lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription. At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module). SAGA preferentially acetylates histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and deubiquitinates histone H2B. SAGA interacts with DNA via upstream activating sequences (UASs). Within the SAGA complex, participates in a subcomplex with SGF11, SGF73 and UBP8 required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery.
Subcellular Localization:
Nucleus, nucleoplasm. Cytoplasm, P-body.
Sequence:
MYDLIFSTKMTTEKIVEQLYETGDYERLANELEYKLESCGWTTQLRDYTRGIVNSDSKIDFQKLYESALQSATESIPDSVKMDLLKDIKTCVLKLANPPESANGGNKM
The following text describes a protein:
Function:
May be involved in mRNA splicing.
Sequence:
MGERKGVNKYYPPDFNPEKHGSLNRYHNSHPLRERARKLSQGILIIRFEMPYNIWCDGCKNHIGMGVRYNAEKKKVGNYYTTPIYRFRMKCHLCVNYIEMQTDPANCDYVIVSGAQRKEERWDMADNEQVLTTEHEKKQKLETDAMFRLEHGEADRSTLKKALPTLSHIQEAQSAWKDDFALNSMLRRRFREKKKAIQEEEERDQALQAKASLTIPLVPETEDDRKLAALLKFHTLDSYEDKQKLKRTEIISRSWFPSAPGSASSSKVSGVLKKLAQSRRTALATCPITVGDLGIVRRRSRDVPESPQHAADTPKSGEPRVPEEAAQDRPMSPGDCPPETTETPKCSRPRGQEGSRQDKPLSPAGSSQEAADTPDTRHPCSLGSSLVADYSDSESE
The following text describes a protein:
Function:
Synthesis of cross-linked peptidoglycan from the lipid intermediates.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Domain:
The enzyme has an N-terminal penicillin insensitive transglycosylase domain (formation of linear glycan strands) and a C-terminal penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits).
Sequence:
MSRAAPRRASQSQSTRPARGLRRPPGAQEVGQRKRPGKTQKARQAQEATKSRPATRSDVAPAGRSTRARRTRQVVDVGTRGASFVFRHRTGNAVILVLMLVAATQLFFLQVSHAAGLRAQAAGQLKVTDVQPAARGSIVDRNNDRLAFTIEARALTFQPKRIRRQLEEARKKTSAAPDPQQRLRDIAQEVAGKLNNKPDAAAVLKKLQSDETFVYLARAVDPAVASAICAKYPEVGAERQDLRQYPGGSLAANVVGGIDWDGHGLLGLEDSLDAVLAGTDGSVTYDRGSDGVVIPGSYRNRHKAVHGSTVVLTLDNDIQFYVQQQVQQAKNLSGAHNVSAVVLDAKTGEVLAMANDNTFDPSQDIGRQGDKQLGNPAVSSPFEPGSVNKIVAASAVIEHGLSSPDEVLQVPGSIQMGGVTVHDAWEHGVMPYTTTGVFGKSSNVGTLMLSQRVGPERYYDMLRKFGLGQRTGVGLPGESAGLVPPIDQWSGSTFANLPIGQGLSMTLLQMTGMYQAIANDGVRVPPRIIKATVAPDGSRTEEPRPDDIRVVSAQTAQTVRQMLRAVVQRDPMGYQQGTGPTAGVPGYQMAGKTGTAQQINPGCGCYFDDVYWITFAGIATADNPRYVIGIMLDNPARNSDGAPGHSAAPLFHNIAGWLMQRENVPLSPDPGPPLVLQAT
The following text describes a protein:
Function:
Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access their SCP2-bound polyprenyl substrates.
Subcellular Localization:
Cytoplasm.
