINSNHYHQWFYFEVSGMRPGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALNARPWWIRMGTDICYYKNHFSRSSVAAGGQKGKSYYTITFTVVFPHKDDVCYFAYHYPYTYSTLQMHLQKLESAHNPQQIYFRKDVLCETLSGNSCPLVTITAMPESSYYEHICQFRTRPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLREAYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMYGCSIKETVWHTHDNAASCDVVEDMGYRTLPKILSHIAPAFCMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGCDQGRYKGLQIGTRELEEMGAKFCVGLLRLKRLTSPLEYNLPSNLLDFENDLIESSCKVTRKCGSSELQLFAAVL

Rattus norvegicus (Rat)

3.4.17.24

CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623; Evidence={ECO:0000256|ARBA:ARBA00029302}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000256|ARBA:ARBA00029302}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000256|ARBA:ARBA00024524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000256|ARBA:ARBA00024524};

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

Mitochondrion;Reference proteome

adult walking behavior [GO:0007628]; anterograde axonal transport of mitochondrion [GO:0098957]; axonal transport [GO:0098930]; central nervous system neuron development [GO:0021954]; cerebellar Purkinje cell differentiation [GO:0021702]; cerebellar Purkinje cell layer development [GO:0021680]; cerebellum development [GO:0021549]; eye photoreceptor cell differentiation [GO:0001754]; mitochondrion organization [GO:0007005]; negative regulation of cell population proliferation [GO:0008285]; neuromuscular process [GO:0050905]; olfactory bulb development [GO:0021772]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; proteolysis [GO:0006508]; retina development in camera-type eye [GO:0060041]; retrograde axonal transport of mitochondrion [GO:0098958]

axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]

metallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR011989;IPR016024;IPR033852;IPR040626;IPR000834;

2.60.40.3120;1.25.10.10;3.40.630.10;

A0A0G2K047

MKPSWLQCRKVTGAGTLGAPLPGSPSVRGAGVARRALVAGFGGRGCRALTTSSGGGEYKTHFAASVADPERFWGKAAEQISWYKPWTKTLENRYPPSTSWFVEGMLNICYNAIDRHIENGQGDKIAIIYDSPVTDTKATISYKEVLEQVSKLAGVLVKQGVKKGDTVVIYMPMIPQAIYAMLACARIGAIHSLIFGGFASKELSTRIDHVKPKVVVTASFGIEPGRKVEYMPLLEEALRIGQHKPDRLLIYNRPNMEKVPLMSGRDLDWEEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITASCIGLGNSKTPPPGQAGKCVPGYNVMILDDNMQKLKARSLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESVLSHGTVTDCAVVGKEDPLKGHVPLALCVLKKDVNATEEQVLEEIVKHVRQSIGPVAAFRNAVFVKQLPKTRSGKIPRSTLSALVNGKPYKVTPTIEDPSIFGHIEEVLKQAL

Rattus norvegicus (Rat)

FUNCTION: Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids (PubMed:28003429). Propionate is the preferred substrate but can also utilize acetate and butyrate with a much lower affinity (PubMed:28003429). {ECO:0000269|PubMed:28003429}.

6.2.1.1; 6.2.1.17

CATALYTIC ACTIVITY: Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000269|PubMed:28003429}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177; Evidence={ECO:0000305|PubMed:28003429}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA; Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:456215; EC=6.2.1.17; Evidence={ECO:0000269|PubMed:28003429}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374; Evidence={ECO:0000305|PubMed:28003429}; CATALYTIC ACTIVITY: Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate; Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28003429}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173; Evidence={ECO:0000305|PubMed:28003429};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.4 mM for acetate {ECO:0000269|PubMed:28003429}; KM=3.7 mM for butyrate {ECO:0000269|PubMed:28003429}; KM=0.19 mM for propionate {ECO:0000269|PubMed:28003429};

Acetylation;ATP-binding;Ligase;Lipid metabolism;Mitochondrion;Nucleotide-binding;Reference proteome;Transit peptide

lipid metabolic process [GO:0006629]

mitochondrial matrix [GO:0005759]

acetate-CoA ligase activity [GO:0003987]; ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; propionate-CoA ligase activity [GO:0050218]

SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:28003429}.

IPR032387;IPR025110;IPR045851;IPR020845;IPR000873;IPR042099;

3.30.300.30;3.40.50.12780;

A0A0G2K082

MGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDTKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVSSSSPGSGPSSPNNGPAGNVTENEASVLPPTPHPEQLVPQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSPLSASNSLKDKQKCETQMLRQGVPLPGQYGSGIAASSSHAHVAMEGKPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMEERATSKDSGTGKDSSACVEDTLGQVGAVKVKEEPVDSDEDAQMQEMECGEQAAFMQQTPLLESSHTRALSVHQARLAAAGIDGLEKHGLLSRTHSSPAPSMSPHPAADCPRQPASATGIAYDCLMLKHQCICGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQKLDPRTLLALPLVNAGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEGYNVNIAWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGRVALALEGGHDLTAICDASEACINALLGNEPGSLEEDVLHQSVNTNAAASLQKTIEIQSKYWKSIKMVAVARGCALPASQLQEETETVSALASLTVDVEQPFAQEDGRYGSNMGGQCGQ

Rattus norvegicus (Rat)

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|ARBA:ARBA00001028, ECO:0000256|PIRNR:PIRNR037911};

Chromatin regulator;Hydrolase;Metal-binding;Nucleus;Reference proteome;Repressor;Transcription;Transcription regulation;Zinc

cellular response to insulin stimulus [GO:0032869]; cholesterol homeostasis [GO:0042632]; determination of adult lifespan [GO:0008340]; DNA repair [GO:0006281]; heart development [GO:0007507]; negative regulation of cytokine production [GO:0001818]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron differentiation [GO:0030182]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; regulation of skeletal muscle fiber development [GO:0048742]; regulation of skeletal muscle fiber differentiation [GO:1902809]; response to amphetamine [GO:0001975]

cytoplasm [GO:0005737]; histone deacetylase complex [GO:0000118]; histone methyltransferase complex [GO:0035097]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]

DNA-binding transcription factor binding [GO:0140297]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; histone H3K14 deacetylase activity [GO:0031078]; histone H3K9 deacetylase activity [GO:0032129]; histone H4K16 deacetylase activity [GO:0034739]; metal ion binding [GO:0046872]; protein kinase C binding [GO:0005080]; protein lysine deacetylase activity [GO:0033558]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription corepressor activity [GO:0003714]

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;

A0A0G2K105

MSNPGTRRNGSSIKIRLTVLCAKNLAKKDFFRLPDPFAKIVVDGSGQCHSTDTVKNTLDPKWNQHYDLYVGKTDSITISVWNHKKIHKKQGAGFLGCVRLLSNAISRLKDTGFSLQTRDRIGGGGSVVDCRGLLENEGTVYEDSGPGRPLSCLMEEPAPYTDGTGAAAGGGNCRFVESPSQDQRLLVQRLRNPEVRGSLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLQLPSEGSVEDEELPAQRYERDLVQKLKVLRHELSLQQPQAGHCRIEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRGEEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYTLQINPDSSINPDHLSYFHFVGRIMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITPVLDHTFCVEHNAFGRILQHELKPNGRNVPVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNELIPQHLLKPFDQKELELIIGGLDKIDLNDWKSNTRLKHCVADSNIVRWFWQAVETFDEERRARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPYESYEKLYEKLLTAVEETCGFAVE

Rattus norvegicus (Rat)

2.3.2.26

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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};

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

Reference proteome;Ubl conjugation pathway

BMP signaling pathway [GO:0030509]; cell differentiation [GO:0030154]; engulfment of target by autophagosome [GO:0061736]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of ossification [GO:0030279]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization [GO:0061734]; positive regulation of axon extension [GO:0045773]; positive regulation of dendrite extension [GO:1903861]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein export from nucleus [GO:0006611]; protein localization to plasma membrane [GO:0072659]; protein polyubiquitination [GO:0000209]; protein targeting to vacuole involved in autophagy [GO:0071211]; protein ubiquitination [GO:0016567]; receptor catabolic process [GO:0032801]; substrate localization to autophagosome [GO:0061753]; ubiquitin-dependent protein catabolic process [GO:0006511]

axon [GO:0030424]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]

activin receptor binding [GO:0070697]; I-SMAD binding [GO:0070411]; R-SMAD binding [GO:0070412]; SMAD binding [GO:0046332]; transforming growth factor beta receptor binding [GO:0005160]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]

IPR000008;IPR035892;IPR024928;IPR000569;IPR035983;IPR001202;IPR036020;

2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10;

A0A0G2K134

MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPVPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPTAAPISTSELKKVVALYDYMPMNANDLQLRKGEEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSTGEPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLISRLKYPVSKQNKNAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIREGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKHLHGVYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKIPYERFTNSETAEHIAQGLRLYRPHLASDRVYTIMYSCWHEKADERPSFKILLSNILDVMDEES

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|RuleBase:RU362096};

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

Adaptive immunity;ATP-binding;Cytoplasm;Immunity;Kinase;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;SH2 domain;SH3 domain;Transferase;Tyrosine-protein kinase;Zinc;Zinc-finger

adaptive immune response [GO:0002250]; B cell affinity maturation [GO:0002344]; B cell receptor signaling pathway [GO:0050853]; cell maturation [GO:0048469]; cellular response to interleukin-7 [GO:0098761]; cellular response to molecule of fungal origin [GO:0071226]; cellular response to reactive oxygen species [GO:0034614]; eosinophil homeostasis [GO:1990959]; histamine secretion by mast cell [GO:0002553]; intracellular signal transduction [GO:0035556]; monocyte proliferation [GO:0061516]; negative regulation of B cell activation [GO:0050869]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of cytokine production [GO:0001818]; negative regulation of interleukin-10 production [GO:0032693]; negative regulation of leukocyte proliferation [GO:0070664]; neutrophil homeostasis [GO:0001780]; phosphorylation [GO:0016310]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of interleukin-17A production [GO:0150153]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; positive regulation of phagocytosis [GO:0050766]; positive regulation of synoviocyte proliferation [GO:1901647]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type I hypersensitivity [GO:0001812]; positive regulation of type III hypersensitivity [GO:0001805]; proteoglycan catabolic process [GO:0030167]; response to lipopolysaccharide [GO:0032496]; response to organic substance [GO:0010033]; T cell receptor signaling pathway [GO:0050852]

cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; protein tyrosine kinase activity [GO:0004713]

IPR035574;IPR011009;IPR011993;IPR001849;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR036028;IPR001452;IPR001562;

2.30.29.30;3.30.505.10;2.30.30.40;1.10.510.10;

A0A0G2K1F2

MVLLLFLTCLVFSCLTISWLKIWGKMTDSKPLSNSKVDASLLSSKEESFSASDQSEEHGDCSCPLTTPDQEELASHGGPVDASQQRNSVPSSHQKPPRNPLSSNDTCSSPELQTNRVAAPGSEVPEANGLPFPARPQTQRTGSPTREDKKQAHIKRQLMTSFILGSLDDNSSDEDPSASSFQTSSRKGSRASLGTLSQEAALNTADPESHTPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGNRVIETVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADQYVPVPGGPNNNNYANVELIIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKISSTIVAQTLQIPTLPWSGSGLTVEWTEDSQHQGKCISVPEDVYEQGCVRDVDEGLQAAEKVGFPLMIKASEGGGGKGIRRAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPVSFETPLSPPIARGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQAEKPDIMLGVVCGALNVADAMFRTCMTEFLHSLERGQVLPADSLLNIVDVELIYGGIKYVLKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGSSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLMQYTVEDGQHVEVGSSYAEMEVMKMIMTLNVQESGRVKYIKRPGAVLEAGCVVAKLELDDPSKVHAAQPFTGELPAQQTLPILGERLHQVFHSVLENLTNVMNGYCLPEPFFSMKLKDWVEKLMMTLRHPSLPLLELQEIMTSVAGRIPVPVEKAVRRVMAQYASNITSVLCQFPSQQCWASGMLGKHSTTELQPELLKIATILDCHAATLQRKVDREAFFMNTQSIVQLIQRYRSGTRGYMKAVVLDLLRRYLNVEHHFQQAHYDKCVINLREQFKPDMTRVLDCIFSHSQVAKKNQLVTMLIDELCGPDPTLSEELTSILKELTQLSRSEHCKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRELPDGTCVVEFQFMLPSSHPNRMAMPINVSDPDLLRHSKELFMDSGFSPLCQRMGAMVAFRRFEEFTRNFDEVISCFANVPTDTPLFSKACTSLYSEEDSKSLQEEPIHILNVAIQCADHMEDERLVPVFRAFVQSKKHILVDYGLRRITFLIAQEREFPKFFTFRARDEFAEDRIYRHLEPALAFQLELSRMRNFDLTAVPCANHKMHLYLGAAKVKEGLEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPLKIEESVRAMVMRYGSRLWKLRVLQAEVKINIRQTTSDCAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSFGNKQGSLHGMLINTPYVTKDLLQAKRFQAQSLGTTYVYDFPEMFRQALFKLWGSPEKYPKDILTYTELVLDSQGQLVEMNRLPGCNEVGMVVFKMRFKTPEYPEGRDTIVIGNDITFQIGSFGIGEDFLYLRASEMARTEGIPQIYLAANSGARMGLSEEIKQIFQVAWVDPEDPYKGFRYLYLTPQDYTQISSQNSVHCKHIEDEGESRYVIVDVIGKDSSLGVENLRGSGMIAGEASLAYEKNVTISMVTCRAIGIGAYLVRLGQRVIQVENSHIILTGAGALNKVLGREVYTSNNQLGGVQIMHTNGVSHVTVPDDFEGVCTILEWLSYIPKDNQSPVPIITPSDPIDREIEFTPTKAPYDPRWLLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRSVEVAVPADPANLDSEAKIIQQAGQVWFPDSAFKTAQVIRDFNQEHLPLMIFANWRGFSGGMKDMYEQMLKFGAYIVDSLRLFKQPVLIYIPPGAELRGGAWVVLDSSINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLVKTIRRIDPVCKKLLGQLGTAQLPDKDRKELESQLKAREDLLLPIYHQVAVQFADLHDTPGHMLEKGIISDVLEWKTTRTYFYWRLRRLLLEAQVKQEILRASPELSHEHTQSMLRRWFVETEGAVKAYLWDSNQVVVQWLEQHWSARDNLRSTIRENINYLKRDSVLKTIQSLVQEHPEATMDCVAYLSQHLTPAEQMQVVQLLSTTESPASH

Rattus norvegicus (Rat)

6.4.1.2

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|ARBA:ARBA00001448}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11309; Evidence={ECO:0000256|ARBA:ARBA00001448};

COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000256|ARBA:ARBA00001953};

PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.

ATP-binding;Biotin;Fatty acid biosynthesis;Fatty acid metabolism;Ligase;Lipid biosynthesis;Lipid metabolism;Manganese;Multifunctional enzyme;Nucleotide-binding;Phosphoprotein;Proteomics identification;Reference proteome;Signal

acetyl-CoA metabolic process [GO:0006084]; energy homeostasis [GO:0097009]; fatty acid biosynthetic process [GO:0006633]; fatty acid oxidation [GO:0019395]; glucose import [GO:0046323]; intracellular aspartate homeostasis [GO:0090459]; intracellular glutamate homeostasis [GO:0090461]; lactic acid secretion [GO:0046722]; malonyl-CoA biosynthetic process [GO:2001295]; negative regulation of fatty acid beta-oxidation [GO:0031999]; negative regulation of fatty acid oxidation [GO:0046322]; negative regulation of gene expression [GO:0010629]; negative regulation of lipid catabolic process [GO:0050995]; pentose-phosphate shunt [GO:0006098]; positive regulation of heart growth [GO:0060421]; positive regulation of lipid storage [GO:0010884]; protein homotetramerization [GO:0051289]; purine nucleotide metabolic process [GO:0006163]; regulation of cardiac muscle hypertrophy in response to stress [GO:1903242]; regulation of glucose metabolic process [GO:0010906]; response to nutrient [GO:0007584]; response to nutrient levels [GO:0031667]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]; tricarboxylic acid metabolic process [GO:0072350]

mitochondrial fatty acid beta-oxidation multienzyme complex [GO:0016507]; mitochondrion [GO:0005739]; nucleus [GO:0005634]

acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; biotin binding [GO:0009374]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]

IPR049076;IPR049074;IPR034733;IPR013537;IPR011761;IPR013815;IPR005481;IPR011764;IPR005482;IPR000089;IPR005479;IPR029045;IPR011763;IPR011762;IPR016185;IPR011054;IPR011053;

2.40.50.100;3.40.50.20;3.30.1490.20;3.30.470.20;2.40.460.10;3.90.1770.10;

A0A0G2K1Q8

MVVLRQLRLLLWKNYTLKKRKVLVTVLELFLPLLFSGILIWLRLKIQSENVPNATVYPDQHIQELPLFFSFPPPGGSWELAYVPSHSDAARTITEAVRREFMIKMRVHGFSSEKDFEDYVRYDNHSSNVLAAVVFEHTFNHSKDPLPLAVRYHLRFSYTRRNYMWTQTGNLFLKETEGWHTASLFPLFPSPGPREPSSPDGGEPGYIREGFLAVQHAVDKAIMHYHANASAHQLFQKLTVITKRFPFPPYISDPFLIAIQYQLPLLLMLSFTYTSLTIIRAVVQEKEKKLKEYMRMMGLSSWLHWSAWFLMFLLFSLIVVSFMTLLFCVKVKKDIAVLSNSDPSLVLAFLLCFAISSISFSFMVSTFFSKANMAATVGGFLYFFTYTPYFFVAPRYNWMTLSQKLLSCLLSNVAMAMGAQLIGKFEAKGTGIQWCDLLNPVNVDDDFCFGQVLGMLLLDSVLYGLVTWYVEAVFPGQFGVPQPWYFFLMPSYWCGNPRTVVGKEEEGGDPEKAFRTEYFEAEPEDLAAGIKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSMLTGLFPPTSGHAYIRGYEISQDMVQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSVQKCPEEVKQMLHTLGLEDKRDSRSKFLSGGMKRKLAIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYGAGYHMTLVKEPHCNPEGISQLVHHHVPNAMLESHAGAELSFILPKESTHRFESLFAKLEKKQKELGIASFGASVTTMEEVFLRVGKLVDTSMDIQAIQLPALQYQHERRASDWALDSNLCGVMDPTNGIGALIEEEEVLVKLNTGLALHCQQFWAMFLKKAAYSWREWRMVAAQILVPVTCLTLALLAINYTSEIFDDPPLKLSLNEYGTTVVPFSVPGTSRLGQQLSEHLRDMLQAERQEPREVLGDLEEFLVFRASVEGGGFNERCLVATSFKDSGERTVVTALFNNQAYHSPATALAIVDNLLFKLLCGPRASIEISNYPQPRSTLQVAKDQFNEGRKGFDIALNLLIAMAFLASTFSILAVSERAVQAKHVQFVSGVHVATFWLSALLWDLISFLVPSLLLLVVFRAFDVHAFTRDGHMADLLLLLMLYGWAIIPLMYLLSFFFSAASTAYTRLTIFNILSGIATFIVVTIMRIPAVKLEELSRTLDHVFLVLPNHCLGMAVSNFYENYETRRYCTSSEVATHYCKKYNIQYQENFYAWSTPGIGKFVTSMAASGGIYLTLLFLIETNLLWRLRTFVCAFRRRWTLAELQNRTSVLPEDQDVADERSRVLVPSLDSMLDTPLIINELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLIDACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLQAKVRSEGKQEVLEEFKAFVDLTFPGSVLEDEHQDMVHYHLPGCDLSWAKVFGILEKAKEKYGVDDYSVSQISLEQVFLSFAHLQPPTTEDGR

Rattus norvegicus (Rat)

FUNCTION: Catalyzes the ATP-dependent transport of phospholipids such as phosphatidylcholine and phosphoglycerol from the cytoplasm into the lumen side of lamellar bodies, in turn participates in the lamellar bodies biogenesis and homeostasis of pulmonary surfactant. Transports preferentially phosphatidylcholine containing short acyl chains. In addition plays a role as an efflux transporter of miltefosine across macrophage membranes and free cholesterol (FC) through intralumenal vesicles by removing FC from the cell as a component of surfactant and protects cells from free cholesterol toxicity. {ECO:0000250|UniProtKB:Q99758}.

7.6.2.1; 7.6.2.2

CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000250|UniProtKB:Q99758}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66272, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99758}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66273; Evidence={ECO:0000250|UniProtKB:Q99758}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:Q99758}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66340, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:72999, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99758}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66341; Evidence={ECO:0000250|UniProtKB:Q99758}; CATALYTIC ACTIVITY: Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) + phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99758}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052; Evidence={ECO:0000250|UniProtKB:Q99758}; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(in) + ATP + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66344, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64716, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q8R420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66345; Evidence={ECO:0000250|UniProtKB:Q8R420};

ATP-binding;Cytoplasmic vesicle;Disulfide bond;Endosome;Glycoprotein;Lipid transport;Lysosome;Membrane;Nucleotide-binding;Reference proteome;Repeat;Translocase;Transmembrane;Transmembrane helix;Transport

lipid transport [GO:0006869]; lung development [GO:0030324]; organelle assembly [GO:0070925]; phosphatidylcholine metabolic process [GO:0046470]; phosphatidylglycerol metabolic process [GO:0046471]; phospholipid homeostasis [GO:0055091]; phospholipid transport [GO:0015914]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of phospholipid efflux [GO:1902995]; positive regulation of phospholipid transport [GO:2001140]; positive regulation of protein homooligomerization [GO:0032464]; regulation of lipid biosynthetic process [GO:0046890]; regulation of lipid transport [GO:0032368]; regulation of phosphatidylcholine metabolic process [GO:0150172]; response to glucocorticoid [GO:0051384]; surfactant homeostasis [GO:0043129]; xenobiotic export from cell [GO:0046618]; xenobiotic transmembrane transport [GO:0006855]; xenobiotic transport [GO:0042908]

alveolar lamellar body [GO:0097208]; alveolar lamellar body membrane [GO:0097233]; cytoplasmic vesicle membrane [GO:0030659]; intracellular membrane-bounded organelle [GO:0043231]; lamellar body [GO:0042599]; lamellar body membrane [GO:0097232]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; multivesicular body membrane [GO:0032585]; plasma membrane [GO:0005886]

ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; lipid transporter activity [GO:0005319]; phosphatidylcholine flippase activity [GO:0140345]; phosphatidylcholine transfer activity [GO:0120019]

SUBCELLULAR LOCATION: Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q99758}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q99758}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q99758}. Late endosome membrane {ECO:0000250|UniProtKB:Q99758}. Lysosome membrane {ECO:0000250|UniProtKB:Q99758}. Note=Localized in the limiting membrane of lamellar bodies in lung alveolar type II cells. Trafficks via the Golgi, sorting vesicles (SVs) and late endosome/multivesicular body network directly to the outer membrane of lamellar bodies in AT2 lung epithelial cells or to lysosomes and lysosomal-related organelles (LROs) in other cells where undergoes proteolytic cleavage and oligosaccharide processing from high mannose type to complex type. Oligomers formation takes place in a post-endoplasmic reticulum compartment. {ECO:0000250|UniProtKB:Q99758}.

