entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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F4K4E3
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LSM4_ARATH
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Sm-like protein LSM4 (AtLSM4) (Protein EMBRYO DEFECTIVE 1644) (U6 snRNA-associated Sm-like protein LSM4)
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MLPLSLLKTAQGHPMLVELKNGETYNGHLVNCDTWMNIHLREVICTSKDGDRFWRMPECYIRGNTIKYLRVPDEVIDKVQEEKTRTDRKPPGVGRGRGRGVDDGGARGRGRGTSMGKMGGNRGAGRGRG
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Component of LSM protein complexes, which are involved in RNA processing. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates developmental gene expression by the decapping of specific development-related transcripts. Component of the nuclear LSM2-LSM8 complex which is involved splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6 small nuclear RNAs (snRNAs) and is essential for accurate splicing of selected development-related mRNAs through the stabilization of the spliceosomal U6 snRNA. Plays a critical role in the regulation of development-related gene expression.
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F4K5J1
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MYO17_ARATH
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Myosin-17 (Myosin XI K) (AtXIK)
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MVGPVNIIVGSHVWIEDPGAAWIDGEVVKINGEEVHAHTTNGKTVVANIANVFPKDTEAPPGGVDDMTKLSYLHEPGVLNNLAMRYELNEIYTYTGNILIAVNPFQRLPHLYDTHMMEQYKGAGFGELSPHVFAIAEVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVELQFDNCGRISGAAVRTYLLERSRVCQISDPERNYHCFYLLCAAPPEEREKFKLGDPKLFHYLNQSKCYKLDGVDDTEEYLATRRAMDIVGISEEEQDAIFRVVAAILHLGNVNFAKGKEIDSSVLKDEKSRYHLDVCAELLRCDAKKMEDALIKRVMVTPEEVITRTLDPDSATGSRDALAKTIYSRLFDWLVDKINNSIGQDPNSKTIIGVLDIYGFESFKINSFEQFCINFTNEKLQQHFNQHVFKMEQEDYTKEEINWSYIEFVDNKDVLELIEKKPGGVIALLDEACMFPKSTHETFAQKLYQTFKNYKRFTKPKLSRTSFAISHYAGEVTYQADLFLDKNKDYVVAEHQDLLIASSDTFVAGLFPRLPEETSSKTKFSSIGSRFKLQLQSLMETLSSTEPHYIRCVKPNNVLKPAIFENVNVIQQLRCGGVLEAIRISCAGYPTKRTFYEFLNRFGVLAPEVLEGNYDDKVACKMLLDKIGLKGYELGKTKVFLRAGQMAELDARRAEVLGNAARRIQRQSRTFIACKEFRALRGAAIVLQSNCRGKLACNLYEEMRRQAAAVKIQKIFRRHIARESYLRIRHSTITVQTALRGMVARNEFRFRKQMKAATIIQARLRSHLTHSYYKQLQKAALSTQCGWRSRVARKELRTLKMAARDTGALREAKDKLEKRVEELTWRLQLEKRQRTELEEAKTQEYAKQQEALETMRLQVEEANAAVIREREAARKAIEEAPPVIKETPVLVEDTEKINSLTSEVEALKASLQAERQAAENLRKAFSEAEARNSELATELENATRKADQLHESVQRLEEKLSNSESEIQVLRQQALAISPTSRTMATRSKTMLLPRTPENGNYLNGGTKTTPDMTLAVREPESEEKPQKHLNEKQQENQDLLVKCISQNLGYNGDKPVAACVIYKCLLHWRSFEVERTSVFDRIIQTIATAIEVPDNNEVLAYWLSNSATLLLLLQRTLKATGAASLTPQRRRTTSASLFGRMSQGLRGSPQSAGLSFLNRQGLTKLDDLRQVEAKYPALLFKQQLTAFLEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGRAQANAVAQQALIAHWQSIRKSLNSYLNLMKANNAPPFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELEQWCIEATDEYAGSAWDELRHIRQAVGFLVIHQKPKKTLDEITRELCPVLSIQQLYRISTMYWDDKYGTHSVSSDVIANMRVMMTEDSNNAVSSSFLLDDDSSIPFTVEDISKSMQQVDVNDIEPPQLIRENSGFGFLLTRKEGSTS
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Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in the tip growth of root hair cells and in the elongation of trichome stalk and branches. Plays a major role in trafficking of Golgi stacks, mitochondria and peroxisomes during root hair development. Acts as the primary contributor to ER streaming with a major role in the movement of Golgi bodies. Required for development of pavement cells, trichomes, and stigmatic papillae.
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F4K5T2
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CGL_ARATH
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Bifunctional cystathionine gamma-lyase/cysteine synthase (EC 2.5.1.47) (EC 4.4.1.1) (Beta-substituted Ala synthase 4;3) (ARAth-Bsas4;3) (L-cysteine desulfhydrase 1) (DES1) (O-acetylserine (thiol)-lyase) (OASTL) (Protein CS-LIKE)
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MEDRVLIKNDVTELIGNTPMVYLNKIVDGCVARIAAKLEMMEPCSSIKDRIAYSMIKDAEDKGLITPGKSTLIEATGGNTGIGLASIGASRGYKVILLMPSTMSLERRIILRALGAEVHLTDISIGIKGQLEKAKEILSKTPGGYIPHQFINPENPEIHYRTTGPEIWRDSAGKVDILVAGVGTGGTVTGTGKFLKEKNKDIKVCVVEPSESAVLSGGKPGPHLIQGIGSGEIPANLDLSIVDEIIQVTGEEAIETTKLLAIKEGLLVGISSGASAAAALKVAKRPENVGKLIVVIFPSGGERYLSTELFESVRYEAENLPVE
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Involved in maintaining Cys homeostasis through the desulfuration of L-cysteine. Modulates the generation of the signaling molecule sulfide in plant cytosol. Probably unable to interact with SAT and to form the decameric Cys synthase complex (CSC) and is therefore not an enzymatically true OASTL protein.
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F4K5X6
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RVE2_ARATH
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Protein REVEILLE 2 (MYB family transcription factor Circadian 1)
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MAMQERCESLCSDELISSSDAFYLKTRKPYTITKQREKWTEAEHEKFVEALKLYGRAWRRIEEHVGTKTAVQIRSHAQKFFTKVARDFGVSSESIEIPPPRPKRKPMHPYPRKLVIPDAKEMVYAELTGSKLIQDEDNRSPTSVLSAHGSDGLGSIGSNSPNSSSAELSSHTEESLSLEAETKQSLKLFGKTFVVGDYNSSMSCDDSEDGKKKLYSETQSLQCSSSTSENAETEVVVSEFKRSERSAFSQLKSSVTEMNNMRGFMPYKKRVKVEENIDNVKLSYPLW
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Positive regulator for cold-responsive gene expression and cold tolerance. Part of a regulatory feedback loop that controls a subset of the circadian outputs and modulates the central oscillator. Negatively self-regulates its own expression.
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F4K6B8
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RGI4_ARATH
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Leucine-rich repeat receptor-like serine/threonine-protein kinase RGI4 (EC 2.7.11.1) (Protein RECEPTOR OF RGF1 2) (Protein RGF1 INSENSITIVE 4) (Protein STERILITY-REGULATING KINASE MEMBER 2)
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MPRNPRFCFFLFLLFHSSLFFSIPCFSIDEQGLALLSWKSQLNISGDALSSWKASESNPCQWVGIKCNERGQVSEIQLQVMDFQGPLPATNLRQIKSLTLLSLTSVNLTGSIPKELGDLSELEVLDLADNSLSGEIPVDIFKLKKLKILSLNTNNLEGVIPSELGNLVNLIELTLFDNKLAGEIPRTIGELKNLEIFRAGGNKNLRGELPWEIGNCESLVTLGLAETSLSGRLPASIGNLKKVQTIALYTSLLSGPIPDEIGNCTELQNLYLYQNSISGSIPVSMGRLKKLQSLLLWQNNLVGKIPTELGTCPELFLVDLSENLLTGNIPRSFGNLPNLQELQLSVNQLSGTIPEELANCTKLTHLEIDNNQISGEIPPLIGKLTSLTMFFAWQNQLTGIIPESLSQCQELQAIDLSYNNLSGSIPNGIFEIRNLTKLLLLSNYLSGFIPPDIGNCTNLYRLRLNGNRLAGNIPAEIGNLKNLNFIDISENRLIGNIPPEISGCTSLEFVDLHSNGLTGGLPGTLPKSLQFIDLSDNSLTGSLPTGIGSLTELTKLNLAKNRFSGEIPREISSCRSLQLLNLGDNGFTGEIPNELGRIPSLAISLNLSCNHFTGEIPSRFSSLTNLGTLDVSHNKLAGNLNVLADLQNLVSLNISFNEFSGELPNTLFFRKLPLSVLESNKGLFISTRPENGIQTRHRSAVKVTMSILVAASVVLVLMAVYTLVKAQRITGKQEELDSWEVTLYQKLDFSIDDIVKNLTSANVIGTGSSGVVYRVTIPSGETLAVKKMWSKEENRAFNSEINTLGSIRHRNIIRLLGWCSNRNLKLLFYDYLPNGSLSSLLHGAGKGSGGADWEARYDVVLGVAHALAYLHHDCLPPILHGDVKAMNVLLGSRFESYLADFGLAKIVSGEGVTDGDSSKLSNRPPLAGSYGYMAPEHASMQHITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAHLVQWVRDHLAGKKDPREILDPRLRGRADPIMHEMLQTLAVSFLCVSNKASDRPMMKDIVAMLKEIRQFDMDRSESDMIKGGKCEKWQPQPLPPEKIVSTPRGSSNCSFAYSDESV
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Receptor with a serine/threonine-protein kinase activity (By similarity). Together with SKM1, LRR-rich receptor-like kinase (LRR-RLK) required for male fertility by the perception of CLE43 and CLE45 peptides and the transduction of their promoting action in pollen tubes, especially under relatively high temperature (at 30 degrees Celsius), thus conferring tolerance against high temperature probably through the maintenance of mitochondrial activity. Seems to not be involved in the perception of CLE45 peptide in roots. Together with RGI1, RGI2, RGI3, RGI4 and RGI5, acts as receptor of RGF1, a peptide hormone that maintains the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHORA (PLT). Links RGF1 signal with its downstream components.
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F4K933
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ET2_ARATH
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Protein EFFECTOR OF TRANSCRIPTION 2 (AtET2)
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MEFGDGVSFAVVPTVFKREDYKRTKHDTVFSKWQVLIGSNDWEDFKNGKDGVGRYRVQNLPRKSCPGLYELGVAVIGQEQCRKLEPDIVLASYLGQAESVRSRLQRYGRSGAHLRNVNNLNDCETIESPVKAVTGGLFEDIFSKGGSILYRWAPMGSKREAEATEGMLLSTFDYAWNKGSNGERRQLDLLKKLGDREFMSKRKSGISRMLFPFLRNQVGIRIKGEKHVLKEERKLTCDVDEEKSNNFLTSILKLTRSRPQPVSDRFDEVDGSCSDIVCGVLLEDGGCCIRSPVKGRKRCIEHKGQRVCRVSPEKQTPPKSEIFTGQDHHNHKDSDVVCGVILPDMEPCNKRPVPGRKRCEDHKGMRINAFLFLLNQTDREKTVKDEKPDPESHTESIEEEALTRFCEATTKNGLPCTRSSPKGSKRCWQHKEKTSSDTSPVYFQPEAAKNVACGVKLGNGLICERSPVKGRKRCEEHKGMRIT
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Transcriptional regulator involved in the regulation of cell differentiation in meristems. Probably regulates the expression of various KNAT genes involved in the maintenance of the cells in an undifferentiated, merismastic state. Plays a role in the regulation of gibberellin 20 oxidase and the gibberellin-regulated protein GASA4. Localizes in the nucleus during the cellular differentiation state and may act via a single strand cutting domain. Transcriptional regulator required for the induction of dormancy during late seed development. Interacts genetically with FUS3 and may be component of the same regulatory pathway during embryogenesis. Binds both linear and supercoiled DNA without sequence preference.
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F4KAB8
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MCM6_ARATH
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DNA replication licensing factor MCM6 (EC 3.6.4.12) (Minichromosome maintenance protein 6) (AtMCM6)
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MEAFGGFVMDEQAIQVENVFLEFLKSFRLDANKPELYYEAEIEAIRGGESTMMYIDFSHVMGFNDALQKAIADEYLRFEPYLRNACKRFVIEMNPSFISDDTPNKDINVSFYNLPFTKRLRELTTAEIGKLVSVTGVVTRTSEVRPELLYGTFKCLDCGSVIKNVEQQFKYTQPTICVSPTCLNRARWALLRQESKFADWQRVRMQETSKEIPAGSLPRSLDVILRHEIVEQARAGDTVIFTGTVVVIPDISALAAPGERAECRRDSSQQKSSTAGHEGVQGLKALGVRDLSYRLAFIANSVQIADGSRNTDMRNRQNDSNEDDQQQFTAEELDEIQQMRNTPDYFNKLVGSMAPTVFGHQDIKRAVLLMLLGGVHKTTHEGINLRGDINVCIVGDPSCAKSQFLKYTAGIVPRSVYTSGKSSSAAGLTATVAKEPETGEFCIEAGALMLADNGICCIDEFDKMDIKDQVAIHEAMEQQTISITKAGIQATLNARTSILAAANPVGGRYDKSKPLKYNVNLPPAILSRFDLVYVMIDDPDEVTDYHIAHHIVRVHQKHEAALSPEFTTVQLKRYIAYAKTLKPKLSPEARKLLVESYVALRRGDTTPGTRVAYRMTVRQLEALIRLSEAIARSHLEILVKPSHVLLAVRLLKTSVISVESGDIDLSEYQDANGDNMDDTDDIENPVDGEEDQQNGAAEPASATADNGAAAQKLVISEEEYDRITQALVIRLRQHEETVNKDSSELPGIRQKELIRWFIDQQNEKKKYSSQEQVKLDIKKLRAIIESLVCKEGHLIVLANEQEEAAEAEETKKKSSQRDERILAVAPNYVIE
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Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells.
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F4KAF2
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MORC4_ARATH
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Protein MICRORCHIDIA 4 (AtMORC4) (EC 3.6.-.-) (Protein CRT1-homolog 4) (CRT1-h4)
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MEPIVKQENPVTTSTLSTWKPAARNKTIPPPESVIELSSSNEGSELGENLDEIAEIQSVDRTGGDDVSGTKRARSDSIASPAKRLAVMIPDDDEEFLLSTTSGQAILALPATPCNVVAAPSSWGSCKQFWKAGDYEGTSGGDWEVSAGGFDHVRVHPKFLHSNATSHKWSLGAFAELLDNALDEVRSGATFVNVDMIQNRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSAKSKLADTIGQYGNGFKTSTMRLGADVIVFSRCLGKDGKSSTQSIGLLSYTFLKSTGKEDIVVPMLDYERRDSEWCPITRSSVSDWEKNVETVVQWSPYATEEELLCQFNLMKKHGTRIIIYNLWEDDEGMLELDFDTDPHDIQLRGVNRDDKNIVMASQFPNSRHYLTYKHSLRSYASILYLKISHEFRIILRGKDVEHHNIVNDMMQTEKITYRPKEAADVSQLSAVVTIGFVKDAKHHVDVQGFNVYHKNRLIKPFWRIWNAAGSDGRGVIGVLEANFVEPAHDKQGFERTTVLSRLEARLLHMQKDYWRSKCHKIGYAKRQGRKSAKDTEKDTEDRESSPEFDPKGSASSRKRTVPSSFKTPTAAPRFNTPTAASEKFNPRSNVNGGGKGSVKVSKDIGYKSSEKGGKLGNSFSKSNKRAKPQGARAVEVTNSDDDYDCDSSPERNVTELPGKSSELPKPQSGPRTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENLRIKLEEASNTIQKLIDGKARGR
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Exhibits ATPase activity. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing. Together with MORC7, acts to suppress a wide set of non-methylated protein-coding genes, especially involved in pathogen response. Positive regulator of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa).
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F4KAK5
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PSD2_ARATH
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Phosphatidylserine decarboxylase proenzyme 2 (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 2 beta chain; Phosphatidylserine decarboxylase 2 alpha chain]
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MGNGNSREAKESRRSRLRHKLQKFRIHRRHLRSSRNSAGMVIQRTVSAEDFSGIALLTLIGAEMKFKDKWLACVSFGEQTFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPESTCKSFNLLDPTSSNVVGSIFLSCAIEDPVETERRFAKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALLALQQEQEPIINNCPVCGEALQVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDRQASYGWMFKLSEWTHLSTYDVGLNTGSSASYIVVIDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMSSVESAQKIPRFLEFFKDQINMAEVKYPLQHFKTFNEFFIRELKPGARPIACMNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVNPNAFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNSKYCNVFTENKRTVAIISTAEFGKVAFVAIGATMVGSINFVRKEGEHVKKGDELGYFSFGGSTVICVFEKDAIGIDNDLLVNSGRSLETLVSVGMQLGVSTRTFARSTLI
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Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Contributes only to a minor proportion of PtdEtn production. {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:17449644}.
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F4KB17
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KTN83_ARATH
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Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.3
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MNTKRAYKLQEFVAHSAAVNCLKIGRKSSRVLVTGGEDHKVNLWAIGKPNAILSLYGHSSGIDSVTFDASEGLVAAGAASGTIKLWDLEEAKVVRTLTGHRSNCVSVNFHPFGEFFASGSLDTNLKIWDIRKKGCIHTYKGHTRGVNVLRFTPDGRWIVSGGEDNVVKVWDLTAGKLLHEFKSHEGKIQSLDFHPHEFLLATGSADKTVKFWDLETFELIGSGGTETTGVRCLTFNPDGKSVLCGLQESLKIFSWEPIRCHDGVDVGWSNLSDMNVHEGKLLGCSYNQNCVGVWVVDLSRTEPMSGGATQSNSHPEKTSGSGRDQAGLNDNSSKVILGKLPGSQKVDPLLKETKSLGKLSVSQNSDPLPKDTKSTGRSSVSQSSDPLVKEPKPLGRFSATHSSDTVKESRTLSSTGSVSDSPHRVTLTSAPKSASGISTVVPNAAASKRNFGKANPKANPPVVNKEDYFPVIVPRTEPIIEQASESRAELDIIGRTMPYSLQSKAADSRRLSSSRNEPDLPTSSLLERSQSQPIEPITLQDGNTYPSDEGGSWDTAERTNKESKCRVFGRFNSRSLVRSPPRNHDENSDLISYNANRDSSPTESRKGGRLHSLVLNRERRGRFSNFEGPVSSSSGGNMTAPNSRPSNMLKQRGNHVPVDQGITSASEEDIVADIMGQHDQFVSSMHSRLAKLQVVRRYWERNDIKNSISSIEKMADNAVIADVLLIVNERPEILTLDTCTSLLPLLTALLGSNMDSHLSVCLDLLLKLVRMYGSQIYSSLSAPSSVGVDIEAEQRMERYSCCFVEFEKIKACLPSLARRGNLVAKTLHELNLTFQEVSS
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May participate in a complex which severs microtubules in an ATP-dependent manner (By similarity). Microtubule severing may promote rapid reorganization of cellular microtubule arrays (By similarity). Confers precision to microtubule (MT) severing by specific targeting of KTN1 to MT cleavage sites such as crossover or branching nucleation sites. Together with other KTN80s, regulates cell elongation by modulating MT organization. {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28978669}.
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F4KBF5
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KITHB_ARATH
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Thymidine kinase b (AtTK1b) (EC 2.7.1.21)
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MFGVSMRTLISPSLAPFSLHLHKPSLFSTALRFSFSINNITPTNSPPSTISTRKLQTKATRVTSSSSSQPLSSSSPGEIHVVVGPMFSGKTTTLLRRILAERETGKRIAIIKSNKDTRYCTESIVTHDGEKYPCWSLPDLSSFKERFGFDDYENRLDVIGIDEAQFFGDLYEFCREAADKEGKTVIVAGLDGDFMRRRFGSVLDLIPIADTVTKLTSRCEVCGKRALFTMRKTEEKETELIGGAEVYMPVCRSHYVCGQNVLETARAVLDSSNNHSVVASSL
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Part of the salvage pathway for purine and pyrimidine deoxyribonucleotide synthesis. Phosphorylates preferentially purines over pyrimidines.
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F4KBP5
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CHR4_ARATH
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Protein CHROMATIN REMODELING 4 (AtCHR4) (EC 3.6.4.-) (Protein PICKLE RELATED 1)
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MKDSGSEMIKRDWVMKQKRRKLPSILDILDQKVDSSMAFDSPEYTSSSKPSKQRLKTDSTPERNSSKRKGNDGNYFECVICDLGGDLLCCDSCPRTYHTACLNPPLKRIPNGKWICPKCSPNSEALKPVNRLDAIAKRARTKTKKRNSKAGPKCERASQIYCSSIISGEQSSEKGKSISAEESKSTGKEVYSSPMDGCSTAELGHASADDRPDSSSHGEDDLGKPVIPTADLPSDAGLTLLSCEDLSESKLSDTEKTHEAPVEKLEHASSEIVENKTVAEMETGKGKRKKRKRELNDGESLERCKTDKKRAKKSLSKVGSSSQTTKSPESSKKKKKKNRVTLKSLSKPQSKTETPEKVKKLPKEERRAVRATNKSSSCLEDTNSLPVGNLQVHRVLGCRIQGLTKTSLCSALSDDLCSDNLQATDQRDSLVQDTNAELVVAEDRIDSSSETGKSSRDSRLRDKDMDDSALGTEGMVEVKEEMLSEDISNATLSRHVDDEDMKVSETHVSVERELLEEAHQETGEKSTVADEEIEEPVAAKTSDLIGETVSYEFLVKWVDKSNIHNTWISEAELKGLAKRKLENYKAKYGTAVINICEDKWKQPQRIVALRVSKEGNQEAYVKWTGLAYDECTWESLEEPILKHSSHLIDLFHQYEQKTLERNSKGNPTRERGEVVTLTEQPQELRGGALFAHQLEALNWLRRCWHKSKNVILADEMGLGKTVSASAFLSSLYFEFGVARPCLVLVPLSTMPNWLSEFSLWAPLLNVVEYHGSAKGRAIIRDYEWHAKNSTGTTKKPTSYKFNVLLTTYEMVLADSSHLRGVPWEVLVVDEGHRLKNSESKLFSLLNTFSFQHRVLLTGTPLQNNIGEMYNLLNFLQPSSFPSLSSFEERFHDLTSAEKVEELKKLVAPHMLRRLKKDAMQNIPPKTERMVPVELTSIQAEYYRAMLTKNYQILRNIGKGVAQQSMLNIVMQLRKVCNHPYLIPGTEPESGSLEFLHDMRIKASAKLTLLHSMLKVLHKEGHRVLIFSQMTKLLDILEDYLNIEFGPKTFERVDGSVAVADRQAAIARFNQDKNRFVFLLSTRACGLGINLATADTVIIYDSDFNPHADIQAMNRAHRIGQSKRLLVYRLVVRASVEERILQLAKKKLMLDQLFVNKSGSQKEFEDILRWGTEELFNDSAGENKKDTAESNGNLDVIMDLESKSRKKGGGLGDVYQDKCTEGNGKIVWDDIAIMKLLDRSNLQSASTDAADTELDNDMLGSVKPVEWNEETAEEQVGAESPALVTDDTGEPSSERKDDDVVNFTEENEWDRLLRMRWEKYQSEEEAALGRGKRLRKAVSYREAYAPHTSGPVNESGGEDEKEPEPELKKEYTPAGRALKEKFTKLRERQKNLIARRNSVEESLPSGNVDQVTEVANQDEESPTSMDLDDSKASQQCDAQKRKASSSDPKPDLLSQHHHGAECLPSLPPNNLPVLGLCAPNFTQSESSRRNYSRPGSRQNRPITGPHFPFNLPQTSNLVEREANDQEPPMGKLKPQNIKEEPFQQPLSNMDGWLPHRQFPPSGDFERPRSSGAAFADFQEKFPLLNLPFDDKLLPRFPFQPRTMGTSHQDIMANLSMRKRFEGTGHSMQDLFGGTPMPFLPNMKIPPMDPPVFNQQEKDLPPLGLDQFPSALSSIPENHRKVLENIMLRTGSGIGHVQKKKTRVDAWSEDELDSLWIGIRRHGYGNWETILRDPRLKFSKFKTPEYLAARWEEEQRKFLDSLSSLPSKSSRTDKSTKSSLFPGLPQGIMNRALHGKYATPPRFQSHLTDIKLGFGDLASPLPLFEPSDHLGFRSEHFPPMANLCTDNLPGEPSAGPSERAGTSTNIPNEKPFPLNSLGMGNLGSLGLDSLSSLNTLRAEEKRDAIKRGKLPLFLDMPLPQMLDSSNNVFLGRSANPSFLHPNRGLNPSNPMGRDIMGISSSENKLPHWLRNVVTVPTVKSPEPPTLPPTVSAIAQSVRVLYGEDSTTIPPFVIPEPPPPAPRDPRHSLRKKRKRKLHSSSQKTTDIGSSSHNAVESSSQGNPQTSATPPLPPPSLAGETSGSSQPKLPPHNLNSTEPLSSEAIIIPPPEEDSVIAAAPSEAPGPSLEGITGTTKSISLESQSSEPETINQDGDLDPETDEKVESERTPLHSDEKQEEQESENALNKQCEPIEAESQNTNAEEEAEAQEEDEESMKMVTGNSLSDD
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Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 (By similarity). Probable chromatin remodeling factor.