Sequence:
MMPQEVVLLVCAAIEMGLKQLQTQAGGAYARQRQLHGKVFRIQLTQLSWPIYLIFAKEIQVLSRYEGDVDVSLHADATTLYHVSEGANLTELIKQDKLKLEGDLNLLQSFSQYLRSIEFDFAEPISSYLGDGPTHKLISTGHQAKSFALEVLRKTRSHLGQLAIEEYRIAPHRLELIHFCDQMDDLVSDTRTLEQRIAKLRDQIKP
The following text describes a protein:
Function:
Catalyzes the last step of the cholesterol synthesis pathway, which transforms cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol,7-DHC) into cholesterol by reducing the C7-C8 double bond of its sterol core. Can also metabolize cholesta-5,7,24-trien-3beta-ol (7-dehydrodemosterol, 7-DHD) to desmosterol, which is then metabolized by the Delta(24)-sterol reductase (DHCR24) to cholesterol. Modulates ferroptosis (a form of regulated cell death driven by iron-dependent lipid peroxidation) through the metabolic breakdown of the anti-ferroptotic metabolites 7-DHC and 7-DHD which, when accumulated, divert the propagation of peroxyl radical-mediated damage from phospholipid components to its sterol core, protecting plasma and mitochondrial membranes from phospholipid autoxidation; Component of the microsomal antiestrogen binding site (AEBS), a multiproteic complex at the ER membrane that consists of an association between cholestenol Delta-isomerase/EBP and DHCR7. This complex is responsible for cholesterol-5,6-epoxide hydrolase (ChEH) activity, which consists in the hydration of cholesterol-5,6-epoxides (5,6-EC) into cholestane-3beta,5alpha,6beta-triol (CT). The precise role of each component of this complex has not been described yet; Oxidoreductase that catalyzes the last step of the cholesterol synthesis pathway, which transforms cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol,7-DHC) into cholesterol by reducing the C7-C8 double bond of its sterol core. Can also metabolize cholesta-5,7,24-trien-3beta-ol (7-dehydrodemosterol, 7-DHD) to desmosterol, which is then metabolized by the Delta(24)-sterol reductase (DHCR24) to cholesterol. Modulates ferroptosis (a form of regulated cell death driven by iron-dependent lipid peroxidation) through the metabolic breakdown of the anti-ferroptotic metabolites 7-DHC and 7-DHD which, when accumulated, divert the propagation of peroxyl radical-mediated damage from phospholipid components to its sterol core, protecting plasma and mitochondrial membranes from phospholipid autoxidation.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMACDQYSCALTGPVVDIVTGHARLWDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGYFFPTSTRDCKFTGNFFYNYMMGVEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQRELHGHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCLACGGSHLLPYFYIIYMAILLTHRCLRDEHRCASKYGQDWERYTAAVPYRLLPGVF
The following text describes a protein:
Function:
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (By similarity). May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required for correct morphology of nociceptive multi-dendritic sensory neurons. Required for normal mechanical amplification in hearing.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MATKRRPLRPNLGGTAGSPSSSGSNMNFRPGGPDITRSEARGTRPTAAPTSIREILVMGVIHLCKKTIFFNTDLKVALYLGSLFVISVIGDFVPFPKTYFARSDNLFNQYFVKIGWGWTLLFVVPFLVLSAYTITCGDHKRMLRHHFPRIVIATFFWFFWTKLFNVVENSYGRCTTKGYATKSSCLKAGHLWKGFDISGHAFILIHSSLVLIEEARPIIRWETIKEHIRNERHNRSTAENSGTNPLRTLNEEQMRSLQFLYKRLTPIIRTLFIGMAALQLLWDIMLVGTMLYYHRMIEKVISGIIAILTWYFTYRFWYPTPGLLPEAPGNGSFSYQREIPTFPFKRPSHLSTGAATTSSGSNSSRTNLNGKAATTGVPRDQQIPTFMGMPLFTSPKAASAAANLLMSDQQKRERDREQQTLES
The following text describes a protein:
Function:
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Miscellaneous:
MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
Sequence:
MAGGKIPIVGIVACLQPEMGIGFRGGLPWRLPSEMKYFRQVTSLTKDPNKKNALIMGRKTWESIPPKFRPLPNRMNVIISRSFKDDFVHDKERSIVQSNSLANAIMNLESNFKEHLERIYVIGGGEVYSQIFSITDHWLITKINPLDKNATPAMDTFLDAKKLEEVFSEQDPAQLKEFLPPKVELPETDCDQRYSLEEKGYCFEFTLYNRK
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MISRCIKRCYRSGYMIFPPNRLQSTIRSKEEINSSRHKFNIADTSVRKQYNEELVFTKDAKENAEAKKVSSKVKKDRKNHSAAMEGVNINVPGIYRDVYPLPNEDVEMHEAKKKENICKKENLSKTVLVRQLAEIYFANSNKYVVDENGLDDLIQQAFKNPNDVFQPLPSKRDGDNMRLFIETEEEADMTSIKQHAIEVVLQDFQEEQPLEDKRDTIE
The following text describes a protein:
Function:
Cardioactive peptide. Corazonin is probably involved in the physiological regulation of the heart beat (By similarity).