PTM: N-glycosylated. Localization at intracellular vesicles is accompanied by processing of oligosaccharide from high mannose type to complex type. N-linked glycosylation at Asn-124 and Asn-140 is required for stability and efficient anterograde trafficking and prevents from proteasomal degradation. {ECO:0000250|UniProtKB:Q99758}.; PTM: Proteolytically cleaved by CTSL and to a lower extent by CTSB within multivesicular bodies (MVB) and lamellar bodies (LB) leading to a mature form of 150 kDa. {ECO:0000250|UniProtKB:Q99758}.

IPR003593;IPR013525;IPR003439;IPR017871;IPR026082;IPR027417;

3.40.50.300;

A0A0G2K210

MVVPACVLVFCVAVVAGVTSEPPGPEQRVGRRAAEVPGPEPSQQEQVAFGSGDTVELSCHPPGGAPTGPTLWAKDGVGLVASHRILVGPQRLQVLNATHEDAGVYSCQQRLTRRVLCHFSVRVTDAPSSGDDEDGEDVAEDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGKEFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKSWISENVEADARLRLANVSERDGGEYLCRATNFIGVAEKAFWLRVHGPQAAEEELMEVDEAGSVYAGVLSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKVSRFPLKRQQVSLESNSSMNSNTPLVRIARLSSGEGPVLANVSELELPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDRTAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGMDYSFDACRLPEEQLTCKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAVPSQRPTFKQLVEDLDRILTVTSTDEYLDLSVPFEQYSPGGQDTPSSSSSGDDSVFTHDLLPPGPPSNGGPRT

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|PIRNR:PIRNR000628};

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

alveolar secondary septum development [GO:0061144]; astrocyte differentiation [GO:0048708]; axonogenesis involved in innervation [GO:0060385]; bone development [GO:0060348]; bone maturation [GO:0070977]; bone mineralization [GO:0030282]; bone morphogenesis [GO:0060349]; bone trabecula morphogenesis [GO:0061430]; calcium ion homeostasis [GO:0055074]; cartilage development [GO:0051216]; cell population proliferation [GO:0008283]; cell-cell signaling [GO:0007267]; central nervous system myelination [GO:0022010]; cochlea development [GO:0090102]; digestive tract morphogenesis [GO:0048546]; endothelial cell proliferation [GO:0001935]; epithelial cell fate commitment [GO:0072148]; epithelial cell proliferation [GO:0050673]; ERK1 and ERK2 cascade [GO:0070371]; fibroblast growth factor receptor apoptotic signaling pathway [GO:1902178]; fibroblast growth factor receptor signaling pathway [GO:0008543]; forebrain development [GO:0030900]; inner ear auditory receptor cell differentiation [GO:0042491]; inner ear development [GO:0048839]; lens fiber cell development [GO:0070307]; lens morphogenesis in camera-type eye [GO:0002089]; MAPK cascade [GO:0000165]; mitotic nuclear division [GO:0140014]; morphogenesis of an epithelium [GO:0002009]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of developmental growth [GO:0048640]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of gene expression [GO:0010629]; negative regulation of inner ear auditory receptor cell differentiation [GO:0045608]; negative regulation of mitotic nuclear division [GO:0045839]; negative regulation of neuroblast proliferation [GO:0007406]; negative regulation of smoothened signaling pathway [GO:0045879]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroblast proliferation [GO:0007405]; neuroepithelial cell differentiation [GO:0060563]; neuron apoptotic process [GO:0051402]; oligodendrocyte development [GO:0014003]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of bone mineralization [GO:0030501]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell proliferation in bone marrow [GO:0071864]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway [GO:0090080]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; post-anal tail morphogenesis [GO:0036342]; protein ubiquitination [GO:0016567]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of bone remodeling [GO:0046850]; regulation of collagen metabolic process [GO:0010712]; regulation of ossification [GO:0030278]; regulation of osteoclast differentiation [GO:0045670]; response to axon injury [GO:0048678]; response to sodium phosphate [GO:1904383]; somatic stem cell population maintenance [GO:0035019]; substantia nigra development [GO:0021762]

cell surface [GO:0009986]; cytoplasmic side of plasma membrane [GO:0009898]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; transport vesicle [GO:0030133]

ATP binding [GO:0005524]; fibroblast growth factor binding [GO:0017134]; fibroblast growth factor receptor activity [GO:0005007]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; miRNA binding [GO:0035198]; protein tyrosine kinase activity [GO:0004713]

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}.

IPR016248;IPR007110;IPR036179;IPR013783;IPR013098;IPR003599;IPR003598;IPR011009;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;

6.10.250.1740;2.60.40.10;1.10.510.10;

A0A0G2K2A5

VSGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLETIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAVSRVLILKRPICDCSCYNRLLFKFVLMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWITAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEPMDTDQGSTVLSAIQSEVARNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKAKEKQNAKKAQETK

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, ECO:0000256|PIRNR:PIRNR038120};

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

chromatin remodeling [GO:0006338]; forebrain morphogenesis [GO:0048853]; lateral ventricle development [GO:0021670]; midbrain development [GO:0030901]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of smoothened signaling pathway [GO:0045880]; positive regulation of telomere maintenance in response to DNA damage [GO:1904507]; regulation of cell cycle [GO:0051726]; regulation of chromosome organization [GO:0033044]; regulation of DNA repair [GO:0006282]; regulation of DNA replication [GO:0006275]; regulation of DNA strand elongation [GO:0060382]; regulation of embryonic development [GO:0045995]; regulation of proteasomal protein catabolic process [GO:0061136]; telomere maintenance [GO:0000723]; ubiquitin-dependent protein catabolic process [GO:0006511]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; Ino80 complex [GO:0031011]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]

cysteine-type deubiquitinase activity [GO:0004843]; endopeptidase inhibitor activity [GO:0004866]; proteasome binding [GO:0070628]

IPR038765;IPR001578;IPR036959;IPR017390;IPR033837;IPR041507;

1.20.58.860;3.40.532.10;

A0A0G2K2C7

MTATTRGSPVGGNDNQGQAPDGQSQPPLQQNQTSSPDSSNENSPATPPDEQGQGDAPPQIEDEEPAFPHTDLAKLDDMINRPRWVVPVLPKGELEVLLEAAIDLSKKGLDVKSEACQRFFRDGLTISFTKILTDEAVSGWKFEIHRCIINNTHRLVELCVAKLAQDWFPLLELLAMALNPHCKFHIYNGTRPCESVSSSVQLPEDELFARSPDPRSPKGWLVDLLNKFGTLNGFQILHDRFINGSALNVQIIAALIKPFGQCYEFLTLHTVKKYFLPIIEMVPQFLENLTDEELKKEAKNEAKNDALSMIIKSLKSLASRVPGQEETVKNLEIFRLKMILRLLQISSFNGKMNALNEVNKVISSVSYYTHRHGSSEEEEWLTAERMAEWIQQNNILSIVLRDSLHQPQYVEKLEKILRFVIKEKALTLQDLDNIWAAQAGKHEAIVKNVHDLLAKLAWDFSPEQLDHLFDCFKASWTNASKKQREKLLELIRRLAEDDKDGVMAHKVLNLLWNLAHSDDVPVDIMDLALSAHIKILDYSCSQDRDTQKIQWIDRFIEELRTNDKWVIPALKQIREICSLFGEAPQNLSSSRFSQTQRSPHVFYRHDLINQLQHNHALVTLVAENLATYMESMRLYGRDNEDYDPQTVRVGSRYSHVQEVQERLNFLRFLLKDGQLWLCAPQAKQIWKCLAENAVYLCDREACFKWYSKLMGDEPDLDPDINKDFFESNVLQLDPSLLTENGMKCFERFFKAVNCREGKLVAKRRAYMMDDLELIGLDYLWRVVIQSNDDIASRAIDLLKEIYTNLGPRLQVNQVVIHEDFIQSCFDRLKASYDTLCVLDGDKDSINCARQEAVRMVRVLTVLREYINECDSDYHEERTILPMSRAFRGKHLSFIVRFPNQGRQVDDLEVWSHTNDTIGSVRRCILNRIKANVAHTKIELFVGGELIDPGDDRKLIGQLNLKDKSLITAKLTQISSNMPSSPDSSSDSSTGSPGNHGNHYSDGPNPEVESCLPGVIMSLHPRYISFLWQVADLGSSLNMPPLRDGARVLMKLMPPDSTTIEKLRAICLDHAKLGESSLSPSLDSLFFGPSASQVLYLTEVVYALLMPAGAPLADDSSDFQFHFLKSGGLPLVLSMLTRNNFLPNADMETRRGAYLNALKIAKLLLTAIGYGHVRAVAEACQPGVEGVNPMTSVNQVTHDQAVVLQSALQSIPNPSSECMLRNVSVRLAQQISDEASRYMPDICVIRAIQKIIWTSGCGGLQLVFSPNEEVTKIYEKTNAGNEPDLEDEQVCCEALEVMTLCFALIPTALDALSKEKAWQTFIIDLLLHCHSKTVRQVAQEQFFLMCTRCCMGHRPLLFFITLLFTVLGSTARERAKHSGDYFTLLRHLLNYAYNSNINVPNAEVLLNNEIDWLKRIRDDVKRTGETGVEETILEGHLGVTKELLAFQTPEKKFHIGCEKGGANLIKELIDDFIFPASNVYLQYMRNGELPAEQAIPVCGSPATINAGFELLVALAVGCVRNLKQIVDSLTEMYYIGTAITTCEALTEWEYLPPVGPRPPKGFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDEKQDNESNVDPRDDVFGYPQQFEDKPPLSKTEDRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVNPESQLIQQNEQSESEKAGSTKYRLVGVLVHSGQASGGHYYSYIIQRNGGDGEKNRWYKFDDGDVTECKMDDDEEMKNQCFGGEYMGEVFDHMMKRMSYRRQKRWWNAYILFYERMDTIDHDDEVIRYISEIAITTRPHQIVMPSAIERSVRKQNVQFMHNRMQYSLEYFQFMKKLLTCNGVYLNPPPGQDHLSPEAEEITMISIQLAARFLFTTGFHTKKIVRGSASDWYDALCILLRHSKNVRFWFAHNVLFNVSNRFSEYLLECPSAEVRGAFAKLIVFIAHFSLQDGPCPSPFASPGPSSQAYDNLSLSDHLLRAVLNLLRREVSEHGRHLQQYFNLFVMYANLGVAEKTQLLKLSVPATFMLVSLDEGPGPPIKYQYAELGKLYSVVSQLIRCCNVSSRMQSSINGNPSLPNPFGDPNLSQPIMPIQQNVVDILFVRTSYVKKIIEDCSNSDETVKLLRFCCWENPQFSSTVLSELLWQVAYSYTYELRPYLDLLLQILLIEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIKCMVALFSSCPVAYQILQGNGDLKRKWTWAVEWLGDELERRPYTGNPQYTYNNWSPPVQSNETSNGYFLERSHSARMTLAKACELCPEEEPDDQDAPDEHESPPPEDAPLYPHSPGSQYQQNNHVHGQPYTGPAAHHMNNPQRTGQRAQENYEGSEEVSPPQTKDQ

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]; DNA dealkylation involved in DNA repair [GO:0006307]; 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;

A0A0G2K2H0

MGRVPLAWCVALCCWGCAAPKDTQTEADSPFVGNPGNITGARGLTGTLRCELQVQGEPPEVMWLRDGQILELADNTQTQVPLGEDWQDEWKVVSQLRISALQLSDAGEYQCMVHLEGRTFVSQPGFVGLEGLPYFLEEPEDKAVPANTPFNLSCQAQGPPEPVTLLWLQDAVPLAPVAGYSFQHSLQAPGLNKTSSFSCEAHNAKGVTTSRTATITVLPQRPHNLHVVSRHPTELEVAWIPSLSGIYPLTHCTLQAVLSDDGVGVWLGESDPPEEPLTVQVSVPPHQLRLEKLLPHTPYHIRVSCTSSQGPSPWTHWLPVETTEGVPLGPPENVSAMRNGSQALVRWQEPREPLQGTLLGYRLAYRGQDTPEVLMDIGLTREVTLELRGDRPVANLTVSVAAYTSAGDGPWSLPVPLEPWRPVSEPPPPAFSWPWWYVLLGALVAAACVLILTLFLVHRRKKETRYGEVFEPTVERGELVVRYRARKSYSRRTTEATLNSLGISEELKEKLRDVMVDRHKVALGKTLGEGEFGAVMEGQLNQDDSILKVAVKTMKIAICTRSELEDFLSEAVCMKEFDHPNVMRLIGVCFQGSDREGFPEPVVILPFMKHGDLHSFLLYSRLGDQPVFLPTQMLVKFMADIASGMEYLSTKRFIHRDLAARNCMLNENMSVCVADFGLSKKIYNGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQPLDCLDGLYALMSRCWELNPRDRPSFAELREDLENTLKALPPAQEPDEILYVNMDEGGSHLEPRGAAGGADPPTQPDPKDSCSCLTEADVHSAGRYVLCPSTAPGPTLSADRGCPAPPGQEDGA

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};

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

animal organ regeneration [GO:0031100]; apoptotic cell clearance [GO:0043277]; apoptotic process [GO:0006915]; blood vessel remodeling [GO:0001974]; cell differentiation [GO:0030154]; cell maturation [GO:0048469]; cell migration [GO:0016477]; cellular response to extracellular stimulus [GO:0031668]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to interferon-alpha [GO:0035457]; cellular response to lipopolysaccharide [GO:0071222]; dendritic cell differentiation [GO:0097028]; enzyme-linked receptor protein signaling pathway [GO:0007167]; erythrocyte homeostasis [GO:0034101]; establishment of localization in cell [GO:0051649]; forebrain cell migration [GO:0021885]; inflammatory response [GO:0006954]; lymphocyte activation [GO:0046649]; natural killer cell differentiation [GO:0001779]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cytokine production [GO:0001818]; 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]; response to axon injury [GO:0048678]; secretion by cell [GO:0032940]; spermatogenesis [GO:0007283]; substrate adhesion-dependent cell spreading [GO:0034446]; symbiont entry into host cell [GO:0046718]; tissue regeneration [GO:0042246]; tissue remodeling [GO:0048771]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vagina development [GO:0060068]

cell surface [GO:0009986]; extracellular space [GO:0005615]; membrane [GO:0016020]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; growth factor binding [GO:0019838]; metal ion binding [GO:0046872]; myosin heavy chain binding [GO:0032036]; phosphatidylinositol 3-kinase binding [GO:0043548]; phosphatidylserine binding [GO:0001786]; protein tyrosine kinase activity [GO:0004713]; 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;

A0A0G2K2H4

MPARWLLLLLALLLLPPGPGSFGRASTVTLPEALLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGGKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYIWQREGLRKVVHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDLKFDPGLKGKSKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKRSFEEVINLVGQTSENTPTTVSQDVEEKLPRAPAKPEAPVDSMLKDMATIILSTFLLVGWVAFIITYPLSMHQQRQLQHQQFQKELEKIQLLQQQQLPFHPHGDLTQDPDFLDSSGLFSESSGTSSPSPSPRASNHSLNSSSSASKAGTSPSLEPDDEDEETRMVIVGKISFCPKDVLGHGAEGTIVYKGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLHQTTSGLAHLHSLNIVHRDLKPHNILLSMPNAHGRIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGNHPFGKSLQRQANILLGACSLDCFHSDKHEDVIARELIEKMIAMDPQQRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVRQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKRHHYRELPLEVQETLGSIPDDFVRYFTSRFPHLLSHTYRAMELCRHERLFQTYYWHEPTEAQPPGIPDAL

Rattus norvegicus (Rat)

2.7.11.1

ATP-binding;Kinase;Membrane;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Signal;Transferase;Transmembrane;Transmembrane helix

cellular response to glucose stimulus [GO:0071333]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to unfolded protein [GO:0034620]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; endoplasmic reticulum unfolded protein response [GO:0030968]; endothelial cell proliferation [GO:0001935]; insulin metabolic process [GO:1901142]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; IRE1-mediated unfolded protein response [GO:0036498]; mRNA splicing, via endonucleolytic cleavage and ligation [GO:0070054]; phosphorylation [GO:0016310]; positive regulation of endoplasmic reticulum unfolded protein response [GO:1900103]; positive regulation of RNA splicing [GO:0033120]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; response to endoplasmic reticulum stress [GO:0034976]

AIP1-IRE1 complex [GO:1990597]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; IRE1-RACK1-PP2A complex [GO:1990630]; IRE1-TRAF2-ASK1 complex [GO:1990604]; mitochondrion [GO:0005739]; nuclear inner membrane [GO:0005637]

ADP binding [GO:0043531]; ATP binding [GO:0005524]; endonuclease activity [GO:0004519]; enzyme binding [GO:0019899]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; platelet-derived growth factor receptor binding [GO:0005161]; protein homodimerization activity [GO:0042803]; protein serine/threonine kinase activity [GO:0004674]; RNA endonuclease activity [GO:0004521]; unfolded protein binding [GO:0051082]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR045133;IPR010513;IPR038357;IPR011009;IPR018391;IPR000719;IPR011047;IPR008271;IPR015943;

1.20.1440.180;1.10.510.10;2.130.10.10;

A0A0G2K2Y2

MATDSGEPASTEDSEKPDGVSFQSRVARAVAPLTVEARIKEKYSTFSASGETIERKRFFRKSVEMTEDDKVAQSSRRDERKVATNISRVEKVPTNVLRGGQEVKYEQCSKATSESSKDCFKEKTEKEMEEEAEMKAVATSPSGRFLKFDIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESILKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLMRTSFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTDPEVKEIIEGCIRQNKSERLSIKDLLNHAFFAEDTGLRVELAEEDDCSNSSLALRLWVEDPKKLKGKHKDNEAIEFSFNLEADTPEEVAYEMVKSGFFHESDSKAVAKSIRDRVTLIKKIREKKPAGCLEERRDSQCKHARNVNPQQQTATLRPAPGPHNAAECEETEVDQHVRQQLVQGKAQQQPSSVRGDTSSEPAAGPVLHSDTSSHPTVAYSSNQATSSQLQEQPKLTRSPVLPVVQGQSSVMPIYAAGPAVASQSQISPLTIQKVSQIKPVSQPIGAEQQATPPNPDFVRSLNQDVTSVKENTNSPDTPSGNGKQDRIKQRRASCPRPEKGTKFQLTVLQVSVSGDNMVECQLETHNNKMVTFKFDVDGDAPEDIADYMVEDNFVLENEKEKFVEELRAIVGQAQEILHVHSAAEKSIGVDSVALESNSNQTGSSEQVLINSASTQTSNNTSNQEISQDTLFTVPGHHVVFTSKLDGKIGERASVETEQTSVPYQAEDDKLKAPATDTSNYSATLVCPDPAGCEALTSQAGMFIPTYPCQQAAVPADVLMSHPGESVQIGSNAVVTSVLVSSDQKPQSLSVQQPTIDAEFISQEGETTVNSETSSPKAVGATQTPGFEPTVLLPATILESDGERPPKMEFTDNRIKTLDEKLRNLLYQEHSISTICPESQKDTQSIDSPFSSSAEDILSSPMPEVIAISHCGIQDSQAQSPNFQPTGSKILSNVAASQPAHIPVLKRDLNVITSVPSELCLHEMSPDASLPGDPEAYPAAVSSDGTIHLQTGVETEDKRSAIASDPIPLTREFSADTRALSRCKAMSGSFQRGRFQVITVPQQQPVKMMSFGKEHRPPSKKTTAQSNEQALTFTEAAVTQLIEVEPAIPTHKASVSSQKLRTLYETFKEDKGDPEQGDILSLSTARETSVSSVTTEKNVEETSTTGISVQSGSEMLDKEKDESTPGKQTCTNEFSATPAGSGKSVAKAAPKSGQHLPARAQTQSSLFYSPSSPMSSDNESEIEDEDLKAELQRLREKHIQEVVSLQTQQNKELQELYERLRATKDSKAQSSEVPMPPASPRRPRSFKSKLRSRPQSLTHSDNLVVVKDVQRAESNTAPRQQSPASKKGMFTDDLHKLVDDWTRETVGNFPSKPSLNQLKQSQQKSEAENWNKLHESTPSTVGYTSTWISSLSQIRGAAPSSLPHGLPLPSFPGPLASYGMPHACQYNPVGAASYPVQWVGISGAAQQSVVLPTQSGGLFQPGMNLQSFPAPPVQNPPSIPPGPK

Rattus norvegicus (Rat)

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};

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

cell volume homeostasis [GO:0006884]; cellular hyperosmotic response [GO:0071474]; intracellular signal transduction [GO:0035556]; maintenance of blood-brain barrier [GO:0035633]; monoatomic ion homeostasis [GO:0050801]; negative regulation of apoptotic process [GO:0043066]; negative regulation of pancreatic juice secretion [GO:0090188]; negative regulation of protein localization to plasma membrane [GO:1903077]; negative regulation of sodium ion transport [GO:0010766]; non-membrane-bounded organelle assembly [GO:0140694]; osmosensory signaling pathway [GO:0007231]; phosphorylation [GO:0016310]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of potassium ion import across plasma membrane [GO:1903288]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of sodium ion transport [GO:0010765]; protein localization to plasma membrane [GO:0072659]; regulation of calcium ion import [GO:0090279]; regulation of monoatomic cation transmembrane transport [GO:1904062]

adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytosol [GO:0005829]

ATP binding [GO:0005524]; molecular condensate scaffold activity [GO:0140693]; potassium channel inhibitor activity [GO:0019870]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]

IPR011009;IPR024678;IPR000719;IPR008271;

1.10.510.10;

A0A0G2K344

MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLVTIKHELFKEARKYPLHQLLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFVIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPIDSFTMPSYSRRISTATPYMNGETATKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSREAGFSYSHTGLSNRLARDNELRENDKEQLRALCTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAMELLDCNYPDPMVRSFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRQPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQEYTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFTKQMNDAHHGGWTTKMDWIFHTIKQHALN

Rattus norvegicus (Rat)

FUNCTION: Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides. Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins (PubMed:20236230). Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. In addition to its lipid kinase activity, it displays a serine-protein kinase activity that results in the autophosphorylation of the p85alpha regulatory subunit as well as phosphorylation of other proteins such as 4EBP1, H-Ras, the IL-3 beta c receptor and possibly others (By similarity). Plays a role in the positive regulation of phagocytosis and pinocytosis (By similarity). {ECO:0000250|UniProtKB:P42336, ECO:0000250|UniProtKB:P42337, ECO:0000269|PubMed:20236230}.