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F4KCC2
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PRT6_ARATH
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E3 ubiquitin-protein ligase PRT6 (EC 2.3.2.27) (Protein GREENING AFTER EXTENDED DARKNESS 1) (Protein PROTEOLYSIS 6) (RING-type E3 ubiquitin transferase PRT6)
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METNSSLFGLVSPSSHDLVIERLASVGVPKKYRSKRGLVEFVRANPAKISELVSALLPTDDDVKLGLKEARERPRKSAVSPTMKKRFRESMNMLQWLMFQDEPDVSLRNLAKLNLDQRGVCGSVWGQNDIAYRCRTCENDPTCAICVPCFQNGDHNSHDYSIIYTGGGCCDCGDETAWKPDGFCSNHKGSEQIRPLSENLANSVGPILDALFTCWNNKLLSAESSGQKGARSNDTLVILQKMSNELTFIVVEMLLEFSMSSESLLSFVSRRIISSSGLLSILLKAERFLDQDVMKKLHDLFLKLIGDPVFKCEFAKAFVSYYPVVISEVVKQGTDNAFKKYPLLSTFSVQILTVPTLTPFLVKEMNLLAMLLGCLSDIFVSCSGEDGLLQATKLERLCETSERVIGDLKFVMSHAIVSKYATHEHRELSRSWLTLLTFAQGMNPLKRETGIPIDEENDYMHLFFVLGHSIAVIHSLLVNGTYSAASDEEIENDRNAKEEFDKCDGDGERYAKVGRLSHEDSVCTAIVSSSSFDSSMASEVHKIDPFHALLPSSAIYLIRECLKVLETCLGNDEGISKFLCKLSSSSGRNIPESKMSWPRRDLLNVETGGSVSSNLASSSRDPSTGLSPLCGDIQTNLSLDNVCGPYGVVQTDVTADSKRVSCNSADLTKNASGLRILGLCDWPDIHYDVSSQAISVHLPLHRLLSLLIQKALRICYGESASYNGVSISHEIPHADFFSSVIGDFHPCGFSALVMEHVLQIRVFCAQVIAGMWKKNGDSALVSCEWYRSVRWSEQGLELDLFLLQCCAALAPADSYVDKLLSRFGLSSYLSLNPDITNEYEPVLVQEMLGLLIQILQERRFCGLSTAESLRREIIFKLATGDFTHSQLVKSLPRDLSKSDELQEVLDDVSVYCNPSGMNQGKYSLQSSCWKELDLYHPRWQSRDLQSAEERFSRYCGVSALTTQLPRWRMIYPPLKGLARIGTCKATFQIISSALYYALQSGTSVKSRAPDGVLITALQLLSLSLDICTQQRQSNSQDCCLENSIPILELAGLEIIGIAQGTEKESLLSLLVSLMKTRMGDGRHQFPEPGSCNISSWIGNLLKKFSAIDSVCMNLLQSLAPEVVGQSGFDKVMSGSTSDEKRKAKAKERQAAIMAKMKAEQSKFLSTLSSSMDDDDPRSEFETSDSVMEHDSEIAVREVCSLCHDPDSKDPVSFLIFLQKSKLLSFVDRGPPSWDQCPQSEKKISVDGAPDLLRMNASSDSLRISSPLMLQLSDDTISESANMIESIKARLIGNGQTEKRSSDGRGKDESNMESLEIAMYQTVRNKIENMINQSLTRVDHQPHEAENCSEKNSVGGPSTLQGRFPDIRSRQTSRRPDAGSDGFHPIDCDGVYLSSCGHAVHQSCLERYLKSLKERSGRRTVFEGAHIVDLKKKEFLCPVCRRLANSVLPECPGDLCSVSKLQDSPRTKLRRKDALQPSLWLSEALCLLRSAAEVIEDGDRGKTVTPQGDGPRRKDLKSVSKMLWDFYFPKPEDKTLKRLWLPPQSIVMWDTLKYSLISMEIGTRFAKNSMLPVYCIDSLYEELKTSKGTILSVLLRVVQSSRTKNTIHVRQRFVGMKHLAESICYGVSSSSSSSIFGSEGTTGSLKNIDLLWNRASDPVLAHDPFSSLMWALFCLPFPFLTCEESLLSLVHIFHSVSLVQTVIAYCACRPSELSELNFGENLLNDISNALRESGGWEYFRSNNMDLSCDIKDTIRKYSLPFLRRCALLWKLLKSTPRKLHEESDMFDLPSDPTTDNMDFIYSPQSELNHVQELEKMFNIPPIDIILNDELLRSSTQIWLQHFQREYRVNRVKRSLCITPVVPFQLMKLPNLYQDLLQRCIKKRCVNCTKVIEEPVLCLLCGSLCSPIWSPCCRESGCPNHAITCGAGTGVFLLIRRTTILLQRFARQSPWPSPYLDTFGEEDIDMIRGKRLYLNEERYAALTYLVGSHGLDRSSKVLGQTTIGAVLH
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Ubiquitin protein ligase which is a component of the N-end rule pathway with arginine specificity, and functions with the arginyltransferases ATE1 and ATE2. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Does not participate in degradation of proteins with N-terminal Phe or Leu. The N-end rule pathway regulates seed after-ripening, seedling sugar sensitivity, seedling lipid breakdown, and abscisic acid (ABA) sensitivity of germination. The N-end rule pathway regulates various aspects of leaf and shoot development. Involved in the ubiquitination and subsequent degradation of RAP2-12, an activator of hypoxic gene expression. The ubiquitination occurs after the N-arginylation of RAP2-12 by ATE1 or ATE2 under aerobic conditions. The end-rule pathway plays a role in regulating the timing and amplitude of the immune response following infection with the bacterial pathogen Pseudomonas syringae pv tomato. Regulates the biosynthesis of plant-defense metabolites such as glucosinolates, and the biosynthesis and response to the phytohormone jasmonate (JA), which plays a key role in plant immunity. Controls the expression of specific defense-response genes, activates the synthesis pathway for the phytoalexin camalexin, and influences basal resistance to the hemibiotroph pathogen Pseudomonas syringae pv tomato. Coordinates the mobilization of seed storage reserves and regulates the abundance and activities of several proteases following seed germination.
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F4KCE9
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KNL2_ARATH
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Kinetochore-associated protein KNL-2 homolog (Protein KINETOCHORE NULL 2)
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MTEPNLDEDGSKSSFQKTVVLRDWWLIKCPKEFEGKQFGVAGFEESVETRAMRVFTSSPITKALDVFTLLASDGIYITLRGFLNKERVLKNGFNPEISREFIFGFPPCWERVCNSCFEGDSFGTDVNTVPSTIEKACPPILSPCKYSNRNLKDNPAESREKSNVTETDIAEINDKGGSGARDIKTARRRSLHLQIKRILESSKVRKTANDGDHGSEFLNTAKRGDVERDGCEVINNEDSEWKLDESEVQNLCNDGDNGSEGFIKAKSSDVEKDKSEAIDNDVISPAVGSGIKHTGADNVDKVTSASATGESLTSEQQNGLLVTTASPHSLLKDLAKSSKPEKKGISKKSGKILRSDDNVVDPMNYSGTKVKSAENKRKIDASKLQSPTSNVAEHSKEGLNNAKSNDVEKDVCVAINNEVISPVKGFGKRLSGTDVERLTSKNATKESLTSVQRKGRVKVSKAFQDPLSKGKSKKSEKTLQSNSNVVEPMNHFRSEAEEAEENLSWEKIKRKIDFDVEVTPEKKVKQQKTNAASTDSLGQKRSRSGRVLVSSLEFWRNQIPVYDMDRNLIQVKDGSETNSAPSKGKGSDSRKRRNLKIK
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Involved in recognition of centromeres and centromeric localization of the centromere-specific histone CENH3. Required for normal progression of mitosis and meiosis. May play a role in the determination of the epigenetic status of centromeres. Binds DNA and RNA in vitro.
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F4KCH3
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SOP15_ARATH
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Serine rich endogenous peptide 15 (AtSCOOP15) (Phytocytokine SCOOP15) (Precursor of serine rich endogenous peptide phytocytokine 15) (Secreted transmembrane peptide 8)
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MSKEKSYVIALLLSLLLCLSFQVGVSEANYNAVTTRYSDSPRCANGSSASPPTRHCPRGRPRPPTPRVAVHSNSTKGKGP
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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. Inhibits root growth.
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F4KDA5
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MIP_ARATH
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Mitochondrial intermediate peptidase, mitochondrial (EC 3.4.24.-) (AtOCT1)
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MWKLTRRLQPHINSTRWLVRNFRNGGAGDATGLYGFDHLKTAKGFQRFVADAIERSGELVSYISGMPSSPEIIKAMDEISDTVCCVVDSAELCRQTHPDREFVEEANKAAIEMNDYLHHLNTNHTLYAAVKKAEQDSNLLTKEASRTAHHLRMDFERGGIHLDPEKLDKVNNLTTNIFQLCREFSENIADDPGHVDIFPGSRIPRHLHHLLNPTYRSTSGGSRGSTRSAHKSKQKGFRINTDPRTVSSILQWTSDEEVRKMVYIQGNSVPHANHGVLEKLIAARHELSQMMGCNSYADIMVEPNLAKSPKVVTSFLQELSKTVKPKADEEFIAIRDFKREKCGNPSAELEPWDETYYTSMMKSSINDVDTAVVASYFPLPQCIEGLKVLVESLFGATFHTIPLAPGESWHPNVVKLSLHHPDEGDLGYLYLDLYSRKGKYPGCASFAIRGGRKISETEYQLPVIALVCNFSRACDSSIVKLNHSEVEVLFHEFGHALHSLLSRTDYQHFSGTRVALDLAEMPSNLFEYYAWDYRLLKRFARHYSTGETIPEKLVNSLQGARNMFAATEMQRQVFYALIDQMLFGEQPETARDVSHLVAELKRQHTSWNHVEGTHWYIRFSHLLNYGAGYYSYLYAKCFASTIWQSICEEDPLSLNTGTLLREKFFKHGGAKDPAELLTDLAGKEIISVHGEGIVPATTYLLNELRL
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Aminopeptidase which cleaves preproteins, imported into the mitochondrion, to their mature size. Could cleave both preproteins and preprotein intermediates already cleaved by the mitochondrial processing peptidase (MPP).
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F4KDF5
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MUPS1_ARATH
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Protein MULTIPOLAR SPINDLE 1 (Protein PUTATIVE RECOMBINATION INITIATION DEFECTS 2) (AtPRD2)
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MSSSVAEANHTEKEESLRLAIAVSLLRSKFQNHQSSSSTSRCYVSSESDALRWKQKAKERKKEIIRLQEDLKDAESSFHRDLFPANASCKCYFFDNLGVFSGRRIGEASESRFNDVLRRRFLRLARRRSRRKLTRSSQRLQPSEPDYEEEAEHLRISIDFLLELSEADSNDSNFSNWSHQAVDFIFASLKKLISMGRNLESVEESISFMITQLITRMCTPVKGNEVKQLETSVGFYVQHLIRKLGSEPFIGQRAIFAISQRISILAENLLFMDPFDESFPEMDECMFILIQLIEFLICDYLLPWANEAFDNVMFEEWIASVVHARKAVKALEERNGLYLLYMDRVTGELAKRVGQITSFREVEPAILDKILAYQEIE
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Involved in meiotic spindle organization in meiocytes thus regulating chromosome segregation. Required for formation of meiotic DNA double-strand breaks (DSBs) during early recombination processes.
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F4KDH9
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FIPS5_ARATH
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FIP1[V]-like protein (AtFIP1(V)) (Factor interacting with poly(A) polymerase 1-like 5) (AtFIPS5) (Protein HOMOLOG OF YEAST FIP1 [V])
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MEEDDEFGDLYSDVLQPFQPPVVLPPPPPLPHRSIDLNLRSQDQDVSEPNSAPISRVSDNDAVKLSTQDATRQAIVDGGGDDKDMSFDIEEPDADSTPTIPGLFVTGALPGLATDRGVSQVTTRIEQQVGGGGDGGYGGQGEGDDWDSDSEDDLQIVLNDSSRNVMIGGADRRSRMGDNEDDDDEDDEDPLVIVADTDPNQPMEEQMWGEDGLQGIEGDGKDGGEAGKGSGPGGATGPPKAGYSSHGYHPFHSQFKYVRPGAAPIPGGAASVGGPSSGQVRPPANLGPMAGRGRGDWRPLGMRNASAAQKGFHQPWGSNTAGRGLDFTLPSHKTIFEVDIDSFEEKPWRYPGVEMTDYFNFGLNEESWKDYCKQLDQHRIQTTMQSRIRVYESGRTDQGYDPDLPPELAAATGAQGVPVDSSNLVKPDSVQGDSAKVPANVRPTLPPGRPIPVETGSGERLPSIDTRAPRMRDLDAIIEIVCQDSHEDEPSGENGTDQADSSLPGENVPVETSYVNNKRPDTESAEHSPAQDEPHKNLLKKQDDEISRSTDSGQSFRSSSPVGDRGTRSSSVDREDVGGEAGKDAEMGEELKMSFTSPQSAVQEDDGGESKTERSSESSKARSGSHRDFQQEEDVIQDKHSSRPANNRKQYDNNAPHQSRKNQDRGKEMERTRAASKGGRENSNPHMELDSTYIYSIASREDFDKRKERDVDGAVWRRKEDDPYSRRGGDEGSRKRDREDDPGFRQRGKMRENEIRSKDDQVPSRKHMDDAGMRNIYEPDDHINKRRKDEEYLRRSRPEKNEISYGQRESMSRVKRERDDRLEHQKRDVQHKIRDDFDDHGSLRQRDDIYMQRDGNERLRERDVLDKLKLPHEDGISARGRERQVAVRGHRGSEDRSSRMKDEYKASDKEHVTKDTLRHAKQTKRRDYPGEESSSHHRGHEDFSARTDNIVNNEKKPRQERTGAKIDKFIDTLDGQRLQDRKHKDSRRKIKEQREGTESLSKQGEQNGSSVVTGSKGTNDARNCRSEIPHQPNTAKRHKENASSGDEIHDSKRGRTKLERWASHKEREDAVSAKSSSISSKLEEKENNTNGRLSEPVHGSIGKSRDVTEEKIGHDLADTKDGSEKGPGDRHLDTVEKLKKRSERFKLPMPTEKDTTGVKKMESETLPSAKIEGPVDSEGEYVWDERSCVRIGREYA
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Essential gene. Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex (By similarity).
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F4KDN0
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HEN4_ARATH
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KH domain-containing protein HEN4 (Protein HUA ENHANCER 4)
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MERNSVKFHAEKRSGAFDPGSGFGSSKRVKTHHTQLLSALVVPVGHAAFRLLCPLSHVGAVIGKSGNVIKQLQQSTGAKIRVEEPPSGSPDRVITIIAQADSKSRVKLGANNNGNAEGEKKEEEVEVSKAQGALIKVFELLAAEADSDTVVCRLLTESSHAGAVIGKGGQMVGSIRKETGCKISIRIENLPICADTDDEMVEVEGNAIAVKKALVSISRCLQNCQSIDKVRMVGNRPLEKEFQASLHRPIETIIQESLPRSVEVNPYDYRLRNDEIFPRGTVARANDVIPHDTLHLRRIEAVPQGALRMHIEADRQDVLRRHVEADRQDALRRRIDVVPQETLYMPSDVLRGDCFRQHRERDDSHDSLHRPFEMVPRDAMGMPFESFPRDAYGRPIETMTQETLRGQSADYLAHRYSTLDTHPHSFTTSASMANTATMKPPPSEVEVGNQDVVFKILCSTENAGGVIGTGGKVVRMLHSETGAFINVGNTLDDCEERLIAVTASENPECQSSPAQKAIMLIFSRLFELATNKILDNGPRSSITARLVVPTSQIGCVLGKGGVIVSEMRKTTGAAIQILKVEQNPKCISENDQVVQITGEFPNVREAIFHITSRLRDSVFSNSMKNSLAKSSSALTTERFYDRQSDNPLSIGSHQSVSNPATNSSSLHRRSEDSFLSGSHSSVNYSRSVGTDPYIRPEDPFPDRFNPSAGYSHNFGRRFTMDHSDNSHHLTEAPSRLWASPPPAAPRGLSDASGGLSSARAGHVLGSGHKSAIVTNTTVEIRVPANAMSFVYGEQGYNLEQLRQISGARVIIHEPPLGTSDRIIVISGTPDQTQAAQNLLHAFILTGETSLSKKYNLN
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Functions in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. Functions in association with HUA1 and HUA2.
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F4KE59
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PAIP2_ARATH
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Protein PARALOG OF AIPP2 (PHD finger-containing protein 2)
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MADRRVGKRQMGQRGFSKVESGTCNVCSAPCSSCMHRNVGFTGSKLDESSDENCHGVVGSQCSVNEDDLLPSSMVNAHKSLNNTASEASNLVNSSHDALSENAESKETIRCSGISDDSGAAAMTSKPSLSGSRMKHKVSASANMLDQSSNCIEDQEDGILSADRAKQLKSGCSNNEIGNKDLADGSALNSDPIPGGSRKDEVKLESLQNPSSNHDDRVSSEKGNFKEKSRPGGNKERQEPSVEGSTRSGENRKDGKSSKSSSSNSSAVSESESDDSEMVEHDVKVCDICGDAGREDLLAICSGCSDGAEHTYCMREMLDEVPEGDWLCEECAEEAEKQKQEAKRKRETEVTFNTYSSGKRHADKIEAAPDAKRQVVEASTGSPKKSILPRVGALSRETSFKGLDRLRGKLNHQTSFSDDTESARSAGSQLQPPKGAFLKSSSFNCSSSKPKVQLMDDAIHPRQKTGKEDTALDLKVGGFRNVGKSMPSRTTDAGNSGGSDSQAKMLGSKVYHSQEGKSLKQVKDRNREANASASSIDQKLKSRGNSSVSHANNNRDLKGLQSDGKRGNLTKQVSNLSRNRLENSVVSGGDISTNEKCSASEQSSSQADCKDELPSTSCTGEGMPNHGTVALQDGLPRSRVPREVGKKSKEAFSKRQRSSLLAGAKGLPSSQKGGQTAESSDTSGVSDSDLSTTKNVKEDLNKGNRLRAAVDAALRKKPSFGKNRVLEQSDASLVANVDSSSEKTLRNQLPSKMHKNHVSHEGLQGGHPILWPTSDPYKQTIVTNEKQLIFPGADTIPSRLVEPEVSFPAVKPVMRDLPLVPSPVMLRSSAIPDHEFIWQGDLEVRKIINQSAMHSGIQAHLSTLASPRVAEVVNKFPETFSLNEVPRKSTWPTQFEKLGTKEAHIALFFFAKDTESYERNYKPLVDNMIKNDLALKGNLDNVDLLIFASNQLPSNCQRWNMLYFLWGVFQGRKETNPQKNTSLPTSNVLPRDRDPKELCQTSSPSKHLEKGSSLRESSSNGIETRNGTDARSHENPNNRESSIERSPSKKEDIALKVEEAGVNHIPPQVTGSNSGDSLVRKVQKVEEQELGGRKDLPLTVMGSGIQSHGQDNPLEKDLNSSQASHRKRPLWELSNPANENSSAINQKVELNNDGLCEGSPNKKLKTENGSSSLCRDTSGHDSGIMKKSPKVVFPLDLNDDSEMVDNLSPLGNDENNNNRRLISGTVPNLELALGAEETTEATMGLLPFLSRSSNSGEQSNNSMNKEKQKADEEEEDDAEVAASLSLSLSFPGTEERKNVNTPLFLFRDLPR
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Together with AIPP2 and AIPP3/BDT1, cooperates to form a BAH-PHD bivalent histone reader complex able to read histone H3 lysine 27 trimethylation (H3K27me3) and low-methylated H3K4 histone marks in order to regulate transcription, especially to prevent early flowering promotes AIPP3/BDT1 binding to H3K27me3. CPL2 is subsequently recruited to form a BAH-PHD-CPL2 complex (BPC) in order to silence several H3K27me3 and low-methylated H3K4 enriched loci, including AGO5, via the phosphorylation state-dependent inhibition of Pol II release from the transcriptional start site (e.g. Ser5P-Pol II dephosphorylation). The BPC complex represses flowering by inhibiting the expression of several genes, including AGL6, FT, FUL and SOC1.
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F4KEV7
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FHIT_ARATH
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Bifunctional bis(5'-adenosyl)-triphosphatase/adenylylsulfatase FHIT (EC 3.6.1.29) (Adenosine 5'-monophosphoramidase FHIT) (EC 3.9.1.-) (Adenylylsulfatase) (EC 3.6.2.1) (Adenylylsulfate-ammonia adenylyltransferase) (EC 2.7.7.51) (Fragile histidine triad protein)
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MLNLQVTGKTILSSIRCQRKMSSTCSSYAFGPYKIDPREVFYATPLSYAMVNLRPLLPAHVLVCPRRLVPRFTDLTADETSDLWLTAQKVGSKLETFHNASSLTLAIQDGPQAGQTVPHVHIHILPRKGGDFEKNDEIYDALDEKEKELKQKLDLDKDRVDRSIQEMADEASQYRSLFDC
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Possesses dinucleoside triphosphate hydrolase activity. Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate. Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2. Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate.
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F4KF14
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FTSI4_ARATH
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Probable inactive ATP-dependent zinc metalloprotease FTSHI 4, chloroplastic (AtFTSHI4) (Protein EMBRYO DEFECTIVE 3144) (Protein FTSH INACTIVE PROTEASE 4)
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MTFYISSSLTPTHFSKPLNPSNTLFPSQFRGSLSSFVRRRKPTEAKLSSKFNLFPSRRNGLITCCSTSSFESTESSVSQEEDAESNRLFEKLRETERERLSNMEELERKANVQLERQLVMASDWSRTLLTMRGKLKGTEWDPETSHRINFSDFMKLLDSNSVQYMEYSNYGQTISVILPYYKDGEPLGEEEDSKKEIIFRRHIVDRMPIDGWNDVWKKLHQQIVNVEVFNVDVVPAEVYTTVATFVVWSMRLALFVSLYVWIDSITRPIYAKLIPCDLGTPTKKIRQPLKRQALGSLGKSRAKFISAEEKTGVTFDDFAGQEYIKRELQEIVRILKNDEEFQNKGIYCPKGVLLHGPPGTGKTLLAKAIAGEAGLPFFAANGTDFVEMFVGVAASRVKDLFASSRSYAPSIIFIDEIDAIGSKRGGPDIGGGGAEREQGLLQILTEMDGFKVTTSQVLVIGATNRLDILDPALLRKGRFDKIIRVGLPSKDGRLAILKVHARNKFFRSEDEKEELLQEVAENTEDFTGAELQNVLNEAGILTARKDLDYIGREELLEALKRQKGTFETGQEDSTEVPEELKLRLAYREAAVAVLACYLPDQYRPISETDINSIRSQPNMRYSETSGRVFARKSDYVNSIIRACAPRVVEEEMFGIENLCWISAKSTLEASQRAEFLILQTGMTAFGKAYYRNQRDLVPNLVPKLEALRDEYMRFAVEKCSSILQEYQSALEEITDVLLEKGEIKADEIWNIYNTAPRIPQKPVRPVDEYGALIYAGRWGIHGVSLPGRVTFSPGNIGFATFGAPRPMETQIISDDTWKLVDEIWDKKVEEIKAEAVIQIEEEKKKPQILMATHFF
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Functions in chloroplast biogenesis and chloroplast division. Required for plastid development during embryogenesis. Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex.