Subcellular Localization:
[Corazonin]: Secreted; [Corazonin precursor-related peptide]: Secreted.
Sequence:
MVTNITLILTLMTLASVTAQTFQYSRGWTNGKRDGHKRDELRDEVLERILTPCQLDKLKYVLEGKPLNDRLFVPCDYIEEEVNQPKRYKGERNHELFDVFQ
The following text describes a protein:
Function:
The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MQPSYKDLHCACQSNSQTNQSSVYSMSDDIWEDDDEDEEQEEYDRGDNSNDYNKDGVGSRQQNKQTQSLAMNEIARRHRKQGYVDGLAKHQEENLQKGFDFAYSIGADLGIKVGRLLARACIADGANNDLKDKSGGSGNDLGSLKECMNALNISKVLDLKYFDDHLNLKDGKHGLIEEWQNKSN
The following text describes a protein:
Function:
Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development.
Subcellular Localization:
Chromosome.
Sequence:
MERSAIAALQPPALFSMPSYSRLTLCLDISDGTVYKVTSVDGPRSEGQMEIGSHDRLQEGVLSLALTNGVNPYHKDDEASLATEQHRAGSVPPGLRWVPGHGKVSDTQEPQPCWRNSGDTTPSEPNHHADIEDAQNLVAFSAIAGSLPPCSSSSCPPVQPNTAQLYEKFTREMGAGGAHSGGTPEGSCLAPEDLATLQTALSQAKHGHKPPNCDCEGPDCPDYLEWLEKKIKLAARENQGFHKRAEGAPHLQQPHLQHQPPPNRKVNGDHLMPALCSQQQGVTQGPHPDQVPCSKPSIPCSPQVLSIAKEKNISLQTAIAIDALTQLSGTSPQTLNCSGQNQQKNSFHNHQQSQNIPLDMILASPGSDSSSRSQSVPPGLQTKQQASPAFEQYRPQSQGHPPHASTLPSSTSSFPGQGKTPSLNTIAQQWQQGVGRGPEQRNPWMFMKSEPQSHLAVAPHNRSDPMSELKQLLHDTSGKLNNGSFKLPNSSQIGFNQNGGIQGQGNPVLARIKQEPDSNEHYHHAASMGQYGISNGQHQGQHFPGIPMSPGQTAISHSTQAALQQHLHYKRNLFPNHLSGFGAGQNLKKWWPQAEGEGIPHLPIKQELKEPKKKKSSQGSPLFKAMTGMLIGPPLPKPKQIIIKKTKQKASMPTFLPQNQISIQKPPLHLMDRAPVAANLQACSNPSMPFQNLPSQAVPAGLPAPGQSQVSISNTPMTPYSTVTVSTESTPAVVGPQSPPVASAVHGSSAEMGSHALSKTSTTKPLTSTSPSSTSQLQKLINIDPKYEELIRQFEAEFGDTAPDTSASQPKENAPSPETGNQTPTSSQDPSLILSNTPQSVSNCHTNSISGSKDQTMEVNPSESWTQSEATVSQASTENLLVKQNQELVDDSQNKETVLGKQQSRELEETFSMPCSPLPKRIKFETSGDVAVLSTTCYPEESTPTKDGLPCSPSLKGFLESPLRYLDTPTKSLLDTPSKDPQLDFPTCTCVEQILEKDEGPYYNHLGSGPTVASIRTLMEARFGEKGDAVRIEKVVYTGKEGKSSHGCPIAKWVIRRGSEKEKVLCLVRHRAGHHCENAVIIILILAWEGVPKALADKLYREVTDTLTKYGNPTSRRCGLNDDRTCACQGKDPETCGASFSFGCSWSMYFNGCKYARSKMPRKFRLQGDHPEEEEKLRDNFQNLATEVAPLYKRLAPQAYSNQCLSEDKASDCRLGLKEGRPFSGITACMDFCAHAHKDQHNLHNGCTVVCTLTKEDNRKVGGIPEDEQLHVLPLYTVSHTDEFGSAEAQRIKMQTGAIQALQTFRREVRKLPEPAKSCRQRRLEAKKAASEKKKNKIMQQGAETPEKAVFKAEVCVPSSPQPLGSKVIKQEMKPNIKMEPLNGSIDGYPVQAADPFNNIYQHPAYYARGALSPASQPSAADSLNNFPPNRSMVPYNYYNYATNGLFPRKLRTYEGRNGPLPKTGGKPVEVDKKPDIQSLQVRMAQSSSHPEQQNQLNHTVYSQPADYNQSRPSSNSSEPSIRGSPLIKQEPMDVPVYEGALPNQAGANTSRTTPQPAAWPGYKPNIIPTTWDDHLKRKQSSEGSSMNLDKQQFHQHSQQQQSSPFPQQWTSFPGSNLPIASSSPSLQVTPSPPPSPHLGTVIQASLQGSTRHVSPHPGTPLQPGTSHSRSLTPQPGLQGPGLPRHLASPASSPQPNAWAMGPAPCSPGLKHSNPAGAYPDKMWSKTGENRCSTPLGLQEKAWKSCGGSLAGSTPSPAPEGRLFPDALQQSGQAYCDPGRVESDTESIQHREDDEEEVWSDSEHNFLDPSIGGVGVAPAHGSVLIECARRELHATTPIKKPDRSHPTRISLVFYQHKNLNQPMHGLALWEAKMKLLAERALQRQQEAALLGLPQEDIKTLGKKRKWGAMATGASPGPGQSKDRKEGPVTRLAPTFCSTSVVTVSPFAFTQLTGPYSHFV
The following text describes a protein:
Function:
Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation (By similarity). Inhibits the fungal growth of Alternaria brassicicola, Sclerotinia sclerotiorum, Fusarium graminearum, yeast (Saccharomyces) and Botrytis cinerea, thus being an antimicrobial peptide (AMP). Prevents global growth and development.
Subcellular Localization:
Cell membrane. Secreted, extracellular space, apoplast. Endoplasmic reticulum. Golgi apparatus. Note=Observed in a reticular pattern and a perinuclear ring. The precursor of STMP9 accumulates at the plasma membrane and is proteolytically cleaved to release the STMP9 in the apoplasm.
Sequence:
MAMKNTSHVLLLSLLLCLMFVIGLVEASIPDDDMGPAIYTPPSGSCGAPISKYDFQVLAKRPPPCRRPRLENTEDVTHTTRP
The following text describes a protein:
Function:
Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MSAVDTTESAAAEVNAAKFGHDTASNMSIHSIANTPDMSATNCNESCTSSTPSDNNPNHDSAAHVTTWSRLSGGLSLLMTRALHSIQSLDMASELSRFTKYHRPYLSSAASSGIPTLDPNSPIVFLAQTYSSLAHPHFLDDFHSRLWMTYRKGFAAIKPTGYTCDSGWGCMLRSGQMLVANALLFHELGRDWRLGDSNDRDTWLTYCSILTKFLDVNTSPYSIQRIATLGIRFDKQIGEWFGPSTISQVLKVLVNDDQRISLKVHVSNDGVVYKNEINTILSATRDDGKTPAVLIMIPLRLGVETMNPVYYPGVKHCFAMSHCVGIAGGRPNSSLFFLGVDGDHLIYLDPHHLRPSVDSRDITSYKMEDLLSYHCEKVRLLPIASMDPSLVIGFYCHSLKDFDVLCAKMTELATGSAPLFSIEEMTPDFDPDVDIISEYDF
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Subcellular Localization:
Cytoplasm. Mitochondrion intermembrane space.