2.7.1.137; 2.7.1.153; 2.7.11.1

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.153; Evidence={ECO:0000250|UniProtKB:P42336}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293; Evidence={ECO:0000250|UniProtKB:P42336}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000250|UniProtKB:P42336}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000250|UniProtKB:P42336}; 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:0000250|UniProtKB:P32871}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:P32871}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:55632, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83416, ChEBI:CHEBI:83419, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P42336}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55633; Evidence={ECO:0000250|UniProtKB:P42336}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol 3,4,5-triphosphate) + ADP + H(+); Xref=Rhea:RHEA:43396, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77137, ChEBI:CHEBI:83243, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P42336}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43397; Evidence={ECO:0000250|UniProtKB:P42336};

PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis. {ECO:0000250|UniProtKB:P42336}.

Angiogenesis;ATP-binding;Kinase;Nucleotide-binding;Phagocytosis;Proto-oncogene;Reference proteome;Serine/threonine-protein kinase;Transferase

actin cytoskeleton organization [GO:0030036]; adipose tissue development [GO:0060612]; angiogenesis [GO:0001525]; autosome genomic imprinting [GO:0141068]; cardiac muscle cell contraction [GO:0086003]; cell migration [GO:0016477]; cellular response to glucose stimulus [GO:0071333]; cellular response to hydrostatic pressure [GO:0071464]; cellular response to insulin stimulus [GO:0032869]; energy homeostasis [GO:0097009]; glucose metabolic process [GO:0006006]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; liver development [GO:0001889]; negative regulation of actin filament depolymerization [GO:0030835]; negative regulation of anoikis [GO:2000811]; negative regulation of fibroblast apoptotic process [GO:2000270]; negative regulation of gene expression [GO:0010629]; negative regulation of neuron apoptotic process [GO:0043524]; phagocytosis [GO:0006909]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein localization to membrane [GO:1905477]; positive regulation of smooth muscle cell proliferation [GO:0048661]; regulation of actin filament organization [GO:0110053]; regulation of cellular respiration [GO:0043457]; regulation of gene expression [GO:0010468]; regulation of multicellular organism growth [GO:0040014]; regulation of protein phosphorylation [GO:0001932]; relaxation of cardiac muscle [GO:0055119]; response to activity [GO:0014823]; response to butyrate [GO:1903544]; response to dexamethasone [GO:0071548]; response to leucine [GO:0043201]; response to muscle inactivity [GO:0014870]; response to muscle stretch [GO:0035994]; vascular endothelial growth factor signaling pathway [GO:0038084]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943]; phosphatidylinositol 3-kinase complex, class IB [GO:0005944]; plasma membrane [GO:0005886]

1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; insulin receptor substrate binding [GO:0043560]; kinase activity [GO:0016301]; protein kinase activator activity [GO:0030295]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]

DOMAIN: The PI3K-ABD domain and the PI3K-RBD domain interact with the PI3K/PI4K kinase domain. The C2 PI3K-type domain may facilitate the recruitment to the plasma membrane. The inhibitory interactions with PIK3R1 are mediated by the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1, and the C2 PI3K-type domain, the PI3K helical domain, and the PI3K/PI4K kinase domain with the nSH2 (N-terminal SH2) region of PIK3R1. {ECO:0000250|UniProtKB:P42336}.

IPR016024;IPR035892;IPR011009;IPR000403;IPR036940;IPR018936;IPR002420;IPR003113;IPR001263;IPR042236;IPR000341;IPR037704;IPR015433;IPR029071;

2.60.40.150;1.10.1070.11;1.25.40.70;

A0A0G2K3I9

MSGSFELSVQDLNDLLSDGSGCYSLPSQPCNEVIPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMHVNTSASFYKDTGITYMGIKANDTQEFNLSAYFERAADFIDQALAHKNEASWVHGSFPIQAIPKENSLPLDLEKFY

Rattus norvegicus (Rat)

FUNCTION: Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues, with a preference for phosphotyrosine as a substrate. {ECO:0000256|RuleBase:RU366038}.

3.1.3.16; 3.1.3.48

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:0000256|RuleBase:RU366038}; 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:0000256|RuleBase:RU366038}; 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:0000256|RuleBase:RU366038};

Hydrolase;Protein phosphatase;Proteomics identification;Reference proteome

cellular response to epidermal growth factor stimulus [GO:0071364]; dephosphorylation [GO:0016311]; in utero embryonic development [GO:0001701]; negative regulation of cell migration [GO:0030336]; negative regulation of chemotaxis [GO:0050922]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of JNK cascade [GO:0046329]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of T cell activation [GO:0050868]; negative regulation of T cell receptor signaling pathway [GO:0050860]; positive regulation of focal adhesion disassembly [GO:0120183]; positive regulation of mitotic cell cycle [GO:0045931]; regulation of focal adhesion assembly [GO:0051893]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; immunological synapse [GO:0001772]; nucleus [GO:0005634]

cytoskeletal protein binding [GO:0008092]; MAP kinase phosphatase activity [GO:0033549]; myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; phosphoprotein phosphatase activity [GO:0004721]; protein kinase binding [GO:0019901]; protein tyrosine kinase binding [GO:1990782]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; receptor tyrosine kinase binding [GO:0030971]

IPR020405;IPR000340;IPR029021;IPR020422;

3.90.190.10;

A0A0G2K3N6

MEPATALPPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKAIAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTSDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEEATEARTHNLRRRMGCATPKRENEKEVKSTIKQEPTEKKDCVLESEKDKPKSRAKKTATAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLLPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKISPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCIKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYNLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQSQLTVNELRQFVTQLCALPCVLSQTPLLKDLLNRVEDFQQQSQRLLSEERPRASELQQLLDVSFTFDVELPQLAEMRIRLEQARWLEEVQQACLDSSSLSLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLRARPRHSLSSLATAVKEMEEIPAYLPNGTVLKDSVQKARDWVQDVDALQAGGRVPVLETLIELVARGRSIPVHLNSLPRLEMLVSEVHAWKESAAKTFLLENSPYSLLEVLCPRCDIGLLGLKRKQRKLKDPLPSGKKRSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRFANEEKLLSPAQDVETKVCLCQKTPATPMIQCELCRDAFHTSCVAVSSISQSSRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKLVQDQAGSGLLFSRWPASAGTASAADKVSQPPGTTSFSLPEDWDNRTSYLHSPFSTGQSCIPLHGLSPEVNELLMEAQLLQVSLPEVQELYQTLLTKPSSAQQADRSSPVRPSSEKNDCLRGKRDAINSLERKLKRRPEREGLPSERWDRVKKMRTPQKKKIKLSHPKDMNNFKLERERSYDLVRNAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVDWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTGKDAPSRK

Rattus norvegicus (Rat)

1.14.11.67

CATALYTIC ACTIVITY: Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67; Evidence={ECO:0000256|ARBA:ARBA00000604};

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|ARBA:ARBA00001954};

Chromatin regulator;Dioxygenase;Metal-binding;Nucleus;Oxidoreductase;Reference proteome;Repeat;Transcription;Transcription regulation;Zinc;Zinc-finger

branching involved in mammary gland duct morphogenesis [GO:0060444]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to leukemia inhibitory factor [GO:1990830]; chromatin remodeling [GO:0006338]; lens fiber cell differentiation [GO:0070306]; mammary duct terminal end bud growth [GO:0060763]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of gene expression [GO:0010628]; positive regulation of mammary gland epithelial cell proliferation [GO:0033601]; post-embryonic development [GO:0009791]; regulation of DNA-templated transcription [GO:0006355]; regulation of estradiol secretion [GO:2000864]; response to fungicide [GO:0060992]; single fertilization [GO:0007338]; uterus morphogenesis [GO:0061038]

chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]

DNA binding [GO:0003677]; histone binding [GO:0042393]; histone H3K4 demethylase activity [GO:0032453]; histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; nucleic acid binding [GO:0003676]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270]

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

IPR001606;IPR036431;IPR003347;IPR003349;IPR048615;IPR047981;IPR047978;IPR047979;IPR013637;IPR019786;IPR004198;IPR011011;IPR001965;IPR019787;IPR013083;

1.10.150.60;2.60.120.650;3.30.40.10;

A0A0G2K3V4

MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVAEQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADTTNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKSRQEYEDIAVKLGTDLEYLKKIRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA

Rattus norvegicus (Rat)

2.4.1.255

PATHWAY: Protein modification; protein glycosylation. {ECO:0000256|ARBA:ARBA00004922}.

Glycosyltransferase;Reference proteome;Repeat;TPR repeat;Transferase

apoptotic process [GO:0006915]; cellular response to glucose stimulus [GO:0071333]; circadian regulation of gene expression [GO:0032922]; hemopoiesis [GO:0030097]; mitophagy [GO:0000423]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of protein ubiquitination [GO:0031397]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of proteolysis [GO:0045862]; positive regulation of TORC1 signaling [GO:1904263]; positive regulation of transcription from RNA polymerase II promoter by glucose [GO:0000432]; positive regulation of translation [GO:0045727]; protein O-linked glycosylation [GO:0006493]; protein processing [GO:0016485]; regulation of gluconeogenesis [GO:0006111]; regulation of glycolytic process [GO:0006110]; regulation of insulin receptor signaling pathway [GO:0046626]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; regulation of Rac protein signal transduction [GO:0035020]; regulation of synapse assembly [GO:0051963]; response to insulin [GO:0032868]

cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; NSL complex [GO:0044545]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein N-acetylglucosaminyltransferase complex [GO:0017122]

chromatin DNA binding [GO:0031490]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; protein O-acetylglucosaminyltransferase activity [GO:0097363]

IPR029489;IPR011990;IPR001440;IPR019734;

3.30.720.150;3.40.50.11380;3.40.50.2000;1.25.40.10;

A0A0G2K490

MASDSPARSLDEIDLSALRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPPGMDDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKSKKWSKKFQSFIESCLVKNHGQRPATEQLMKHPFIRDQPNERQVRIQLKDHIDRTKKKRGEKDETEYEYSGSEEEEEENDSGEPSSILNLPGESTLRRDFLRLQLANKERSEALRRQQLEQQQRENEEHKRQLLAERQKRIEEQKEQRRRLEEQQRREKELRKQQEREQRRHYEEQMRREEERRRAEHEQEYIRRQLEEEQRQLEILQQQLLHEQALLLEYKRKQLEEQRQAERLQRQLKQERDYLVSLQHQRQEQRPLEKKPLYHYKEGMSPSEKPAWAKEVEERSRLNRQSSPAMPHKVANRISDPNLPPRSESFSISGVQPARTPPMLRPVDPQIPQLVAVKSQGPALTASQSVHEQPTKGLSGFQEALNVTSHRVEMPRQNSDPTSENPPLPTRIEKFDRSSWLRQEEDIPPKVPQRTTSISPALARKNSPGNGSALGPRLGSQPIRASNPDLRRTEPVLESSLQRTSSGSSSSSSTPSSQPSSQGGSQPGSQAGSSERTRVRANSKSEGSPVLPHEPSKVKPEESRDIPRPSRPASYKKAIDEDLTALAKELRELRIEETNRPLKKVTDYSSSSEESESSEEEEEDGESETHDGTVAVSDIPRLIPTGAPGKNEQYNMGMVGTHGLETSHADTFGGSISREGTLMIRETAEEKKRSGHSDSNGFAGHINLPDLVQQSHSPAGTPTEGLGRVSTHSQEMDTGAEYGMGSSTKASFTPFVDPRVYQTSPTDEDEEDDESSAAALFTSELLRQEQAKLNEARKISVVNVNPTNIRPHSDTPEIRKYKKRFNSEILCAALWGVNLLVGTENGLMLLDRSGQGKVYNLINRRRFQQMDVLEGLNVLVTISGKKNKLRVYYLSWLRNRILHNDPEVEKKQGWITVGDLEGCIHYKVVKYERIKFLVIALKNAVEIYAWAPKPYHKFMAFKSFADLQHKPLLVDLTVEEGQRLKVIFGSHTGFHVIDVDSGNSYDIYIPSHIQGNITPHAIVILPKTDGMEMLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIHSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVFFMTLNRNSMMNW

Rattus norvegicus (Rat)

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;Nucleotide-binding;Reference proteome

actin cytoskeleton organization [GO:0030036]; cytoskeleton organization [GO:0007010]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; microvillus assembly [GO:0030033]; neuron projection morphogenesis [GO:0048812]; phosphorylation [GO:0016310]; positive regulation of JNK cascade [GO:0046330]; positive regulation of protein phosphorylation [GO:0001934]; protein localization to plasma membrane [GO:0072659]; regulation of dendrite morphogenesis [GO:0048814]; regulation of MAPK cascade [GO:0043408]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; response to organonitrogen compound [GO:0010243]

apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic density, intracellular component [GO:0099092]; presynapse [GO:0098793]; recycling endosome [GO:0055037]

ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]

IPR001180;IPR011009;IPR000719;IPR017441;IPR008271;

1.10.510.10;

A0A0G2K5I7

MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRTSYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPPIYGADVNGTLYEQHVDEWNIGRLKTILDLVEKESGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRRFQPERYKLWKAGKDSTVIDHTLPTPEAAEFLKDSGLTPRAGNEECPEEDSEAAEQGEEGDVKRSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEELSSGQYEMTECQATLAPVRPTHSSVRQVEDSLPFPDYSDPTEVKFEELKNVKLEEEDEDEEPEAAALDLSVNPESVEGRLVFSGSKKKASSSLGSSSSQDSVSSDSETTESVSCQGQEKTVLTVHSYSRGDGKAAPGEPSVKRQRSAPRSISEQELAEVADEYMLSLEENKKTKGRRQPLSKLPRHHPLVLQECGSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNELMAQQAPHCAVCMIFQTYHQVEFGGFSQSCGNASEPAAQPQRTKPLIPEMCFTTTGCSTDINLSTPYLEEDGTSMLVSCKKCSVRVHASCYGVPPAKASEEWMCSRCSANALEEDCCLCSLRGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCVFCKKRRKRNAGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKIPNLERAKGALLSITAGQKVISKHKNGRFYQCEVVRLTTETFYEVNFDDGSFSDNLYPEDIVSQDCLQLGPPAEGEVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVKRDDVYTLDEELPKRVKSRLSVASDMRFNEIFTEKEVKQEKKRQRVINSRYREDYIEPALYRAIME

Rattus norvegicus (Rat)

1.14.11.66

CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|ARBA:ARBA00001954};

Chromatin regulator;Dioxygenase;Metal-binding;Nucleus;Oxidoreductase;Reference proteome;Transcription;Transcription regulation;Zinc;Zinc-finger

apoptotic chromosome condensation [GO:0030263]; cardiac muscle hypertrophy in response to stress [GO:0014898]; chromatin remodeling [GO:0006338]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of autophagy [GO:0010507]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron differentiation [GO:0045666]; regulation of gene expression [GO:0010468]; response to nutrient levels [GO:0031667]

chromatin [GO:0000785]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]

histone demethylase activity [GO:0032452]; histone H3K36 demethylase activity [GO:0051864]; histone H3K9 demethylase activity [GO:0032454]; histone H3K9me2/H3K9me3 demethylase activity [GO:0140684]; methylated histone binding [GO:0035064]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]

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

IPR034732;IPR003347;IPR047482;IPR003349;IPR040477;IPR002999;IPR047479;IPR047481;IPR011011;IPR001965;IPR013083;

2.30.30.140;3.10.330.70;2.60.120.650;3.30.40.10;

A0A0G2K5L6

MVLLLFLTCLVFSCLTISWLKIWGKMTDSKPLSNSKVDASLLSSKEESFSASDQSEEHGDCSCPLTTPDQEELASHGGPVDASQQRNSVPSSHQKPPRNPLSSNDTCSSPELQTNRVAAPGSEVPEANGLPFPARPQTQRTGSPTREDKKQAHIKRQLMTSFILGSLDDNSSDEDPSASSFQTSSRKGSRASLGTLSQEAALNTADPESHTPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGNRVIETVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADQYVPVPGGPNNNNYANVELIIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKISSTIVAQTLQIPTLPWSGSGLTVEWTEDSQHQGKCISVPEDVYEQGCVRDVDEGLQAAEKVGFPLMIKASEGGGGKGIRRAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPVSFETPLSPPIARGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQAEKPDIMLGVVCGALNVADAMFRTCMTEFLHSLERGQVLPADSLLNIVDVELIYGGIKYVLKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGSSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLMQYTVEDGQHVEVGSSYAEMEVMKMIMTLNVQESGRVKYIKRPGAVLEAGCVVAKLELDDPSKVHAAQPFTGELPAQQTLPILGERLHQVFHSVLENLTNVMNGYCLPEPFFSMKLKDWVEKLMMTLRHPSLPLLELQEIMTSVAGRIPVPVEKAVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKVDREAFFMNTQSIVQLIQRYRSGTRGYMKAVVLDLLRRYLNVEHHFQQAHYDKCVINLREQFKPDMTRVLDCIFSHSQVAKKNQLVTMLIDELCGPDPTLSEELTSILKELTQLSRSEHCKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRELPDGTCVVEFQFMLPSSHPNRMAMPINVSDPDLLRHSKELFMDSGFSPLCQRMGAMVAFRRFEEFTRNFDEVISCFANVPTDTPLFSKACTSLYSEEDSKPSFFLSQSLQEEPIHILNVAIQCADHMEDERLVPVFRAFVQSKKHILVDYGLRRITFLIAQEREFPKFFTFRARDEFAEDRIYRHLEPALAFQLELSRMRNFDLTAVPCANHKMHLYLGAAKVKEGLEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPLKIEESVRAMVMRYGSRLWKLRVLQAEVKINIRQTTSDCAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSFGNKQGSLHGMLINTPYVTKDLLQAKRFQAQSLGTTYVYDFPEMFRQALFKLWGSPEKYPKDILTYTELVLDSQGQLVEMNRLPGCNEVGMVVFKMRFKTPEYPEGRDTIVIGNDITFQIGSFGIGEDFLYLRASEMARTEGIPQIYLAANSGARMGLSEEIKQIFQVAWVDPEDPYKGFRYLYLTPQDYTQISSQNSVHCKHIEDEGESRYVIVDVIGKDSSLGVENLRGSGMIAGEASLAYEKNVTISMVTCRAIGIGAYLVRLGQRVIQVENSHIILTGAGALNKVLGREVYTSNNQLGGVQIMHTNGVSHVTVPDDFEGVCTILEWLSYIPKDNQSPVPIITPSDPIDREIEFTPTKAPYDPRWLLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRSVEVAVPADPANLDSEAKIIQQAGQVWFPDSAFKTAQVIRDFNQEHLPLMIFANWRGFSGGMKDMYEQMLKFGAYIVDSLRLFKQPVLIYIPPGAELRGGAWVVLDSSINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLVKTIRRIDPVCKKLLGQLGTAQLPDKDRKELESQLKAREDLLLPIYHQVAVQFADLHDTPGHMLEKGIISDVLEWKTTRTYFYWRLRRLLLEAQVKQEILRASPELSHEHTQSMLRRWFVETEGAVKAYLWDSNQVVVQWLEQHWSARDNLRSTIRENINYLKRDSVLKTIQSLVQEHPEATMDCVAYLSQHLTPAEQMQVVQLLSTTESPASH

Rattus norvegicus (Rat)

6.4.1.2

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|ARBA:ARBA00001448}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11309; Evidence={ECO:0000256|ARBA:ARBA00001448};

COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000256|ARBA:ARBA00001953};

PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.