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F4KFS7
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MEB2_ARATH
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Membrane protein of ER body 2
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MEKSNQPVHVTLSELKDGDKEIVDAEFLVDLLESYRFGKDNVPAREFRSKAAATAPAPVNTTEIELEEDNDGSQAQGNNSVSESTSSLFSDSDPIVLESTVSETGSNEESETGSNEENGNNWLESSSTNLPNVENKRQRNGEDCEIEEEEENNERSLSDSEEKSNLEKLLGTQENYELGNEDEEKNERSSSDSEEKSNLENLLATQENYELYCPSCSTCITRNVVLKKRKRGKHVNSSLDLKPDIPVVEPDEPSDIEEMESPVKVYVPETRIEDDQEDKEGTIFTCLVCDLKYFIRLGTKFLQLDYIRGKPVEKSVEEYIDVRKSINTTQSPPQIQPDGERFAIELLKSTVYGGLTETITSLGVVSSASASGSSTMNILALAVANLAGGLIVLAQNFQDLRNSSDQEKDRYEELLGRRTKSRIHILVAVMSYIFFGLIPPLVYAFSFYETGIKNYKLISVFLGSLVCVILLGSIKVYVRKPTNSCGSTKAYLKSAAYYTSIVVASCGISYVVGDIMGEYIEKLSLVGLDQISITSPCYGIKPEECRFTSF
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May sequester excess cytosolic iron and manganese into endoplasmic reticulum to reduce metal ion toxicity. Not essential for the accumulation of ER body components, including PYK10.
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F4KFT7
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TENAC_ARATH
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Bifunctional TH2 protein, mitochondrial (THIAMINE REQUIRING 2) [Includes: Thiamine phosphate phosphatase (EC 3.1.3.100); Aminopyrimidine aminohydrolase (EC 3.5.99.2)]
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MRFLFPTRLINNSSLGLLRSPHTTAPIRSLWFRTKSPVFRSATTPIMTAVAFSSSLSIPPTSEEALPGKLWIKFNRECLFSIYSPFAVCLAAGNLKIDTFRQYIAQDVHFLKAFAHAYELAADCADDDDDKLAISDLRKSVMEELKMHDSFVQDWDLDINKEVSVNSATLRYTEFLLATASGKVEGCKAPGMLDTPFEKTKVAAYTLGAVTPCMRLYAFLGKEFGSLLDLSDVNHPYKKWIDNYSSDAFQASAKQTEDLLEKLSVSMTGEELDIIEKLYQQAMKLEVEFFHAQPLAQPTIVPLLKNHSKDDLVIFSDFDLTCTVVDSSAILAEIAIVTAPKDEQSRSGQQIHRMLSSDLKNTWNLLSKQYTEHYEECIESILNKKKADKFDYEGLCKALEQLSDFEKEANNRVIESGVLKGLNLEDIKRAGERLILQDGCINVFQKILKTENLNAELHVLSYCWCGDLIRAAFSAGGVDAVEVHANEFTFEESISTGEIERKVESPINKAQQFKSILQNRKNENNKKSFLSVYIGDSVGDLLCLLEADIGIVVSSSSSLRRVGSHFGVSFVPLFSGIVQKQKQHTEESSSSAWKGLSGTLYTVSSWAEIHSFALGWE
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May be involved in the salvage of thiamine breakdown products. This protein has a haloacid dehalogenase family domain fused to its TenA domain. Phosphatase with the highest activity against thiamine monophosphate (ThMP) and, with a lower activity, against thiamine diphosphate (ThDP), flavin mononucleotide, inorganic pyrophosphate, CTP and dATP. Has a thiamine salvage hydrolase activity, but only against 4-amino-5-aminomethyl-2-methylpyrimidine (amino-HMP) and not against N-formylamino-HMP, desthiothiamine, thiamine, ThMP, and ThDP.
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F4KGN5
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S40A2_ARATH
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Solute carrier family 40 member 2 (Ferroportin-2) (Iron-regulated transporter 2) (AtIREG2)
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MEEETETRVFLSNEQHQEEEEEEEEEPSLPRSMVISLYLGYFLARWGARTWEFSVALYMIYLWPNSLFLTAMYGVVESGSATLFGPIVGQMIDGMSYVKVLRLWLVTQNLSFIVAGGAVVALLVVPDLKSQNFPVFATLVVLTNLSGAIGVLSTLAGTVLIERDWVVVMSEGHSPAVLTRMNSVIRGIDLSSKLLSPVITGLIISFVSLRASAITFAAWATITVWIEYWLFISVYNGVPAIVQSDERRSLRSSQSQAEETDSASSFYVPLLHEEESYRNTQSRSRILRILERISESSFVSAWRNYLNQEIVLPGVSLALLFFTVLSFGTLMTATLEWKGIPTYIIGIGRGISAGVGLAATVLYPLMQSRISPLRTGVWSFWSQWTCLLVCVGSIWVEKEKIASYMLMAGVAASRLGLWMFDLAVIQQMQDLVPESDRCVVGGVQNSLQSALDLMANLLGIIVSNPKDFWMLTLISFATVSLAGILYTIHLYRIRKHLFHLEKIPLLNNFFAS
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Vacuolar transporter that is involved in the transport of excess nickel into the vacuole under iron deficiency, increasing cellular tolerance to nickel under iron deficiency stress response.
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F4KGQ0
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ALFC4_ARATH
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Fructose-bisphosphate aldolase 4, cytosolic (AtFBA4) (EC 4.1.2.13) (Cytosolic aldolase 3) (cAld3)
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MSCFKSKFAGKSYFRRTFHSSIIQFHPQLSILIWHRRYSIIRTYELIANAAYIGTPGKGILAADESTGTIGKRFVSINVENVESNRRALRELLFTTPGALQYISGIILFEETLYQKTASGKLFVDVMKEAGVLPGIKVDKGTVELAGTNGETTTTGLDGLGDRCKKYYEAGARFAKWRAVLKIGNNEPSELAIHENAYGLARYAVICQENGLVPIVEPEILVDGSHDIEKCAYVTERVLAACYKALSDHHVILEGTLLKPNMVTPGSDSGSKVKPEVIAKHTVRALQRTVPAAVPAVVFLSGGQSEEEATVNLNAINQLKGKKPWSLTFSYGRALQQSTLKAWGGKEENVDKAQKAFLARAKANSEATLGGYKGDAQLGEGASESLHVKDYKY
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Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis.
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F4KH86
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TAD3_ARATH
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tRNA-specific adenosine deaminase TAD3 (AtTAD3) (EC 3.5.4.33) (Protein EMBRYO DEFECTIVE 2820) (tRNA-specific adenosine-34 deaminase TAD3)
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MDSDAWEIIHIPEKPSLSPDHQPTVKVYASLIKPRFANTIVRHLCKIAPLEDLRHVKRVKKKILPDCGETQLTVILCLAPEHNDQLSDMPPDVQRLVDPYELSPFITQVCKYAAVSKEEWEEQSKIWPTSFHPPTYNIDGIGGFSEEETQSICKFMRVVIDMAVSGHTPLVNAAVIVDPSVRRIIASETDQVYASSAPRDMTSAETRPFEETGEICLNDTLEKQNGSLSALSCLNPWQWSLQPHDTENCSQWHPLRHASMVAIESSSARDRNLFPNPSKIFDQDHVPPSNTDSPAKKQKTSSQSPDVQNDSREETVRDPSMERPYLCTGYDIFLLLEPCTMCAMALVHQRIKRIFYAFPNTTAGGLGSVHRLQGEKSLNHHYAVFRVLLPDDALRQMTTV
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Involved in RNA editing. Catalyzes the specific deamination of adenosine-34 in several cytosolic tRNA species. Generates inosine at the wobble position of the anticodon loop.
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F4KHI3
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VICTR_ARATH
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Protein VARIATION IN COMPOUND TRIGGERED ROOT growth response (EC 3.2.2.6)
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MASSSSSRNWVYDVFLSFSGKDVRVTFRSHFLKELDRKLISAFRDNEIERSHSLWPDLEQAIKDSRIAVVVFSKNYASSSWCLNELLEIVNCNDKIIIPVFYGVDPSQVRYQIGEFGSIFEKTCKRQTEEVKNQWKKALTDVANMLGFDSAKWDDEAKMIEEIANDVLAKLLLTSSTDSAENSIGIEDHIANMSVLLKLEAEEVRMVGIWGSSGIGKTTIARALFNQLSRHFPVSKFIDRAFVYKSRETYKGANPDDPNMKLHLQGCFLSEILGKKDIKIDHLGALGERLKHQKTLIIIDDLDDLVVLDSLVGKTNWFGCGSRIIVITNNKQFLRAHGIDHIYEVSLPSKERAQEMFCQSAFGENSPPEGFEELVVEIAWLAGSLPLGLTVFGSALRGRKKEYWVKMLPRLQNDLDGNIEETLKVSYDAIGNVKDQALFRLIACLFNHVKVRDIELLLADSGLDVNIALENLVDKSLIHVRNDHVEMHRLLQETGRNIVRSQSTDNPGEREFLVDSNDSRTVLSEGIGTRKVLGISLDTSKVSEFCVHENAFKGMGNLLFLDISSKTFIEEEVKVHLPEKINYYSVQPKQLIWDRFPLKCMPYTFLRNLVKLEMHDSKLEKLWEGAMSFTCLKELDMWASKYLKEIPDLSKATNIEKLDFGHCWSLVELPSSIRNLNKLLELNMEYCGELETLPTGFNLKSLDYLNFNECWKLRTFPEFATNISNLILAETSIEEYPSNLYFKNVRELSMGKADSDENKCQGVKPFMPMLSPTLTLLELWNIPNLVELSSSFQNLNNLERLDICYCRNLESLPTGINLESLVSLNLFGCSRLKRFPDISTNIKYLDLDQTGIEEVPWQIENFFNLTKLTMKGCRELKCVSLNIFKLKHLGEVSFSNCGALTRVDLSCYPSGVEMMKADNADIVSEETTSSLPDSCVLNVNFMDCVNLDREPVLHQQSIIFNSMILPGEEVPSYFTYRTSDSQPFGTSSSLPIPLLPTQLSQPFFRFRVCAVVSASNGVYIGVYSRFKGRIGNKFDSFGEVHNFMEIEKGIHLCIFDCRIRLYKDNVPLSQLNYDHVDINIHITSGDWRSTVVLKEWGIRLLETGSSAENRLGNPNSTLPHVSQAEEGNMGYYTHVQGLVNEIENSEDSGDNNVETERSKKRMRLHHFI
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Disease resistance protein of the TIR-NB-LRR-type. Part of the RPS6 locus that contains a cluster of several paralogous disease resistance (R) genes. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth (By similarity). Required for [5-(3,4-dichlorophenyl)furan-2-yl]-piperidine-1-ylmethanethione-(DFPM-) induced root growth arrest due to reduced number of meristem cells in the division zone of the primary root and inhibition of abscisic acid- (ABA-) induced stomatal closing. {ECO:0000250, ECO:0000269|PubMed:23275581}.
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F4KHQ8
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NCER3_ARATH
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Neutral ceramidase 3 (AtNCER3) (N-CDase 3) (NCDase 3) (EC 3.5.1.23) (Acylsphingosine deacylase 3) (N-acylsphingosine amidohydrolase 3)
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MTRWSMSMHCTLFLLFLLRLTCIFSDSDYLMGLGSYDITGPAADVNMMGYANMEQVASGVHFRLRARAFIVAEPYKKRIAFVNLDAGMASQLVTIKVIERLKQRYGELYTEENVAISGTHTHAGPGGYLQYILYLVTSLGFVHQSFNALVDGIEQSIIQAHENLRPGSILINKGELLDAGVNRSPSAYLNNPAHERSKYEYDVDKEMTLVKFVDDQWGPVARIMEDWFERENGCRSVDVESPRRVSSIISDPYDQDLMEMASSLLSTGGKTVTRMSSVARRVRSRFRHADKPRFVSAFCQTNCGDVSPNVLGAFCIDTGLPCEFNQSTCGGKNEQCYGRGPGYPDEFESTRIIGERQFKKAADLFTKASEEIQGKVDYRHAYVDFSQLEVTINGQNGGSEVVKTCPAAMGFGFAAGTTDGPGAFDFKQGDDQGNPFWRLVRNLLKNPTEEQVRCQRPKPILLDTGEMKQPYDWAPSILPVQILRIGQLVILCVPGEFTTMAGRRLRDAVKTVLKEGSNGREFSVVIAGLTNSYSQYIATFEEYQVQRYEGASTLYGPHTLSGYIQEFKKLANDLLSAQTTDPGPQPPDLLHKQISLLTPVVADMTPIGTAFGDVTSDVPRLSKFRKGADIVRVQFRSANPRNDLMTEGTFALVERWLEGRETWVPVYDDDDFCLRFKWSRPFKLSTQSTATIEWRIPETASPGVYRITHFGSAKTPISSIHHFSGSSSAFVVY
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Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid (By similarity). Promotes oxidative stress resistance.
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F4KIX0
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JMJ13_ARATH
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Lysine-specific demethylase JMJ13 (EC 1.14.11.-) (Jumonji domain-containing protein 13) (AtJMJ13) (Protein JUMONJI 13) (Lysine-specific histone demethylase JMJ13) ([histone H3]-trimethyl-L-lysine(27) monodemethylase JMJ13)
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MAERRICLSKEAKDGLEFLKRKKLQKMRSDSVNETVGFSTMARSGGDALRPTSASCGMRLRVTSSDTVSKVHGASTVRGGLMKEKVEKLETDDLKWTERLPECPVYRPTKEEFEDPLTYLQKIFPEASKYGICKIVSPLTATVPAGAVLMKEKSNFKFTTRVQPLRLAEWDSDDKVTFFMSGRTYTFRDYEKMANKVFARRYCSGGSLPDSFLEKEFWKEIACGKTETVEYACDVDGSAFSSAPGDPLGSSKWNLNKVSRLPKSTLRLLETSIPGVTEPMLYIGMLFSMFAWHVEDHYLYSINYQHCGASKTWYGIPGSAALKFEKVVKECVYNDDILSTNGEDGAFDVLLGKTTIFPPKTLLDHNVPVYKAVQKPGEFVVTFPRAYHAGFSHGFNCGEAVNFAMGDWFPFGAIASCRYAHLNRVPLLPHEELICKEAMLLNSSSKSENLDLTPTELSGQRSIKTAFVHLIRFLHLARWSLMKSGLCTGLVSNTYGTIVCSLCKRDCYLAFINCECYSHPVCLRHDVKKLDLPCGTTHTLYLRDNIEDMEAAAMKFEKEDGVSDLITTDEDLYKYPSSITLPAAKEDGYTPYSTIYFDFYTEVEMTSHDQLQSGNPVMSYEANASCISSVADDYECSDYVNRRANCSSSSDSKLSEEVACSSSKKTRFFPVVQDEQLVADQESDGSDSECFRVKRRSSLKFENRTVVLDTRESDHHQELKRLKKSHHHEGRYSSSSSVSRQEEEEDELVISNRKETQQQSDVKMQKKRIENHFGGFKRLKVKGLIKP
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Histone demethylase that demethylates 'Lys-27' (H3K27me) of histone H3 with a specific activity for H3K27me3 and involved in the regulation of gene expression. Acts as a temperature and photoperiod dependent flowering repressor.
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F4KU78
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IYD_HALH1
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Iodotyrosine deiodinase (EC 1.21.1.1) (Halotyrosine dehalogenase)
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MKQKPAFIPYAGAQFEPEEMLSKSAEYYQFMDHRRTVREFSNRAIPLEVIENIVMTASTAPSGAHKQPWTFVVVSDPQIKAKIRQAAEKEEFESYNGRMSNEWLEDLQPFGTDWHKPFLEIAPYLIVVFRKAYDVLPDGTQRKNYYVQESVGIACGFLLAAIHQAGLVALTHTPSPMNFLQKILQRPENERPFLLVPVGYPAEGAMVPDLQRKDKAAVMVVY
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Catalyzes the dehalogenation of halotyrosines such as 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine. Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity). Activity towards 3-iodo-L-tyrosine is much stronger than activity towards 3,5-diiodo-L-tyrosine and 2-iodophenol.
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F5A6E9
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TPIS_PROCL
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Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Methylglyoxal synthase) (EC 4.2.3.3) (Triose-phosphate isomerase) (allergen Pro c 8.0101)
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MANQRKFFVGGNWKMNGDRAGIDSIISFMKGPLSADTEVVVGCPQCYLMYTREHLPSNIGVAAQNCYKVAKGAFTGEISPSMIKDCGCEWVILGHSERRNVFNEPDTLISEKVGHALEAGLKVIPCIGEKLEERESNRTEEVVFAQMKALVPNISDWSRVVIAYEPVWAIGTGKTATPEQAQEVHAKLRQWLRDNVNAEVADSTRIIYGGSVTPGNCKELAKTGDIDGFLVGGASLKPDFVQIINARD
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Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids.
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F5BHA2
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T19H_CATRO
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Tabersonine/lochnericine 19-hydroxylase (EC 1.14.14.-) (Cytochrome P450 71BJ1)
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MLSSLKDFFVLLLPFFIGIAFIYKLWNFTSKKNLPPSPRRLPIIGNLHQLSKFPQRSLRTLSEKYGPVMLLHFGSKPVLVISSAEAAKEVMKINDVSFADRPKWYAAGRVLYEFKDMTFSPYGEYWRQARSICVLQLLSNKRVQSFKGIREEEIRAMLEKINQASNNSSIINGDEIFSTLTNDIIGRSAFGRKFSEEESGSKLRKVLQDLPPLLGSFNVGDFIPWLSWVNYLNGFEKKLNQVSKDCDQYLEQVIDDTRKRDEENGANNNGGNHGNFVSVLLHLQKEDVKGFPSEKGFLKAIILDMIVGGTDTTHLLLHWVITELLKNKHVMTKLQKEVREIVGRKWEITDEDKEKMKYLHAVIKEALRLHPSLPLLVPRVAREDINLMGYRVAKGTEVIINAWAIARDPSYWDEAEEFKPERFLSNNFDFKGLNFEYIPFGSGRRSCPGSSFAIPIVEHTVAHLMHKFNIELPNGVSAEDFDPTDAVGLVSHDQNPLSFVATPVTIF
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Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway MIAs are used in cancer treatment and other medical applications. Cytochrome P450 catalyzing the conversion of (-)-tabersonine to 19-hydroxytabersonine, of lochnericine to horhammericine and of (-)-vincadifformine to (-)-minovincinine.
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F5GUE5
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DAF14_CAEEL
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Smad-related protein daf-14 (Abnormal dauer formation protein 14)
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MSNEQEDFGSLFNNQGELGIMDDFAEFGFQTTTTPTNWAAAGNYMYPDQVHLPASINNPNMPINDWLEDAPMPDCYNVPSTSTDENNDPFPFSNISSQSSLKPKTPEKAVVEVRPTGNEMLDPEPKYPKEEKPWCTIFYYELTVRLGKAFEAKVPTITIDGATGASDECRMSLTSQPSSRNSKSSQIRNTVGAGIQLAYENGELWLTVLTDQIVFVQCPFLNQTLNKPLKYVFRLQNKGDQKRMKIFDKEQFEQEKTLALGPLTEKEVADERMRIFSNIRVSFCKGFGETYSRLKVVNLPCWIEIILHEPADEYDTVFRINNERPEIGSRS
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Probably an atypical receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta-like daf-7 signaling. Plays a role in TGF-beta-like daf-7 signaling in regulating entry into a developmentally arrested larval state known as dauer, in response to harsh environmental conditions partially redundant with R-SMAD daf-8.
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F5H094
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SO1BT_HUMAN
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SLCO1B3-SLCO1B7 readthrough transcript protein (Liver specific transporter-3 transmembrane 12) (LST-3TM12) (Organic anion transporting polypeptide 1B3-1B7) (OATP1B3-1B7) (Solute carrier organic anion transporter family member 1B3-1B7) (SLCO1B3-SLCO1B7)
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MDQHQHLNKTAESASSEKKKTRRCNGFKMFLAALSFSYIAKALGGIIMKISITQIERRFDISSSLAGLIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCLLMGTGSILTSLPHFFMGYYRYSKETNIDPSENSTSNLPNCLINQMLSLNRTPSEIIERGCVKESGSHMWIYVFMGNMLRGIGETPIVPLGISYIDDFAKEGHSSLYLGTVNVMGMTGLVFAFMLGSLFAKMYVDIGYVDLSTIRITPKDSRWVGAWWLGFLVSGIVSIISSIPFFFLPLNPNKPQKERKVSLFLHVLKTNDKRNQIANLTNRRKYITKNVTGFFQSLKSILTNPLYVIFVIFTLLHMSSYIASLTYIIKMVEQQYGWSASKTNFLLGVLALPAVAIGMFSGGYIIKKFKLSLVGLAKLAFCSATVHLLSQVLYFFLICESKSVAGLTLTYDGNSPVRSHVDVPLSYCNSECNCDESQWEPVCGNNGITYLSPCLAGCKSSSGNKEPIVFYNCSCVEVIGLQNKNYSAHLGECPRDDACTRKSYVYFVIQVLDAFLCAVGLTSYSVLVIRIVQPELKALAIGFHSMIMRSLGGILVPIYFGALIDTTCMKWSTNSCGARGACRIYNSTYLGRAFFGLKVALIFPVLVLLTVFIFVVRKKSHGKDTKVLENERQVMDEANLEFLNDSEHFVPSAEEQ
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Mediates the Na(+)-independent uptake of organic anions. Transports the conjugated steroids 17-beta-glucuronosyl estradiol (17beta-estradiol 17-O-(beta-D-glucuronate) or E2G) and dehydroepiandrosterone 3-sulfate (DHEAS) at the smooth endoplasmic reticulum membrane (SER), granting access to metabolizing enzymes. Contributes to the metabolism of bile acids such as taurocholate (cholyltaurine) and lithocholate, by functioning as a doorway between SER and cytosol, thereby decreasing their circulating levels and protecting the organism from their detergent properties. Regulates access or exit of drugs to the SER lumen.
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F5HDE4
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ORF45_HHV8P
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Protein ORF45
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MAMFVRTSSSTHDEERMLPIEGAPRRRPPVKFIFPPPPLSSLPGFGRPRGYAGPTVIDMSAPDDVFAEDTPSPPATPLDLQISPDQSSGESEYDEDEEDEDEEENDDVQEEDEPEGYPADFFQPLSHLRPRPLARRAHTPKPVAVVAGRVRSSTDTAESEASMGWVSQDDGFSPAGLSPSDDEGVAILEPMAAYTGTGAYGLSPASRNSVPGTQSSPYSDPDEGPSWRPLRAAPTAIVDLTSDSDSDDSSNSPDVNNEAAFTDARHFSHQPPSSEEDGEDQGEVLSQRIGLMDVGQKRKRQSTASSGSEDVVRCQRQPNLSRKAVASVIIISSGSDTDEEPSSAVSVIVSPSSTKGHLPTQSPSTSAHSISSGSTTTAGSRCSDPTRILASTPPLCGNGAYNWPWLD
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Prevents the establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of host interferon regulatory factor 7/IRF7, a transcription factor critical for the induction of interferons alpha and beta. Mechanistically, ORF45 competes with the associated IRF7 and inhibits its phosphorylation by IKBKE or TBK1 by acting as an alternative substrate. Acts as an activator of the NLRP1 inflammasome via interaction with the N-terminal part of host NLRP1: interaction promotes translocation of the N-terminal part of NLRP1 into the nucleus, relieving autoinhibition of the NLRP1 inflammasome and leading to its activation. Also plays a role in promoting the late transcription and translation of viral lytic genes by constitutively activating host extracellular signal-regulated kinase (ERK)-p90 ribosomal S6 kinase/RPS6KA1. In addition, supports the viral replication cycle by modulating host p53/TP53 signaling pathway. Interacts with host p53/TP53 and prevents its interaction with the deubiquitinase USP7, leading to sequestration of P53/TP53 in the host cytoplasm thereby diminishing its transcriptional activity.
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F5HKX0
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CLB9_ANOGA
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CLIP domain-containing serine protease B9 (EC 3.4.21.-) (Phenoloxidase-activating enzyme B9) [Cleaved into: CLIP domain-containing serine protease B9 light chain; CLIP domain-containing serine protease B9 heavy chain]
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MTSYNRSVAWLTVCVLLALHIGGSHQQQQQCTTPTRLRGRCISIYECDSILDYFKQRILTWEEREFLRKSQCTGATSGRQPFVCCPGNGSKPVVAPATTVPAGTASTTPAGPAATAPSGDAALADQLVGGLLPNPKKNECGVSIGMRIYGGQNADIDEFPWLALLQYENRKGERKYSCGGSLINRRYVLTAAHCVIGEVERKEGKLVSVRLGEYNTKTEIDCVTEEQEEICADPPIDAGIESVIVHPGYQDMAHADDIALLRLAQSIEYTSFVQPVCLPLTDFRASKTGEVNFVTGFGRTLQESRSAVKQKLGIKVYDHARCQEKYATKNSSITTNQLCAGGEYAKDSCHGDSGGPLMKLQKVWYLEGIVSYGNRCGLEDWPGVYTHVPAYMAWVRSNIKE
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Serine protease that functions in the melanization-mediated immune response. Cleaves and activates prophenoloxidase (PPO), which is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products.
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F5HSE3
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NIPLA_DANRE
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Nipped-B-like protein A
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MNGDMPHVPITTLAGIAGLTDLLNQLPLPSPLPGTTTKSLLYNGRVAEDVGHLLGCRDETLVSQLANSLSQVSTEHIELKDSLGSDELEGDVPVLLQLLMSRNPNIFRNKTAPNTPQYPAQAGISQQSMAPPYKITHGSMQGSPASANYQQASMSHSPSGHFVPGQSGPGGRFLPQQGSPVPSPYAPQSPATGYRQYPHPPAYSQHQHLQQGSVASPMIPGAMRNVHENKDQMRMGFTSHLLQSSPPYTPPCDGTKDLHLGSQDKQRGQKSSEGEQDSPDKATVYDIVGSPAKDHTKLILRPSRARPAEVELGGMYPGSDPEGELVEALAAIERMESEAAMETERSAKEVQDKDKPLKKRKQDSHPQEPGAAGTAGSGSGAPGGGGGANAGHRLAPQEASAAGTSASRPGLQVSLEQAGRVEDDCMGMPIPASEAQRWPQEPQEGVTPKAVKHEHDHDPEHPHYDDKQPDTPRQKHRPEGRHGDGGAQRAAVQSGSKQVELPPYMLGENTGVLKNFTIPKIRKGELGGGDIPEGWKQPCVRLERLEADVDVKKSVKPVVVLQKLSIDEVQRLMRERDSRASKSGKNRLSSGRSGKGGIDPSVLKDLPPELLAEIESTMPLCERVKMNKRKRSTVNERPKYAEDSSEDEEFSSRKRQRKDRDRTWEAEERDRRSSGEHRRGNFDARRGSGSRYDDSDQDSPPPSLNEVARRLKMKQKKRKVYEPKLTPEEMMDSSTFKRFTLSIDNILENLEDVDFTAQDDDEIPQELLLGKQQLNELGSESAKIKAMGITSRIPSDKLVKLLNILEKNILDGASLSTLMNLDNEGEDEERLWRDLIMERVTKSADACLTALNIMTSTHMPKAVYIEDVIERVLQYTKFHLQNTLYPQYDPVYRVNPKGGSMLSSRAKRAKCSTAKQKVIIMLYNKVCDVVSNISELLEIQLMTDTTILQVSSMGITPFFVENVSELQLCAIKLVTAVFSRYEKHRQLILEEIFTSLARLPTSKRSLRNFRLNSSDDEGEPIYIQMVSALVLQLIQCVVHLPADRDSEDDHKKVDDDVFITNSYETARRTAQNFLSVFLKKCGSKQGEEDYRPLFENFVQDLLSTVNKPDWPASELLLSLLGRLLVHQFSNKQTEMALRVASLDYLGTVAARLRKDSVTSRMDQKAIERIIRENTEGDETQRLQKALLDYMDENAETDPALAFARKFYIAQWFRDCTTETEKAMRSQNQKEDDSDGAQHAKELQATGDIMQRAETRKKFLHSVVKSTPNQFTTLRMNSDTVDYDDACLIVRYLASTRPFSQSFDIYLTQILRVLGESAIAVRTKAMKCLSEVVAVDPSILARSDMQRGVHGRLMDNSTSVREAAVELLGRFVLSRPQLTEQYYDMLIERILDTGISVRKRVIKILRDICLEQPNFSKITEMCVKMIRRVNDEEGIKKLVNETFQKLWFTPTPNHDKETMNRKILNITDVVSACKDTGYDWFEQLLQNLLKSEEDSSYKPTRKACVQLVDNLVEHILKYEEALAEHKSVNSTRLVACITTLYLFSKIRAQLMVKHAMTMQPYLTTKCSSQSDFMVICNVAKILELVVPLMDHPSESFLTTIEEDLMKLILKYGMTVVQYCVSCLGAIVNKVTHNYKFVWACFNRYYGALTKLKVQHQEGTNSMALAATKAALLRSLFTAGALCRHFDFDLEQFKGTTKVVIKEKVLELLLYFTNHEDEEVKCKAIIGLGFLFIMHPSQMFVPEVKTLYNGLLSDKRSSITLKIQVLKNLQMYLQEEDTRMQEADREWQKLSKQEDLKEMGDISSGMSSSIMQLYLKQVLESFFHAQSSVRHFALNVIALTLSQGLIHPVQCVPYLIAMGTDAEPTMRNKADQQLVEIDKKYTGFIHMKAVAGMKMSYQVQQAVFGSAGSVIRGFRQDESNSAQCSHLYSMVRANRQHRRAFLISLLNLFDDSSKMEVNMLLFIADNLAYFPYQSQEEPLFIMHHIDITLSVSGSNLLQTFKESLVKIPGRKSRKRRRRRRRPQRQQPPPPPPQQQQQQNGSEEERGAQDEERERHSGDEEYDDDDYEEDEDGHRVRKPKPTEDIRQSESDSDSDLDDVDAVMERLPDDSTSLVDFARASQGILLLLVLKQHLKNLYGFSDGKIQKYSPSESAKVYDKAVNRKTLANFNPQQTIDFLRHHDVHGELTYELKRKIVKQFLDFKLLMEHLDPDEEDEDGDTSANVRNKAITALLGGAAASPRNHHTGDSEEDDERSEGEERTPGASRRGRRTGDSADLLSANMNESVSALDIIAIHCPKYRDRPQIARVIQKNSDGYSIHWMAGSYSSTWAEAKKRDGRKLVPWVDSIKETDIIYKKITLTSGNKLNHKVAQTLRSLYAAKDRNSS
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May play a structural role in chromatin. Involved in sister chromatid cohesion, possibly by facilitating the cohesin complex loading. Transcription factor, which may promote cortical neuron migration during brain development by regulating the transcription of crucial genes in this process (By similarity).
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F6NXI9
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TRNT1_DANRE
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CCA tRNA nucleotidyltransferase 1, mitochondrial (EC 2.7.7.72)
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MWAKLFLRPSFVNRVHLTWSCRALLTMQLKTKEFESLFTDGLVGLAEIFQKNQFELRIAGGAVRDLLSGKRPEDVDFATTATPEEMKSMFQTAGVRMINNKGEKHGTITARLHEENFEVTTLRVDVQTDGRHAEVEFTTDWQKDAERRDLTINSMFLGLDGTLYDYFQGYEDLKNRKVRFVGSASLRIQEDYLRILRYFRFYGRVAAEPGQHEPETLEAIRENARGLAGISGERIWVELKKMLVGNHAGHLLELVYELGLAQYTGLPADGDVEEMKQVWQRAHVSSPKPMTVLAALFRKQADVENLDQRLKVSREEKNLGLFLVKYRRDLVKGHDEHDTMKPYTDFITDSREPDTQSKVLELLKYQGENKLLDELRRWSIPRFPVSGHDLRKLGYTSGKEIGTILQELRDMWKKSRYQMSKDELLSTLSQS
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Nucleotidyltransferase that catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs, which is necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair (By similarity). Promotes tRNA repair and recycling downstream of the ribosome-associated quality control (RQC) pathway by mediating addition of the tRNA 3'-terminal CCA following cleavage by ankzf1 and repair by elac1 (By similarity). Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs and tRNA-like transcripts (By similarity). While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs beginning with GG are marked with CCACCA and rapidly degraded (By similarity). The structural flexibility of RNA controls the choice between CCA versus CCACCA addition: following the first CCA addition cycle, nucleotide-binding to the active site triggers a clockwise screw motion, producing torque on the RNA (By similarity). This ejects stable RNAs, whereas unstable RNAs are refolded while bound to the enzyme and subjected to a second CCA catalytic cycle (By similarity).
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F6Q1T7
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FUT1_BOVIN
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Galactoside alpha-(1,2)-fucosyltransferase 1 (Alpha(1,2)FT 1) (Blood group H alpha 2-fucosyltransferase) (Fucosyltransferase 1) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1) (Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT1) (EC 2.4.1.69) (Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT1) (EC 2.4.1.344)
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MWAPGHHHLCLIFLLTCVFACVFFLLIHQNLFHSGLDLFLPCPDRSRVRSPVAILCLSGTLMNPNATFTCPRHSASVSGTWTIDPKGRFGNQMGQYATLLALAQLNGRQAFIQPSMHAVLAPVFRITLPVLAPEVDRHAPWQELELHDWMSEEYAHLKEPWLKLTGFPCSWTFFHHLRDQIRSEFTLHEHLRQEAQRSLSGLRFPRTGGRPSTFVGVHVRRGDYLQVMPLHWKGVVGDRAYLQQAMDWFRARHKAPIFVVTSNGMKWCRENIDTSRGDVIFAGDGQEGAPNKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTIYLANFTLPDSSFLKIFKPEAAFLPEWVGINADLSPLQ
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Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose residue of glycoconjugates through an alpha(1,2) linkage leading to H antigen synthesis that is an intermediate substrate in the synthesis of ABO blood group antigens. H antigen is essential for maturation of the glomerular layer of the main olfactory bulb, in cell migration and early cell-cell contacts during tumor associated angiogenesis (By similarity). Preferentially fucosylates soluble lactose and to a lesser extent, fucosylates glycolipids gangliosides GA1 and GM1a.
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F6QV99
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ATAD1_BOVIN
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Outer mitochondrial transmembrane helix translocase (EC 7.4.2.-) (ATPase family AAA domain-containing protein 1) (Thorase)
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MVHAETFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDPLNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEESHDEDEIRPVQQQDLHRAIEKMKKSKDAAFQNVLTHVCLD
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Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria (By similarity). Specifically recognizes and binds tail-anchored transmembrane proteins: acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane (By similarity). Also plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory. Required for NMDA-stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane these activities are ATPase-dependent (By similarity).
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F6RG56
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MCLN3_CALJA
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Mucolipin-3 (Transient receptor potential channel mucolipin 3) (TRPML3)
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MANPEIVISSCSSHEEENRCNFNQHTSPSEELLLEDQMRRKLKFFFMNPCEKFWARGRKPWKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTVAFKHLFLKGYIDRMDDTYAVYTQSDVYDQIIFAVNQYLQLYNVSVGNHAYENKGTDQSAMAICQHFYKRGNIYPGNDTFDIDPEIETDCFFVEPDEPFHIGTPAENKLNLTLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIRECKDWHVSGSIQKNTHNMMIFDAFVILTCLVSLILCIRSVISGLQLQQEFVNFFLLHYKKDVSVSDQMEFVNGWYIMIIISDILTIIGSILKMEIQAKSLTSYDVCSILLGTSTMLVWLGVIRYLGFFAKYNLLILTLQAALPNVIRFCCCAAMIYLGYCFCGWIVLGPYHNKFRSLNMVSECLFSLINGDDMFATFAKMQQKSYLVWLFSRIYLYSFISLFIYMILSLFIALITDTYETIKHYQQDGFPETELRTFISECKDLPNSGKFRLEDDPPVSLFCCCKK
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Nonselective ligand-gated cation channel probably playing a role in the regulation of membrane trafficking events. Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity (By similarity). Mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal acidification and is involved in the regulation of membrane trafficking and fusion in the endosomal pathway (By similarity). Does not seem to act as mechanosensory transduction channel in inner ear sensory hair cells. Proposed to play a critical role at the cochlear stereocilia ankle-link region during hair-bundle growth. Involved in the regulation of autophagy. Through association with GABARAPL2 may be involved in autophagosome formation possibly providing Ca(2+) for the fusion process (By similarity). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Possible heteromeric ion channel assemblies with TRPV5 show pharmacological similarity with TRPML3 (By similarity).
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F6SEU4
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SYGP1_MOUSE
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Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1)
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MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDRPGWNPRFCIISGNQLLMLDEDEIHPLLIRDRRSESSRNKLLRRTVSVPVEGRPHGEHEYHLGRSRRKSVPGGKQYSMEAAPAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRSASGDTVFWGEHFEFNNLPAVRALRLHLYRDSDKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTGSGGSGGMGSGGGGGSGGGSGGKGKGGCPAVRLKARYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDISTALRNPNIQRQPSRQSERTRSQPMVLRGPSAEMQGYMMRDLNSSIDLQSFMARGLNSSMDMARLPSPTKEKPPPPPPGGGKDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGDGPGGRLNSSSVSNLAAVGDLLHSSQASLTAALGLRPAPAGRLSQGSGSSITAAGMRLSQMGVTTDGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSSGHGPPSSHHHHHHHHHHRGGEPPGDTFAPFHGYSKSEDLSSGVPKPPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQITIGPQRPAPSGPGGGSGGGSGGGQPPPLQRGKSQQLTVSAAQKPRPSSGNLLQSPEPSYGPARPRQQSLSKEGSIGGSGGSGGGGGGGLKPSITKQHSQTPSTLNPTMPASERTVAWVSNMPHLSADIESAHIEREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQERQLPPLGPTNPRVTLAPPWNGLAPPAPPPPPRLQITENGEFRNTADH
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Major constituent of the PSD essential for postsynaptic signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of the NMDAR signaling complex in excitatory synapses, it may play a role in NMDAR-dependent control of AMPAR potentiation, AMPAR membrane trafficking and synaptic plasticity. Regulates AMPAR-mediated miniature excitatory postsynaptic currents. Exhibits dual GTPase-activating specificity for Ras and Rap. May be involved in certain forms of brain injury, leading to long-term learning and memory deficits (By similarity).
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F6SZT2
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KHDC3_MACMU
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KH domain-containing protein 3 (ES cell-associated transcript 1 protein) (KHDC3-like protein)
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MDTPRRFPTLVQLMQPKAMPVEVLGHLPKRFSWFHSEFLKNPKVVRLEVWLVEKIFGRDRERIPHVQGMSQILIHVNRLDPNGEAEILVFGRPSYQEDTIKMIMNLADYHRQLQAKGSGKALAQDVATKKAEIQLSSTEVREAGTQRSVEVREVGTQGSPVEVRETGTQQSLEAANQSGTQRSPEAASKAVTQRFSEDTRAPVTRL
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As part of the OOEP-KHDC3 scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart. Regulates homologous recombination-mediated DNA repair via recruitment of RAD51 to sites of DNA double-strand breaks, and sustainment of PARP1 activity, which in turn modulates downstream ATM activation. Activation of ATM or ATR in response to DNA double-strand breaks may be cell-type specific (By similarity). Its role in DNA double-strand break repair is independent of its role in restarting stalled replication forks (By similarity). As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for maintenance of euploidy during cleavage-stage embryogenesis (By similarity). Required for the formation of F-actin cytoplasmic lattices in oocytes which in turn are responsible for symmetric division of zygotes via the regulation of mitotic spindle formation and positioning (By similarity). Ensures proper spindle assembly by regulating the localization of AURKA via RHOA signaling and of PLK1 via a RHOA-independent process (By similarity). Required for the localization of MAD2L1 to kinetochores to enable spindle assembly checkpoint function (By similarity). Promotes neural stem cell neurogenesis and neuronal differentiation in the hippocampus. May regulate normal development of learning, memory and anxiety (By similarity). Capable of binding RNA (By similarity).
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F6TQD1
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RN212_MOUSE
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Probable E3 SUMO-protein ligase RNF212 (EC 2.3.2.-) (Probable E3 SUMO-protein transferase RNF212) (RING finger protein 212)
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MASWVFCNRCFQSPHRKSSFSLTSCGHVYCHSCLLKGTKNECVICQAPCQTVLLSKHTNSNIQTFFLGIDGLCKKYSQETSQISEFQEKHRRRLVAFYQEKISQLEESLRKSVLQIKQLQSMRSSQQPAFNKIKNSVSTKPNGYLFLPPNSSLPDRIESMDIDLTPPARKPEMSAGPSRISVISPPQDGRMGSVTCRGPQHLSLTPSHASMTKASRVPPLQMPYKELSPPPASQLSSRATQGPSPSVSSSWTGPPRQPISISGLLQRQCAGSASPRGMDTEKMSPFLPSTPTNLRSVASPWHACVHR
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SUMO E3 ligase that acts as a regulator of crossing-over during meiosis: required to couple chromosome synapsis to the formation of crossover-specific recombination complexes. Localizes to recombination sites and stabilizes meiosis-specific recombination factors, such as MutS-gamma complex proteins (MSH4 and MSH5) and TEX11. May mediate sumoylation of target proteins MSH4 and/or MSH5, leading to enhance their binding to recombination sites. Acts as a limiting factor for crossover designation and/or reinforcement and plays an antagonist role with CCNB1IP1/HEI10 in the regulation of meiotic recombination.
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F6UA42
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UHRF1_XENTR
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E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)
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MWIQVRTMDGRDTRRIDSLSKLTKVEDLRARIQQIFGVALESQRLFYRGKQMENGHTLFDYSVGLNDIVQLLVRQIPDSVPTKDKECGISDADSGCGSGQGESDKNSSCGEGATDVDGQPAGINSENVGPSLYKKNDLVDARDLNMGAWFEAQIVSVSKRVNPDGMSAEILDTSAASDDIIYHVKYEDYPENGVVQLTYKDVRLRARTTLPWHDLKVGQVVMVNYNPDEPKERGYWYDAEILRKRETRTIKEIYVKVLLGDAGDSLNDCRIRFVDEIYKIEEPGSAYITTESPQKRQNGPECKHCKDNPKRACRMCACYVCGGKQDPEKQLLCDECDMAFHIYCLKPPLSAIPQDEDWYCPDCRNDASEVVLAGEKLKESKKKAKMASASSSSQRDWGKGMACVGRSRECTIVPSNHYGPIPGVPVGTLWKFRVQVSESGVHRPHVAGIHGRSNDGSYSLVLAGGYEDDVDNGSEFTYTGSGGRDLSGNKRTAEQSCDQKLTNMNRALALNCSAPINDKEGAVAKDWRAGKPVRVVRNTKGKKHSKYAPEDGNRYDGIYKVVKYWPEKGKSGFLVWRYLLRRDDEEPAPWSKEGKERIKKLGLVMQYPDGYLESLASKEREKENKTEDELSESPSKGKRKRNSAGSGLSDAKSTPKKTKVESYKLSLDQKTLIKQDDLNAKLWREVMSFLKEGPKFLSKVEETFLCICCQEVVYEPITTECHHNICKGCLDRSFKALVHNCPACRHDLGKNYSLNVNKPLQAILSQLFPGYERGR
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Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits dnmt1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins. However, it is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo.
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F6UH96
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SPRTN_XENTR
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DNA-dependent metalloprotease SPRTN (EC 3.4.24.-) (Protein with SprT-like domain at the N terminus) (Spartan)
|
MQLSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGIEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVQTLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINKRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGEFVKIKEPENYSQKRKRNNDPTKSELGNSSHVKINKGKSNGVDIRTVIPFSGTGYKLFEPSKSDAQLKIQNDNPTKDKAVMHHTPPSTNQTDSTFLSRKIVSAKKISVANTKVFINLNGSPIKLPSSSNNKSHQDSSKQKSVLHFFKTQKDNSIDLTSSSQSFPSTSQGPNREETEHFYKKLQMDDKESKDTFIIHSLNKTNVSDSLNNKSCAGPAATINSGLNHTKVCCPVCGTEIFESKINDHLDTCLQNYNT
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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 (By similarity). 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. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as top1, top2a, histones H3 and H4 (By similarity). 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 (By similarity). 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 (By similarity).
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F6VAN0
|
ATF6A_MOUSE
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Cyclic AMP-dependent transcription factor ATF-6 alpha (cAMP-dependent transcription factor ATF-6 alpha) (Activating transcription factor 6 alpha) (ATF6-alpha) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 alpha]
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MESPFSPVLPHGPDEDWESTLFAELGYFTDTDDVHFDAAHEAYENNFDHLNFDLDLMPWESDLWSPGSHFCSDMKAEPQPLSPASSSCSISSPRSTDSCSSTQHVPEELDLLSSSQSPLSLYGDSCNSPSSVEPLKEEKPVTGPGNKTEHGLTPKKKIQMSSKPSVQPKPLLLPAAPKTQTNASVPAKAIIIQTLPALMPLAKQQSIISIQPAPTKGQTVLLSQPTVVQLQSPAVLSSAQPVLAVTGGAAQLPNHVVNVLPAPVVSSPVNGKLSVTKPVLQSATRSMGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLGLEARLKAALSENEQLKKENGSLKRQLDEVVSENQRLKVPSPKRRAVCVMIVLAFIMLNYGPMSMLEQESRRVKPSVSPANQRRHLLEFSAKEVKDTSDGDNQKDSYSYDHSVSNDKALMVLSEEPLLYMPPPPCQPLINTTESLRLNHELRGWVHRHEVERTKSRRMTNSQQKARILQGALEQGSNSQLMAVQYTETTSISRNSGSELQVYYASPGSYQGFFDAIRRRGDTFYVVSFRRDHLLLPATTHNKTTRPKMSIVLPAININDNVINGQDYEVMMQIDCQVMDTRILHIKSSSVPPYLRDHQRNQTSTFFGSPPTTTETTHVVSTIPESLQ
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[Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR).
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F6W2R2
|
DMRT3_HORSE
|
Doublesex and mab-3 related transcription factor 3
|
MNGYGSPYLYMGGPVSQPPRAPLQRTPKCARCRNHGVLSWLKGHKRYCRFKDCTCEKCILIIERQRVMAAQVALRRQQANESLESLIPDSLRALPGPPPPGDAAAAAPQPPPTSQPSQPPPPQRPAAELAAAAALRWATEPQPGALQAQLAKPDLTEERLGDGSSADNTETFSDKDTDQRSSPDVVKSKGCFTPESPEVVSVDEGGYAVQKNGGTSESRPDSPKYHGEQNHLLIEGPSGTVSLPFSLKANRPPLEVLKKIFPNQKPTVLELILKGCGGDLVSAVEVLLSSRSSASAADRTSAEPESLVLPSNGHIFEHTLSSYPISSSKWSVGSAFRVPDTLRFSADSSNVVPNPLAVPLQHPFPQPPRYPLMLRNTLARNQSSPFLPNDVTLWNTMTLQQQYQLRSQYVSPFPGSSPSVFRSSPVLPTRAPEDPRISIPDDGCPIVSKQSLYTEDDYDERSDSSDSRILNTSS
|
Probable transcription factor that plays a role in configuring the spinal circuits controlling stride in vertebrates. Involved in neuronal specification within a specific subdivision of spinal cord neurons and in the development of a coordinated locomotor network controlling limb movements. May regulate transcription during sexual development.
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F6Y5S8
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IMPA3_CALJA
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Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase (Golgi-resident PAP phosphatase) (gPAPP) (EC 3.1.3.7) (3'(2'), 5'-bisphosphate nucleotidase 2) (Inositol monophosphatase domain-containing protein 1) (Myo-inositol monophosphatase A3) (Phosphoadenosine phosphate 3'-nucleotidase)
|
MAPMGIRLSPLGVAVFCLLGLGVLYHLYSGFLAGRFSLFGLGGEPAGGAAGPPAAADGGTVDLREMLAVSVLAAVRGGDEVRRVRESNVLHEKSKGKTREGADDKMTSGDVLSNRKMFYLLKTAFPSVQINTEEHVDAADQEVILWDHKIPEDILKEVTAPKEVPAESVTVWIDPLDATQEYTEDLRKYVTTMVCVAVNGKPVLGVIHKPFSEYTAWAMVDGGSNVKARSSYNEKTPRIVVSRSHSGMVKQVALQTFGNQTTIIPAGGAGYKVLALLDVPDKSQEKADLYIHVTYIKKWDICAGNAILKALGGHMTTLSGEEISYTGSDGIEGGLLASIRMNHQALVRKLPDLEKMGH
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Exhibits 3'-nucleotidase activity toward adenosine 3',5'-bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. Has no activity toward 3'-phosphoadenosine 5'-phosphosulfate (PAPS) or inositol phosphate (IP) substrates including I(1)P, I(1,4)P2, I(1,3,4)P3, I(1,4,5)P3 and I(1,3,4,5)P4.