Domain:
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation; The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters; The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Sequence:
MADLQGKAVLTIAVPEAKADQIEAEILRLRAATTEAGSVQLEQFDRLEQVFLAPSSYDVIFSGHIALPAKSHADSALAKLAAALKPGGRLALRESLNSRNETALRSALTMGGFVNVQVSTSEHALEAHADKPVYEVGAAAPLKLSFAKKKQSGAAAPAAQVAEVWTIATDDFDDDDLLENDGDELLDAEDLALATTAPEGDDCEVGAGGKRRACKNCTCGRADAEAEQAAKPTLTGPLPASSCGNCYLGDAFRCASCPYLGMPAFKPGEKVTLSDRQLKADA
The following text describes a protein:
Function:
Confers resistance to heavy metal ions (e.g. aluminium) by chelating them at the plasma membrane of root cells, thus stopping their entry and reducing their accumulation (By similarity). Binds to and confers tolerance to aluminium (Al) (By similarity).
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MYNPPAAQEMSYSDHVKKRHEDKGCLYACLFTLCCCFCCYETCECCLECLCCC
The following text describes a protein:
Function:
Required for activation of the spg1 GTPase signaling cascade which leads to the initiation of septation and the subsequent termination of mitosis. May act as a scaffold at the spindle pole body to which other components of the spg1 signaling cascade attach.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
Sequence:
MDEAFGDSLSTDYRWLGHSHFDSHPSAGDSIYFDSLDEDADPSRTARIDRIAELLDGLNDEQISELVNGVNSTTIKENTKKEISNPNDSTRLPLEQIPGSNNLFLDPRHQLGDNSQNAQRHHEPSFNSEKASYTSTPYKNVAPKVIDSPSARHMHSNSPSFPPSQSHTSSYDQSPKGQLRDNISVPNQQDGLDPEVFNQQSKETKKSLQVPPSRNVPPPVTRPNQYNPEPNFSLSSGYPQQHFSQPELQNRNVHLETVPESYPVPPSGYPLTSSTCVSSISQPIQSTDCQKAQENLSNNKQMSSNDQDIDPFKQAITDLPPSFVNIVLEMNATIQSLSNQCQQRDKQIENITKQLLMNQQDYCPTTMSTTVSTPLCPPKRFPKSTKDFKEQKPDTKQVRSATISNDFNLKGNGRYNEKSQIAVPSEIRVQLSTLDAILLQFEHLRKELTQARKEIQILRHTSQNGDQESNESSKNAITTKTTDKGNNKENTMLNDGSTAPAKNDIRNVINTNNLDAKLSDESELMIEKNKSYSTPASSTIPTFHTSQPLTSLNMPDSRFNLAKEKQLYYRLGLQHIDQQCSVETANMLKTVLVQLNIPFAIFPSTIGQVRRQLQQGRRLYQWARNIHYLIYEENMRDGLVSKQCLADMLKKIRELKKRSL
The following text describes a protein:
Function:
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Miscellaneous:
MISCELLANEOUS: The a and c carboxylates of hydrogenobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CobB catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.