ATP-binding;Biotin;Fatty acid biosynthesis;Fatty acid metabolism;Ligase;Lipid biosynthesis;Lipid metabolism;Manganese;Multifunctional enzyme;Nucleotide-binding;Phosphoprotein;Proteomics identification;Reference proteome;Signal

acetyl-CoA metabolic process [GO:0006084]; energy homeostasis [GO:0097009]; fatty acid biosynthetic process [GO:0006633]; fatty acid oxidation [GO:0019395]; glucose import [GO:0046323]; intracellular aspartate homeostasis [GO:0090459]; intracellular glutamate homeostasis [GO:0090461]; lactic acid secretion [GO:0046722]; malonyl-CoA biosynthetic process [GO:2001295]; negative regulation of fatty acid beta-oxidation [GO:0031999]; negative regulation of fatty acid oxidation [GO:0046322]; negative regulation of gene expression [GO:0010629]; negative regulation of lipid catabolic process [GO:0050995]; pentose-phosphate shunt [GO:0006098]; positive regulation of heart growth [GO:0060421]; positive regulation of lipid storage [GO:0010884]; protein homotetramerization [GO:0051289]; purine nucleotide metabolic process [GO:0006163]; regulation of cardiac muscle hypertrophy in response to stress [GO:1903242]; regulation of glucose metabolic process [GO:0010906]; response to nutrient [GO:0007584]; response to nutrient levels [GO:0031667]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]; tricarboxylic acid metabolic process [GO:0072350]

mitochondrial fatty acid beta-oxidation multienzyme complex [GO:0016507]; mitochondrion [GO:0005739]; nucleus [GO:0005634]

acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; biotin binding [GO:0009374]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]

IPR049076;IPR049074;IPR034733;IPR013537;IPR011761;IPR013815;IPR005481;IPR011764;IPR005482;IPR000089;IPR005479;IPR029045;IPR011763;IPR011762;IPR016185;IPR011054;IPR011053;

2.40.50.100;3.40.50.20;3.30.1490.20;3.30.470.20;2.40.460.10;3.90.1770.10;

A0A0G2K5V8

MTVFRQENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIRHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILSGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYDFEEEFFRNTSTLAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDTQQALSRKASAVNMEKFKKFAARKKWKQSVRLISLCQRLSRSFLSRSNMSVARSDDTLDEEDSFVMKAIIHAINDDNVPGLQHLLGSLSSYDVNQPNKHGTPPLLIAAGCGNIQMLQLLIKRGSRIDVQDKGGSNAIYWASRHGHVDTLKFLNENKCPLDVKDKSGETALHVAARYGHADVVQLLCSFGSNPDFQDKEEETPLHCAAWHGYYSVARALCEVGCNVNIKNREGETPLLTASARGYHDIVECLAEHGADLNASDKDGHIALHLAVRRCQMEVIKTLLGHGCLVDFQDRHGNTPLHVACKDGSAPIVVALCEASCNLDISNKYGRTPLHLAANNGILDVVRYLCLMGANVEALTLDGKTAEDLAKAEQHEHVAGLLARLRKDTHRGLFIQQLRPTQNLQPRIKLKLFGHSGSGKSTLVESLKCGLLRSFFRRRRPRLSSTNSTRFPPSPLATKPTVSVSINNLYPGCENVSVRSRSMMFEPGLTKGMLEVFVAPSHHLHCSTDDQSTKAIDIQNAYLNGVGDFSVWEFSGNPVYFCCYDYFAANDPTSIHIIVFSLEEPYEIQLNQVIFWLSFLKSLVSVEEPIAFGGKLKNPLRVVLVATHADIMNIPRPAGGEFGYDKDTSLLKEIRNRFGNDLHVSNKLFVLDAGASGSKDIKVLRNHLQEIRSQIVSGCPPMTHLCEKIISTLPSWRKLNGPNQLMSLQQFVYDVQDQLNPLASEDDLRRIAQQLHSTGEINIMQSETVQDVLLLDPRWLCTNVLGKLLSVETPRALHHYRGRYTMEDIQRLVPDSDVEELLQILDAMDICARDLSSGTMVDIPALIKTDSLQRSWADEEDEVMVYGGVRIVPVEHLTPFPCGIFHKVQVNLCRWIHQQSTEGDADIRLWVSGCRIANRGAELLVLLVNHGQGIEVQVRGLETEKIKCCLLLDSVCSTIETVMATTLPGLLTVKHYLSPQQLREHHEPVMVYQPRDFFRAQTLKESSLTNTMGGYKESFSSITCFGCHDVYSQASLGMDIHASDLSLLTRRKLSRLLDPPDPMGKDWCLLAMNLGLPDMVAKHNVNTRASRDFLPSPVHALLQEWTSYPESTVGILISKLRELGRRDAADFLLKASSVFKINLDGNGQEAYASSCNSGTSYNSISSVVSRRDSHAWTPLYDL

Rattus norvegicus (Rat)

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};

ANK repeat;ATP-binding;GTP-binding;Kinase;Nucleotide-binding;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase

apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to hydroperoxide [GO:0071447]; cellular response to type II interferon [GO:0071346]; defense response to tumor cell [GO:0002357]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; intracellular signal transduction [GO:0035556]; negative regulation of apoptotic process [GO:0043066]; negative regulation of translation [GO:0017148]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagic cell death [GO:1904094]; positive regulation of autophagy [GO:0010508]; regulation of response to tumor cell [GO:0002834]

actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; DAPK1-calmodulin complex [GO:1990722]; glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]

ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; syntaxin-1 binding [GO:0017075]

IPR002110;IPR036770;IPR020676;IPR011029;IPR000488;IPR011009;IPR027417;IPR000719;IPR017441;IPR020859;IPR008271;

1.25.40.20;1.10.533.10;1.20.5.460;1.10.510.10;

A0A0G2K612

MSNPGTRRNGSSIKIRLTVLCAKNLAKKDFFRLPDPFAKIVVDGSGQCHSTDTVKNTLDPKWNQHYDLYVGKTDSITISVWNHKKIHKKQGAGFLGCVRLLSNAISRLKDTGYQRLDLCKLNPSDTDAVRGQIVVSLQTRDRIGGGGSVVDCRGLLENEGTVYEDSGPGRPLSCLMEEPAPYTDGTGAAAGGGNCRFVESPSQDQRLLVQRLRNPEVRGSLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPSPLGTIPGGDEAFLYEFLLQGHTSEPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLQLPSEGSVEDEELPAQRYERDLVQKLKVLRHELSLQQPQAGHCRIEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRGEEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYTLQINPDSSINPDHLSYFHFVGRIMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITPVLDHTFCVEHNAFGRILQHELKPNGRNVPVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNELIPQHLLKPFDQKELELIIGGLDKIDLNDWKSNTRLKHCVADSNIVRWFWQAVETFDEERRARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPYESYEKLYEKLLTAVEETCGFAVE

Rattus norvegicus (Rat)

2.3.2.26

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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885, ECO:0000256|PIRNR:PIRNR001569};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.

Reference proteome;Transferase;Ubl conjugation pathway

BMP signaling pathway [GO:0030509]; cell differentiation [GO:0030154]; engulfment of target by autophagosome [GO:0061736]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of ossification [GO:0030279]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization [GO:0061734]; positive regulation of axon extension [GO:0045773]; positive regulation of dendrite extension [GO:1903861]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein export from nucleus [GO:0006611]; protein localization to plasma membrane [GO:0072659]; protein polyubiquitination [GO:0000209]; protein targeting to vacuole involved in autophagy [GO:0071211]; protein ubiquitination [GO:0016567]; receptor catabolic process [GO:0032801]; substrate localization to autophagosome [GO:0061753]; ubiquitin-dependent protein catabolic process [GO:0006511]

axon [GO:0030424]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]

activin receptor binding [GO:0070697]; I-SMAD binding [GO:0070411]; R-SMAD binding [GO:0070412]; SMAD binding [GO:0046332]; transforming growth factor beta receptor binding [GO:0005160]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]

IPR000008;IPR035892;IPR024928;IPR000569;IPR035983;IPR001202;IPR036020;

2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10;

A0A0G2K6C7

MASSVLEMIKEEVTCPICLELLKEPVSTDCNHSFCRACITINYESNRNTEGEGSCPVCRVCYLFRNLRPNRHVANIVERLKGFKSIPEEEQKVNVCAQHGEKLQLFCKKDKMAICWLCERSQEHHGHKTALVEEVDHEYKEKLQAALQKLMADKKEFENWKDDLQKERTYWQNQIQKDVENVQSEFKGMRDIMDSEEKKELQKLMQEKEDIMSSLEESENEYSQQSKLLGDLILDVEHQLQCSATEMLQGVENTIKRSHTFSMRKPKTIPKEQRRVFRAPDLQGMLQVLQEVTEAQRYWVQVTLVESNNPNIFITADKRQIRYEDHQARHFARPTENCHAGVLGYPAIQSGKHYWEVDVSGKGSWVLGLSDGSYLFNPIFRSNAERPPNPPLFRLNLSNDSHSRLSLSNDSHYQPKYGFWVIGLWGNSVYNAFEECTFTGKPSVLTLSLMVRPCRVGIFLDCAAGTLSFYNISNHGTLIYRFCAGSFPDRVFPYFNPMGSSEPLTICWPDS

Rattus norvegicus (Rat)

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};

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

Acetylation;Antiviral defense;Autophagy;Coiled coil;Cytoplasm;Immunity;Innate immunity;Metal-binding;Nucleus;Proteomics identification;Reference proteome;Transferase;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger

activation of innate immune response [GO:0002218]; autophagy [GO:0006914]; innate immune response [GO:0045087]; negative regulation of viral entry into host cell [GO:0046597]; positive regulation of autophagy [GO:0010508]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of MAPK cascade [GO:0043410]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; regulation of lipopolysaccharide-mediated signaling pathway [GO:0031664]; regulation of protein localization [GO:0032880]; regulation of viral entry into host cell [GO:0046596]; suppression of viral release by host [GO:0044790]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; P-body [GO:0000932]

identical protein binding [GO:0042802]; pattern recognition receptor activity [GO:0038187]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein-macromolecule adaptor activity [GO:0030674]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]

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

IPR001870;IPR043136;IPR003879;IPR013320;IPR003877;IPR027370;IPR000315;IPR001841;IPR013083;IPR017907;

2.60.120.920;3.30.160.60;3.30.40.10;

A0A0G2K6D0

MKSCGVSLATAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQLENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKNCSNTSGLAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGNAVPHPPVQQQTHSWCLTPQKLQMRQTGVAQVRPTGIPNGPTADSSLPTNSASGQQPQLPLTRMPSVSQPGVQPACPRQALANGPFSAGHVPCSTSRTLGSTDTILIGNNHVTGSGSNGNVPYLQRNAPTLPHNRTNLTSSTEEPWKNQLSNSTQGLHKGQSSHLAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNTLTLPETNRQTGETPNSTASVEGLPNHVHQVMADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGPGTCDIVNNIHPTVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPIKTDLLLVSHRPSPQIIPSVSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYYINNLVGCIFVLILLTSFIYLWLTYKDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGKRRRGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMVKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCAWKTSGNLENFVVLEQYKMEDLMQVYDQFTLVSEINM

Rattus norvegicus (Rat)

1.14.11.68

CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.68; Evidence={ECO:0000256|ARBA:ARBA00034421};

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|ARBA:ARBA00001954}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000256|ARBA:ARBA00001961};

Iron;Membrane;Metal-binding;Nucleus;Oxidoreductase;Proteomics identification;Reference proteome;TPR repeat;Transmembrane;Transmembrane helix

cellular response to angiotensin [GO:1904385]; cellular response to endothelin [GO:1990859]; cellular response to hypoxia [GO:0071456]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to vitamin D [GO:0071305]; chromatin remodeling [GO:0006338]; circulatory system development [GO:0072359]; embryonic organ development [GO:0048568]; heart development [GO:0007507]; heart morphogenesis [GO:0003007]; in utero embryonic development [GO:0001701]; mesodermal cell differentiation [GO:0048333]; multicellular organism growth [GO:0035264]; negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway [GO:1903298]; neural tube closure [GO:0001843]; neural tube development [GO:0021915]; notochord morphogenesis [GO:0048570]; positive regulation of cell size [GO:0045793]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein modification process [GO:0036211]; regulation of gene expression [GO:0010468]; respiratory system process [GO:0003016]; response to hypoxia [GO:0001666]; somite rostral/caudal axis specification [GO:0032525]

histone methyltransferase complex [GO:0035097]; membrane [GO:0016020]; MLL3/4 complex [GO:0044666]; nucleus [GO:0005634]

chromatin DNA binding [GO:0031490]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]

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

IPR003347;IPR046941;IPR048562;IPR048560;IPR011990;IPR019734;

1.20.58.1370;2.10.110.20;2.60.120.650;1.25.40.10;

A0A0G2K6D8

MVLLGVDRMRGLIFRPTRGRWITQMSQLRSHGSTGLFVPPSPPLDHEKIKELQRFISLSKKLLVMTGAGISTESGIPDYRSEKVGLYARTDRRPIQHIDFIRSAPVRQRYWARNFVGWPQFSSHQPNPAHWALSNWEKLGKLHWLVTQNVDALHSKAGNQRLTELHGCMHRVLCLSCGEQTARRVLQDRFQALNPSWSAEAQGVAPDGDVFLTEEQVRSFRVPCCDRCGGPLKPDVVFFGDTVNPDKVDFVHQRVKEADSLLVVGSSLQVYSGYRFILTAREKKLPIAILNIGPTRSDDLACLKLDSRCGELLPLIDPQ

Rattus norvegicus (Rat)

FUNCTION: Acts as NAD-dependent protein lipoamidase, biotinylase, deacetylase and ADP-ribosyl transferase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner. Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest. In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation. Acts as a tumor suppressor. Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis. Does not seem to deacetylate PC. Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1-PPARA interaction probably through the regulation of NAD(+) levels. Down-regulates insulin secretion. {ECO:0000256|HAMAP-Rule:MF_03161}.

2.3.1.-; 2.3.1.286; 2.4.2.-

CATALYTIC ACTIVITY: Reaction=H2O + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NAD(+) = 2''-O-lipoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:63640, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10474, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:83099, ChEBI:CHEBI:189572; Evidence={ECO:0000256|HAMAP-Rule:MF_03161}; 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:0000256|HAMAP-Rule:MF_03161}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-biotinyl-L-lysyl-[protein] + NAD(+) = 2''-O-biotinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:70479, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:83144, ChEBI:CHEBI:189573; Evidence={ECO:0000256|HAMAP-Rule:MF_03161}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + NAD(+) = H(+) + nicotinamide + S-(ADP-D-ribosyl)-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56612, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14624, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57540, ChEBI:CHEBI:140607; Evidence={ECO:0000256|HAMAP-Rule:MF_03161};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-Rule:MF_03161}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03161};

Metal-binding;Mitochondrion;NAD;Reference proteome;Transferase;Transit peptide;Zinc

cellular response to hypoxia [GO:0071456]; DNA damage response [GO:0006974]; glutamine metabolic process [GO:0006541]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of fatty acid oxidation [GO:0046322]; negative regulation of insulin secretion [GO:0046676]; negative regulation of protein processing involved in protein targeting to mitochondrion [GO:1903217]; positive regulation of lipid biosynthetic process [GO:0046889]; regulation of glutamine family amino acid metabolic process [GO:0000820]; tricarboxylic acid metabolic process [GO:0072350]

mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]

histone deacetylase activity [GO:0004407]; lipoamidase activity [GO:0061690]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+ binding [GO:0070403]; NAD-dependent protein biotinidase activity [GO:0106420]; NAD-dependent protein deacetylase activity [GO:0034979]; NAD-dependent protein lipoamidase activity [GO:0106419]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-Rule:MF_03161}.

IPR029035;IPR003000;IPR026591;IPR026587;IPR026590;

3.30.1600.10;3.40.50.1220;

A0A0G2K6M9

MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPVPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPTAAPISTSELKKVVALYDYMPMNANDLQLRKGEEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSTGEPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLISRLKYPVSKQNKNAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIREGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKIPYERFTNSETAEHIAQGLRLYRPHLASDRVYTIMYSCWHEKADERPSFKILLSNILDVMDEES

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|RuleBase:RU362096};

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

Adaptive immunity;ATP-binding;Cytoplasm;Immunity;Kinase;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;SH2 domain;SH3 domain;Transferase;Tyrosine-protein kinase;Zinc;Zinc-finger

B cell affinity maturation [GO:0002344]; B cell receptor signaling pathway [GO:0050853]; cell maturation [GO:0048469]; cellular response to interleukin-7 [GO:0098761]; cellular response to molecule of fungal origin [GO:0071226]; cellular response to reactive oxygen species [GO:0034614]; eosinophil homeostasis [GO:1990959]; histamine secretion by mast cell [GO:0002553]; intracellular signal transduction [GO:0035556]; monocyte proliferation [GO:0061516]; negative regulation of B cell activation [GO:0050869]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of cytokine production [GO:0001818]; negative regulation of interleukin-10 production [GO:0032693]; negative regulation of leukocyte proliferation [GO:0070664]; neutrophil homeostasis [GO:0001780]; phosphorylation [GO:0016310]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of interleukin-17A production [GO:0150153]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; positive regulation of phagocytosis [GO:0050766]; positive regulation of synoviocyte proliferation [GO:1901647]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type I hypersensitivity [GO:0001812]; positive regulation of type III hypersensitivity [GO:0001805]; proteoglycan catabolic process [GO:0030167]; response to lipopolysaccharide [GO:0032496]; response to organic substance [GO:0010033]; T cell receptor signaling pathway [GO:0050852]

cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; protein tyrosine kinase activity [GO:0004713]

IPR035574;IPR011009;IPR011993;IPR001849;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR036028;IPR001452;IPR008266;IPR020635;IPR001562;

2.30.29.30;3.30.505.10;2.30.30.40;1.10.510.10;

A0A0G2K6S0

GALALALLGLAATLGASPTSGQRWPVPYKRFSFRPKTDPFCQAKYTFCPTGSPIPVMKDNDVIEVLRLQAPVWEFKYGDLLGHFKIMHDAIGFRSTLTGKNYTIEWYELFQLGNCTFPHLRPEVNAPFWCNQGAACFFEGIYDKHWKENGTLSLVATISGNTFNKVAEWVKQDNETGIYYETWTVRASPGKGAQTWFESYDCSNFVLRTYEKLAEFGTEFKKIETNYMKIFLYSGEPIYLGNETSIFGPKGNKTLALAIKKFYGPVKRYSSTKDFLLNFLKIFDTVIMHREFYLFYNFEYWFLPMKPPFKPPFVKITYEETPLPTRHTIFTDL

Rattus norvegicus (Rat)

FUNCTION: Exhibits palmitoyl protein thioesterase (S-depalmitoylation) activity in vitro and most likely plays a role in protein S-depalmitoylation. {ECO:0000256|ARBA:ARBA00044494}.

3.1.2.22

CATALYTIC ACTIVITY: Reaction=2 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77599, ChEBI:CHEBI:139150, ChEBI:CHEBI:139152, ChEBI:CHEBI:197411; Evidence={ECO:0000256|ARBA:ARBA00044481}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77600; Evidence={ECO:0000256|ARBA:ARBA00044481}; CATALYTIC ACTIVITY: Reaction=2 3-hexadecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-hexadecanoyl-sn-glycero-1-phospho-(3'-hexadecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77607, ChEBI:CHEBI:44859, ChEBI:CHEBI:197411, ChEBI:CHEBI:197415; Evidence={ECO:0000256|ARBA:ARBA00044455}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77608; Evidence={ECO:0000256|ARBA:ARBA00044455}; CATALYTIC ACTIVITY: Reaction=2 3-octadecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-octadecanoyl-sn-glycero-1-phospho-(3'-octadecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77603, ChEBI:CHEBI:197411, ChEBI:CHEBI:197412, ChEBI:CHEBI:197414; Evidence={ECO:0000256|ARBA:ARBA00044460}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77604; Evidence={ECO:0000256|ARBA:ARBA00044460}; CATALYTIC ACTIVITY: Reaction=2 3-tetradecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-tetradecanoyl-sn-glycero-1-phospho-(3'-tetradecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77611, ChEBI:CHEBI:197411, ChEBI:CHEBI:197413, ChEBI:CHEBI:197416; Evidence={ECO:0000256|ARBA:ARBA00044453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77612; Evidence={ECO:0000256|ARBA:ARBA00044453}; CATALYTIC ACTIVITY: Reaction=2 a 3-acyl-sn-glycero-1-phospho-(1'-sn-glycerol) = a 3-acyl-sn-glycero-1-phospho-(3'-acyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77619, ChEBI:CHEBI:77717, ChEBI:CHEBI:197411, ChEBI:CHEBI:197425; Evidence={ECO:0000256|ARBA:ARBA00044472}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77620; Evidence={ECO:0000256|ARBA:ARBA00044472}; CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000256|ARBA:ARBA00037021}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234; Evidence={ECO:0000256|ARBA:ARBA00037021};

Glycoprotein;Reference proteome;Signal

brain development [GO:0007420]; glycosylation [GO:0070085]; lysosomal lumen acidification [GO:0007042]; lysosome organization [GO:0007040]; neurogenesis [GO:0022008]; retrograde transport, endosome to Golgi [GO:0042147]; signal peptide processing [GO:0006465]; visual perception [GO:0007601]

endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; vacuolar lumen [GO:0005775]

bis(monoacylglycero)phosphate synthase activity [GO:0160121]; hydrolase activity, acting on glycosyl bonds [GO:0016798]; mannose binding [GO:0005537]

IPR026138;

A0A0G2K719

IDLRDVHSEYSYLVICFFFLGFYDKDSSGWSSSKDKDAYSSFGSRGDSRGKSSFFGDRGSGSRGRFDDRGRGDYDGIGGRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYADGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGAEIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEEIDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAFEHHYKGSSRGRSKSSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGSVHLRFGEIQHCGYGGFYNSDGYGGNYNSQGVDWWGN

Rattus norvegicus (Rat)