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F6ZDS4
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TPR_MOUSE
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Nucleoprotein TPR (NPC-associated intranuclear protein) (Translocated promoter region and nuclear basket protein)
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MTSGGSASRSGHRGVPMTSRGFDGSRRGSLRRAGARETASEAADGAAPAAGLRASPCSLASPSAAAAVAAIPADMAAVLQQVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVTETRECQNLRLELEKLNNQVKVLTEKTKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVAVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVLRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEANKTIQDHLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKQENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSSVLERDNQRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALRELGETREREEQETTSSKIAELQHKLENSLAELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLLSTPKRSSTSQTVSTPAPEPVIDSTEAIEAKAALKQLQEIFENYKKEKIDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLNSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTEINLHLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSTSNVEQYRAMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLSELKKTLSTVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMTSIRQHLEETTQKAESQLLECKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKDAVQAPLNVSLNEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNVEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQQLINQQKDPDTEEYRKLLSEKEIHTKRIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLREDLSKARTEKEGIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQFEELKAQQNKAMETSTQSSGDHQEQHISVQEMQELKDTLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTVQLQSELSRLRQDLQDKTTEEQLRQQMNEKTWKTLALAKSKITHLSGVKDQLTKEIEELKQRNGALDQQKDELDVRMTALKSQYEGRISRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGNASGSVRSTSPNVQPSISQPILTVQQQTQATAFVQPTQQSHPQIEPTNQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTMEAGDQVSEDTVEMPLPKKLKMVTPVGTEEEVMAEESTDGEAETQAYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTSSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDDDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGAESHQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETAAGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGISHAMGGRGGINRGNIN
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Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Plays a limited role in the regulation of nuclear protein export. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Also plays a role as a structural and functional element of the perinuclear chromatin distribution involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity).
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F7B113
|
SL9A9_HORSE
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Sodium/hydrogen exchanger 9 (Na(+)/H(+) exchanger 9) (NHE-9) (Sodium/hydrogen exchanger) (Solute carrier family 9 member 9)
|
MERQRRFMSEKDEYQFQHQGAVELLVFNFLLILTILTIWLFKNHRFRFLHETGGAMVYGLIMGLILRYATAPTDIESGTVYDCGKLAFSPSTLLINITDQVYEYKYKREISQHNINPHLGNAILEKMTFDPEIFFNVLLPPIIFHAGYSLKKRHFFQNLGSILTYAFLGTAISCIVIGLIMYGFVKAMVYAGQLKNGDFHFTDCLFFGSLMSATDPVTVLAIFHELHVDPDLYTLLFGESVLNDAVAIVLTYSISIYSPKENPNAFDAAAFFQSVGNFLGIFAGSFAMGSAYAVVTALLTKFTKLCEFPMLETGLFFLLSWSAFLSAEAAGLTGIVAVLFCGVTQAHYTYNNLSLDSKMRTKQLFEFMNFLAENVIFCYMGLALFTFQNHIFNALFILGAFLAIFVARACNIYPLSFLLNLGRKHKIPWNFQHMMMFSGLRGAIAFALAIRDTESQPKQMMFSTTLLLVFFTVWVFGGGTTPMLTWLQIRVGVDLDEDLKERPSSHQEANNLEKSTTKTESAWLFRMWYGFDHKYLKPILTHSGPPLTTTLPEWCGPISRLLTSPQAYGEQLKEDDAECIVNQDELAMNYQEQAASPCSPPTRLGLDQKAAPQTPGKENIYEGDLGLGGYELKLEQTPGQSQLN
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Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A9 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Regulates organellar pH and consequently, endosome maturation and endocytic trafficking of plasma membrane receptors and neurotransporters (By similarity). Promotes the recycling of transferrin receptors back to the cell surface to facilitate additional iron uptake in the brain (By similarity). Regulates synaptic transmission by regulating the luminal pH of axonal endosomes. Regulates phagosome lumenal pH, thus affecting phagosome maturation, and consequently, microbicidal activity in macrophages. Can also be active at the cell surface of specialized cells, e.g., in the inner ear hair bundles uses the high K(+) of the endolymph to regulate intracelular pH (By similarity).
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F7B909
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STAR3_MACMU
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StAR-related lipid transfer protein 3 (Metastatic lymph node gene 64 protein) (MLN 64) (START domain-containing protein 3) (StARD3)
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MSKLPGELARDLECSLPAVASLGSSLSHSQSLSSHLLPPPEKRRAISDVRRTFCLFVTFDLLFISLLWIIELNTNTGIRKNLEQEIIQYNFKTSFFDIFVLAFFRFSGLLLGYAVLRLQHWWVIAVTTLVSSAFLIVKVILSELLSKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAAQAAVARGPLLFSGALSEGQFYSPPESFAGSDNESDEEVAGKKSFSAQEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQILQRVEDNTLISYDVSAGAAGGMVSPRDFVNVRRIERRRDRYLSSGIATAHSAKPLTHKYVRGENGPGGFVVLKSASNPCVCTFVWILNTDLKGRLPRYLIHQSLAATMFEFAFHLRQRISELGARA
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Sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes. The sterol transport mechanism is triggered by phosphorylation of FFAT motif that leads to membrane tethering between the endoplasmic reticulum and late endosomes via interaction with VAPA and VAPB. Acts as a lipid transfer protein that redirects sterol to the endosome at the expense of the cell membrane and favors membrane formation inside endosomes. May also mediate cholesterol transport between other membranes, such as mitochondria membrane or cell membrane. However, such results need additional experimental evidences probably mainly mediates cholesterol transport from the endoplasmic reticulum to endosomes. Does not activate transcriptional cholesterol sensing. Able to bind other lipids, such as lutein, a xanthophyll carotenoids that form the macular pigment of the retina (By similarity). Able to bind other lipids, such as lutein, a xanthophyll carotenoids that form the macular pigment of the retina.
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F7BJB9
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MORC3_MOUSE
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MORC family CW-type zinc finger protein 3 (Nuclear matrix protein 2) (Zinc finger CW-type coiled-coil domain protein 3)
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MAAQPPTGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAMVFTKNGETMSVGFLSQTYLEVIKAEHVVVPIVTFNKHRQMINLTESKASLAAILEHSLFSTEQKLLAELNAIMGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDETAGRKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIIIRGQKVKTQLVSKSLAYIERDVYRPKFLTRTVRITFGFNCRNKDHYGIMMYHKNRLIKAYEKVGCQLKANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTILALGEKLNDYWNEMKVKKNAEYPVNLPVEDIQKRPDQTWVQCDACLKWRKLPDGIDQLPEKWYCSNNPDPQFRNCEVPEEPEDEDLVHPTYEKTYKKTSKERFRIRQPEILPRILPQINPELLYQTSVSSQSFSPVKESVPRPHLSEVTSPFAARIINLNLASPASEPENSSMKRKLGVHSSILNAKTRRLSNPPVENSSYKNDDDEDVIILEENSTPKPAVDLEVKSDIEVKSEQSHTEQSGIHVDLVSSPKPCVQASSTSTSTSRSDPGITVSTQTDAPGLTVKKEESMEEDMGVRNGTATLSCVGTEAKVQETSAESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDKCVKKEKCHQSTETDAVFLLDSVNGQAESLDHLGSQYQQALQEIERLKRQCSALQQVKSECSQASCTESKSEVDEMAVQLDDVFRQLDKCTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEEPVSYVDGESLKLRSLRVNVGQLLAMIVPDLDLQQVNYDVDVVDEILGQVVEQMSEISST
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Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response. Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function. Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity. Binds RNA in vitro. Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3. The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0.
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F7BWT7
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TSN15_MOUSE
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Tetraspanin-15 (Tspan-15) (Transmembrane 4 superfamily member 15)
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MPRGDSEQVRYCARFSYLWLKFSLIIYSTVFWLIGGLVLSVGIYAEAERQKYKTLESAFLAPAIILILLGVVMFIVSFIGVLASLRDNLCLLQSFMYILGICLVMELIGGIVALIFRNQTIDFLNDNIRRGIENYYDDLDFKNIMDFVQKKFKCCGGEDYRDWSKNQYHDCSAPGPLACGVPYTCCIRNTTDVVNTMCGYKTIDKERLNAQNIIHVRGCTNAVLIWFMDNYTIMAGLLLGILLPQFLGVLLTLLYITRVEDIILEHSVTDGLLGPGAKSRTDTAGTGCCLCYPD
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Regulates maturation and trafficking of the transmembrane metalloprotease ADAM10. Promotes ADAM10-mediated cleavage of (CDH2). Negatively regulates ligand-induced Notch activity probably by regulating ADAM10 activity (By similarity).
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F7D4X9
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SIR5_MONDO
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NAD-dependent protein deacylase sirtuin-5, mitochondrial (EC 2.3.1.-) (Regulatory protein SIR2 homolog 5) (SIR2-like protein 5)
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MSLLHFATRRLILQVLRELGLKAPPVHKTLKICIAMSRPSSNMADFRRFFARAKHIAIITGAGVSAESGVPTFRGPGGFWRKWKAEDLATPEAFAQNPSLVWEFYHYRREVILKKHPNAAHVAIAACEERLSLQGRRVVVITQNIDEFHTKAGTKNILELHGSLFKTRCCSCGNVRVNYNNPICPALEGKGLPDPNAPDAQIPLENLPRWKTTGDFSVLFLLDASPLYPSNLSCSHPVGAPALSEVADLGRWVGTSSLVYPAGMFGPHVALRGIPVAEFNTVTTPVTQNFRFHFSGLCGTTIPEALSPHESEKTG
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NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinylation. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX. {ECO:0000255|HAMAP-Rule:MF_03160}.
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F7E540
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TTLL7_XENTR
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Tubulin polyglutamylase TTLL7 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 7)
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MPSLPNESDHQATCSLSLHSDLPYQPSSSIKRKVRKKKKNGAITANVVGTKYEIVRLVTEEMMFTKARDDDETANLIWNDCAVQHEKIAELRNYQRINHFPGMGEICRKDCLARNMTKMIKCQPHEYNFIPRTWIFPAEYTQFQTYIKELKKKRRQKTFIIKPANGAMGHGISLTRNGEKLQAQDHLIVQEYLEKPFLLESYKFDLRIYILVTSCDPLRIFLYNDGLVRMGTEKYHPPSESNLSQLYMHLTNYSVNKHNENFERDETENRGSKRSIKWFTEFLRANDYDISKFWNDISDLVVKTLIVAEPHVLHAYRMCRPGQHPTSESVCFEVLGFDIILDRKLKPWLLEINRAPSFGTDQKIDHDVKKGVLLNALKLLNIRASDKKKNLAKQKAEAQKRLYGQGSMKRLSPASSDWEKQRHTLERRKEELKERLAQVRKQISREEYENRHLGNYRRIYPPEDKLLLEKYEGLLATAFQTFLAGRAASLQREMNNPLKRMKEEDILDLLEQCELDDEKLSGKPTRPKEPRTLSSMPESTQTLKKLKNYSSHSSSNSTGSSSDTEEEEDEKEGKEKKVSYDLEEHKYKSLERSSRIHWKPPLKAARPFSNSSSPSSAASMRRSVSCPRSITALNTQSPTTDQRPFSSRISSTITRPLSGNRTNSLNRSSSSNRVPQSGTSGSVYPSISESRLDHLTKEQEEELTKQTLYALRDMRIRIPGKGVEEITHSHIDEIMDNWTYHKSKVASYWLIKLDSVKQRKVLDIVRTNIRSVLQRIWKVSDVECLHIYRSFNRVFNRLLWNHGQGLWSCFSNSGTSWETIFCKSTEVVTPQQFQCCQRLVQLCKDCLLAVYKYATDSRVAGMSPDWDDSRYLFPVVPQFTMKSSSSGVNCSSSRLPRSSILFNPRHNHY
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Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction. Preferentially modifies the beta-tubulin tail over an alpha-tail. Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions.
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F7EQ49
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GPER1_MACMU
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G-protein coupled estrogen receptor 1 (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30)
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MEVTSQARGMGLEMYPGTMQPAAPNTTSPELNLSHPLLGASLANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHEQYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALARAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRVLVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLNPLIYSFLGETFREKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV
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G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells (By similarity). Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. {ECO:0000250, ECO:0000269|PubMed:19131510}.
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F7EZ75
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SIR5_MACMU
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NAD-dependent protein deacylase sirtuin-5, mitochondrial (EC 2.3.1.-) (Regulatory protein SIR2 homolog 5) (SIR2-like protein 5)
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MRPLQIVPSRLISQLYCGLKPPASTRNQICLKMARPSSSMADFRKCFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPLAFAHNPSRVWEFYHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKAGTKNLLEIHGSLFKTRCTSCGIVAENYKSPICPALSGKGAPEPGTQDASIPVEKLPRCEEAGCGGLLRPHVVWFGENLDPAILEEVDKELGRCDLCLVVGTSSVVYPAAMFAPQVAARGVPVAEFNTETTPATNRFRFHFQGPCGTTLPEALARHENETVS
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NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinylation. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX. {ECO:0000255|HAMAP-Rule:MF_03160}.
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F7FIH8
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NNRE_MONDO
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NAD(P)H-hydrate epimerase (EC 5.1.99.6) (Apolipoprotein A-I-binding protein) (AI-BP) (NAD(P)HX epimerase)
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MSGLRTLLGLGLLVSSSRFPRVVARGGPRCPGPAWWAARPMHLGDSTMAGGTVKYLSQEEAQAVDEELFNEYKFSVDQLMELAGLSCATAIAKAYPLSSFGSNPPAVLVICGPGNNGGDGLVCARHLKLFGYEPKIHYPKKPNKPLFDALVTQCQKMDIPFLPEVPPEPMLIDELYELVVDAIFGFSFKGAVREPFGTILSIMNGLTVPIASIDIPSGWDVEKGNPEGIRPDLLISLTAPKKAATLFKGRHHYLGGRFVPSDLEKKYQLNLPPYPGTDCVLQLQ
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Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (By similarity).
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F7FQM7
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APOA1_MACMU
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Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I]
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MKATVLTLAVLFLTGSQARHFWQQDEPPQTPWDRVKDLVTVYVEALKDSGKDYVSQFEGSALGKQLNLKLLDNWDSVTSTVSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELHEGTRQKLHELHEKLSPLGEEVRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKASEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLSTQ
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Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
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F7HUS6
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APOA1_CALJA
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Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I]
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MKAAVLTLAMLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDSVKESGKDYVSQFESSMLGKQLNLKLLDNWDSLTSTVNKLREQLGPVTQEFWENLEKETEVLRQEMSKDLEEVKAQVQPYLDDFEKKWEEEMKLYSQKLEPLRTELQEGALQKLQDLQEKLSSLGEQVRDRARVHVDTLRTQLAPYSDKLRQRLATRLEALKESGGASLAEYHAKASEHLSTLGEKAKPLLEDLRQGLLPVLESFKASFLSALEEYTKLSSQ
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Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
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F7IX06
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PETH2_THEAE
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Cutinase est2 (EC 3.1.1.74) (Poly(ethylene terephthalate) hydrolase) (PET hydrolase) (PETase) (EC 3.1.1.101) (TaCut2)
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MSVTTPRRETSLLSRALRATAAAATAVVATVALAAPAQAANPYERGPNPTESMLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAIAISPGYTGTQSSIAWLGERIASHGFVVIAIDTNTTLDQPDSRARQLNAALDYMLTDASSAVRNRIDASRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKSWRDITVPTLIIGAEYDTIASVTLHSKPFYNSIPSPTDKAYLELDGASHFAPNITNKTIGMYSVAWLKRFVDEDTRYTQFLCPGPRTGLLSDVEEYRSTCPF
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Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (By similarity). Can also depolymerize the synthetic polyesters poly(epsilon-caprolactone) (PCL), poly(butylene succinate-co-adipate) (PBSA), poly(butylene succinate) (PBS), and poly(lactic acid) (PLA).
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F7J0M4
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RGA4R_ORYSJ
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Disease resistance protein RGA4 (Os11gRGA4) (SasRGA4)
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MEAALLSGFIKAILPRLFSLVDDKHKLHKGVKGDIDFLIKELRMIVGAIDDDLSLDHPAAAAVQTLCMEDLRELAHGIEDCIDGVLYRAARDQQQSPVRRAVQAPKKLQRNLQLAQQLQRLKRMAAEANQRKQRYTAAAPGQHGQVYSSAAAQVDEPWPSCSSASDPRIHEADLVGVDADREELLEQLAERQPEQLKVIAIVGFCGLGKTALAAEAYNRETGGGRFERHAWVCAGHRSAREVLGELLRRLDADGRSFHGDSDAGQLCVDIRQQLEKNRYFIVIDDIQTEDQWKSIKSAFPTDKDIGSRIVVTTTIQSVANACCSANGYLHKMSRLDKNCSKQLLSKKACPERYSHYKQPDSAAILKKCDGQPLALVTIGEFLQANGWPTGPNCEDLCNRLHYHLENDKTLERMWRVLVRNYTSLPGHALKACLLYFGMFPSDHPIRRKSLLRRWLAEGFVEPLSSSSNIDSTAAFNVLMDRNIIEPINVSNNDKVKTCQTYGMMREFISHMSISQNFVTFFCDDKFVPKYVRRLSLHGDTVVNGDNFNGIDLSLVRSLAVFGEAGTTVLDFSKYQLLRVLDLEKCDDLKDDHLKEICNLVLLKYLSLGGNISKLPKDIAKLKDLEALDVRRSKVKIMPVEVFGLPCLIHLLGKFKLSDKVKQKTEVQEFLLKGKSNLQTLAGFASNGSEGFLHLMRYMNKLRKLKIWCTSSAGSTDWTDLREAIQQFILDEKEANIGTRSLSLHFSGCSEDAINSLKEPCYLSSLKLHGNFPQLPQFVTSLRGLKELCLSSTKFTTGLLEALSNLSYLQYLKLVADELEKFIIKVQGFPRLLRLCIVLQYPTFPVIEEGALPFLVTLQLLCKDLHGLSDIQIECFKHLQEVTLHSGVTPATRQEWVKAAKEHPNRPKVLLLKSVDTAESEHTDVDSVMEAVKSETTEYSIAPEGPEQVNNKMQLDHGLESSSVLNKQNNFADQSSSKDQLHYSFNNMGLSDVSCCE
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Disease resistance (R) protein. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Contribution of RGA5 is required to recognize the effector avirulence proteins AVR-Pia and AVR1-CO39 from M.oryzae. Acts as a constitutively active cell death inducer that is repressed by RGA5. Immune response triggered by the RGA4-RGA5 -mediated recognition of AVR1-CO39 confers resistance to X.oryzae pathovars.
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F7J0N2
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RGA5R_ORYSJ
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Disease resistance protein RGA5 (Os11gRGA5) (SasRGA5)
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MDAPASFSLGAMGPLLRKLDSLLVAPEIRLPKPLKEGIELLKEDLEEIGVSLVEHSVVDSPTHKARFWMDEVRDLSYHIEDCIDTMFSMRSGGDDGKPRSERRHKVGRAKIDGFSKKPKPCTRMARIAELRALVREASERLERYQLGDVCGSSSPVVFTADGRARPLHHGVSANLVGVDEFKTKLNRWLSDEEGPHLKVAAIVGPAGIGKTALATELYRDHRWQFECRAFVRASRKPDMQRLLGGILSQVQRRQRSSDAYADSTVQSLIDNLREHLQDRRYLIIIDGLWETAVWNIANSAFPDVNSFSRILITADIEQVALECCGYKYDYIMRMEPLGSLDSKKVFFNKVFGSEDQCPPELKEVSNTILEKCGGLPLAIISIAGLLGSQPENPVLWDYVTKYLCSSLGTNPTLKDVVKETLNLSYNSLPHPFKTCLLYLGMYPDGHIMLKADLMKQWSAEGFVSANEAKDTEEIVDKYFDELVNRGILEPVEINKNGKVLSCTLHHAVHDLVMPKFNDDKFTMSVDYSQTITGPSTMVRRLSLHFSSTRYATKPAGIILSRVRSLAFFGLLNCMPCIGEFKLLRVLILEFWGSHGEQRSLNLIPVCRLFQLRYLKTSGDVVVQLPAQISGLQYLETLEIDARVSAVPFDLVHLPNLLHLQLQDETKLPDGIGCMRSLRTLQYFDLGNNSVDNLRGLGELTNLQDLHLSYSAPSSNEGLMINLNAITSSLSRLSNLKSLILSPGAISMVIFFDISSIISVVPVFLQRLELLPPICIFCRLPKSIGQLHKLCILKVSVRELLTTDIDNLTGLPSLTVLSLYAQTAPEGRFIFKDGTLPVLKYFKFGCGELCLAFMAGAMPNLQRLKLVFNIRKSEKYRHTLFGIEHLVSLQDIATRIGVDTSTGESDRRAAESAFKETVNKHPRCLRSSLQWVVSTEEESHPLEKQHHKREKGSSAGHGVLEKESVEDSEKNTDRVQTLLSPQLSNMESVVESALTGQRTKIVVKVHMPCGKSRAKAMALAASVNGVDSVEITGEDKDRLVVVGRGIDPVRLVALLREKCGLAELLMVELVEKEKTQLAGGKKGAYKKHPTYNLSPFDYVEYPPSAPIMQDINPCSTM
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Disease resistance (R) protein that recognizes the AVR-Pia and AVR1-CO39 effector avirulence proteins from M.oryzae. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Contribution of RGA4 is required to recognize the effector avirulence proteins AVR-Pia and AVR1-CO39 from M.oryzae. Acts as a repressor of the RGA4-mediated cell death activation. Upon infection, recognition and binding of the AVR effectors relieve the RGA5-mediated repression and triggers the hypersensitive response. Immune response triggered by the RGA4-RGA5 -mediated recognition of AVR1-CO39 confers resistance to X.oryzae pathovars.
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F8G0M4
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HSPB_PSEP6
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6-hydroxy-3-succinoylpyridine 3-monooxygenase HspB (EC 1.14.13.163) (6-hydroxy-3-succinoylpyridine hydroxylase) (HSP hydroxylase)
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MSMKQRVIIVGGGPVGLLTALGLAKAGTNVVVLEAESQPSDSPRALVYHFPVLPHLKRLGVLDDCVAAGLMRQNFAWRVHSTSEMIFWDLSCLEGDVELPYALHLGQDKLSRILIEHLKALPNVEVRYSSPVVDCEVGPRSVRVVLGGESPGVIVEGDWLIGADGANSFVRREVLNQNFFGITWPQRYVATNTRFDFDKLGFGKTTMQVDDVYGSVICNIDADSLWRVTFMEDPNLPMEGIRGRIDQVFKELLPTNDPYEVVAFSPYRMHQRVTDRMRNGRVILIGDAAHVTNPTGGLGLTGGMFDAFALTSVLNQVIHDGRSEDILDVFEADRRRKFIELVSPRASDNLRNLYHQKPGEGKNDWVNNTRSISKDIDRMRDALRFPETMETFL
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Involved in the nicotine degradation. Catalyzes the cleavage of 6-hydroxy-3-succinoylpyridine (HSP) by incorporation of oxygen at the 3-position to produce to 2,5-dihydroxypyridine (DHP) and succinic semialdehyde.
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F8J4S0
|
TOP4A_OXYTA
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Oxyopinin-4a (Oxt-4a)
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MKISQVFIFVFLLMISVAWANEAYEEESNYLSERFDADVEEITPEFRGIRCPKSWKCKAFKQRVLKRLLAMLRQHAF
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Disrupts cell membranes through the formation of pores (Probable). Has antibacterial activity against Gram-positive bacteria S.aureus (MIC=10 uM) and B.subtilis (MIC=0.5 uM) as well as Gram-negative bacteria P.fluorescens (MIC=1 uM) and E.coli (MIC=0.5 uM). Has hemolytic activity against human erythrocytes (EC(50)=7 uM).