Domain:
Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and hydrogenobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Sequence:
MRVSAVAVAAPASGSGKTTIATGLIGALRQAGHTVAPFKVGPDFIDPGYHALAAGRPGRNLDPVLVGERLIGPLYAHGVAGADIAVIEGVLGLFDGRIGPAGGAPAAGSTAHVAALLGAPVILVVDARGQSHSVAALLHGFSTFDTATRIAGVILNRVGSARHEQVLRQACDQAGVAVLGAIPRTAELELPTRYLGLVTAVEYGRRARLAVQAMTAVVARHVDLAAVIACAGSQAAHPPWDPVIAVGNTARQPATVAIAAGRAFTFGYAEHAEMLRAAGAEVVEFDPLSETLPEGTDAVVLPGGFPEQFTAELSANDTVRRQINELAAAGAPVHAECAGLLYLVSELDGHPMCGVVAGSARFTQHLKLGYRDAVAVVDSALYSVGERVVGHEFHRTAVTFADSYQPAWVYQGQDVDDVRDGAVHSGVHASYLHTHPAATPGAVARFVAHAACNTPRA
The following text describes a protein:
Function:
Modulates RecA activity.
Subcellular Localization:
Cytoplasm.
Sequence:
MSAQLTDEEALNRVASYCSAAEHCRAEVNEKLQRWGIAYETIARILERLETEKYIDDERYCRAFVNDKFRFAKWGKMKIAQGLYMKKIPSDVAWRHLNEIDEEEYLSILRDLLASKRKSIHAKDDYELNGKLMRFAVSRGFELKDIRRCIEIPEEEEQFS
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MLREFSKWGVEASPGKAWERKRSLLRGAVGRYRGATGGDLFWAPFPSWGTMEFPEHSQQLLQSLREQRSQGFLCDCTVMVGSTQFLAHRAVLASCSPFFQLFYKERELDKRDLVCIHNEIVTAPAFGLLLDFMYAGQLTLRGDTPVEDVLAAASYLHMNDIVKVCKRRLQARALAEADSTKKEEETNSQLPSLEFLSSTSRGTQPSLASAETSGHWGKGEWKGSAAPSPTVRPPDEPPMSSGADTTQPGMEVDAPHLRAPHPPVADVSLASPSSSTETIPTNYFSSGISAVSLEPLPSLDVGPESLRVVEPKDPGGPLQGFYPPASAPTSAPAPVSAPVPSQAPAPAEAELVQVKVEAIVISDEETDVSDEQPQGPERAFPSGGAVYGAQPSQPEAFEDPGAAGLEEVGPSDHFLPTDPHLPYHLLPGAGQYHRGLVTSPLPAPASLHEPLYLSSEYEAAPGSFGVFTEDVPTCKTCGKTFSCSYTLRRHATVHTRERPYECRYCLRSYTQSGDLYRHIRKAHNEDLAKRSKPDPEVGPLLGVQPLPGSPTADRQSSSGGGPPKDFVLAPKTNI
The following text describes a protein:
Function:
Putative gamma-glutamylcyclotransferase.
Sequence:
MAEKLRMAARVFVYGTLKRGEPNHHWLTKKENGQARFLGRGKTETKFPLVVGTRYNIPFLLARPGEGNHIEGEVYEVDETMLSKLDILEDYPDYYDREQQTILMEQNETIQCWLYLIRNFPDKMLAKELLISYHNTPERPYNEKSVRTVSARDDLSY
The following text describes a protein:
Function:
Catalyzes cyanide-resistant oxygen consumption. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
VQQTHIEPKDLSDRVALTAIRIIRKGFDFFSGYMFGPINETKFLRRAIFLETVAGIPGMVAGSLRHLRSLRGMQRDNGWIHTLLEEAENERMHLLTFTKVKQPGIIFRSMVLAAQGIMWNAYFVAYLVSPRTCHRFIGYLEEEAVKTYSHAIEALDKGMMPTWNNKEAPEIAKTYWGLADDALMRDVLLAVRADEANHRDVNHTLSTLKTDATNPYVNLK
The following text describes a protein:
Function:
Required for the inhibition of NifA activity in response to oxygen and low level of fixed nitrogen.