3.6.4.13

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

cell differentiation [GO:0030154]; cellular response to arsenic-containing substance [GO:0071243]; cellular response to osmotic stress [GO:0071470]; cellular response to virus [GO:0098586]; chromosome segregation [GO:0007059]; cytosolic ribosome assembly [GO:0042256]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; gamete generation [GO:0007276]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway [GO:0097193]; lipid homeostasis [GO:0055088]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of gene expression [GO:0010629]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of translation [GO:0017148]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell growth [GO:0030307]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of gene expression [GO:0010628]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of protein acetylation [GO:1901985]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of protein K63-linked ubiquitination [GO:1902523]; positive regulation of toll-like receptor 7 signaling pathway [GO:0034157]; positive regulation of toll-like receptor 8 signaling pathway [GO:0034161]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of translation [GO:0045727]; positive regulation of translation in response to endoplasmic reticulum stress [GO:0036493]; positive regulation of translational initiation [GO:0045948]; positive regulation of type I interferon production [GO:0032481]; positive regulation of viral genome replication [GO:0045070]; primary miRNA processing [GO:0031053]; protein localization to cytoplasmic stress granule [GO:1903608]; response to virus [GO:0009615]; RNA secondary structure unwinding [GO:0010501]; stress granule assembly [GO:0034063]; translational initiation [GO:0006413]; Wnt signaling pathway [GO:0016055]

cell leading edge [GO:0031252]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosolic small ribosomal subunit [GO:0022627]; eukaryotic translation initiation factor 3 complex [GO:0005852]; NLRP3 inflammasome complex [GO:0072559]; nucleus [GO:0005634]; P granule [GO:0043186]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; CTPase activity [GO:0043273]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; eukaryotic initiation factor 4E binding [GO:0008190]; gamma-tubulin binding [GO:0043015]; GTPase activity [GO:0003924]; mRNA 5'-UTR binding [GO:0048027]; mRNA binding [GO:0003729]; poly(A) binding [GO:0008143]; primary miRNA binding [GO:0070878]; protein serine/threonine kinase activator activity [GO:0043539]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; ribosomal small subunit binding [GO:0043024]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA stem-loop binding [GO:0035613]; RNA strand annealing activity [GO:0033592]; signaling adaptor activity [GO:0035591]; translation initiation factor binding [GO:0031369]

IPR011545;IPR014001;IPR001650;IPR027417;IPR000629;IPR014014;

3.40.50.300;

A0A0G2K736

MLSGKKAAAAAAAAAAAAAGTEAGPGAAGGAENGSEVAAPPAGLAGPADIATGAAGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTAGPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGQAGGLQDDSSGGYGDGQASGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQADTVKVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM

Rattus norvegicus (Rat)

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;Nucleus;Oxidoreductase;Proteomics identification;Reference proteome;Repressor;Transcription;Transcription regulation

cell differentiation [GO:0030154]; cellular response to cAMP [GO:0071320]; cellular response to gamma radiation [GO:0071480]; cellular response to UV [GO:0034644]; cerebral cortex development [GO:0021987]; chromatin remodeling [GO:0006338]; DNA repair-dependent chromatin remodeling [GO:0140861]; granulocyte differentiation [GO:0030851]; guanine metabolic process [GO:0046098]; muscle cell development [GO:0055001]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of neurogenesis [GO:0050768]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron maturation [GO:0042551]; neuron projection extension [GO:1990138]; pituitary gland development [GO:0021983]; positive regulation of cell size [GO:0045793]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of megakaryocyte differentiation [GO:0045654]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein modification process [GO:0036211]; regulation of DNA methylation-dependent heterochromatin formation [GO:0090308]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of neurogenesis [GO:0050767]; regulation of primitive erythrocyte differentiation [GO:0010725]; regulation of protein localization [GO:0032880]; regulation of transcription by RNA polymerase II [GO:0006357]; response to fungicide [GO:0060992]; response to organic cyclic compound [GO:0014070]; transcription by RNA polymerase II [GO:0006366]

chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; DNA repair complex [GO:1990391]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]

chromatin binding [GO:0003682]; demethylase activity [GO:0032451]; DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; FAD-dependent H3K4me/H3K4me3 demethylase activity [GO:0140682]; flavin adenine dinucleotide binding [GO:0050660]; histone demethylase activity [GO:0032452]; histone H3K4 demethylase activity [GO:0032453]; histone H3K9 demethylase activity [GO:0032454]; histone H3K9me2/H3K9me3 demethylase activity [GO:0140684]; identical protein binding [GO:0042802]; lncRNA binding [GO:0106222]; MRF binding [GO:0043426]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; oxidoreductase activity [GO:0016491]; p53 binding [GO:0002039]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; telomeric repeat-containing RNA binding [GO:0061752]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]

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;

A0A0G2K7W4

MANDSPAKSLVDIDLSSLRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNTKGNTLKEDWIAYISREILRGLAHLHIHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDLWSCGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRIQLKDHIDRTRKKRGEKDETEYEYSGSEEEEEEVPEQEGEPSSIVNVPGESTLRRDFLRLQQENKERSEALRRQQLLQEQQLREQEEYKRQLLAERQKRIEQQKEQRRRLEEQQRREREARRQQEREQRRREQEEKRRLEELERRRKEEEERRRAEDEKRRVEREQEYIRRQLEEEQRHLEILQQQLLQEQAMLLECRWREMEEHRQAERLQRQLQQEQAYLLSLQHDHRRPHAQQPPPPQQQDRSKPSYHAPEPKPHYDPADRAREVEDRFRKTNHSSPEAQAKQTGRGLEPPVPSRSESFSNGNSESVHPALQRPAEPQVQWSHLASLKNNVSPVSRSHSFSDPSPKFAHHHLRSQDPCPPSRSEGLSQSSDSKSEVPEPTQKAWSRSDSDEVPPRVPVRTTSRSPVLSRRDSPLQGSGQQNSQAGQRNSTSSIEPRLLWERVEKLVPRPGSGSSSGSSNSGSQPGSHPGSQSGSGERFRVRSSSKSEGSPSQRLENAAKKPEDKKEVFRPLKPADLTALAKELRAVEDVRPPHKVTDYSSSSEESGTTDEEEEDVEQEGADDSTSGPEDTRAASSLNLSNGETESVKTMIVHDDVESEPAMTPSKEGTLIVRQSTVDQKRASHHESNGFAGRIHLLPDLLQQSHSSSTSSTSSSPSSSQPTPTMSPQTPQDKLTANETQSASSTLQKHKSSSSFTPFIDPRLLQISPSSGTTVTSVVGFSCDGLRPEAIRQDPTRKGSVVNVNPTNTRPQSDTPEIRKYKKRFNSEILCAALWGVNLLVGTESGLMLLDRSGQGKVYPLISRRRFQQMDVLEGLNVLVTISGKKDKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDLEGCVHYKVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFGELVHKPLLVDLTVEEGQRLKVIYGSCAGFHAVDVDSGSVYDIYLPTHIQCTIKPHAIIILPNTDGMELLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIRSNQTMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVYFMTLGRTSLLSW

Rattus norvegicus (Rat)

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;Nucleotide-binding;Proteomics identification;Reference proteome

intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; negative regulation of neuron projection development [GO:0010977]; negative regulation of neuron projection regeneration [GO:0070571]; neuron projection morphogenesis [GO:0048812]; phosphorylation [GO:0016310]; positive regulation of ARF protein signal transduction [GO:0032014]; positive regulation of cell migration [GO:0030335]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of focal adhesion disassembly [GO:0120183]; positive regulation of JNK cascade [GO:0046330]; positive regulation of keratinocyte migration [GO:0051549]; regulation of JNK cascade [GO:0046328]; regulation of MAPK cascade [GO:0043408]

cytoplasm [GO:0005737]; focal adhesion [GO:0005925]

ATP binding [GO:0005524]; creatine kinase activity [GO:0004111]; microtubule binding [GO:0008017]; protein serine/threonine kinase activity [GO:0004674]

IPR001180;IPR011009;IPR000719;IPR017441;IPR008271;

1.10.510.10;

A0A0G2K7X2

MKLPLLQPAHRQFLCTSDMLQSKEYHISMETKSINTSEFLLPKMEPSKKMGAAGAAQPNPPLKLQPDRGAASVLVPEQGGYKEKFAKTVEDKYKCEKCRLVLCNPKQTECGHRFCESCMAALLSSSSPKCTACQESIIKDKVFKDNCCKREILALQIYCRNEGRGCVEQLTLGHLLVHLKNECQFEELPCLRADCKEKVLRRDLRDHVEKACKYREATCAHCKSQVPMITLQKHEDTDCPCVVVSCPHKCSVQTLLRSELSAHLSECVNAPSTCSFKRYGCVFQGTNQQIKAHEASSAVQHVNLLKEWSNSLEKKVSLLQNESVEKNKSIQSLHNQICSFEIEIERQKEMLRNNESKILHLQRVIDSQAEKLKELDKEIRPFRQNWEEADSMKSSVESLQNRVTELESVDKSAGQAARNTGLLESQLSRHDQMLSVHDIRLADMDLRFQVLETASYNGVLIWKIRDYKRRKQEAVMGKTLSLYSQPFYTGYFGYKMCARVYLNGDGMGKGTHLSLFFVIMRGEYDALLPWPFKQKVTLMLMDQGSSRRHLGDAFKPDPNSSSFKKPTGEMNIASGCPVFVAQTVLENGTYIKDDTIFIKVIVDTSDLPDP

Rattus norvegicus (Rat)

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|PIRNR:PIRNR015614};

Coiled coil;Cytoplasm;Isopeptide bond;Metal-binding;Reference proteome;Repeat;Ubl conjugation;Zinc;Zinc-finger

innate immune response [GO:0045087]; positive regulation of type I interferon production [GO:0032481]; protein K63-linked ubiquitination [GO:0070534]; regulation of apoptotic process [GO:0042981]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of cytokine production [GO:0001817]; regulation of defense response to virus [GO:0050688]; regulation of interferon-beta production [GO:0032648]; regulation of proteolysis [GO:0030162]; Toll signaling pathway [GO:0008063]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; tumor necrosis factor-mediated signaling pathway [GO:0033209]

CD40 receptor complex [GO:0035631]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; endosome [GO:0005768]; endosome membrane [GO:0010008]; mitochondrion [GO:0005739]

identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; thioesterase binding [GO:0031996]; tumor necrosis factor receptor binding [GO:0005164]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR015614}.

IPR002083;IPR012227;IPR008974;IPR049440;IPR037304;IPR027128;IPR049342;IPR001841;IPR013083;IPR017907;IPR001293;

3.30.40.10;

A0A0G2K8S8

MPRFALTIIRHGETRLNKEKIIQGQGVDAPLSETGFRQAAATGQFLSNVHFTHAFSSDLTRTKQTIHGILEKSRFCKDIAVKYDSRLRERMYGVAEGKPLSELRAMAKAAGEECPMFTPPGGETVEQQVKMRGKDFFDFICQLILGKAGQRENFLPGAPDNCLESSLAEVFPVGKHGSLGTDPKHGALGLTASILVVSHGAYMRSLFGYFLSDLRCSLPATIDKFELSSITPNTGISVFIIDCEEARKPTVQCVCMNLQEHLNKGVEKH

Rattus norvegicus (Rat)

3.1.3.46

CATALYTIC ACTIVITY: Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46; Evidence={ECO:0000256|ARBA:ARBA00000464};

Cytoplasm;Nucleus;Reference proteome

cardiac muscle cell apoptotic process [GO:0010659]; cellular response to cobalt ion [GO:0071279]; cellular response to hypoxia [GO:0071456]; DNA damage response [GO:0006974]; fructose 2,6-bisphosphate metabolic process [GO:0006003]; glucose catabolic process to lactate via pyruvate [GO:0019661]; glycolytic process [GO:0006096]; intestinal epithelial cell development [GO:0060576]; mitophagy [GO:0000423]; negative regulation of glucose catabolic process to lactate via pyruvate [GO:1904024]; negative regulation of glycolytic process [GO:0045820]; negative regulation of mitophagy [GO:1901525]; negative regulation of programmed cell death [GO:0043069]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of DNA repair [GO:0045739]; positive regulation of pentose-phosphate shunt [GO:1905857]; reactive oxygen species metabolic process [GO:0072593]; regulation of pentose-phosphate shunt [GO:0043456]; regulation of response to DNA damage checkpoint signaling [GO:1902153]; response to gamma radiation [GO:0010332]; response to ischemia [GO:0002931]; response to xenobiotic stimulus [GO:0009410]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634]

fructose-2,6-bisphosphate 2-phosphatase activity [GO:0004331]

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

IPR013078;IPR029033;IPR001345;

3.40.50.1240;

A0A0G2K8T2

MRAGRVRPLRASDMKKDVRILLVGEPRVGKTSLIMSLVSEEFPEEVPPRAEEITIPADVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPLINERTDKDSRLPLILVGNKSDLVEYSSMETILPIMNQYTEIETCVECSAKNLKNISELFYYAQKAVLHPTGPLYCPEEKEMKPACIKALTRIFKISDQDNDGTLNDAELNFFQRICFNTPLAPQALEDVKNVVRKHLSDGVADSGLTLRGFLFLHTLFIQRGRHETTWTVLRRFGYDDDLDLTPEYLFPLLKIPPDCTTELNHHAYLFLQSTFDKHDLDRDCALSPDELKDLFQVFPYIPWGPDVNNTVCTNESGWITYQGFLSQWTLTTYLDVQRCLEYLGYLGYSILTEQESQASAITVTRDKKIDLQKKQTQRNVFRCNVIGVKGCGKTGVLQSLLGRNLMRQKKIRDDHKSYYAINTVYVYGQEKYLLLHDISESEFLTEAEIVCDVVCLVYDVTNPKSFEYCARIFKQHFMDSRIPCLIVAAKSDLHEVKQEHSVSPTDFCRKHKMPPPQAFTCNTADAPSKDIFVKLTTMAMYPEDHYRGSLSRDMGSTDRIENLRKIWVFLKTALHVTQADLKSSTFWLRASFGATVFAVVGFAMYRALLKQR

Rattus norvegicus (Rat)

FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. {ECO:0000256|PIRNR:PIRNR037488}.

3.6.5.-

Calcium;GTP-binding;Hydrolase;Membrane;Metal-binding;Mitochondrion;Mitochondrion outer membrane;Nucleotide-binding;Proteomics identification;Reference proteome;Repeat;Transmembrane;Transmembrane helix

actin filament organization [GO:0007015]; cellular homeostasis [GO:0019725]; cortical cytoskeleton organization [GO:0030865]; engulfment of apoptotic cell [GO:0043652]; establishment of mitochondrion localization by microtubule attachment [GO:0034640]; establishment or maintenance of cell polarity [GO:0007163]; mitochondrial outer membrane permeabilization [GO:0097345]; mitochondrion organization [GO:0007005]; mitochondrion transport along microtubule [GO:0047497]; mitotic cytokinesis [GO:0000281]; motor neuron axon guidance [GO:0008045]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; regulation of mitochondrion organization [GO:0010821]; regulation of neurotransmitter secretion [GO:0046928]; regulation of organelle transport along microtubule [GO:1902513]; signal transduction [GO:0007165]; small GTPase-mediated signal transduction [GO:0007264]

cell projection [GO:0042995]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; mitochondrial outer membrane [GO:0005741]

calcium ion binding [GO:0005509]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004200, ECO:0000256|PIRNR:PIRNR037488}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004200, ECO:0000256|PIRNR:PIRNR037488}.

IPR011992;IPR018247;IPR013566;IPR013567;IPR002048;IPR021181;IPR020860;IPR027417;IPR005225;IPR001806;IPR003578;

1.10.238.10;3.40.50.300;

A0A0G2K9L3

MPVQAAQWTEFLSCPICYNEFDENVHKPISLGCSHTVCKTCLNKLHRKACPFDQTAINTDIDVLPVNFALLQLVGAQVPDHQSIKLSNLGENKHYEVAKKCVEDLALYLKPLSGGKGVASLNQSALSRPMQRKLVTLVNCQLVEEEGRVRAMRAARSLGERTVTELILQHQNPQQLSANLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRSYEALRREHDAQIVHIAMEAGLRISPEQWSSLLYGDLAHKSHMQSIIDKLQSPESFAKSVQELTIVLQRTGDPANLNRLRPHLELLANIDPNPDAVSPTWEQLENAMVAVKTVVHGLVDFIQNYSRKGHETPQPQPNSKYKTSMCRDLRQQGGCPRGTNCTFAHSQEELEKYRLRNKKMSATVRTFPLLNKVAVNSTVTTTAGNVISVIGSTETTGKIVPSTNGISNTESSVSQLIPRSADSAGRTLETVKKVGKVGTNGQNAGPSAESVSENKIGSPPKTPVSNAAATSAGPSNFGTELNSLPPKSSPFLTRVPVYPQHSENIQYFQDPRTQIPFEVPQYPQTGYYPPPPTVPAGVTPCVPRFVRSNNVPESSLPPASMPYADHYSTFSPRDRMNSSPYQPPPPQQYGPVPPVPSGMYAPVYDSRRIWRPAMYQRDDIIRSNSLPPMDVMHSSVYQTSLRERYNSLDGYYSVTCQPPNDPRTTVPLPREPCGHLKSSCEEQLRRKPDQWTQYHTQKTPVSSTLPVATQSPTPPSPLFSVDFRSDFSESGSGTKFEEDHLSHYSPWSCGTIGSCINAIDSEPKDVIANSNAVLMDLDSGDVKRRVHLFEAQRRTKEEDPIIPFSDGPIISKWGAISRSSRTGYHTTDPVQATASQGSATKPISVSDYVPYVNAVDSRWSSYGNDATSSAHYIERDRFIVTDLSGHRKHSSTGDLLSLELQQAKSNSLLLQREANALAMQQKWNSLDEGRHLTLNLLSKEIELRNGENDYTEDTVDTKPDRDIELELSALDTDEPDGQSEQIEEILDIQLGISSQNDQLLNGTAVENGHPVQQHQKDPVKQKRQSLGEDHVILSKVFIILEKMVHPVSGMKSGVQEPHQ

Rattus norvegicus (Rat)

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};

Metal-binding;Reference proteome;Transferase;Zinc;Zinc-finger

B cell homeostasis [GO:0001782]; limb development [GO:0060173]; lung alveolus development [GO:0048286]; lymph node development [GO:0048535]; multicellular organism growth [GO:0035264]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; post-embryonic development [GO:0009791]; post-transcriptional regulation of gene expression [GO:0010608]; protein polyubiquitination [GO:0000209]; regulation of gene expression [GO:0010468]; regulation of miRNA metabolic process [GO:2000628]; spleen development [GO:0048536]; T cell homeostasis [GO:0043029]; T cell proliferation [GO:0042098]; T cell receptor signaling pathway [GO:0050852]; T follicular helper cell differentiation [GO:0061470]; ubiquitin-dependent protein catabolic process [GO:0006511]

cell surface [GO:0009986]; cytoplasmic stress granule [GO:0010494]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; P-body [GO:0000932]

DNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; RNA stem-loop binding [GO:0035613]; ubiquitin protein ligase activity [GO:0061630]

SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}.

IPR041523;IPR048575;IPR000571;IPR036855;IPR001841;IPR013083;IPR017907;

1.20.120.1790;4.10.1000.10;3.30.40.10;

A0A0G2K9T1

MSDSAPQLDSMGSLTMKSQLQITVISAKLKENKKNWFGPSPYVEVTVDGQSKKTEKCNNTNSPKWKQPLTVIVTPMSKLCFRVWSHQTLKSDVLLGTAGLDIYETLKSNNMKLEEVVMTLQLVGDKEPTETMGDLSVCLDGLQVEAEVVTNGETSCSEGATQNDAGCRPKDETRVSTNGSEDPEVAASGENKRANGNNSPSLSNGGFKPSRPPRPSRPPPPTPRRPASVNGSPSTNSDSDGSSTGSLPPTNTNVNSSASEGAASGLIIPLTISGGSGPRPLNTVSQAPLPPGWEQRVDQHGRVYYVDHVEKRTTWDRPEPLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIFGNQDLFATSQNKEFDPLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQGQLNEKPLPEGWEMRFTVDGIPYFVDHNRRATTYIDPRTGKSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQHIKITVTRKTLFEDSFQQIMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECGLEMYFSVDKEILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRHYTRTSKQIVWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVGKENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFGQE

Rattus norvegicus (Rat)

2.3.2.26

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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885, ECO:0000256|PIRNR:PIRNR001569};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.