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F8KAY7
|
RSAKS_PSESP
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(R)-specific secondary-alkylsulfatase ((R)-specific sec-alkylsulfatase) (EC 3.1.6.19) (Inverting sec-alkylsulfatase Pisa1) (Inverting secondary alkylsulfatase 1) (Type III (R)-specific secondary-alkylsulfatase)
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MSRFIRASQRRTLLATLIAATLAQPLLAAESLDSKPASAITAAKNAEVLKNLPFADREEFEAAKRGLIAPFSGQIKNAEGQVVWDMGAYQFLNDKDAADTVNPSLWHQAQLNNIAGLFEVMPKLYQVRGLDPANMTIIEGDSGLVLIDTLTTAETARAALDLYFQHRPKKPIVAVVYSHSHIDHFGGARGIIDEADVKAGKVKVFAPSGFMEHAVSENILAGTAMARRGQYQSGVMVPRGAQAQVDSGLFKTTATNATNTLVAPNVLIEKPYERHTVDGVELEFQLTLGSEAPSDMNIYLPQFKVLNTADNAPPAMHNLLTPRGAEVRDAKAWAGYIDASLEKYGDRTDVLIQQHNWPVWGGDKVRTYLADQRDMYAFLNNRALNLMNKGLTLHEIAAEVSKLPGELDRKWYLRSYYGALSTNLRAVYQRYLGFYDGNPANLDPFPPVEAGKRYVEAMGGADAVLKQMRAAIDKGDYRWAVQLGNHLVFADPANKDARALQADAMEQLGYQTENALWRNMYMTGAMELRHGVPTYDSRGKSEMGRALTPDMFFDLLAIRLDTDKAVGHDMTLNWVFEDLKQDIALTLRNGVLTQRVGSLNPKADVTVKLTKPTLDQIAARKLDLPTAIKQGTVKLDGDGKKLGEFFGLLDSFSPKFNIVEPLE
|
Alkylsulfatase that catalyzes the enantioselective hydrolysis of secondary-alkylsulfates with strict inversion of configuration, leading to the formation of homochiral (S)-configurated alcohols and nonreacted sulfate esters (PubMed:21770430, Ref.2, PubMed:23061549). The substrate spectrum includes a range of linear, branched or cyclic sec-alkylsulfates. Can use sec-alkylsulfate esters bearing aromatic, olefinic and acetylenic moieties (Ref.2). Acts by cleaving the C-O bond, resulting in inversion at the carbon.
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F8QN53
|
PA2A2_VIPRE
|
Acidic phospholipase A2 Vur-PL2B (Vur-PL2) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
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MRILWIVAVCLIGVEGNLYQFGKMIRYKTGKSALLSYSDYGCYCGWGGQGKPKDATDRCCFVHDCCYGRVNGCDPKLTIYSYSFENGDIVCGGDDSCKRAVCECDRVAAICFGENLNTYDKKYKNYPSSQCTETEQC
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Snake venom phospholipase A2 that causes internal bleeding, shows very strong anticoagulant activities and inhibits ADP-induced platelet aggregation. Shows very low cytotoxicity. Is not able (or very weakly) to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis neurons (IC(50)>30 uM) and to compete with alpha-bungarotoxin for binding to muscle- and alpha-7 neuronal nAChR types, as well as to AChBPs. In inhibition of alpha-bungarotoxin binding, this toxin is similarly active against T.californica nAChR (IC(50)>100 uM), human alpha-7 nAChR (IC(50)=29 uM), and L.stagnalis AChBP (IC(50)>30 uM).
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F8QN54
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PA2B_VIPRE
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Basic phospholipase A2 vurtoxin (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
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MRTLWIVAVCLIGVEGSLLEFGMMILEETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCNPKIDRYKYHRKNGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNHIYKYYPDFLCKKESEKC
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Snake venom phospholipase A2 that may have a strong anticoagulant activity. Is able to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis neurons (IC(50)=10.5 uM) and to compete with alpha-bungarotoxin for binding to muscle- and alpha-7 neuronal nAChR types, as well as to AChBPs. In inhibition of alpha-bungarotoxin binding, this toxin is mostly active against T.californica nAChR (IC(50)=0.26 uM), it is moderately active against human alpha-7 nAChR (IC(50)=14 uM), and is not active against L.stagnalis and A.californica AChBP (IC(50)>30 uM).
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F8S296
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ATG2_ARATH
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Autophagy-related protein 2 (AtAPG2) (Protein PEROXISOME UNUSUAL POSITIONING 1)
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MVFPWNIAKSAEEAFSRWAVKRVVKFLLKKKLGKLILGDIDLDQLDIQLRDGTIQLSDLAINVDYLNDKFDAPLVIKEGSIGSLLVKMPWKTNGCQVEVDELELVLAPRLESNKSSSNEASTSASTREDLHNIRLEIGKHENEMLMNAAKSASIDVHEGVKTVAKIVKWFLTSFHVKIKNLIIAFDPDFGKKQSEAGPRPTLVLRMTEIECGISEEQVSANEVSPDNFLGINRLANCVKFQGAVVELLNMDDDDDGDKTCDKKTSNDVTLIMTGVGGGFSGSLNFSIPWKNGSLDIRKVDADISIDPVEVRFQPSTIRWFLQLWKTFTSFGSDCFPSVSHSDFLTDSPTIPTNVMVTPPATLSLSGGQELEHDTTPNLQFIPDWFPSSFSKKEEDGEVDIGASVDQFFECFDAMRSYQSASGSQGMWNWTSSVFTAINAASSLASGSLLLPSEQQHVETSCKVSFAGVSVVLFFQDEVNWKGVSTRIHYLGAELRDISVSFQVCLHDLRLEGEVNSMEIADYCQGGNVVDTANAESQTCLIKDLQAKVQTSLPPFASSDMHSDSERLSEIVSDGFLFRNKGFAVKTLLVIAAGGSGFQFTVNFQSSKASHRGSNSFSLSLPPTTFWLNLHSVEMLVNLFNDVSESIPITSHERNQVASSSKSESLRGSVSICNARVILWFPFESISERFCNSLGQQFIVVDLSSSPPSDKERAKERSPGEMHFPSATRSICFSVGDASIYLVTSDLKDSETNSYHRQVEFSAYNILHTNNKTRHQLSTIGMFWQDRPTVSPWLVERAKMLATQEESIQTDKSGGRGLEFAAVATPKDQDDIYSRSRKEIILASSFCLYVHLLPLAIHLDSWQYSKLCNLIEEAKNWLSRMAANTAEQTEESVVCQTSLVVDCDSIDILVRPEPRMGIKKQLQTELPGSWIQFNLRVQKLNLMSVPNLGSVSGADFFWLAHGEGTLLGSVTGLPDQELLLLSCNNSAIKRGNGGGSNALSSRFAGLDFLHLQEPGICNDYLAVSARGCTISAVGGRLDWIEVATSFFSFEDEKKTQEINSSSSSGSSFILNFVDVGLSYEPHHENTDHLRQASDPWVACLVAASSFSLSKKSLVDSIRNDYRIRIQDLGLLLSVDFDLSKLGGTYSSEHLHESGYVKVANDSLIEAILRTNSENGLLWELECSKSHLVIETCSDTTSGLIRLATQLQQLLAPDLEESAVHLQTRWDSIQQANARNDLDISDRLSSSDSSGEMKYLRLESENETGVIGLMDEINEDAFQFDVNPTYQSDSVECQNNYMSPHGISHGQAYNWVPATEKLPSNQSICGSSSRINSESSQVFLERESLPEIFENYCLSEFRPSSEVPQEGDSSGRELFPETDLRRGNSGWYDDASLRIVEDHVSEATEEDHEEHILDGECSSFGQTSYSAVAANGRILLKNIDLKWRIYSGSDWHDSRKKGENFKHTKGRDTTSCLELELSGVQFLYETFPIGEICTSKLSLMVQDFYLYDRSDNAPWTLVLGYYNSKDHPRDSSSYAFKLELKAVRPDPETPLEENRLRVALLPILLHLHQSQLDFLISFFGANSLEKPVVSMGDSGGSTMSVSVQGHNIIEEALLPYFQKFDIWPVNVRVDYSPHHVDIAALTGGKYAELVNLVPWKGIELQLKHVHAAGIYGWGNVCETILGEWLEDVSQNQIHQLLKGIPTVRSLSALYAAALKLVSSPVESYRKDRRLVKGVQRGTVAFLRSISLEAVGLGVHLAAGAHDILLRAEYIFASSPSLPQPQGRTKTNVRHNQPRNAKQGMLKACESIGDGIGKTASALVRTPLKKYQRGDGAGSAFATVVQGVPTAAIAPASACARAVHSALVGIRNSLDPEHKKESMEKYLGPDKQRKQDQHR
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Lipid transfer protein involved in autophagosome assembly. Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion (By similarity). Binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, and extracts phospholipids from the membrane source to the IM for membrane expansion (By similarity). Plays an essential role in plant nutrient recycling. Involved in the negative regulation of plant defense responses to biotrophic pathogens. Involved in a negative feedback loop that modulates NPR1-dependent salicylic acid (SA) signaling and limits senescence and immunity-related programmed cell death (PCD) in plants. Involved in the degradation of damaged peroxisomes.
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F8VPN2
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TEX15_MOUSE
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Testis-expressed protein 15
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MTYFFIYVSTERACSLNNCTIAKRIGKGKDATVIFEHFRKPVDPFVQENCPCKALNSEMGPFSSDTSSSYGNVQNGNNSVLEAYNRQTENSSNLRDASQVYTHNSGFSFIPTGNTASGNGDLFSVTYLRSILSSISAAFPSHNNTGSSTVITSKLIKDPRLMKREQSMRNKSDTAGLSDVLPLDKSLGCGDSQIKLTCMPTSSISSSEVPADNTITSCLNASCFKFSSESSHYQAHNSSSKGHDCIASSSIAVTEQFKEQHSSSFPSSLSNAFSDVRKQKHSEEQVQRAQMRSNVPVLTALSSESRNSDESENTCSNDSQGHFSQESPSSDINSIYKVGHQMSTVFPAQKKGNLCEYIQDTGMMRASISTEDSTKDGVNHTWCKETVLSNETVSSPIDNSNTLYQEHKEGGNLNSLSGNCEKIGVTHKLQVPKFPISSTGDKNELYRAALELECSLTPTIECLSQKYPQHSLEHEDNTNFAMTQGLIELKTVQNNQNFGNILSDAFQEAKDVPLASEKLIDRVISSAAIDISLDSSVCNIIGEYTCVRRENENGEASPYNCHKEEASRVKDGVQDHSLSYDAELSCDLNLKINLQEQRDDKNPNEAKEHNTDNINGSEKQDCLANDHFTNIVEMREIKSNTEVEILNSEECFTFNSFRGKNGKPAETASSESEAVEQRHAPNDQRGLEHLVSSFPEIEGSSVCVASNATKQIVGTTVLTVSTSLGDHQKDELKEICSSESSDLGLVKHSISECEIDTDKDKLQDFHQLVNENSALKTGLGSEIEVDLEHDNASVFQQNMHSQGNDLCEEFELYESLKSRIDWEGLFGSSYEEIESSSFARREGTDQHSSTECNCVSFCSQDKRELHNPIFLPDLQVTITNLLSLRISPTDESLELKDNFYKQVTESTEPETNKEGNASGFGMCSQPSGENSSFSCANKFGNSVQESGDVSKSESSHSSNSSHNTHVDQGSGKPNNDSLSTEPSNVTVMNDKSKCPTKSKPVFNDTRNKKDMQSRSSKRTLHASSSRGQNIANKDLREHETHEKKRRPTSHGSSDRFSSLSQGRIKTFSQSEKHIRNVLNILNNEASLCKSKHLSRKLNKAVLHLKKAHRRVHTSLQLISKVGQKRKGPLPKAYAVIHNNFWESCDHQGDSLMSERRYSKHFLSKRKYDKQGDKRFLRFDIEESLTPVSKHRLYRTNRERIAECLSNEVMSGHVSSSLTTFHVREFCDEEQFPEPQLPLAYTSQSISQLEYTNSIVGNESSSELEHFSETSGNMLDPKETLTEKEYQTHTQLCNSDSAKLKNHTTHSIRDIAKECNSEDKTVLCESNPVYLSFIKENTSHSPDKSYDSNCKANTDIHISVLGSKKKHILSVDIYEQDNCVSDGVKSGEAIFPIEKCTVPMETTSSIPTENIASKSYTIPPVSSILVTAGEEESSVGENGLFDVNENEMNITMHSKLDLTSVTEESKICKKNMKNLSCNDSSMLLKENITGPSKRYMAKYIEEEKIRKIEQAVYKKIITEGSPISFKYKSQNKILKEKSFHVNKKIITNNLTDSHLSIKNSTVDTIALKDIPNQLKERKEAGQIKVNNNSHSDCLSKPAIVETNHRPVLHGNPKVATLQKELKEHRSPNYTSHVTELSQILQRADEAASLQILEEETKLCQNILPLFVQAFERQQECSIDQILISRKLLVEQNLWNNCRLKLKPCAVDTWVELQMAMETIQFIENKKRFLEGKPTFRSLLWYDESLYSELLRRPRGYQLQSNFYPGFQGRLKYNAFCELQNYHNQLVEFLTETKKENNSYYALLKYKRQINECEAIMKHYSDCFDFCLSVPFACGVNFGDSLGDLETLRKSTLKLISVPGGSPKVHSYPGKKDHLWIIIEIVSSKVSFIKSNEEISIKICLYGLEHIYFDAAKSLVWKEKSCSLPKKHSEKNREMEEINERAFSKLKKIYDVLSKGLNNEPTSIGLQEDAIIASKQSTLGSISNCRLNKAWLSYPDISCVGEILDQAKSADLEELQGLTLRCTDHLEILKKYFQMLQEDNIDNIFIMEENVLDMLSNHNLGAVILKPEAIEIYIEIVMISETIHYLKNLIAKKLHNQRFRGMLWFDWSLLPELIGCQEEVVSLSVGDTQTHCLWKLVETAISVLKKELAVIYEYGEASNCSYALHLFYRELKELTGVKRLLNNSKYSVSTYIDLVPHTASVNFGNTVAELEHNYKQFFLLLKNVMSVPQKDFGKMVHIIKVMKTIEHMKLLSAKDTKLSTHLLFLQMLRNKRNALQQNRQEKMETPVTEPGEDSSQPGVSEQTPPGTECTVKNISDSSKKRPVTADTCEVSQGKGNTDTVPSWKKQKVTMKDVGNIQTVSKHPSTTGSPPNDENKIGSNSSDSLKSISASPEVVKRQSSVLGSVSPAESVQDTCTPKSESKVEPTDSLPDSLASLTEQQENSNVIEKRNGNSSVAETNDKKDCPLVTCDQKDIDASYSPDHTPAQESHKTPVDHTQISPSNLTAGNDDPLVPDASLLSVSASQSEKDVYLSGTDFHHENNKILNLSTEDCTGTSSPEPVCIKDKISVLQVDKTQPIKSESPKKSMTDAPNPNTAPFGSYGNSALNVNGTVQHTHSEQNSKVLTQKVGTSRNIPPQSACSPVHNSSAHSFGTSYPYYSWCFYQYSSSNGTAVTHTYQGMTAYEIQQPPPPVLTTVASTVQSTHFNRSYSEHFSYFPGQPQANSFNPGNGYFPSHTPVSYNYQQPVYSQFASHQPVPQATYPYPPNPGAPPQVPWTYAPWQQNPFLRRP
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Required during spermatogenesis for normal chromosome synapsis and meiotic recombination in germ cells. Necessary for formation of DMC1 and RAD51 foci on meiotic chromosomes, suggesting a specific role in DNA double-stranded break repair. Essential executor of PIWIL4-piRNA pathway directed transposon DNA methylation and silencing in the male embryonic germ cells. PIWIL4-piRNA binds to nascent transposon transcripts and interacts with TEX15, which may in turn recruit the epigenetic silencing machinery to the transposon loci. Not required for piRNA biosynthesis.
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F8VPQ2
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ARI4A_MOUSE
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AT-rich interactive domain-containing protein 4A (ARID domain-containing protein 4A) (Retinoblastoma-binding protein 1)
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MKAADEPAYLTVGTDVSAKYRGAFCEAKIKTVKRLVKVKVLLKQDNTTQLVQDDQVKGPLRVGAIVETRTSDGSIQEAIISKLTDASWYTVVFDDGDERTLRRTSLCLKGERHFAESETLDQLPLTNPEHFGTPVIAKKTNRGRRSSLPITEDEKEEESSEEEDEDKRRLNDELLGKVVSVASTAESTGWYPALVVSPSCNDDVTVKKDQCLVRSFIDSKFYSIARKDIKELDILTLPESELCARPGLRRASVFLKGRIVPDNWKMDISEILESSSSDDEECPAEEHEEEKEKEAKKEEEELPEEELDPEERDNFLQQLYKFMEDRGTPINKPPVLGYKDLNLFKLFRLVYHQGGCGNIDSGAVWKQIYMDLGIPILNSAASYNVKTAYRKYLYGFEEYCRSANIQFRTIHHHEPKVKEEKKDFEDSMDEALKEAPEMPLLDVKSEPEENTDSNSESDREDTELKSPRGRRKIVRDANCIKKEIEEEKIEDKFLRDDLENKDAGDDDDDGDPAAKREHELLFGRKSTPKNKEKKIKKPEDSERDSDEEEEKSQEREETESRCDSEGEDEEDDTEPCLTGTKVKVKYGRGKTQKIYEASIKSTEMDDGEILYLVHYYGWNVRYDEWVKADRIIWPLDKGGPKKKQKKKVKNKEDSEKDEKRDEERQKSKRGRPPLKSTFSPNMPYSLSKTSNSEGKSDSCSSDSEADDQLEKSSGGEDLSPDVKEELEKNENAHDDKLDEENPKIVHISKENDRTQAQPSDTLTVEAGDSDQIVHIFGDKVDQVEEFKKQVEKSPKGKGRRSKTKDLSLELIKISPFGQEEAGSEAHGDVHSLEFSSLECKNFSSTEDDIDPYEKEKKLKRKILGQQSPEKKLRLDNGMEMTTGVSQERSDDGAGAEGMKGAHVEQHFETEGEGMPSLTAEPDQGLQELTSEKSDSPAEEEPVHTPLKEEEDAMPLIGPETLVCHEVDLDDLDEKDKTSIEDVVVEGSESNSLASVPPALPPVAQHNFSVASPLTLSQDESRSIKSESDITIEVDSIAEESQEGLCERESANGFEASVASGACSIIAHERESREKGQKRPSDGNSGLIAKKQKRTPKRTSAAAKTEKNGAGQSSDSEDLPAMDSSSNCTPVKRLTLPKSQKLPRSPARTSPHIKDAEKEKHREKHPNSSPRTYKWSFQLNELDNMNSTERISFLQEKLQEIRKYYMSLKSEVATIDRRRKRLKKKDREVSHAGASMSSASSDTGMSPSSSSPPQNVLAVECR
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DNA-binding protein which modulates activity of several transcription factors including RB1 (retinoblastoma-associated protein) and AR (androgen receptor). May function as part of an mSin3A repressor complex (By similarity). Has no intrinsic transcriptional activity. Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting center near the SNRPN promoter, where it might function as part of a complex with RB1 and ARID4B. Involved in spermatogenesis, together with ARID4B, where it acts as a transcriptional coactivator for AR and enhances expression of genes required for sperm maturation. Regulates expression of the tight junction protein CLDN3 in the testis, which is important for integrity of the blood-testis barrier. Plays a role in myeloid homeostasis where it regulates the histone methylation state of bone marrow cells and expression of various genes involved in hematopoiesis. May function as a leukemia suppressor.
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F8VPU2
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FARP1_MOUSE
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FERM, ARHGEF and pleckstrin domain-containing protein 1 (FERM, RhoGEF and pleckstrin domain-containing protein 1)
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MGEIEQKPTPASRLGAPENSGISTLERGQKPPPTPSGKLMTVKIQMLDDTQEAFEVPQRAPGKVLFDAVCNHLNLVEGDYFGLEFPDHRKIVVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYVPQQDALEDRIMEFHHSHVGQTPAESDFQLLEVARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDVNSSYQDTLEFLMAGRDFCKSFWKICVEHHAFFRLFEEPKPKPKPVLFSRGSSFRFSGRTQKQVLDYVKEGGHKKVQFERKHSKIHSTRSLVSQPTAPNSEVPKQSPQSASLTFGEGTESPGGQSCQQAKETKACTLELGPHQSPALPKSPPGSKAADGTTVVPPEEEEEEEGGKDGIRPSNPQPPQPSTGSLTGSPHLSELSINSQGGAAPANVTLSPNLSPDNKQASPLISPLLNDQACPRTDDEEEGRRKRFPTDKAYYIAKEVSTTERTYLKDLEVIASWFQSTVSKEDSMPEALKSLIFPNFEPLHKFHTNFLKEIEQRLALWEGRSNAHVRGDYQRIGDVMLKNIQGMKHLAAHLWKHSEALEALETSIKGSRRLEHFCRDFELQKVCYLPLNTFLLRPLHRLMHYKHVLERLCKHHPPNHADFRDCRAALAEITEMVAQLHGTMIKMENFQKLHELKKDLIGIDNLVTPGREFIRLGSLSKLSGKGLQQRMFFLFNDVLLYTSRGLTASNQFKVHGQLPLYGMTIEESEEEWGVPHCLTLRGQRQSIIVAASSRSEMEKWMEDIQMAIDLAEKSNGPTPELLASSPPDNKSPDEATAADQESEDDLSASRTSLERQAPHRGNTMVHVCWHRSTSVSMVDFSIAVENQLSGNLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDSHPLASLPLLGYSLTIPSESENIHKDYVFKLHFKSHVYYFRAESEYTFERWMEVIRSATSSASRAHILSHKESHLY
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Functions as guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity).
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F8VPZ5
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ERCC6_MOUSE
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DNA excision repair protein ERCC-6 (EC 3.6.4.-) (ATP-dependent helicase ERCC6) (Cockayne syndrome protein CSB)
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MFHEEVPNSTHPQEQDCLPSQHANAYKDMPVGQENGGVSEAGECLSSTSCEYGPSTSAEACVLAATRRGPTLLHIDRHQIPAVEPSAQALELQGLGVDVYDQAVLEQGVLQQVDSAMHEASCVAQLADAEKEYQSVLDDLMSCTTSLRQINKIIEQLSPQAASNRDINRKLDSVKRQKYNKEQQLKKITAKQKRLQAILGGAGVQVELDHASLEEDDAEPGPSCLGSMLMPAQETAWEELIRTGQMTPFGTPAPQKQEKKPRKIMLNEASGFEKYLAEQAQLSFERKKQAATKRTAKKAIVISESSRAAIETKADQRSQVLSQTDKRLKKHSRKLQRRALQFQGKVGLPSGKKPLEPEVRPEAEGDTEGEESGSSPTDGEEEEEQEEEEGVASLSSDDVSYELKPLRKRQKYQKKVPVQEIDDDFFPSSEEEDEAMEGRGGGRKVARRQDDGDEDYYKQRLRRWNRLRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGSNYRFEGLGPTIIVCPTTVMHQWVKEFHTWWPPFRVAVLHETGSYTHKKERLIRDIVYCHGVLITSYSYIRLMQDDISRHDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINPYLLRRMKSDVKMSLSLPDKNEQVLFCRLTDEQHKVYQNFIDSKAVYRILNGENQIFSGLVALRKICNHPDLFSGGPKNASGPPEDELEEEQFGHWRRSGKMIVVESLLKIWHRQGQRVLLFSQSRQMLHILEVFLRAHKYSYLKMDGTTTIASRQPLITKYNEDTSIFVFLLTTRVGGLGVNLTGANRVIIYDPDWNPSTDTQARERAWRIGQKKQVTVYRLLTAGTIEEKIYHRQIFKQFLTNRVLKDPKQRRFFKSNDLYELFTLTSPDASQGTETSAIFAGTGSSIQTPKCQLKKRTSTVLGTDPKCKKPPVSDTPANAATLIGEKPKAAGATGRSVTSGESGPFKGDHDTNGNRASSVAFGEETDAGSTLEHLSVMSGDGKHSDSPTVDHTSRPPVEASTSEKQGSSYAGARCQAQTEPVPMSEQMEGQFSKYKSKRKHDASEEETTEKRPQPKQKAKNSKHCRDAKFEGTRVPHLVKKRRYRQQTSEQEGGAKDRSSDDYVLEKLFKKSVGVHSVVRHDAIIDGSSPDYVLVEAEANRVAQDALKALRLSRQQCLGAASGVPTWTGHRGISGAPTGVKNRFGQKRDSSLPVQHPSSLTEKTQNNMKKEGKAHTPEHFSGKEDGASVSGAPSSSSLLARMRARNHMILPERLESDSEHLAEAAAVPPCGTEHDDLLVDMRNFIAFQAQVDGQASTQEILQEFESKLSVAQSCVFRELLRNLCNFHRTPGGEGIWKLKPEYC
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Essential factor involved in transcription-coupled nucleotide excision repair which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (By similarity). Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA (By similarity). It is required for transcription-coupled repair complex formation. It recruits the CSA complex (DCX(ERCC8) complex), nucleotide excision repair proteins and EP300 to the sites of RNA polymerase II-blocking lesions (By similarity). Plays an important role in regulating the choice of the DNA double-strand breaks (DSBs) repair pathway and G2/M checkpoint activation DNA-dependent ATPase activity is essential for this function (By similarity). Regulates the DNA repair pathway choice by inhibiting non-homologous end joining (NHEJ), thereby promoting the homologous recombination (HR)-mediated repair of DSBs during the S/G2 phases of the cell cycle (By similarity). Mediates the activation of the ATM- and CHEK2-dependent DNA damage responses thus preventing the premature exit from the G2/M checkpoint (By similarity). Acts as a chromatin remodeler at DSBs DNA-dependent ATPase-dependent activity is essential for this function (By similarity). Remodels chromatin by evicting histones from chromatin flanking DSBs, limiting RIF1 accumulation at DSBs thereby promoting BRCA1-mediated HR (By similarity). Required for stable recruitment of ELOA and CUL5 to DNA damage sites (By similarity). Involved in UV-induced translocation of ERCC8 to the nuclear matrix (By similarity). Essential for neuronal differentiation and neuritogenesis regulates transcription and chromatin remodeling activities required during neurogenesis (By similarity).