Sequence:
MTPANPTLSNEPQAPHAESDELLPEIFRQTVEHAPIAISITDLKANILYANRAFRTITGYGSEEVLGKNESILSNGTTPRLVYQALWGRLAQKKPWSGVLVNRRKDKTLYLAELTVAPVLNEAGETIYYLGMHRDTSELHELEQRVNNQRLMIEAVVNAAPAAMVVLDRQHRVMLSNPSFCRLARDLVEDGSSESLVALLRENLAAPFETLENQGSAFSGKEISFDLGGRSPRWLSCHGRAIHIENEQAHVFFAPTEERYLLLTINDISELRQKQQDSRLNALKALMAEEELLEGMRETFNAAIHRLQGPVNLISAAMRMLERRLGDKAGNDPVLSAMREASTAGMEALENLSGSIPVRMAESKMPVNLNQLIREVITLCTDQLLAQGIVVDWQPALRLPWVMGGESSQRSMIKHLVDNAIESMSQNQVSRRELFISTRVENHLVRMEITDSGPGIPPDLVLKVFEPFFSTKPPHRVGRGMGLPVVQEIVAKHAGMVHVDTDYREGCRIVVELPFSAST
The following text describes a protein:
Function:
Plays a role in the early steps of cytochrome c oxidase subunit II (MT-CO2/COX2) maturation and is required for the stabilization of COX20 and the newly synthesized MT-CO2/COX2 protein.
Sequence:
MAARFLWKVAAMVERHRTGFLTISCAGLFGANLTFHILPEDTFRPLYQAWAKGKPVELPENVQHLFHEVLIEGRIQSGNRYRAFVVFSFHPVSAGLPWLPAGCLVGIPANFCDTTDDEHKIANHVVVIEGKEVDWESPEGLILKGTLTFSPEAQKFAIAREAMYLQNNGPLTRAVVAPVCLAGTYVCGVAIKQLLGLYSGPVLLRGLYNIAVLAVGLLGYCLSYDAVSQAVEYKADRSAASISTDFARGGVEFYNKILSQNKSFRALMGKSGEKIYAPNGNLSPTYWIRLKHAPYTSRRDSIINILNLPQA
The following text describes a protein:
Function:
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA (By similarity).
Subcellular Localization:
Nucleus, nucleolus. Nucleus, nucleoplasm. Mitochondrion. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.
Sequence:
MGITKLAHLIHFDAPASMRSKEIGDYSGKIIALDTSIVVNQFRSALPGHLKLSPLAGLFYRTLAFLEHDIKPVFVLDGKPPHQKRAVLEKRAQSTGWSSSQSPNTGSAFNQECLRLLHLMGVPCIKAPGEAEALCAHLAKIGTVNAVASEDMDTLAFGGTVLLRQLNAKRDSEITEYSLPKLLEALQLKYEEFVDLCILLGCDYCDKIGGLGPSRALKLIKEHHTIEGVMEHVNRKTHPIPLNWQYKDARKLFFETPKIDDPVLAWSEPDEEGLVQFLCKEKPLKEERVRGRMKKFREMLLKRRKQREVNMQMGQTRQSRLEDFFPATRKRRAESAAVKESSGRKQFKIK
The following text describes a protein:
Function:
First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Subcellular Localization:
Nucleus.
Sequence:
MDIGKMINDDNGSDSRRTSVKSLLNSPPTGLPSSDDRPDSKASSTSDLAQQLTNEMESGEDDDDEDAAAAVNHKPRRYSRPPIWATKWQGTGRHAERDHRPPPHRQDRRDPRMERQSGGSRALPASSTTTITGCPPSISGIKPFESVTRTVTSWLHAHLSTMSPEQLQTVELEAKIGTIQHKKAGADRARLDLPIVTEAVVNQQYVQAQCSFSSQLPESLLEEAKRILDAADPKFIKSTEHTIHRDEIYEGQQDKGNLRITRDDVTGRQVAKIRKKAIAHIMIHCPTDPFDIRLSLATESPTDDVPQGVCRTRRKDRISYLYDGFRADLTKVSGSSMSSELEMEADSHKLIGYFTDRNDPHNMDKVEELLQILLDSMRYVNRRLKA