Reference proteome;Transferase;Ubl conjugation pathway

CD4-positive, alpha-beta T cell proliferation [GO:0035739]; negative regulation of apoptotic process [GO:0043066]; negative regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000562]; negative regulation of cytoplasmic pattern recognition receptor signaling pathway [GO:0039532]; negative regulation of defense response to virus [GO:0050687]; negative regulation of JNK cascade [GO:0046329]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of receptor catabolic process [GO:2000646]; positive regulation of T cell anergy [GO:0002669]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein catabolic process [GO:0030163]; protein K29-linked ubiquitination [GO:0035519]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; receptor internalization [GO:0031623]; regulation of protein deubiquitination [GO:0090085]; T cell anergy [GO:0002870]; ubiquitin-dependent protein catabolic process [GO:0006511]

cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]

arrestin family protein binding [GO:1990763]; CXCR chemokine receptor binding [GO:0045236]; ligase activity [GO:0016874]; ribonucleoprotein complex binding [GO:0043021]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-like protein ligase binding [GO:0044389]; ubiquitin-protein transferase activity [GO:0004842]

IPR000008;IPR035892;IPR024928;IPR000569;IPR035983;IPR001202;IPR036020;

2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10;

A0A0G2KAC1

MPSVALNSPRLRRVFVVGVGMTKFMKPGGENSRDYPDLAKEAGQKALADAQIPYSAVEQACVGYVYGESTCGQRAIYHSLGLTGIPIINVNNNCSTGSTALFMAQQLVQGGLANCVLALGFEKMEKGSLGTKYSDRSNPLEKHIDVLINKYGMSACPFAPQLFGSAGKEHMETYGTKVEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEIMKSRPVFDFLTVLQCCPTSDGAAAAIVSSEEFVQKHGLQSKAVEIVAQEMVTDMPSTFEEKSVIKMVGYDMSKEAARKCYEKSGLGPSDVDVIELHDCFSTNELLTYEALGLCPEGQGGALVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAAVVTLYRMGFPEAASSFRTHQISAAPTSSAGDGFKANLIFKEIEKKLEEEGEEFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGSVLPDSDKKADCTITMADSDLLALMTGKMNPQSPICRSWLCQPTCRENRHQERLPSFKD

Rattus norvegicus (Rat)

2.3.1.155; 2.3.1.16; 2.3.1.176

CATALYTIC ACTIVITY: Reaction=3-oxo-(9Z-octadecenoyl)-CoA + CoA = (7Z)-hexadecenoyl-CoA + acetyl-CoA; Xref=Rhea:RHEA:47400, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:87695, ChEBI:CHEBI:87698; Evidence={ECO:0000256|ARBA:ARBA00024514}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47401; Evidence={ECO:0000256|ARBA:ARBA00024514}; CATALYTIC ACTIVITY: Reaction=3-oxohexadecanedioyl-CoA + CoA = acetyl-CoA + tetradecanedioyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084; Evidence={ECO:0000256|ARBA:ARBA00024540}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344; Evidence={ECO:0000256|ARBA:ARBA00024540}; CATALYTIC ACTIVITY: Reaction=4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3-oxopristanoyl-CoA + CoA; Xref=Rhea:RHEA:10408, ChEBI:CHEBI:57287, ChEBI:CHEBI:57291, ChEBI:CHEBI:57351, ChEBI:CHEBI:57392; EC=2.3.1.176; Evidence={ECO:0000256|ARBA:ARBA00029348}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10410; Evidence={ECO:0000256|ARBA:ARBA00029348}; CATALYTIC ACTIVITY: Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out); Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759; Evidence={ECO:0000256|ARBA:ARBA00029287}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA; Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16; Evidence={ECO:0000256|ARBA:ARBA00024485}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566; Evidence={ECO:0000256|ARBA:ARBA00024485}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoA; Xref=Rhea:RHEA:31111, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57371, ChEBI:CHEBI:62418; Evidence={ECO:0000256|ARBA:ARBA00024476}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113; Evidence={ECO:0000256|ARBA:ARBA00024476}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + decanoyl-CoA = 3-oxododecanoyl-CoA + CoA; Xref=Rhea:RHEA:31183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61430, ChEBI:CHEBI:62615; Evidence={ECO:0000256|ARBA:ARBA00024559}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185; Evidence={ECO:0000256|ARBA:ARBA00024559}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + dodecanoyl-CoA = 3-oxotetradecanoyl-CoA + CoA; Xref=Rhea:RHEA:31091, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57375, ChEBI:CHEBI:62543; Evidence={ECO:0000256|ARBA:ARBA00024598}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093; Evidence={ECO:0000256|ARBA:ARBA00024598}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + hexadecanoyl-CoA = 3-oxooctadecanoyl-CoA + CoA; Xref=Rhea:RHEA:35279, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57379, ChEBI:CHEBI:71407; Evidence={ECO:0000256|ARBA:ARBA00024549}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281; Evidence={ECO:0000256|ARBA:ARBA00024549}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA; Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:62619, ChEBI:CHEBI:62620; Evidence={ECO:0000256|ARBA:ARBA00024462}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205; Evidence={ECO:0000256|ARBA:ARBA00024462}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + octanoyl-CoA = 3-oxodecanoyl-CoA + CoA; Xref=Rhea:RHEA:31087, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57386, ChEBI:CHEBI:62548; Evidence={ECO:0000256|ARBA:ARBA00024542}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089; Evidence={ECO:0000256|ARBA:ARBA00024542}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA; Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155; Evidence={ECO:0000256|ARBA:ARBA00024455}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163; Evidence={ECO:0000256|ARBA:ARBA00024455}; CATALYTIC ACTIVITY: Reaction=choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA; Xref=Rhea:RHEA:16865, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, ChEBI:CHEBI:57392, ChEBI:CHEBI:58507; EC=2.3.1.176; Evidence={ECO:0000256|ARBA:ARBA00024509}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16867; Evidence={ECO:0000256|ARBA:ARBA00024509}; CATALYTIC ACTIVITY: Reaction=propanoyl-CoA + tetradecanoyl-CoA = 3-oxo-2-methylhexadecanoyl-CoA + CoA; Xref=Rhea:RHEA:46344, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:57392, ChEBI:CHEBI:86042; Evidence={ECO:0000256|ARBA:ARBA00024471}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:46346; Evidence={ECO:0000256|ARBA:ARBA00024471};

Acetylation;Acyltransferase;Lipid transport;Lipid-binding;Mitochondrion;Peroxisome;Proteomics identification;Reference proteome;Transferase;Transport

lipid transport [GO:0006869]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]

cytoplasm [GO:0005737]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]

acetyl-CoA C-acyltransferase activity [GO:0003988]; acetyl-CoA C-myristoyltransferase activity [GO:0050633]; collagen binding [GO:0005518]; lipid binding [GO:0008289]; propanoyl-CoA C-acyltransferase activity [GO:0033814]; propionyl-CoA C2-trimethyltridecanoyltransferase activity [GO:0050632]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Peroxisome {ECO:0000256|ARBA:ARBA00004275}.

IPR003033;IPR036527;IPR016039;IPR020615;IPR020617;IPR020613;IPR020616;

3.40.47.10;3.30.1050.10;

A0A0G2KB10

MRLEHFGVLFLREEENEAKIENVQKTGFIKGPIFKGVASSRFLPKGTKTKVNLEEQGRQKVSFSFSLTKKTLQNRFFTALSNEKQSDSPHSPATPQVDSNPKAKMEAGDTFPATEESSPPKSRVELGRIHFKKHLLHVTSRPQLATTTTVASLLPPTTQLPVAIAESTVDSPPSSPPPPPPPPQVSSPSPPAPISEPVALPHPPVTALMTSTPGPLPVDAAVRAQKEPPMKSVPESLELDMKQDIVSNSLEEHTNQTLKEQADNALQKEDSHIGKEEEVSDGSKISLSSKKASSKKKSSQFEGTFLGSESDEDSVRTSSSQRSHDLKSSTSIEKERDFKKSSAPSKSEDLGKSSRSKTERDDKYFSYSKLERDTRYVSTRCRSERDRRRSRSRSRSDRVSRTSLSYSRSERSHYYDSERRYHRSSPYRERTRYSRPYTDNRARESSDSEDEYKKTYPRRTSAHSYRDLRTSSSYSKFDRDCKTETSYLEMERRGKYSSKLERESKRTSEHEAIKRCCSPPNELGFRRGSSYSKHDNNSTSRYKSALSKSISKSDKFKNSFCCTELNEENKQSHSFSLQTPCSKGSELRTINKIPEREKTGSPSPSNQLNDSPTFKKLDESPILKPEFIGHDSHESIKELELPKMKNDQLRNFCSIELNVNGSPETETDVATFRTSKPDAISMTSDDSVTGSEVSPLIKGCVLSSNGFQSVGRCRERDADDACRQHNKSKSPFRETEPLLSPHHDKVMSLPVKTIDYSKTLIKEPVDKRHSCCKTKDSDRYCSPNESSEAENREISSNCFVNVHLDSKTVVCDNRELTDQHSEFTCDGYKQSIGSTSSASLNHFDDLYESVGSSGISSLQSLPSGIRCEENTSPALDTVQSKKGIDFLKYVGKETDVVSALPDSGKAFSSWENRHNMLSGQSLQESQEEGSSTLHERRGRSEVSLDEEEQRGHTHISDDSEVVFPYDLNLTMEDSDGVTYTLKCDSSGNAPEIVSTVHGDYSASSASSSDESDSEDTESDDSSIPRNRLQSVVVVPKNSTLPMEETSPCSSRSSQSYRHYSDHWEDGLESRRHAYEEKFESMASKGCSQTEKFFLHKGTERNPETSYSQFSRKIDNHLPEIAHSQSDGVDSTSHTDVKSDSVGHLNSEDAIRAKMSRPQELPVYCDDFEDLPNTSRQQMIFSNRPDSSRLGKAELSFSSSCDISRMDGLHSSEELRNLGWDFSQQERPTTTYQQPDSSYGTCGTHKYQQSAEHYGGTHDYWQGNGYWDPRSAGRPPGTGVVYDRIQGQVPDSLTDDREEEENWDQRSGSHFSSPSNKFFFHQKDKGSVQAPEISSNSIKDSLVINERKDFSKNFEKNDIKERGPPKKRRQELESDSESDGELQARKKVRVEIEQGQSSVPQHSELVGPSCAMDDFRDPQRWKEFAKLGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCECTPLSKDERAQGEVACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGKMKKERSRKKDSVDGELEALMENGEGLSDKNQVLSLSRLMVRIETLEQKLTCLKLIQNTHSQSCLKSFLERHGLSLLWIWMAELGDGRESNQKLQEEIIKTLEHLPIPTKNMLEESKVLPIIQRWSQTKTAVPQLSEGDGYSSENTSRAHTPLNTPDPSAKPSTEVDTDTPKKLIFRRLKIISENSMDSAVSDVTSELECKDGKEDLDQLETVTVEEDEELQSQQLLPSQLCESKVESESTIDVSKLPISEPEADTETEPKDSNGTKLEETIAEETPSQDEEEGVSDVESERSQEPPDKTVDISDLATKLLDSWKDLKEVYRIPKKSQTEKESTVTERGRDTAAFRDQTAPKTPNRSREREPDKQSQNKEKRKRRGSLSPPSSAYERGTKRPDDRYDTPTSKKKVRIKDRNKLSTEERRKLFEQEVAQREAQKQQQQMQNLGMTSPLPFDSLGYNASHHPFAGYPPGYPMQAYVDPSNPNAGKVLLPTPSMDPVCSPAPYDHAQPLVGHSTESLAAPPSVPVVPHGAASVEVSSSQYAAQSESVVHQDSSVPGMPVQTPGPVQGQNYSVWDSNQQSVSVQPQYSPAQSQATIYYQGQTCSTVYGVTSPYSQTTPPIVQSYAQPSLQYIQGQQIFTAHPQGVVVQPAAAVTTIVAPGQPQPLQPPEMVVTNNLLDLPPPSPPKPKTIVLPPNWKTARDPEGKIYYYHVITRQTQWDPPTWESPGDDASLEHEAEMDLGTPTYDENPMKTSKKPKTAEADTSSELAKKSKEVFRKEMSQFIVQCLNPYRKPDCKVGRITTTEDFKHLARKLTHGVMNKELKYCKNPEDLECNENVKHKTKEYIKKYMQKFGAVYKPKEDTELE

Rattus norvegicus (Rat)

2.1.1.359

CATALYTIC ACTIVITY: Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359; Evidence={ECO:0000256|ARBA:ARBA00000317};

Chromatin regulator;Chromosome;Methyltransferase;Nucleus;Proteomics identification;Reference proteome;S-adenosyl-L-methionine;Transcription;Transcription regulation;Transferase

angiogenesis [GO:0001525]; cell migration involved in vasculogenesis [GO:0035441]; coronary vasculature morphogenesis [GO:0060977]; defense response to virus [GO:0051607]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic organ development [GO:0048568]; embryonic placenta morphogenesis [GO:0060669]; endodermal cell differentiation [GO:0035987]; forebrain development [GO:0030900]; mesoderm morphogenesis [GO:0048332]; methylation [GO:0032259]; microtubule cytoskeleton organization involved in mitosis [GO:1902850]; mismatch repair [GO:0006298]; morphogenesis of a branching structure [GO:0001763]; neural tube closure [GO:0001843]; nucleosome organization [GO:0034728]; pericardium development [GO:0060039]; positive regulation of autophagy [GO:0010508]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of ossification [GO:0045778]; regulation of cytokinesis [GO:0032465]; regulation of DNA-templated transcription [GO:0006355]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of gene expression [GO:0010468]; regulation of mRNA export from nucleus [GO:0010793]; regulation of protein localization to chromatin [GO:1905634]; response to alkaloid [GO:0043279]; response to metal ion [GO:0010038]; response to organic cyclic compound [GO:0014070]; response to type I interferon [GO:0034340]; stem cell development [GO:0048864]; stem cell differentiation [GO:0048863]; transcription elongation by RNA polymerase II [GO:0006368]; vasculogenesis [GO:0001570]

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

alpha-tubulin binding [GO:0043014]; histone H3K36 methyltransferase activity [GO:0046975]; histone H3K36 trimethyltransferase activity [GO:0140955]; protein-lysine N-methyltransferase activity [GO:0016279]

SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR006560;IPR003616;IPR001214;IPR046341;IPR044437;IPR042294;IPR013257;IPR038190;IPR035441;IPR001202;IPR036020;

2.20.70.10;1.20.930.10;2.170.270.10;1.10.1740.100;

A0A0G2L7I0

MMEDEDFLLALRLQEQFDQETPAAGWPDEDCPSSKRRRVDPSGGLDVIPFTQPRAERPLSIVDESWETLDPNPDVRAMFLQFNDKFFWGKLSGVEVKWSPRMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVQTLLHEMIHALLFVTQNNRDRDGHGPEFCKHMNRINQASGTNITIYHSFHDEVDVYRQHWWRCNGPCQNRRPFFGYVKRAMNRPPSARDPWWADHQRSCGGTYTKIKEPENYGKTGKSDKQRDKMPATEMPKKSKPPSSTSSSGSQDIRNIIPFSGRGFVLGGNAQIPTNKQIQSPPKAPPEPLHSPPDSPLLPRLQLNEDNLKRLSSGTSNIPRKRSVGNTNAFINVNGSPVRISNGNGSGGKQRSVRDLFQAIVLKSPDRGASAVGSSKSSTDASTADYRSNSALDAKPSGKTSLITDHLSYTISGPKTLSAESNISKYFGGSAKTDVQDSKLKTFGSPQKSAIGTPGYVSKAFGSNQRPDSTSSGIRNTGSPQRSHASATSGSSFKHFRGPAKPESNFPSPRNIGSPRTSGTTPSGAKKRSWEEHNSERVFDYFQRTVGESATSTDKKREEVRSEAPPPVRDQQANNPPAQITVHCPVCHIRLPESTINDHLDSCLL

Danio rerio (Zebrafish) (Brachydanio rerio)

FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Catalyzes proteolytic cleavage of the hmces DNA-protein cross-link following unfolding by the brip1/fancj helicase. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as top1, top2a, histones H3 and H4. Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs. May also act as a 'reader' of ubiquitinated pcna: facilitates chromatin association of rad18 and is required for efficient pcna monoubiquitination, promoting a feed-forward loop to enhance pcna ubiquitination and translesion DNA synthesis. Acts as a regulator of translesion DNA synthesis by recruiting vcp/p97 to sites of DNA damage. {ECO:0000250|UniProtKB:A0A1L8G2K9, ECO:0000250|UniProtKB:Q9H040}.

3.4.24.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040};

Autocatalytic cleavage;Chromosome;DNA damage;DNA repair;Hydrolase;Isopeptide bond;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Zinc;Zinc-finger

DNA damage response [GO:0006974]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]

chromatin [GO:0000785]; nucleus [GO:0005634]

double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; polyubiquitin modification-dependent protein binding [GO:0031593]; single-stranded DNA binding [GO:0003697]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:A0A1L8G2K9}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress. {ECO:0000250|UniProtKB:Q9H040}.

PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}.

DOMAIN: The UBZ4-type zinc fingers mediate binding to 'Lys-48'- and 'Lys-63'-linked polyubiquitin. {ECO:0000250|UniProtKB:Q9H040}.

IPR006642;IPR044245;IPR006640;

3.30.160.60;

A0A0G2Q9D6

MGKNEARRSALAPDHGTVVCDPLRRLNRMHATPEESIRIVAAQKKKAQDEYGAASITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGYATTVNVVLLEDGGVEVADDGRGIPVATHASGIPTVDVVMTQLHAGGKFDSDAYAISGGLHGVGVSVVNALSTRLEVEIKRDGYEWSQVYEKSEPLGLKQGAPTKKTGSTVRFWADPAVFETTEYDFETVARRLQEMAFLNKGLTINLTDERVTQDEVVDEVVSDVAEAPKSASERAAESTAPHKVKSRTFHYPGGLVDFVKHINRTKNAIHSSIVDFSGKGTGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGFRSALTSVVNKYAKDRKLLKDKDPNLTGDDIREGLAAVISVKVSEPQFEGQTKTKLGNTEVKSFVQKVCNEQLTHWFEANPTDSKVVVNKAVSSAQARIAARKARELVRRKSATDIGGLPGKLADCRSTDPRKSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDIGKLRYHKIVLMADADVDGQHISTLLLTLLFRFMRPLIENGHVFLAQPPLYKLKWQRSDPEFAYSDRERDGLLEAGLKAGKKINKEDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVDARRSFITRNAKDVRFLDV

Mycobacterium bovis (strain BCG / Pasteur 1173P2)

FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Relaxes negatively supercoiled DNA in an ATP-independent manner. A linear reaction intermediate can be trapped in the presence of the antibiotic ciprofloxacin (PubMed:7503546). Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. {ECO:0000269|PubMed:7503546}.

5.6.2.2

CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01898};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:7503546}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+). {ECO:0000255|HAMAP-Rule:MF_01898};

ATP-binding;Cytoplasm;DNA-binding;Isomerase;Magnesium;Metal-binding;Nucleotide-binding;Topoisomerase

DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261]

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

ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA negative supercoiling activity [GO:0034335]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}.

IPR002288;IPR011557;IPR003594;IPR036890;IPR020568;IPR014721;IPR001241;IPR013760;IPR000565;IPR013759;IPR013506;IPR018522;IPR006171;IPR034160;

3.30.230.10;3.40.50.670;3.30.565.10;

A0A0G2Q9F8

MTDTTLPPDDSLDRIEPVDIQQEMQRSYIDYAMSVIVGRALPEVRDGLKPVHRRVLYAMFDSGFRPDRSHAKSARSVAETMGNYHPHGDASIYDTLVRMAQPWSLRYPLVDGQGNFGSPGNDPPAAMRYTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPTVLPSRFPNLLANGSGGIAVGMATNIPPHNLRELADAVFWALENHDADEEETLAAVMGRVKGPDFPTAGLIVGSQGTADAYKTGRGSIRMRGVVEVEEDSRGRTSLVITELPYQVNHDNFITSIAEQVRDGKLAGISNIEDQSSDRVGLRIVIEIKRDAVAKVVINNLYKHTQLQTSFGANMLAIVDGVPRTLRLDQLIRYYVDHQLDVIVRRTTYRLRKANERAHILRGLVKALDALDEVIALIRASETVDIARAGLIELLDIDEIQAQAILDMQLRRLAALERQRIIDDLAKIEAEIADLEDILAKPERQRGIVRDELAEIVDRHGDDRRTRIIAADGDVSDEDLIAREDVVVTITETGYAKRTKTDLYRSQKRGGKGVQGAGLKQDDIVAHFFVCSTHDLILFFTTQGRVYRAKAYDLPEASRTARGQHVANLLAFQPEERIAQVIQIRGYTDAPYLVLATRNGLVKKSKLTDFDSNRSGGIVAVNLRDNDELVGAVLCSADDDLLLVSANGQSIRFSATDEALRPMGRATSGVQGMRFNIDDRLLSLNVVREGTYLLVATSGGYAKRTAIEEYPVQGRGGKGVLTVMYDRRRGRLVGALIVDDDSELYAVTSGGGVIRTAARQVRKAGRQTKGVRLMNLGEGDTLLAIARNAEESGDDNAVDANGADQTGN

Mycobacterium bovis (strain BCG / Pasteur 1173P2)

FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Relaxes negatively supercoiled DNA in an ATP-independent manner. A linear reaction intermediate can be trapped in the presence of the antibiotic ciprofloxacin (PubMed:7503546). Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. {ECO:0000269|PubMed:7503546}.

5.6.2.2

CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01897};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:7503546}; Note=Reaction requires Mg(2+). {ECO:0000269|PubMed:7503546};

Antibiotic resistance;ATP-binding;Cytoplasm;DNA-binding;Isomerase;Nucleotide-binding;Topoisomerase

DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261]; response to antibiotic [GO:0046677]

chromosome [GO:0005694]; cytoplasm [GO:0005737]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330]

ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA negative supercoiling activity [GO:0034335]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.