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F8VQ03
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ADAM3_MOUSE
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A disintegrin and metallopeptidase domain 3 (Cyritestin)
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MLPLFLVLSYLGQVIAAGKDVETPLLQITVPEKIDTNIQDAKEAETQVTYVVRIEGKAYTLQLEKQSFLHPLFGTYLRDKLGTLQPYFSLVKTHCFYQGHAAEIPVSTVTLSTCSGLRGLLQLENITYGIEPLESSATFEHILYEIKNNKIDYSPLKENFANSEQESQSYRILVKPEKGSNSTLTKRILRIKIIMDKAMFDHMGSEVGVATQKVVHIFGLINTMFSQLKMTVMLNSLEIWSEQDKIETNGDADEVLQRFLLWKSKEISQKAQDITYLLLYKDHPDYVGATYHGMACNPNFTAGIALHPKTLAVEGFAIVLSQLLGINLGLAYDDVYNCFCPGSTCIMNPSAIRSQGIKVFSSCSVDEFKQLASQPELDCLRNTSETEFVVQPQGGSYCGNHLLEVPEQCDCGPPETCTHKKCCNPKDCTLIDAAQCGTGPCCDKRTCTIAERGRLCRKSKDQCDFPEFCNGETEGCAPDTKAADLEPCNNETAYCFGGVCRDPDRQCTDLFGKYAKGPNYVCAQEVNLQNDKFGNCHGRCNYSAIFCGKAVCYWNFAEVIQTEKYDVQYTYLGGQVCVSAHLRSQTGTRDDTYVHDGTVCGSGQVCFRGDCLRVHVLRGTRECEADDKCQGHGICNNLNNCQCESGFAPPECDMTPSSPGGSMDDGFWLPFDKSTPLIFKRHGLKYKKVLLISFYILLPFLVVLAFMAVKRMIGKRLAKQNISKALEHKEEAFNRGSMNPGVVSGGNTDQNLMTVPGSFNSYAYHGNTDQNFMTVPGSFNSYSYHGNTDQNFMTVPGSFNSYSYQDVPYYRSIPEDGNDSQQ
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Involved in fertilization by controlling sperm migration into the oviduct. Promotes the binding of sperm to the oocyte zona pellucida.
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F8VQB6
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MYO10_MOUSE
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Unconventional myosin-X (Unconventional myosin-10)
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MDSFFPEGARVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITNQKVTAMHPLHEEGVDDMASLAELHGGSIMYNLFQRYKRNQIYTYIGSIIASVNPYQPIAGLYERATMEEYSRCHLGELPPHIFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSVISQQTLDLGLQEKTSSVEQAILQSSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQQGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLDQGEREEFYLSLPENYHYLNQSGCTEDKTISDQESFRQVITAMEVMQFSKEEVREVLRLLAGILHLGNIEFITAGGAQIPFKTALGRSADLLGLDPTQLTDALTQRSMILRGEEILTPLSVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKDDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNTQKMPDQFDQVVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPDDIRGKCTVLLQVYDASNSEWQLGKTKVFLRESLEQKLEKRREEEIDRAAMVIRAHILGYLARKQYRKVLCGVVTIQKNYRAFLARKKFLHLKKAAIVFQKQLRGQLARRVYRQLLAEKRELEEKKRREEEKKREEEERERERAQREADLLRAHQEAETRRQQELEALQKSQREADLTRELEKQRENKQVEEILRLEKEIEDLQRMKERQELSLTEASLQKLQQLRDEELRRLEDEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEISGEELSELAESASGEKPNFNFSQPYPAEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNYTVVPTSPSADSTVLLAASMQDSASLHNSSSGESTYCMPQNNGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRYSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRTAKEIIDNTSKENGIDIILADRTFHLIAESPEDASQWFSVLSQVHSSTDQEIREMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGTEMEKYALFIYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGQVDKAIESRTIVADVLAKFEKLAATSEAGDAPWKFYFKLYCFLDTDSMPKDSVEFAFMFEQAHEAVIHGHHPAPEESLQVLAALRLQYLQGDYTPHTSIPPLEEVYSVQRLRARISQSTKTFTPYERLEKRRTSFLEGTLRRSFRTGSVVRQKAEEEQMLDMWIKEEVCSARTSIIDKWKKLQGMNQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGKPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSVSSQGSSR
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Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments (By similarity). The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments (By similarity). Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts. [Isoform Headless]: Functions as a dominant-negative regulator of isoform 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion.
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F8VQN3
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GPR31_MOUSE
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12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid receptor (12-(S)-HETE receptor) (12-HETER) (G-protein coupled receptor 31)
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MERTNCSAASTVVETAVGTMLTLECVLGLMGNAVALWTFFYRLKVWKPYAVYLFNLVVADLLLATSLPFFAAFYLKGKTWKLGHMPCQVLLFLLAFSRGVGVAFLTTVALDRYLRVVHPRLRVNLLSLRAAWGISSLIWLLMVVLTPQNLLTCRTTQNSTECPSFYPTGGAKAIATCQEVLFFLQVLLPFGLISFCNSGLIRTLQKRLRESDKQPRIRRARVLVAIVLLLFGLCFLPSVLTRVLVHIFQEFKSCSVQQAIVRASDIAGSLTCLHSTLSPAIYCFSNPAFTHSYRKVLKSLRGRRKAAESPSDNLRDSYS
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High-affinity receptor for 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12-S-HETE), with much lower affinities for other HETE isomers (By similarity). 12-S-HETE is a eicosanoid, a 12-lipoxygenase (ALOX12) metabolite of arachidonic acid, involved in many physiologic and pathologic processes, such as cell growth, adhesion, inflammation and cancer promotion. 12-S-HETE-binding leads to activation of ERK1/2 (MAPK3/MAPK1), MEK, and NF-kappa-B pathways and leads to cell growth. Plays a crucial role for proliferation, survival and macropinocytosis of KRAS-dependent cancer cells by mediating the translocation of KRAS from the endoplasmic reticulum to the plasma membrane (PM) and its association with the PM (By similarity). Contributes to enhanced immune responses by inducing dendrite protrusion of small intestinal CX3CR1(+) phagocytes for the uptake of luminal antigens. Acts also as a key receptor for 12-(S)-HETE-mediated liver ischemia reperfusion injury.
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F8W2M1
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HACE1_DANRE
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E3 ubiquitin-protein ligase HACE1 (EC 2.3.2.26) (HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1) (HECT-type E3 ubiquitin transferase HACE1)
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MERAMEHLNVQLNRLTRSLRRARTVELPEDSETAVYTLMPMVMADQHRSVSELLLNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKRGANPNYQDISGCTPLHLAARNGQKKCMGRLLEYNADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTNVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLPDRNGVTPLDLCVQGGYGETCEILIQHHGRLFQTLIQMTQNDDIKENMLRQVLEHVSQQNDSNYQRILTSLAEVATTNGHKLLSLSSNFEVQTKSLLRIIRIFCHVFCLGPSSPNNGNDMGYNGNKTPRSQVFKPLELLWHSLDEWLVLISTELEKEITDTTRSSSGNDIASLFLKKQEVDHSVSSENPQLLLDASSVMKTPEVYADGQDVISMIANRLSAVIQAFYMCCSCQMPHGMTSPRFIEFVCKHDEVLKCFVTRNPKIIFNHFHFLLECPELMSRFMHIIKGQPFKDRCEWFYEHLLAGQPDSDMVHRPVNENDILLVHRDSLFRSSCEVVSKSSNEKLKQGIAVRFHGEEGMGQGVVREWFDILSNEIINPDYALFTQSADGTTFQPNSNSSVNPDHLNYFRFAGQILGLALYHRQLVNIYFTRSFYKHILGIPVSYQDVSSIDPEYAKNLQWILDNDISDLGLELTFSVETDVFGTMEEVPLKPGGTTIQVTQDNKEEYVQLVTELRMTRAIQPQINAFLQGFHTFIPPSLIQLFDEYELELLLSGMPEIDVMDWKRNTEYTSGYDLQEPVIQWFWEVVENLTQEERVLLLQFVTGSSRVPHGGFAFLMGGSGLQKFTVAAVPYTSNLLPTSSTCINMLKLPEYPSKDVLRDRLLVALHCGSYGYTMA
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E3 ubiquitin-protein ligase involved in Golgi membrane fusion and regulation of small GTPases. Acts as a regulator of Golgi membrane dynamics during the cell cycle: recruited to Golgi membrane by Rab proteins and regulates postmitotic Golgi membrane fusion. Acts by mediating ubiquitination during mitotic Golgi disassembly, ubiquitination serving as a signal for Golgi reassembly later, after cell division.
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F8W2M8
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TPP1_DANRE
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Tripeptidyl-peptidase 1 (TPP-1) (EC 3.4.14.9) (Tripeptidyl aminopeptidase) (Tripeptidyl-peptidase I) (TPP-I)
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MRVAVFVLSFIWLVNGELLEADQDAVVPGDWTFLGRVGPLEEVELTFALKQQNVSKMEELLKLVSDPDSHQYGKYLSLDEVAALSRPSPLTEKVVENWLRSHGVMDCHTIITRDFLQCVMTVEVAEALLPGSKFHRFSKNTKTLLRSTSQYSVHEDVHQHLDFVGGVHRFPQKRKIVSKGWEGARQAILGYHLGVTPAVIRNRYNLTAKDVGTAANNSQAVAQFLEQYYHPADLAEFMSLFGGGFTHMSTVERVVGTQGGGKAGIEASLDVEYIMSSGANISTWVFTNPGRHESQEPFLQWMLLLSNMSAVPWVHTISYGDDEDSLSEAYMNRINIEFMKAGLRGISMLFASGDSGAGCRHLTKERNTFRPSFPASSPYVTTVGGTSFQNPFKLSYEVTDYISGGGFSNVFPMPDYQVDAVRAYLKSVQSLPPQTYFNTTGRAYPDLAALSDNYWVVSNRVPIPWVSGTSASTPVVGGILSLINDQRFLKGLPALGFINPRLYKMQGKGLYDVTVGCHLSCLDDKVEGKGFCASPSWDPVTGWGTPNYPVFLASLMD
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Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (By similarity). Requires substrates with an unsubstituted N-terminus (By similarity).
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F8W3R9
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ALK_DANRE
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ALK tyrosine kinase receptor (EC 2.7.10.1) (Anaplastic lymphoma kinase 2) (alk-2) (Anaplastic lymphoma kinase homolog)
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MIARILYFFLWSAAFLPELQCASQRTADALTTFPTSAFINGTDRKDSNQTSTSRIKRKTLSVDFAVPSLLRYYLALFIKRPLNGDCLSFNGCYTVRANLLMRCVPLQKTIAGLLDAKLAAMNVNRSSTGQLPYRQKRPVPKVLNLGLTSASRKSNQVVVEVGEEMVKTGCGGLHVYEDAPVVFLEMDLTRILEWWLGAEGGRLRVRLMPERKVQVPGKEDKYSAAIRASDARLFIQIASSERPSSTISRNPTVAPKYWNFSWIAEDELTFPEDPVSTSDCTSKAKSCDRRPDGYYPEFAWSLTSAEDSWAIDQTMVKTKASSQGWEEGRFLTVNSSALTGPWVLSPWFRAAHRPCGLDITVFLHPRQSGRYTVWLIERDKPPLALLTTEHPHVIGWAVVHLSLAARSKPFRISSSYSQPGEIETATYDPRYSTNCTTRSSQNVTLRGRYHCRGGREINVSQLCDFSIDCPQGDDEGEHCRQFLNGSYCSFGREDCGWQPVQGRGPQWRAHPSIPQSLRSSCPSPGALLAIDSQPKGQRGSAQVRSPLFFYPLRNAPCMVKFWVCGSSNGALSLWITENSTGPEGQRSLWNSTSEANMGKGWKLITLPLFGLVDLFYLQFSADISSSSGIAFAVDNFTLSMECFLETNGEFPPVAPISPTQALFTQSNENIKTTTTLYGGPGASTESVKWIFHTCGATGQDGPTPTQCSNSYRNTNVNVTVGTKGPFKGIQMWQVPETRKYRITAYGAAGGRSVLAVHKSHGVYMTGDFLLQKDELLYILVGQEGEDACPNMVPTMDRICREQQGPSINKTQLKGGGGGGGGGTYVFKVVNGVHIPLLIAAGGGGRGYSSQSETPEEVMDRDPSIPGRNGKSGTAGGGGGWNDSAPVPQGGRPLILGGQGGEPCQAMGWKTRGGFGGGGGACTAGGGGGGYRGGSAWHDNDPRKDGDDGTSYISPDGEMYLEPLKGMEGNGEVIINPVQNCSHCESGDCHETSEGMVCYCDEELTLAPDGVSCINSTELPLLPAQPSLSHLALGLSVGTSALIAALLLAVSGVMIMYRRKHTELQSIQLELQSPDCKLSKLRASTIMTDYNPNYCFGGKTASVNDLKEVPRRNISLTRGLGHGAFGEVYEGLAVGIPGEPSPMQVAVKTLPEVCSEQDELDFLMEALIISKFSHQNIVRCIGVSLQALPHFILLELMAGGDLKSFLRETRPRLEHPSSLTMVDLLNIARDIARGCQYLEENQFIHRDIAARNCLLTCKGPGRVAKIGDFGMARDIYRASYYRKGGRAMLPVKWMPPEAFMEGIFTSKTDTWSFGVLLWEIFSLGYMPYPSRSNQEVLEFVTNGGRMDPPKNCPGPVYRIMTQSWQHQPEDRPNFSTILERIDYCLQDPDVVNVPLPVEYGPIPEEEERVPMRPEDPSAPSLLVSPQGTEDVPSATHSAQSKKDGEAIHMANLSTDSKLPPVPPSQPHPHHHLQTPVVTAPVPASKPSSTTSNAQDGGHVNLGFMQAHSSEKESRNRKPTNLWNPTYGSWFLQQQQKRQQVQAQRQTSGPRIPGEGQEQVGRTVTVAEALGLQQQHKQQQYQQQLQRQQQQQQQQQQQQGLCRPLLPPPPPPAPTPLLLDSATLAPVPLYRLRRFPCGNIGYGYQEQGLPMEPMQGPQLPPPHPGQQRPISLTRASGPEDSRPLLVTMGTVQDSRLPKMEGHNATVL
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Receptor tyrosine kinase required for neurogenesis in the developing central nervous system. Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen-activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (By similarity).
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F8W3X3
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PCD19_DANRE
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Protocadherin-19
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MHSKDMDFVQMFVCFLLCWTGVDAVFNLKYTVEEELRAGTKIANVTADAKVAGFALGNRQPYLRVISNSEPRWVNLSPAGLLITKQKIDRDAVCRQTPKCFISLEVMSNSMEICVIKIEIIDVNDNAPRFPTNHIDIEISENAAPGTRFPLEGASDPDSGSNGIQTYTITPNDIFGLEIKTRGDGSKIAELVVEKTLDRETQSRYTFELTAEDGGDPPKSGTVQLNIKVIDSNDNNPVFDEPVYTVNVLENSPINTLVIDLNATDPDEGTNGEVVYSFINFVSNLTKQMFKIDPKTGVITVNGVLDHEELHIHEIDVQAKDLGPNSIPAHCKVIVNVIDINDNAPEIKLLSENSEMVEVSENAPLGYVIALVRVSDNDSGANGKVQCRLQGNVPFRLNEFESFSTLLVDGRLDREQRDMYNLTILAEDSGYPPLRSSKSFAVKVTDENDNPPYFTKPHYQAMVLENNVPGAFLLAVSARDPDLGMNGTVSYEIIKSEVRGMSVESYVTVNSNGEIYGVRAFNHEDTRTFEFKVSAKDGGDPPLTSNATVRIVVLDVNDNTPVMTTPPLVNGTAEVSIPKNAGVGYLVTQIKADDYDEGENGRLTYSISEGDMAYFEIDQINGEVRTTKTFGENAKPSYQITVVAHDHGQTSLSASAYIVIYLSPDLNAQEQIGPVNLSLIFIIALGSIAVILFVTMIFVAVKCKRDNKEIRTYNCRVAEYSYGNQKKSSKKKKLSKNDIRLVPRDVEETDKMNVVSCSSLTSSLNYFDYHQQTLPLGCRRSESTFLNVENQNSRNAAPNHGYHHTFTGQGPQQPDLIINGMPLPETENYSIDSSYVNSRAHLIKSTSTFKDMEGNSLKDSGHEESDQTDSEHDVQRGHYADTAVNDVLNMTVPSNNSQIPDQDQSEGFHCQDECRILGHSDRCWMPRVPIPARAKSPEHGRNVIALSIEATTVDVPHYEDCGTTKRTFATFGKDGPDEDRAEQRGRRQTAEPAVCSPKTNGAVREAGNGREAVSPITSPVHLKSPQSKASSTYNTLKCRDAERIANHSLLRQPEGKDSEPAMREINTLLQDGRDKESPGSKRLKDIVL
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Calcium-dependent cell-adhesion protein. Essential for the early stages of neurulation in the anterior neural plate. Shows little cell adhesion activity on its own but exhibits robust homophilic cell adhesion when in a complex with cadherin cdh2 and appears to mediate the adhesion while cdh2 acts as a cell adhesion cofactor in the complex. Functions with cdh2 to coordinate cell adhesion and cell movements during neurulation. Contributes to neural progenitor cell patterning with cdh2 by promoting homophilic cell interactions. Regulates the columnar organization of neurons in the optic tectum.
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F8W4H9
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MRP2A_DANRE
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Melanocortin-2 receptor accessory protein 2A (zMRAP2a)
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MPRFQLSNSTSVPNHNYEWSYEYYDDEEPVSFEGLKAHRYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHPEAAEPYEKRMRLTSCADGLGRQRETDGRTGLSRPLLEESRSLFHCYINEEEREGGRAATDAGALTHGRSGIGNSRGQVEEVGLVVQNMVLESRAEREAALLAHFNIPNFVNSELNSALGDEDLLLGDPPIIMEEARPRCTHHIID
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Inhibitor of melanocortin receptor 4 (mc4r), a receptor involved in energy homeostasis. Plays a role during larval development in the control of energy homeostasis and body weight regulation by decreasing ligand-sensitivity of mc4r and mc4r-mediated generation of cAMP, leading to stimulate growth during larval development. Acts by stabilizing an inactive conformation of mc4r during embryonic development, when all the energy consumed is obtained from the yolk sac, possibly to speed the rapid maturation to the mobile free-feeding juvenile stage reached at 5 dpf.
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F8WQK8
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DPP11_POREA
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Asp/Glu-specific dipeptidyl-peptidase (EC 3.4.14.-) (Dipeptidyl-peptidase 11) (DPP11)
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MNKRFFPTLLLAFVCSTLAYADGGMWLMQQINGQVARMKSLGMQLEAADIYNPNGSSLKDAVVMFDGGCTGVLVSNQGLLLTNHHCGYDQIQKHSSVQHNYLKDGFWSYSLAEELVNPGLEVEIVDEITDVTAAVKKELERIKKPSGLEFLSPRYLSSLAPEIVGKKAASRPGYRYEIKAFYGGNRYYMFTKKVFRDVRLVAAPPSSIGKFGSDTDNWAWPRHTGDFSIFRLYADKNGNPAEYSKDNVPYRPKRWVKVNAQGVKEGDFALIMGYPGTTYKFFTADEVTEWSEIDNNIRIEMRGILQDVMLREMLADPKINIMYAAKYASSQNGYKRAQGANWAIRRRSLREIKLAQQQEVLAWAKQKGIATTEEAVRAISKAIEGRQDLRMRQRYLLEGILMGIEMSNAPAADSDIADHWDDPARREAGLQSIRKQFEAFFNKDYSPEVEKDQLAIALLTRYAERIPAEKQPISIREGIAEYGSAKAYVEMIFDKSIYASRERFEEFMKNPDRDRLLRDPMSRFAASVAYEHQKLAKEVAAFDAPLAAAQRSYVASVLDMKGQPNLAPDANLTLRFTYGEIKGYQPRDVVTYGAKSTLEGVMEKEDPNNWEYVVDPKLKALYEAKNYGRYANSDGSMPVNFCATTHTTGGNSGSPVMNARGELIGLNFDRNWEGVGGDIEYLPNYQRSIILDIRYLLFIIDKFAGCQRLIDEIQPQF
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Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Is likely involved in amino acid metabolism and bacterial growth/survival of asaccharolytic P.endodontalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources.
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F9FRH4
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MNLOX_FUSOF
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Manganese lipoxygenase (MnLOX) (EC 1.13.11.-) (EC 1.13.11.45) (Manganese 11R/13S-lipoxygenase) (11R/13S-MnLOX)
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MVALLIFLGIFTCVETLPLSDSPSSYIPEEVPSSQTADIGLPPPTEFTLPNEDDEILIRKLNIQKTRKEILYGPSLIGKTSFFISGPLGDQISQRDQTLWSRDAAPVVQAVSHDAAAALHDIQIHGGLQNLDDYKILYQGHWSSSVPGGIAKGQFSNFTSDLLFSMERLSTNPYILRRLHPHADELPFAVDSKIVQKLTGSTLPSLHKAGRLFLADHSYQKDYVAQEGRYAAACQALFYLDDRCHQFLPLAIKTNVGSNLTYTPLDEPNDWLLAKVMFNVNDLFHGQMYHLASTHAVAEIVHLAALRTMSSRHPVLALLQRLMYQAYAIRPIGNNILFNPGGLIDQNSVFSNVAVRKFATDFYPTVAGPVRSNYFEANLRSRGLLNATHGPDLPHFPFYEDGARIIKVIRTFIQSFVKSIYKSDKVLAKDWELQAWIAEANGAAEVIDFPPTPLKKRKHLVDILTHMAWLTGVSHHVLNQGEPVTTSGVLPLHPGSLYAPVPGEKGVVDSLLPWLPNEQKSVDQISFLALFNRPQIVENNRTLRYMFNSESLLAGTVRAVAAANERFMEEMGHISQEISNRKFDDDGLSQGMPFIWTGMDPGVIPFYLSV
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Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 9-, 11- and 13-hydroperoxy fatty acids. Oxidizes linoleic acid to mainly 11R-, 13S- and racemic 9-HPODE, and alpha-linolenic acid to 11-HPOTrE.