IPR005743;IPR006691;IPR035516;IPR013760;IPR013758;IPR013757;IPR002205;

3.30.1360.40;2.120.10.90;3.90.199.10;1.10.268.10;

A0A0G2QC09

SSSPSHGGLQPSVMRPKALFWYFGSLFDLEHDLPDELINSTELGLTNGGDISQLQTSLGIVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGMGSSGPNQGPTQSTAGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRPNMQYPNAGMGNAGSLLTEPLQQGSPQMGGQPGLRGPQSHKMGMMSNPTPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVTGGGMANSLPPSVQQPAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHYDTLSVRQILSR

Rattus norvegicus (Rat)

2.3.1.48

Metal-binding;Nucleus;Reference proteome;Transcription;Transcription regulation;Transferase;Zinc;Zinc-finger

animal organ morphogenesis [GO:0009887]; apoptotic process [GO:0006915]; B cell differentiation [GO:0030183]; behavioral defense response [GO:0002209]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to antibiotic [GO:0071236]; cellular response to cAMP [GO:0071320]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucose stimulus [GO:0071333]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to interleukin-1 [GO:0071347]; cellular response to leucine [GO:0071233]; cellular response to mineralocorticoid stimulus [GO:0071389]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to nutrient levels [GO:0031669]; cellular response to organic cyclic compound [GO:0071407]; cellular response to retinoic acid [GO:0071300]; cellular response to trichostatin A [GO:0035984]; cellular response to UV [GO:0034644]; cellular response to xenobiotic stimulus [GO:0071466]; chromatin remodeling [GO:0006338]; circadian rhythm [GO:0007623]; digestive tract development [GO:0048565]; face morphogenesis [GO:0060325]; fat cell differentiation [GO:0045444]; heart development [GO:0007507]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; learning or memory [GO:0007611]; lung development [GO:0030324]; macrophage derived foam cell differentiation [GO:0010742]; megakaryocyte development [GO:0035855]; memory [GO:0007613]; multicellular organism growth [GO:0035264]; negative regulation of autophagy [GO:0010507]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of miRNA metabolic process [GO:2000629]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of transcription by RNA polymerase II [GO:0000122]; platelet formation [GO:0030220]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of axon extension [GO:0045773]; positive regulation of cell growth [GO:0030307]; positive regulation of cell growth involved in cardiac muscle cell development [GO:0061051]; positive regulation of cell size [GO:0045793]; positive regulation of cellular response to hypoxia [GO:1900039]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of glycoprotein biosynthetic process [GO:0010560]; positive regulation of hydrogen peroxide-mediated programmed cell death [GO:1901300]; positive regulation of muscle atrophy [GO:0014737]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein acetylation [GO:1901985]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein secretion [GO:0050714]; positive regulation of proteolysis [GO:0045862]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of sarcomere organization [GO:0060298]; positive regulation of TORC1 signaling [GO:1904263]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of translation [GO:0045727]; protein destabilization [GO:0031648]; protein modification process [GO:0036211]; protein stabilization [GO:0050821]; protein-DNA complex assembly [GO:0065004]; regulation of androgen receptor signaling pathway [GO:0060765]; regulation of angiotensin metabolic process [GO:0060177]; regulation of glycolytic process [GO:0006110]; regulation of mitochondrion organization [GO:0010821]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of tubulin deacetylation [GO:0090043]; response to calcium ion [GO:0051592]; response to cobalt ion [GO:0032025]; response to dexamethasone [GO:0071548]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to fatty acid [GO:0070542]; response to glucose [GO:0009749]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to organic cyclic compound [GO:0014070]; response to retinoic acid [GO:0032526]; response to tumor necrosis factor [GO:0034612]; response to xenobiotic stimulus [GO:0009410]; skeletal muscle tissue development [GO:0007519]; somitogenesis [GO:0001756]; swimming [GO:0036268]; thigmotaxis [GO:0001966]; transcription by RNA polymerase II [GO:0006366]; transcription initiation-coupled chromatin remodeling [GO:0045815]

chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; histone acetyltransferase complex [GO:0000123]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; protein-DNA complex [GO:0032993]; transcription regulator complex [GO:0005667]

acetylation-dependent protein binding [GO:0140033]; acetyltransferase activity [GO:0016407]; acyltransferase activity [GO:0016746]; antigen binding [GO:0003823]; beta-catenin binding [GO:0008013]; bHLH transcription factor binding [GO:0043425]; chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297]; histone acetyltransferase activity [GO:0004402]; histone butyryltransferase activity [GO:0140069]; histone crotonyltransferase activity [GO:0140068]; histone H2B acetyltransferase activity [GO:0044013]; histone H3 acetyltransferase activity [GO:0010484]; histone H3K122 acetyltransferase activity [GO:0140908]; histone H3K18 acetyltransferase activity [GO:0043993]; histone H3K27 acetyltransferase activity [GO:0044017]; histone H4 acetyltransferase activity [GO:0010485]; histone lactyltransferase activity [GO:0120301]; lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [GO:0004468]; metal ion binding [GO:0046872]; mitogen-activated protein kinase binding [GO:0051019]; NF-kappaB binding [GO:0051059]; nuclear androgen receptor binding [GO:0050681]; nuclear glucocorticoid receptor binding [GO:0035259]; nuclear receptor binding [GO:0016922]; p53 binding [GO:0002039]; peptide butyryltransferase activity [GO:0140065]; peptide-lysine-N-acetyltransferase activity [GO:0061733]; peroxisome proliferator activated receptor binding [GO:0042975]; pre-mRNA intronic binding [GO:0097157]; promoter-specific chromatin binding [GO:1990841]; protein antigen binding [GO:1990405]; protein kinase binding [GO:0019901]; protein propionyltransferase activity [GO:0061920]; protein-containing complex binding [GO:0044877]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; SMAD binding [GO:0046332]; STAT family protein binding [GO:0097677]; transcription coactivator activity [GO:0003713]; transcription coactivator binding [GO:0001223]; transcription coregulator binding [GO:0001221]

IPR013178;IPR035898;IPR000197;

1.20.1020.10;

A0A0G2QC33

MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYRRNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAFLDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVVMEEIRRLCRASLPCAGAAALSMESERHCNGLPAGAEVTNRPLAWRPLVLLIPLRLGLTDINEAYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVELTDSCFIPDESFHCQHPPCRMGIGELDPSIAVGFFCKTEEDFNDWCQQVKKLSQLGGALPMFELVEQQPSHLACQDVLNLSLDSSDVERLERFFDSEDEDFEILSL

Rattus norvegicus (Rat)

FUNCTION: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3. In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy. Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS). Compared to other members of the family (ATG4A, ATG4C or ATG4C), constitutes the major protein for proteolytic activation of ATG8 proteins, while it displays weaker delipidation activity than other ATG4 paralogs. Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy. {ECO:0000250|UniProtKB:Q9Y4P1}.

3.4.22.-

CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324, ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940, ChEBI:CHEBI:172941; Evidence={ECO:0000250|UniProtKB:Q9Y4P1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549; Evidence={ECO:0000250|UniProtKB:Q9Y4P1}; CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylserine + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:67576, Rhea:RHEA-COMP:17324, Rhea:RHEA-COMP:17326, ChEBI:CHEBI:15377, ChEBI:CHEBI:57262, ChEBI:CHEBI:172940, ChEBI:CHEBI:172942; Evidence={ECO:0000250|UniProtKB:Q9Y4P1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67577; Evidence={ECO:0000250|UniProtKB:Q9Y4P1};

Acetylation;Alternative splicing;Autophagy;Cytoplasm;Cytoplasmic vesicle;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Isopeptide bond;Mitochondrion;Phosphoprotein;Protease;Protein transport;Reference proteome;S-nitrosylation;Thiol protease;Transport;Ubl conjugation;Ubl conjugation pathway

aggrephagy [GO:0035973]; autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to starvation [GO:0009267]; microautophagy [GO:0016237]; mitophagy [GO:0000423]; otolith mineralization completed early in development [GO:0031173]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of protein catabolic process [GO:0045732]; protein localization to phagophore assembly site [GO:0034497]; protein processing [GO:0016485]; protein transport [GO:0015031]; proteolysis [GO:0006508]

autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]

cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; protein-phosphatidylethanolamide deconjugating activity [GO:0019786]; scaffold protein binding [GO:0097110]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4P1}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y4P1}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9Y4P1}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4P1}. Mitochondrion {ECO:0000250|UniProtKB:Q9Y4P1}. Note=Mainly localizes to the cytoplasm, including cytosol. A samll potion localizes to mitochondria; phosphorylation at Ser-34 promotes localization to mitochondria. {ECO:0000250|UniProtKB:Q9Y4P1}.

PTM: Phosphorylation at Ser-383 and Ser-392 promotes autophagy by increasing protein delipidation activity without affecting proteolytic activation of ATG8 proteins. Phosphorylation at Ser-316 by ULK1 inhibits autophagy by decreasing both proteolytic activation and delipidation activities. Phosphorylation at Ser-316 is dephosphorylated by protein phosphatase 2A (PP2A). Phosphorylation at Ser-34 by AKT2 promotes its hydrolase activity, leading to increased proteolytic activation and delipidation of ATG8 family proteins. Phosphorylation at Ser-34 by AKT1 promotes mitochondrial localization and inhibition of the F1F0-ATP synthase activity, leading to elevation of mitochondrial reactive oxygen species (ROS). {ECO:0000250|UniProtKB:Q9Y4P1}.; PTM: Ubiquitinated by RNF5, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q9Y4P1}.; PTM: S-nitrosylation in response to high glucose decreases both proteolytic activation and delipidation activities. {ECO:0000269|PubMed:28633005}.; PTM: O-glycosylated by OGT, leading to increase protease activity, thereby promoting the proteolytic activation of ATG8 family proteins. {ECO:0000250|UniProtKB:Q9Y4P1}.; PTM: Forms reversible intrachain disulfide bonds in response to oxidative stress. Forms interchain disulfide bonds, leading to formation of homooligomers in response to oxidation. {ECO:0000250|UniProtKB:Q9Y4P1}.

DOMAIN: The LIR motif (LC3-interacting region) is required for the interaction with ATG8 family proteins MAP1LC3A, MAP1LC3B, MAP1LC3C and GABARAPL1. Required for proteolytic activation and delipidation of ATG8 proteins. {ECO:0000250|UniProtKB:Q9Y4P1}.

IPR046793;IPR038765;IPR005078;IPR046792;

A0A0H2UHP1

MLFQNQFAEPVTCVPGAKPAMSSPAQPAVPAPLANLKIQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLADLMERDRLLLAVSINQSLTASTGQSVSMVKRTHGQPSYGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKISQKNS

Rattus norvegicus (Rat)

1.2.1.19; 1.2.1.28; 1.2.1.3; 1.2.1.36

CATALYTIC ACTIVITY: Reaction=(E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH; Xref=Rhea:RHEA:67248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58968, ChEBI:CHEBI:142920; Evidence={ECO:0000256|ARBA:ARBA00036562}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249; Evidence={ECO:0000256|ARBA:ARBA00036562}; CATALYTIC ACTIVITY: Reaction=13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH; Xref=Rhea:RHEA:67332, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:45487, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:169952; Evidence={ECO:0000256|ARBA:ARBA00036540}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67333; Evidence={ECO:0000256|ARBA:ARBA00036540}; CATALYTIC ACTIVITY: Reaction=3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH; Xref=Rhea:RHEA:67244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57990, ChEBI:CHEBI:60777; Evidence={ECO:0000256|ARBA:ARBA00036972}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67245; Evidence={ECO:0000256|ARBA:ARBA00036972}; CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000256|ARBA:ARBA00036645}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106; Evidence={ECO:0000256|ARBA:ARBA00036645}; CATALYTIC ACTIVITY: Reaction=9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH; Xref=Rhea:RHEA:42084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78273, ChEBI:CHEBI:78630; Evidence={ECO:0000256|ARBA:ARBA00036033}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42085; Evidence={ECO:0000256|ARBA:ARBA00036033}; CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate; Xref=Rhea:RHEA:67256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036694}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67257; Evidence={ECO:0000256|ARBA:ARBA00036694}; CATALYTIC ACTIVITY: Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH; Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:88528; Evidence={ECO:0000256|ARBA:ARBA00036723}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67277; Evidence={ECO:0000256|ARBA:ARBA00036723}; CATALYTIC ACTIVITY: Reaction=H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:67252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33190, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:566274; Evidence={ECO:0000256|ARBA:ARBA00036632}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67253; Evidence={ECO:0000256|ARBA:ARBA00036632}; CATALYTIC ACTIVITY: Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH; Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000256|ARBA:ARBA00036545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25295; Evidence={ECO:0000256|ARBA:ARBA00036545}; CATALYTIC ACTIVITY: Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36; Evidence={ECO:0000256|ARBA:ARBA00035919}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42081; Evidence={ECO:0000256|ARBA:ARBA00035919}; CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000256|ARBA:ARBA00036925}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186; Evidence={ECO:0000256|ARBA:ARBA00036925}; CATALYTIC ACTIVITY: Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH; Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.28; Evidence={ECO:0000256|ARBA:ARBA00036598}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11841; Evidence={ECO:0000256|ARBA:ARBA00036598};

PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000256|ARBA:ARBA00004891}.

Oxidoreductase;Proteomics identification;Reference proteome

negative regulation of cold-induced thermogenesis [GO:0120163]

cytoplasm [GO:0005737]

benzaldehyde dehydrogenase (NAD+) activity [GO:0018479]

IPR016161;IPR016163;IPR016160;IPR029510;IPR016162;IPR015590;

A0A0H2UNG0

MRKTPSHTEKKMVYSIRSLKNGTGSVLIGASLVLLAMATPTISSDESTPTTNEPNNRNTTTLAQPLTDTAAGSGKNESDISSPGNANASLEKTEEKPAASPADPAPQTGQDRSSEPTTSTSPVTTETKAEEPIEDNYFRIHVKKLPEENKDAQGLWTWDDVEKPSENWPNGALSFKDAKKDDYGYYLDVKLKGEQAKKISFLINNTAGKNLTGDKSVEKLVPKMNEAWLDQDYKVFSYEPQPAGTVRVNYYRTDGNYDKKSLWYWGDVKNPSSAQWPDGTDFTATGKYGRYIDIPLNEAAREFGFLLLDESKQGDDVKIRKENYKFTDLKNHSQIFLKDDDESIYTNPYYVHDIRMTGAQHVGTSSIESSFSTLVGAKKEDILKHSNITNHLGNKVTITDVAIDEAGKKVTYSGDFSDTKHPYTVSYNSDQFTTKTSWRLKDETYSYDGKLGADLKEEGKQVDLTLWSPSADKVSVVVYDKNDPDKVVGTVALEKGERGTWKQTLDSTNKLGITDFTGYYYQYQIERQGKTVLALDPYAKSLAAWNSDDSKIDDAHKVAKAAFVDPAKLGPQDLTYGKIHNFKTREDAVIYEAHVRDFTSDPAIAKDLTKPFGTFEAFIEKLDYLKDLGVTHIQLLPVLSYYFVNELKNHERLSDYASSNSNYNWGYDPQNYFSLTGMYSSDPKNPEKRIAEFKNLINEIHKRGMGAILDVVYNHTAKVDLFEDLEPNYYHFMDADGTPRTSFGGGRLGTTHHMTKRLLIDSIKYLVDTYKVDGFRFDMMGDHDAASIEEAYKAARALNPNLIMLGEGWRTYAGDENMPTKAADQDWMKHTDTVAVFSDDIRNNLKSGYPNEGQPAFITGGKRDVNTIFKNLIAQPTNFEADSPGDVIQYIAAHDNLTLFDIIAQSIKKDPSKAENYAEIHRRLRLGNLMVLTAQGTPFIHSGQEYGRTKQFRDPAYKTPVAEDKVPNKSHLLRDKDGNPFDYPYFIHDSYDSSDAVNKFDWTKATDGKAYPENVKSRDYMKGLIALRQSTDAFRLKSLQDIKDRVHLITVPGQNGVEKEDVVIGYQITAPNGDIYAVFVNADEKAREFNLGTAFAHLRNAEVLADENQAGPVGIANPKGLEWTEKGLKLNALTATVLRVSQNGTSHESTAEEKPDSTPSKPEHQNEASHPAHQDPAPEARPDSTKPDAKVADAENKPSQATADSQAEQPAQEAQASSVKEAVRNESVENSSKENIPATPDKQAELPNTGIKNENKLLFAGISLLALLGLGFLLKNKKEN

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

FUNCTION: Virulence factor (By similarity). Involved in the degradation of glycogen of the mammalian host cells (PubMed:21565699). Hydrolyzes the alpha-1,6-branchpoints of glycogen (PubMed:20497336, PubMed:21565699). Hydrolyzes pullulan. Does not hydrolyze dextran (PubMed:20497336). Binds to mouse lung alveolar type II cells that are rich in glycogen stores. Is an alpha-glucan-specific carbohydrate-binding protein, which binds to amylose (pure alpha-(1,4)-linked glucose), amylopectin (alpha-(1,4)-linked glucose with alpha-(1,6) branch points), pullulan (linear polymer of mixed alpha-(1,4)- and alpha-(1,6)-linked glucose) and glycogen (similar to amylopectin with more frequent alpha-(1,6) branch points) in vitro. Does not bind to dextran (a linear polymer of alpha-(1,6)-linked glucose) (PubMed:17187076). {ECO:0000250|UniProtKB:A0A0H2ZL64, ECO:0000269|PubMed:17187076, ECO:0000269|PubMed:20497336, ECO:0000269|PubMed:21565699}.

3.2.1.41

CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.; EC=3.2.1.41; Evidence={ECO:0000269|PubMed:20497336, ECO:0000269|PubMed:21565699};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=360 uM for para-nitrophenyl-alpha-D-maltopentaoside (pNP-M5) (at 25 degrees Celsius) {ECO:0000269|PubMed:21565699}; Note=kcat is 270 min(-1) for pNP-M5. {ECO:0000269|PubMed:21565699};

3D-structure;Calcium;Cell wall;Glycosidase;Hydrolase;Metal-binding;Peptidoglycan-anchor;Reference proteome;Secreted;Signal;Virulence

alpha-glucan biosynthetic process [GO:0030979]

cell surface [GO:0009986]; extracellular region [GO:0005576]

amylopectin binding [GO:2001066]; calcium ion binding [GO:0005509]; glycogen binding [GO:2001069]; limit dextrinase activity [GO:0010303]; polysaccharide binding [GO:0030247]; pullulan binding [GO:2001067]; pullulanase activity [GO:0051060]

SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000250|UniProtKB:Q9F930}. Note=Localizes to cytoplasm in the lung alveolar type II cells of the mouse and human hosts. {ECO:0000269|PubMed:17187076, ECO:0000269|PubMed:21565699}.

DOMAIN: The N-terminal tandem family 41 carbohydrate-binding modules (CBM) are involved in carbohydrate binding (PubMed:17187076, PubMed:21565699). The C-terminal glycosyl hydrolase 13 (GH13) domain is involved in catalysis (PubMed:21565699). {ECO:0000269|PubMed:17187076, ECO:0000269|PubMed:21565699}.

IPR013784;IPR005323;IPR014755;IPR006047;IPR004193;IPR013780;IPR017853;IPR013783;IPR014756;IPR019931;IPR011838;IPR040806;IPR005877;

2.60.40.1110;2.60.40.1220;3.20.20.80;2.60.40.1180;2.60.40.10;

A0A0H2URG7

MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

FUNCTION: Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP (PubMed:24936067, PubMed:28246170). Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon (Probable). The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP (experimentally characterized with truncated PsrP-SSR1 constructs); this subunit alone has weak N-acetylglucosaminyl transferase activity that is 10-fold stimulated by GtfB. The complex requires at least a 25 residue-long peptide for activity; the in vitro assay has only been seen to glycosylate Ser residues (PubMed:24936067). The alpha linkage was shown in L.reuteri. {ECO:0000250|UniProtKB:A0A0S4NM89, ECO:0000269|PubMed:24936067, ECO:0000269|PubMed:28246170, ECO:0000305|PubMed:16861665}.

2.4.1.-

CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-alpha-D-glucosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:59872, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15471, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:143279; Evidence={ECO:0000250|UniProtKB:A0A0S4NM89, ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000305|PubMed:24936067};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat for hydrolysis of UDP-N-acetyl-alpha-D-glucosamine with transfer of GlcNAc to PsrP-SSR1 and generation of UDP is 76.0 min(-1) for GtfA-GtfB and 7.35 min(-1) for GtfA alone. {ECO:0000269|PubMed:24936067};

PATHWAY: Protein modification; protein glycosylation. {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:24936067, ECO:0000269|PubMed:28246170}.

3D-structure;Cell membrane;Cytoplasm;Glycosyltransferase;Membrane;Nucleotide-binding;Reference proteome;Transferase

protein O-linked glycosylation via serine [GO:0018242]

cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; protein N-acetylglucosaminyltransferase complex [GO:0017122]

glycosyltransferase activity [GO:0016757]; nucleotide binding [GO:0000166]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01472}. Cell membrane {ECO:0000250|UniProtKB:A1C3L9, ECO:0000255|HAMAP-Rule:MF_01472}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01472}. Note=Cell membrane association requires GtfB. {ECO:0000250|UniProtKB:A1C3L9, ECO:0000255|HAMAP-Rule:MF_01472}.

DOMAIN: Has 2 Rossmann-like domains, called R-fold-1 and R-fold-2. R-fold-1 is interrupted by an extended beta-sheet domain that loops out of the structure and is required for recognizing both PsrP substrate and coactivator GtfB. UDP and N-acetyl-D-glucosamine bind between the Rossmann-like folds. {ECO:0000269|PubMed:24936067}.

IPR001296;IPR014267;

3.40.50.2000;

A0A0H2US87

MKIPEAVNHINVQNNIDLVDGKINPNKDTKALQKNISCVTNSSSSGISEKHLDHCADTVKSFLRKSIAAQSYSKMFSQGTSFKSLNLSIEAPSGARSSFRSLEHLDKVSRHYLSEIIQKTHPLSSDERHLLSIIINSDFNFRHQSNANLSNNTLNIKSFDKIKSENIQTYKNTFSEDIEEIANHDFVFFGVEISNHQETLPLNKTHHTVDFGANAYIIDHDSPYGYMTLTDHFDNAIPPVFYHEHQSFFLDNFKEVVDEVSRYVHGNQGKTDVPIFNTKDMRLGIGLHLIDFIRKSKDQRFREFCYNKNIDPVSLDRIINFVFQLEYHIPRMLSTDNFKKIKLRDISLEDAIKASNYEEINNKVTDKKMAHQALAYSLGNKKADIALYLLSKFNFTKQDVAEMEKMKNNRYCNLYDVEYLLSKDGANYKVLEYFINNGLVDVNKKFQKVNSGDTMLDNAMKSKDSKMIDFLLKNGAILGKRFEI

Shigella flexneri

FUNCTION: ADP-riboxanase effector that inhibits host cell pyroptosis (PubMed:23684308, PubMed:34409271, PubMed:34671164, PubMed:36624349). Acts by mediating arginine ADP-riboxanation of host CASP4/CASP11, blocking CASP4/CASP11 autoprocessing (PubMed:34671164, PubMed:35338844, PubMed:35568036, PubMed:36624349, PubMed:37014865). This prevents CASP4 activation and ability to recognize and cleave GSDMD, thereby inhibiting LPS-induced pyroptosis (PubMed:34671164, PubMed:36624349). ADP-riboxanation takes place in two steps: OspC3 first catalyzes ADP-ribosylation of target Arg, and then initiates a deamination to remove one N-omega group (PubMed:34671164). Independently of its ADP-riboxanase activity, acts as an inhibitor of calcium signaling by inhibiting host calmodulin, preventing activation of the JAK-STAT signaling pathway in response to interferon-beta (PubMed:35568036). Mechanistically, acts by binding to the apo form of calmodulin, preventing calcium-binding and ability to activate host CaMK2 (CAMKII), which is required to stimulate the JAK-STAT signaling pathway in response to interferon-beta (PubMed:35568036). {ECO:0000269|PubMed:23684308, ECO:0000269|PubMed:34409271, ECO:0000269|PubMed:34671164, ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35568036, ECO:0000269|PubMed:36624349, ECO:0000269|PubMed:37014865}.

4.3.99.-

CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + NAD(+) = ADP-riboxanated L-argininyl-[protein] + H(+) + NH4(+) + nicotinamide; Xref=Rhea:RHEA:69500, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17719, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:28938, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:184300; Evidence={ECO:0000269|PubMed:34671164, ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35568036, ECO:0000269|PubMed:36624349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69501; Evidence={ECO:0000269|PubMed:34671164, ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35568036, ECO:0000269|PubMed:36624349};

3D-structure;ANK repeat;Host cytoplasm;Lyase;NAD;Plasmid;Reference proteome;Repeat;Secreted;Toxin;Virulence

modulation by symbiont of defense-related host calcium ion flux [GO:0052162]; symbiont-mediated perturbation of host programmed cell death [GO:0052040]; symbiont-mediated suppression of host calcium or calmodulin-mediated signal transduction [GO:0075135]; symbiont-mediated suppression of host programmed cell death [GO:0052041]; symbiont-mediated suppression of host signal transduction pathway [GO:0052029]

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

ADP-riboxanase activity [GO:0140740]; calmodulin binding [GO:0005516]; toxin activity [GO:0090729]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23684308}. Host cytoplasm {ECO:0000305|PubMed:34409271}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:23684308}.

IPR010366;

A0A0H2USG1

MIKSTNIQAIGSGIMHQINNVYSLTPLSLPMELTPSCNEFYLKTWSEWEKNGTPGEQRNIAFNRLKICLQNQEAELNLSELDLKTLPDLPPQITTLEIRKNLLTHLPDLPPMLKVIHAQFNQLESLPALPETLEELNAGDNKIKELPFLPENLTHLRVHNNRLHILPLLPPELKLLVVSGNRLDSIPPFPDKLEGLALANNFIEQLPELPFSMNRAVLMNNNLTTLPESVLRLAQNAFVNVAGNPLSGHTMRTLQQITTGPDYSGPQIFFSMGNSATISAPEHSLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQLTDEVLALRLSENGSNHIA

Shigella flexneri

FUNCTION: E3 ubiquitin-protein ligase effector that inhibits host cell innate immunity during bacterial infection by catalyzing 'Lys-48'-linked polyubiquitination and subsequent degradation of host RNF31/HOIP and RBCK1/HOIL-1 (PubMed:18997778, PubMed:27572974, PubMed:35294289, PubMed:36610722). Host RNF31/HOIP is the catalytic component of the LUBAC complex, which conjugates linear ('Met-1'-linked) polyubiquitin chains at the surface of bacteria invading the host cytosol to form the ubiquitin coat surrounding bacteria (PubMed:27572974, PubMed:35294289). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:27572974, PubMed:28481331). By promoting degradation of host RNF31/HOIP, IpaH1.4 prevents formation of the bacterial ubiquitin coat and activation of host cell innate immunity (PubMed:27572974, PubMed:28481331). {ECO:0000269|PubMed:18997778, ECO:0000269|PubMed:27572974, ECO:0000269|PubMed:28481331, ECO:0000269|PubMed:35294289, ECO:0000269|PubMed:36610722}.

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:0000269|PubMed:18997778, ECO:0000269|PubMed:27572974, ECO:0000269|PubMed:35294289};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18997778, ECO:0000269|PubMed:27572974, ECO:0000269|PubMed:35294289}.

3D-structure;Host cytoplasm;Leucine-rich repeat;Plasmid;Reference proteome;Repeat;Secreted;Transferase;Ubl conjugation pathway;Virulence

protein ubiquitination [GO:0016567]; symbiont-mediated suppression of host NF-kappaB cascade [GO:0085034]

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

toxin activity [GO:0090729]; ubiquitin protein ligase activity [GO:0061630]

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8VSC3}. Host cytoplasm {ECO:0000250|UniProtKB:Q8VSC3}. Note=Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm. {ECO:0000250|UniProtKB:Q8VSC3}.

DOMAIN: The LRR (leucine-rich repeat) domain forms a slightly curved solenoid and may mediate interaction with target proteins. {ECO:0000250|UniProtKB:P0CE12}.

IPR001611;IPR032675;IPR032674;IPR029487;

1.20.58.90;3.80.10.10;1.20.58.360;1.20.1270.130;

A0A0H2V8B5

MIAYENIEFFICLVNVLGNNMYNILFFIFLSIAIPFLLFLAWKQHLKTKEIRSYLLKEGYNIIFNGEGNSYLAFNISNATFRAGNLTSNDYFQASISYIHDYRWEWKEVEAKKINNIFIIYISNIDFPSQKLFYRNNKSLAEIDWAKLQAIFHQPYEIQNDVMQDNNNTHYDFFISHAKEDKDTFVRPLVDELNRLGVIIWYDEQTLEVGDSLRRNIDLGLRKANYGIVILSHNFLNKKWTQYELDSLINRAVYDDNKIILPIWHNINAQEVSKYSHYLADKMALQTSLYSVKEIARELAEIAYRRR

Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

FUNCTION: Virulence factor that suppresses host Toll-like receptor (TLR)-mediated cytokine production upon infection, thereby increasing bacterial burden in the urinary tract and promoting renal tissue damage (PubMed:18327267, PubMed:20886104). Acts as a NAD(+) hydrolase (NADase) by catalyzing cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide (PubMed:29395922). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (PubMed:29395922). {ECO:0000269|PubMed:18327267, ECO:0000269|PubMed:20886104, ECO:0000269|PubMed:29395922}.

3.2.2.-; 3.2.2.6

CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000269|PubMed:29395922}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000269|PubMed:29395922}; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) + nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349, ChEBI:CHEBI:58673; Evidence={ECO:0000269|PubMed:29395922}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850; Evidence={ECO:0000269|PubMed:29395922};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=196 uM for NAD(+) {ECO:0000269|PubMed:29395922};

Hydrolase;Membrane;NAD;Reference proteome;Secreted;Transmembrane;Transmembrane helix;Virulence

NAD catabolic process [GO:0019677]; negative regulation of MyD88-dependent toll-like receptor signaling pathway [GO:0034125]; signal transduction [GO:0007165]

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

NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18327267}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.

DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity. {ECO:0000255|PROSITE-ProRule:PRU00204}.

IPR000157;IPR035897;

3.40.50.10140;

A0A0H2ZNH9

MLDLLKQTIFTRDFIFILILLGFILVVTLLLLENRRDNIQLKQINQKVKDLIAGDYSKVLDMQGGSEITNITNNLNDLSEVIRLTQENLEQESKRLNSILFYMTDGVLATNRRGQIIMINDTAKKQLGLVKEDVLNRSILELLKIEENYELRDLITQSPELLLDSQDINGEYLNLRVRFALIRRESGFISGLVAVLHDTTEQEKEERERRLFVSNVSHELRTPLTSVKSYLEALDEGALCETVAPDFIKVSLDETNRMMRMVTDLLHLSRIDNATSHLDVELINFTAFITFILNRFDKMKGQEKEKKYELVRDYPINSIWMEIDTDKMTQVVDNILNNAIKYSPDGGKITVRMKTTEDQMILSISDHGLGIPKQDLPRIFDRFYRVDRARSRAQGGTGLGLSIAKEIIKQHKGFIWAKSEYGKGSTFTIVLPYDKDAVKEEVWEDEVED

Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)

FUNCTION: Member of the two-component regulatory system WalK/WalR that regulates genes involved in cell wall metabolism (By similarity). Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to WalR (By similarity). In turn, WalR binds to the upstream promoter regions of target genes to positively and negatively regulate their expression (By similarity). Required to maintain expression of WalRK regulon genes in exponentially growing cells, including peptidoglycan hydrolase pcsB (PubMed:23013245). Phosphorylates WalR and also capable of dephosphorylation of WalR (PubMed:23013245). WalK phosphatase activity is probably involved in preventing cross-talk from PnpS and other non-cognate sensor kinases during exponential growth (PubMed:23013245). May be considered a potential virulence factor (PubMed:20190050). {ECO:0000250|UniProtKB:Q8DPL8, ECO:0000250|UniProtKB:Q9RDT3, ECO:0000269|PubMed:20190050, ECO:0000269|PubMed:23013245}.

2.7.13.3; 3.9.1.-

CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:23013245};

Hydrolase;Kinase;Membrane;Phosphoprotein;Reference proteome;Transferase;Transmembrane;Transmembrane helix;Two-component regulatory system;Virulence

cellular response to phosphate starvation [GO:0016036]; regulation of DNA-templated transcription [GO:0006355]; signal transduction [GO:0007165]

plasma membrane [GO:0005886]

phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673]

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

PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q8DPL8}.

DOMAIN: Transmembrane domain is involved in signal sensing or transduction. {ECO:0000250|UniProtKB:Q8DPL8}.; DOMAIN: PAS domain is involved in phosphatase activity. {ECO:0000250|UniProtKB:Q8DPL8}.

IPR003660;IPR003594;IPR036890;IPR005467;IPR003661;IPR036097;IPR000014;IPR000700;IPR035965;IPR013767;IPR004358;

1.10.287.130;1.10.8.500;3.30.565.10;3.30.450.20;

A0A0H2ZQL5

MDLGDNELTLTPIPGKSGKAYMGSYPDGKRIFVKMNTSPILPGLAREQIAPQLLWSRRLADGRDMCAQEWLTGKILTPYDMNRKQIVNILTRLHRSRPLMTQLSRLGYAMETPVDLLQSWQETAPDALRKNHFISEVMADLRQTIPGFREDHATIVHGDVRHSNWIETDSGLIYLVDWDSVRLTDRMFDVAHMLCHYISEHQWKEWLTYYGYKYNQTVLSKLYWYGQLSYLSQISKYYMNQDLENVNREIHGLRHFRDKYGKRR

Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)

FUNCTION: Plays a role in cell cycle regulation and chromosome integrity. Activates DnaA-dependent chromosomal DNA replication initiation ensuring that the chromosome is replicated at the right time during the cell cycle (PubMed:34373624). May regulate replication initiation through phosphorylation of a possible second messenger or metabolite, and by interacting with replication initiation proteins. Has ATPase activity with D-ribose and 2-deoxy-D-ribose in vitro, but not with choline. Involved in DNA damage response (By similarity). {ECO:0000250|UniProtKB:C0SPC1, ECO:0000269|PubMed:34373624}.

2.7.1.15; 2.7.1.229

CATALYTIC ACTIVITY: Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+); Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216; EC=2.7.1.15; Evidence={ECO:0000250|UniProtKB:C0SPC1}; CATALYTIC ACTIVITY: Reaction=2-deoxy-D-ribose + ATP = 2-deoxy-D-ribose 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:30871, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:62877, ChEBI:CHEBI:90761, ChEBI:CHEBI:456216; EC=2.7.1.229; Evidence={ECO:0000250|UniProtKB:C0SPC1};

ATP-binding;Cell cycle;Cell division;Cytoplasm;DNA damage;DNA replication;Kinase;Nucleotide-binding;Reference proteome;Transferase

cell cycle [GO:0007049]; cell division [GO:0051301]; DNA damage response [GO:0006974]; DNA replication initiation [GO:0006270]; regulation of cell cycle [GO:0051726]

cell division site [GO:0032153]; cytoplasm [GO:0005737]

ATP binding [GO:0005524]; carbohydrate kinase activity [GO:0019200]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]; ribokinase activity [GO:0004747]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:34373624}. Note=Localizes at mid-cell, forming a patchy ring. Disassembles from the old septum to assemble at the newly formed division site. Colocalizes with FtsZ during the full cell cycle. Colocalizes with DnaA in newborn cells. {ECO:0000269|PubMed:34373624}.

IPR002575;IPR011009;

3.90.1200.10;

A0A0H3AIG7

MATLAYSIEVEGLEDETLVVRGFHGQESLSNSVFLGQACYGFRYEVQLASRVSNLTAEQMVDKRAELKLYRNSQLVQRVHGIVRAFSQGDIGHHHTFYQLTLVPALERLSLRHNSRIFQKQTVPEILSILLQEMGINDYAFALKRDGVQREFCVQYRESDIDFLHRLAAEEGLVYSFVHEAGKHTLYFSDASDSLSKLPEPIPYNALVGGAIDTPYIHGLTYRTQAEVSEVQLKDYSFKKPAYSFLQTVQGTELDYQQTRYQHFDAPGRYKDDVNGAAFSQIRLDYLRRHAHTATGQSNEPLLRAGYKFDLQEHLDPAMNRDWVVVSINHQGEQPQALQEDGGSGATTYSNQFSLIPGHLHWRAEPQPKPQVDGPMIATVVGPEGEEIFCDEHGRVKIHFPWDRYSNGNEQSSCWVRVSQGWAGSQYGFIAIPRIGHEVIVEFLNGDPDQPIITGRTYHATNTPPYTLPEHKTKTVLRTETHQGEGFNELSFEDQAGKEQIYLHAQKDFDGLIENDQFTQIKHNQHLTVEWESREAVTGEQVLSIEGSLHVKTGKVRVNEAGTEIHVKAGQKVVIEAGSEITVKAGGSFVKVDPAGVHLSGALVNLNSGGSAGSGSGFGGAMPALPGGLEPAVALAPPQTISYQALLQAEQANVPAVKVCPLAAQEATPAVNSITPPPPPPIAPPMAPPQPIMNPQPTANAQPNLGRSTKATPDFPTHFPKSSIGIENELAGLVVAMPANSAQKFGYVKSAQGDALFMLTKDMNQGSYQRPPSLQDGKNYQNWQTHTVELVSYPCEMDDKAAVETRKQAMLWLATHFTTHIDQSNHQPLAPIQSEDGRFVIEITNAKHVIAAGNGISAESQGQTITMTPSGQQATVGVAAKGFGTSATPELRLLESAPWYQKSLKSQFASLTSAENLDDKELAANVFAYLTSIYLKTAELAKKFGIYINEWDPMSEQITPNANGLTDPKVKNAWEILPRTKPSKIVEILSKSDAKAVMKHIKPQLQSRYSESLSKNVFQYFQDGGEVAGHGINNATVGDKHSPELAILFEFRTVPNELQSYLPKTESTTKSEVKLLDQFDPMKRKTVIQQVESLV

Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)

FUNCTION: Part of the type VI secretion system (T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection (By similarity). Forms the spike at the tip of the elongating tube probably formed by hemolysin co-regulated protein/Hcp. Allows the delivery of the TseL antibacterial toxin to target cells where it exerts its toxicity (By similarity). Acts also directly as an actin-directed toxin that catalyzes the covalent cross-linking of host cytoplasmic monomeric actin. Mediates the cross-link between 'Lys-50' of one monomer and 'Glu-270' of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:22898822). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:22898822). Acts as an acid--amino-acid ligase that transfers the gamma-phosphoryl group of ATP to the 'Glu-270' actin residue, resulting in the formation of an activated acyl phosphate intermediate. This intermediate is further hydrolyzed and the energy of hydrolysis is utilized for the formation of the amide bond between actin subunits (PubMed:22898822). {ECO:0000250|UniProtKB:Q9KS45, ECO:0000269|PubMed:22898822}.

6.3.2.-

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22898822}; Note=Binds 2 Mg(2+) ions per subunit. Can also use Mn(2+) ions instead of Mg(2+). {ECO:0000269|PubMed:22898822};

3D-structure;ATP-binding;Host cytoplasm;Ligase;Magnesium;Metal-binding;Nucleotide-binding;Secreted;Toxin;Virulence

actin filament depolymerization [GO:0030042]; isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine [GO:0018153]

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

acid-amino acid ligase activity [GO:0016881]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; toxin activity [GO:0090729]

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9KS45}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:22898822}. Note=Secreted via the type VI secretion system. {ECO:0000250|UniProtKB:Q9KS45}.

IPR032074;IPR006531;IPR017847;IPR006533;IPR037026;

2.30.110.50;4.10.220.110;1.10.3680.20;3.55.50.10;2.40.50.230;

A0A0H3GDH9

MKIRWIRLSLVAILIIAVVFIGVIGFQKYQFSKSRNKVIMQMDRLMKDQDGGNFRRLDKKENGVEIISYIPKTTEKKDNEIIQKEIGKATDAEVKKLNRDKETQGIIFYTYQKHRMAEQAISYKAVQSEYVKEGRTKFVLKDKKDICKNIVTDAETGALLTLGEVLIKSNQTKLNLKTAVEEELIKTGDFSLKDVGNLGKIKSLVKWNQTDFEITNSEIILPVKIPGAPEPKKVKVKLADIASSVNKRYLPSSVKVPEVPKAKTNKRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQVGSHSWDHPQLTKQSTQEVYNQILKTQKAVFDQTGYFPTTMRPPYGAVNKQVAEEIGLPIIQWSVDTEDWKYRNAGIVTKKVLAGATDGAIVLMHDIHKTTAASLDTTLTKLKSQGYEFVTIDELYGEKLQIGKQYFDKTDSRMVK

Listeria monocytogenes serotype 1/2a (strain 10403S)

FUNCTION: Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan (PG). Deacetylates also N-acetylated PG. Does not deacetylate N-acetylmuramic acid (By similarity). Confers host lysozyme resistance. Critical for virulence and escape from innate immune response of the host (PubMed:21768286, PubMed:25157076). Required for intracellular survival of bacteria in macrophages of the host. Required for successful host colonization. Controls the production of inflammatory mediators in the bone marrow derived macrophages (BMMs) of the infected mouse (PubMed:21768286). Suppresses Toll-like receptor 2 (TLR2)-dependent secretion of interleukin 6 (IL-6) and interferon-beta (IFN-beta) in the macrophages of the infected mouse. May decrease accessibility of pattern recognition receptors (PRRs) such as nucleotide-binding oligomerization domain protein (NOD) 1 of the host to the bacterial cell wall components (By similarity). Protects cells from autolysis induced by lysozyme or by other autolysis-inducing agents (By similarity). {ECO:0000250|UniProtKB:A0A3Q0NBH7, ECO:0000250|UniProtKB:Q8Y9V5, ECO:0000269|PubMed:21768286, ECO:0000269|PubMed:25157076}.

3.5.1.104

CATALYTIC ACTIVITY: Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate.; EC=3.5.1.104; Evidence={ECO:0000250|UniProtKB:A0A3Q0NBH7};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8DP63};

Cell membrane;Cell wall;Hydrolase;Membrane;Metal-binding;Secreted;Transmembrane;Transmembrane helix;Virulence;Zinc

autolysis [GO:0001896]; carbohydrate metabolic process [GO:0005975]; cell wall modification [GO:0042545]; evasion of host immune response [GO:0042783]; evasion of host innate immune recognition [GO:0141043]; negative regulation of lysozyme activity [GO:1903591]

extracellular region [GO:0005576]; Gram-positive-bacterium-type cell wall [GO:0009275]; plasma membrane [GO:0005886]

chitin deacetylase activity [GO:0004099]; lysozyme inhibitor activity [GO:0060241]; N-acetylglucosamine deacetylase activity [GO:0050119]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8Y9V5}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8Y9V5, ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:Q8Y9V5}. Secreted, cell wall {ECO:0000250|UniProtKB:A0A3Q0NBH7}.

IPR011330;IPR002509;IPR017219;

3.20.20.370;

A0A0H3JN63

MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGGGSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDFYTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHYKNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQKKSR

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 GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is channeled to the active site of MurT (PubMed:22291598). {ECO:0000269|PubMed:22291598, ECO:0000269|PubMed:30154570}.

3.5.1.2; 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_02213, ECO:0000269|PubMed:22291598, ECO:0000269|PubMed:30154570}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_02213, ECO:0000269|PubMed:22291598};

PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02213, 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;Cell shape;Cell wall biogenesis/degradation;Glutamine amidotransferase;Hydrolase;Ligase;Peptidoglycan synthesis

cell wall organization [GO:0071555]; cobalamin biosynthetic process [GO:0009236]; glutamine metabolic process [GO:0006541]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]

carbon-nitrogen ligase activity on lipid II [GO:0140282]; glutaminase activity [GO:0004359]

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}.

IPR029062;IPR033949;IPR011698;IPR043702;

3.40.50.880;

A0A0H3JRU9

MKQIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDLGPAESYLNIERIIDVAKQANVDAIHPGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGADLFGEEINMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGDGFQGAEISPYYDSLLVKLSTHAISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEETPELFDIQPSLDRGTKTLEYIGNVTINGFPNVEKRPKPDYELASIPTVSSSKIASFSGTKQLLDEVGPKGVAEWVKKQDDVLLTDTTFRDAHQSLLATRVRTKDMINIASKTADVFKDGFSLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLLRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTGDILNPERSNIYTLEYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMSGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLGERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYMVQNDLDEQSVITDGYKLDFPESVVSFFKGEIGQPVNGFNKDLQAVILKGQEALTARPGEYLEPVDFEKVRELLEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQYGNLSLLDTPTFFFGMRNGETVEIEIDKGKRLIIKLETISEPDENGNRTIYYAMNGQARRIYIKDENVHTNANVKPKADKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKATD

Staphylococcus aureus (strain Mu50 / ATCC 700699)

FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. {ECO:0000269|PubMed:19523900, ECO:0000269|PubMed:23286247}.

6.4.1.1

CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1; Evidence={ECO:0000269|PubMed:19523900, ECO:0000269|PubMed:23286247};

COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000269|PubMed:19523900, ECO:0000269|PubMed:23286247};

3D-structure;ATP-binding;Biotin;Ligase;Manganese;Metal-binding;Nucleotide-binding;Pyruvate

gluconeogenesis [GO:0006094]; pyruvate metabolic process [GO:0006090]

cytoplasm [GO:0005737]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; pyruvate carboxylase activity [GO:0004736]

IPR013785;IPR011761;IPR005481;IPR011764;IPR005482;IPR000089;IPR003379;IPR005479;IPR016185;IPR000891;IPR005930;IPR011054;IPR011053;

2.40.50.100;3.20.20.70;3.30.470.20;3.10.600.10;