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F9UPU7
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KT3K_LACPL
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Probable ketoamine kinase lp_1983 (EC 2.7.1.-)
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MHLTKTWLAQLPLTDIQQVQPVSGGDINAAFQIITRHHQYFLKVQPHNDVTFFDHEVAGLRLLGAVTKTPRVIASGTIATDGYLLLDWLATGTGSQSALGAAVAKVHHQHHAQFGLDHDFTAGKLPKINHWQTDWATFYTQQRLDVLVNLAKEHHLWSETREMHYHRLRQQLLQDSHMHTVKPSLLHGDLWSGNYLFDTTGTPVLIDPDVFYGDREMDLAMTTIFGGFDTDFYQAYQAAYPVAPGMQDRLPSYQLYYLLAHLNLFGETYGPAVDRILMQY
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Ketoamine kinase that phosphorylates ketoamines, such as erythruloselysine, erythrulosecadaverine, ribuloselysine and ribulosecadaverine, on the third carbon of the sugar moiety to generate ketoamine 3-phosphate. Has higher activity on free lysine (erythruloselysine and ribuloselysine), than on ribuloselysine and erythruloselysine residues on glycated proteins.
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F9USS9
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LARA_LACPL
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Lactate racemase (Lar) (EC 5.1.2.1) (Lactate racemization operon protein LarA)
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MVAIDLPYDKRTITAQIDDENYAGKLVSQAATYHNKLSEQETVEKSLDNPIGSDKLEELARGKHNIVIISSDHTRPVPSHIITPILLRRLRSVAPDARIRILVATGFHRPSTHEELVNKYGEDIVNNEEIVMHVSTDDSSMVKIGQLPSGGDCIINKVAAEADLLISEGFIESHFFAGFSGGRKSVLPGIASYKTIMANHSGEFINSPKARTGNLMHNSIHKDMVYAARTAKLAFIINVVLDEDKKIIGSFAGDMEAAHKVGCDFVKELSSVPAIDCDIAISTNGGYPLDQNIYQAVKGMTAAEATNKEGGTIIMVAGARDGHGGEGFYHNLADVDDPKEFLDQAINTPRLKTIPDQWTAQIFARILVHHHVIFVSDLVDPDLITNMHMELAKTLDEAMEKAYAREGQAAKVTVIPDGLGVIVK
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Catalyzes the interconversion between the D- and L-isomers of lactate. May act as a rescue enzyme to ensure D-lactate production in physiological conditions where its production by the D-lactate dehydrogenase LdhD is not sufficient. D-Lactate is absolutely required for growth of L.plantarum and is an essential component of the cell wall peptidoglycan in this species, where it is incorporated as the last residue of the muramoyl-pentadepsipeptide peptidoglycan precursor its incorporation confers high level of vancomycin resistance.
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F9UST4
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LARE_LACPL
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Pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase (EC 4.4.1.37) (Lactate racemase accessory protein LarE) (Lactate racemase activation protein LarE) (Lactate racemase maturation protein LarE) (Lactate racemization operon protein LarE) (Nickel-pincer cofactor biosynthesis protein LarE) (Pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase) (P2CMN sulfurtransferase)
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MATLATKKATLVAALKDLQRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYLSDDHIKNNTPDSWYYAKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQELGLTNWNKVASCSVSSRFPYGTTLTHDNIAQVMAAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLVFNDRVNRQLQSLGFRYVTLDLGGFRSGRMNDTLTKAQLATFA
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Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Catalyzes the ATP-dependent incorporation of two sulfur atoms in pyridinium-3,5-biscarboxylic acid mononucleotide (P2CMN) to yield pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN). The source of sulfur is the enzyme itself: Cys-176 of LarE is the sulfur donor, thereby being converted into dehydroalanine, and is not regenerated in vivo. Thus, two molecules of LarE undergo sacrificial sulfur transfer to create one P2TMN. Binds nickel. Is required for the activation of the lactate racemase LarA. May also be involved in the activation of other nickel-pincer cofactor-dependent enzymes.
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F9VMT6
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FBPAP_SULTO
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Fructose-1,6-bisphosphate aldolase/phosphatase (FBP A/P) (FBP aldolase/phosphatase) (EC 3.1.3.11) (EC 4.1.2.13) (Fructose-1,6-bisphosphatase) (FBPase)
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MKTTISVIKADIGSLAGHHIVHPDTMAAANKVLASAKEQGIILDYYITHVGDDLQLIMTHTRGELDTKVHETAWNAFKEAAKVAKDLGLYAAGQDLLSDSFSGNVRGLGPGVAEMEIEERASEPIAIFMADKTEPGAYNLPLYKMFADPFNTPGLVIDPTMHGGFKFEVLDVYQGEAVMLSAPQEIYDLLALIGTPARYVIRRVYRNEDNLLAAVVSIERLNLIAGKYVGKDDPVMIVRLQHGLPALGEALEAFAFPHLVPGWMRGSHYGPLMPVSQRDAKATRFDGPPRLLGLGFNVKNGRLVGPTDLFDDPAFDETRRLANIVADYMRRHGPFMPHRLEPTEMEYTTLPLILEKLKDRFKKESDVYKAKESIYAKEESQGHD
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Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).
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F9VN79
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RNH_SULTO
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Ribonuclease HI (RNase HI) (Sto-RNase HI) (EC 3.1.26.4)
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MIIGYFDGLCEPKNPGGIATFGFVIYLDNRKIEGYGLAEKPFSINSTNNVAEYSGLICLMETMLRLGISSPIIKGDSQLVIKQMNGEYKVKAKRIIPLYEKAIELKKKLNATLIWVPREENKEADRLSRVAYELVRRGKLRDIGCIILT
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Nuclease that specifically degrades the RNA of RNA-DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. In the presence of Mn(2+) or Co(2+) can also cleave an RNA-RNA hybrid the dsRNase activity is 10- 100-fold lower than RNase H activity. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant.
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G0HV10
|
PYRG_HALHT
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CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
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MPTEPETDYDPELGRKFIFVTGGVMSGLGKGITAASTGRLLKNAGFDVTAVKIDPYLNVDAGTMNPFQHGEVYVLKDGGEVDLDLGNYERFLDIDMTFDHNVTTGKTYQHVIEKERSGDYLGRTVQIIPHITDDIKRRIREAAEGNDVCIIEVGGTVGDIEGMPYLEALRQFAHEEDEDDILFTHVTLVPYSKNGEQKTKPTQHSVKELRSIGLQPDILVGRCSDKLDIDTKEKIALFCDVPTEAVFSNPDVDDIYHVPLMVEEEGLDQYVMEELDIATEALPEDERENRWRDLVTQNTEGEVDIALVGKYDLEDAYMSVHEALKHAGLEKNVDVNVQWVNSEKMNDHHADRMREADAIVVPGGFGARGTEGKIEAIRYARENDIPFLGLCLGFQMAVVEYARNVLDLDDAHSAELDEDTPHPVIDILPEQYEIEDMGGTMRLGAHETEIDANTLAATLYGGESCTERHRHRYEVNPEYIDDLEAAGLKFSGYAENRMEILELAPEDHPYFIGTQFHPEFRSRPTRASPPFVGLLEAVLGDDPHTVTTEEVSH
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Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. {ECO:0000255|HAMAP-Rule:MF_01227}.
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G0L322
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AGAA_ZOBGA
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Beta-agarase A (EC 3.2.1.81) [Cleaved into: Beta-agarase A catalytic chain (AgaAc)]
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MKKNYLLLYFIFLLCGSIAAQDWNGIPVPANPGNGMTWQLQDNVSDSFNYTSSEGNRPTAFTSKWKPSYINGWTGPGSTIFNAPQAWTNGSQLAIQAQPAGNGKSYNGIITSKNKIQYPVYMEIKAKIMDQVLANAFWTLTDDETQEIDIMEGYGSDRGGTWFAQRMHLSHHTFIRNPFTDYQPMGDATWYYNGGTPWRSAYHRYGCYWKDPFTLEYYIDGVKVRTVTRAEIDPNNHLGGTGLNQATNIIIDCENQTDWRPAATQEELADDSKNIFWVDWIRVYKPVAVSGGGNNGNDGATEFQYDLGTDTSAVWPGYTRVSNTTRAGNFGWANTNDIGSRDRGASNGRNNINRDINFSSQTRFFTQDLSNGTYNVLITFGDTYARKNMNVAAEGQNKLTNINTNAGQYVSRSFDVNVNDGKLDLRFSVGNGGDVWSITRIWIRKVTSNSANLLAAKGLTLEDPVETTEFLYPNPAKTDDFVTVPNSEIGSSIIIYNSAGQVVKKVSVVSENQKISLEGFAKGMYFINLNGQSTKLIVQ
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Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place.
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G0LXV8
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LATA_LATHA
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Alpha-latrotoxin-Lh1a (Alpha-LTX-Lh1a) (Alpha-latrotoxin) (Alpha-LTX)
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SLVRMRREGEEDLTLEEKAELCSELELQQKYVDIGSNIIGDLSSLPIVGKIVGTIAAAAMAVTHVASGRLDIEQTLGGCSDVPFDQIKEILEERFNEIDRKLESHSAALEEITKLVEKSISAVEKTRKQMNKRFDEVMRSIQDAKVSPLVSKINNFARYFDTEKERIRGLKLSDYILKLEEPNGILLHFKESRTPRDDSLQAPLFSIIQERYAVPKSIDDELAFKVLYALLYGTQTYVSVMFFLLEQYSFLANHYYEKGDLEKYDEYFNSLNNVFLDFKSSLVGTGTSNNEGLLDRVLQVLVTVKNSEFLGLEKNGVNEMLNEKINLFNKIKVEIEGKQRMTLSETPENFAQISFDKDITTPIGDWRDGREVRYAVQYASETLFSKISHWSDPVGVREKACPTLRMPVDQTRRNILVFRKFDSSKPQLVGEITPYQSNFIDIDRDLYNTANNPDSAVGFKEFTKLNYDGANIRATFEQGRTVFHAAAKSGNSRIMIGLTFLVKSNELNQPDKKGYTPIHVAADSGNAGIVNLLIQRGVSINSKTYNFLQTPLHLAAQRGFVTTFQRLMESPEININERDKDGFTPLHYAVRGGERILEAFINQIRIDLNAKSNKGLTPFHLAIIKDDWPVASTLLGSKKVDVNAVDENNMTALHYAAILGYLETTKQLINLKEINADVVSSPGLLSALHYAILYKHDDVASFLLRSSNVNVNLKALGGITPLHLAVIQGRTQILSLMFDIGVNIEQQTDEKYTPLHLAAMSKYPELIQILLDQGSNFEAKTNSGATPLHLATFKGKSKAALILLNNEVNWRDTDENGQMPIHGAAMNGLLDVAQAIISIDATVLDIKDKNSDTPLNLAAQKSHIDVIKYFIDQGADINTRNKTGHAPLLAFSKKGNLDMVKYLFDKNANVYIADNDGINFFYYAVRNGHLNIVKYAMSEKDKFEWSNIDNNRRDECPKEECAISHFAVCDAVQFDKIEIVKYFVTTLGNFAICGPLHQAARYGHLDIEKYLVEEEDLNVDGSKPDTPLCYASENGHLAVVQYLVSNGAKVNHDCGNGMTAIDKAITKNHLQVVQFLAANGVDFRRKNKLGATPFLTAVSENAFDIAEYLIRENRQDIDINEQNVDKETALHLAVYYKNLQMIKLLVKYGIDMTIRNAYDKTALDIATDLKNSNIVEYLKTKSGKFRREYKSSYGEHSLLQTNKISSFIDGKNIEHDHPQFINADNESSQLFSDTASNIDVIGPLLLIDVLIRYFSKQGYISKESDSASDGITQAAALSITEKFEDVLNSLHNESAKEQVDLAEVHGKVYAALKSGRNSQIHPILCSSLKSISTLKPEDMEKLGSVIMNSHS
|
Presynaptic neurotoxin that causes massive release of neurotransmitters from vertebrate (but not invertebrate) nerve terminals and endocrine cells via a complex mechanism involving activation of receptor(s) and toxin insertion into the plasma membrane with subsequent pore formation. Binds to neurexin-1-alpha (NRXN1) in a calcium dependent manner, adhesion G protein-coupled receptor L1 (ADGRL1, also termed latrophilin-1 and calcium-independent receptor of latrotoxin (CIRL)), and receptor-type tyrosine-protein phosphatase S (PTPRS), also termed PTP sigma. NRXN1 and PTPRS are suggested to provide a platform for binding and subsequent pore formation events. In contrast, binding to ADGRL1 does not involve oligomerization and channel formation, but direct downstream stimulation of the synaptic fusion machinery (By similarity). Induces rapid muscle contracture and loss of twitch tension when added to the isolated and indirectly stimulated chick biventer cervicis nerve-muscle preparation.
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G0RUP7
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XYN2_HYPJQ
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Endo-1,4-beta-xylanase 2 (Xylanase 2) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase 2) (Alkaline endo-beta-1,4-xylanase)
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MVSFTSLLAGVAAISGVLAAPAAEVESVAVEKRQTIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGNFVGGKGWQPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPSTGATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSVNTANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS
|
Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose.
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G0RV93
|
GCE_HYPJQ
|
4-O-methyl-glucuronoyl methylesterase (EC 3.1.1.117) (Glucuronoyl esterase) (GE)
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MASRFFALLLLAIPIQAQSPVWGQCGGIGWSGPTTCVGGATCVSYNPYYSQCIPSTQASSSIASTTLVTSFTTTTATRTSASTPPASSTGAGGATCSALPGSITLRSNAKLNDLFTMFNGDKVTTKDKFSCRQAEMSELIQRYELGTLPGRPSTLTASFSGNTLTINCGEAGKSISFTVTITYPSSGTAPYPAIIGYGGGSLPAPAGVAMINFNNDNIAAQVNTGSRGQGKFYDLYGSSHSAGAMTAWAWGVSRVIDALELVPGARIDTTKIGVTGCSRNGKGAMVAGAFEKRIVLTLPQESGAGGSACWRISDYLKSQGANIQTASEIIGEDPWFSTTFNSYVNQVPVLPFDHHSLAALIAPRGLFVIDNNIDWLGPQSCFGCMTAAHMAWQALGVSDHMGYSQIGAHAHCAFPSNQQSQLTAFVQKFLLGQSTNTAIFQSDFSANQSQWIDWTTPTLS
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Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin. Does not hydrolyze substrates of other carbohydrate esterases such as acetylxylan esterase, acetyl esterase and feruloyl esterase.
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G0S0Y3
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PAN3_CHATD
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PAN2-PAN3 deadenylation complex subunit PAN3 (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 3) (PAN deadenylation complex subunit 3)
|
MAPLDLTRGQTDACSTENKDILCRNVLIYGHCRYEDQGCTYNHDQNKNSSQPEAPSKKMFNVDSPSFTPSGQSTVLPKKTTLSSQAASAAPFTPRGGGTPTLQTTAESTMFNPAAIREFTPQNYDLGNNNANGISQENGLYPDPFTMSTMGTALPTAGQYNLPLYGDHSGLAAPGAPFYPPHAAYPTGPIQPPHYHLYQPFGPYRQELQPWQRATYDFFMPQNLREDLQKKQFATLQVIPNSGLPQLEHWHSLVPLDTSNRKNTSCFGYPSWVYKAQNSRNGRHYALRRLEGYRLTNEKAILNVMKDWKKIKNASIVTIHEVFTTREFGDSSLIFAYDFHPLSKTLQEHHFQPIHGNRYRPPPAVPENTIWGYICQIANALKTIHSNRLAARCLEPSKIILTDINRIRLSACAILDVVQFGMNSRSVVELQQEDFVKFGKLILSLATGTLPAHLNNIPAALETLGNKYSANLKSAVNWLLDTSSGETKTIEHFMTGIASQMTTFFDLALQDNDEKLFHLAREVENGRIARSLMKLLTILERGDYDGVPSWSETGDRYQLKLFRDYVFHRVDADGKPNLSIGHMLTCMSKLEAGVDENILLTSRDNETVFVLSYRELRQMYDRAFNELVKASKTGAPGANT
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Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1. {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509}.
|
G0S196
|
ATC5_CHATD
|
Phospholipid-transporting ATPase DNF1 (EC 7.6.2.1) (CtDNF1)
|
MAPPQEEGGGNGTELSMQRSRWATRRLTVKSGARKRLSLMTRAQAKNSATEKRQSGVTDDGSPAADGDQKEGSISSSNNGGSAPRKLYFNLPLPPELKDEEGHPIQQFPRNKIRTAKYTPLSFIPKNLWFQFHNIANIFFLFLVILVIFPIFGGVNPGLNSVPLIVIITVTAIKDAIEDYRRTILDIELNNAPVHRLQGWENVNVEKDNVSLWRRFKKANSRFFGSIWHLIERLWKEDAQSMRQRFASADPRMSIETRTAPWDPSHRRSVASHTEEIQMTPVPSPVPHDPDVPTVSSAIENEATLLQNLKGDLINHEIPVSGKARFHKDAWKNLVVGDFVRIYNDDELPADIIILATSDPDGACYVETKNLDGETNLKVRQALRCGRTLKHARDCERAQFVIESEPPQPNLYKYNGAIRWKQRVPWDPHGEPREMSEPIGIDNLLLRGCHLRNTEWALGVVVFTGHDTKIMMNAGITPSKRARIARELNFNVICNFGILLIMCLIAAIANGIAWGKTDASLAWFEYGSIGGTPALTGFITFWAAVIVFQNLVPISLYISLEIVRTLQAFFIYSDVGMYYEKIDQPCIPKSWNISDDVGQIEYIFSDKTGTLTQNVMEFKKATINGQPYGEAYTEAQAGMDRRRGINVEEEAKVIREEIAAAKVRAIRGLRELHDNPYLHDEDMTFIAPDFVEDLAGKNGPEQQQATEHFMLALALCHTVVAEKQPGDPPKMIFKAQSPDEAALVATARDMGFTVLGMSDGGINVNVMGKDMHFPVLSIIEFNSSRKRMSTIVRMPDGRILLFCKGADSVIYSRLKKGEQADMRRETAQHLEMFAVEGLRTLCIAERELSEEEYREWRREHDLAATALENREEKLEEVADKIERDLTLLGGTAIEDRLQDGVPDTIALLADAGIKLWVLTGDKVETAINIGFSCNLLNNDMDLLRLQVNESDASTEDDYLQLAEEQLKTNLERFNMTGDDEELKRARKDHNAPSPTYALVIDGFTLRWVLSDSLKQKFLLLCKQCKSVLCCRVSPAQKAAVVSMVKNGLDVMTLSIGDGANDVAMIQEADVGVGIAGEEGRQAVMSSDFAIGQFRFLQRLVLVHGRWSYRRLAETISNFFYKNMIWTWSIFWYQCYCNFDIAYIFEYTYILMFNLFFTSVPVILMGVLDQDVSDTVSLAVPQLYRRGIERKEWTQTKFWLYMIDGVYQSVMSFFIPFIFVVLTPTAAGNGLDVSERTRLGAYIAHPAVITINGYILINTYRWDWLMLLSIVLSDVFIFFWTGVYTATTYSAGFYQAAPQVYQELTFWMCLIVTPALCLLPRLVVKCIQKQRFPYDVDIIREQANRGDFAAADAAAVAALGGPERVEGESLGSLSSSGKGSGRSKKSKHQQYASVDEDRRPIYPPSIATHNTRAQNGSDGTTYIMQSRTSTELQQEMPFDRDREEETPAVRPSIERTRPSYDRIRRSIDRVRPSFEASNDFTSAARLSRIESTHSSLGHTYSHQRESYAGESSGAQQGQEPGQRRFNLATVRKRGLSAFSKKSIDTTEGEPPREPPM
|
Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and phosphatidylserine from the lumenal to the cytosolic leaflet of membranes and ensures the maintenance of asymmetric distribution of phospholipids. May also transport glucosylceramide and phosphatidylethanolamine (By similarity).
|
G0S3J5
|
RIO1_CHATD
|
Serine/threonine-protein kinase RIO1 (EC 2.7.11.1) (EC 3.6.3.-)
|
MTPAPEPQDPPTIHEPVATEQTDDISDWDVESDYEDGYGAPSKSQAQGGASAADRPKINAHARIDDQMTDLARHASKIRLDNLTMQQIFRDKDRTDNATSDQVLDNHTRMIILNMLNRNIISEIYGTISTGKEANVYNAVAYDNNGERIERAVKVYKTIILGFKDRERYLAGEQRFKTIVDKALSAPRKMIKLWAEKEFRNLKRLHTAGIPCPEPIYLKYNVMVMGFLGDHTNGYAFPRLHDTKITGETLEETEAEWRRLYINLLSMMRRMYQVCGLVHGDLSEYNILYNEGVLYIIDVSQSVEHDHIEATNFLRMDIRNVNDFFARRGVDTLSDRTVYHFITDSTGAVDENGMRKAIDNLYATRPPLAESEEARAEQEIDNQVFRNQFIPTTLEEVYNLEVELGKKVDTRLYQHMLADSKVPESTGGEHKSGEGGESGSEDEEGDEGESGEVESGDEEREEGEGDRFEKKRPRGKKHLDKAEKHAHKMAVKEAKREKRKEKMPKHVKKKLVAANKKRK
|
Involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit (By similarity). In vitro, has strong ATPase activity and only low protein kinase activity.
|
G0S4X6
|
ODP2_CHATD
|
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (MRP3) (Pyruvate dehydrogenase complex component E2) (PDC-E2) (PDCE2)
|
MLAQVLRRQALQHVRLARAAAPSLTRWYASYPPHTIVKMPALSPTMTSGNIGAWQKKPGDAITPGEVLVEIETDKAQMDFEFQEEGVLAKILKETGEKDVAVGSPIAVLVEEGTDINAFQNFTLEDAGGDAAAPAAPAKEELAKAETAPTPASTSAPEPEETTSTGKLEPALDREPNVSFAAKKLAHELDVPLKALKGTGPGGKITEEDVKKAASAPAAAAAAPGAAYQDIPISNMRKTIATRLKESVSENPHFFVTSELSVSKLLKLRQALNSSAEGRYKLSVNDFLIKAIAVACKRVPAVNSSWRDGVIRQFDTVDVSVAVATPTGLITPIVKGVEAKGLETISATVKELAKKARDGKLKPEDYQGGTISISNMGMNPAVERFTAIINPPQAAILAVGTTKKVAVPVENEDGTTGVEWDDQIVVTASFDHKVVDGAVGAEWMRELKKVVENPLELLL
|
The 10-megadalton pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) and catalyzes the overall oxidative decarboxylation of pyruvate to form acetyl-CoA and CO(2). Within the complex, pyruvate and thiamine pyrophosphate (TPP or vitamin B1) are bound by pyruvate dehydrogenase E1 subunits alpha and beta and pyruvate is decarboxylated leading to the 2-carbon hydrohyethyl bound to TPP. The E2 component contains covalently-bound lipoyl cofactors and transfers the hydroxyethyl group from TPP to an oxidized form of covalently bound lipoamide, and the resulting acetyl group is then transferred to free coenzyme A to form acetyl-CoA and reduced dihydrolipoamide-E2. Finally, the flavoprotein dihydrolipoamide dehydrogenase (E3) re-oxidizes the lipoyl group of dihydrolipoamide-E2 to form lipoamide-E2 and NADH. A fourth subunit, E3BP, is responsible for tethering E3 in proximity to the core, forming the entire metabolon (Probable).
|
G0SAK8
|
PAN2_CHATD
|
PAN2-PAN3 deadenylation complex catalytic subunit PAN2 (EC 3.1.13.4) (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 2) (PAN deadenylation complex subunit 2)
|
MDADWDEVTRIAYPAPGTNDFPRPATAVAFDPIAELLWAGFDRGRVCSFYGRDLTRYTAFKIQPASEGPVRQFLFHDKGVIVLGTRSVHMAMRRGPALWNIRHENMKDLRCMSFTSKGTQEIIVAGWQDTMLVIDVLKGDIIKQIPAQHHYSIMKKSRYICAATKTGSVDLIDPLSFKIVRSWQAHASYINDMDAQNDFIVTCGGSLKQQAAQTYMLDPYVNVFDLKNMASMKPMPFPPLAAHVRLHPRMLTTAIVTSQHGQMHVVDIMNPNSSTVRYANISSYVKLFEIAPSGEALVIGDADCNIHLWGSPTKIHFTDMAIPIELPEPEEPAPVLDWSIETPLSSIGLPYYREPLFSAWPADIISDVGAPPLQLEPSFVATLKQAEWGLYGKNTRNVRRNQVEDTRNTNKQSNALQAPKFLSERARESALSSGGDSSSDPQVDQEPEDPNEIESLKPEAPPLYRNLEIKYSKFGVDDFDFGYYNKTRYAGLENHIPNSYANSLLQLMHYTPLLRNMALQHAATACVSDLCLLCELGFVFDMLQKAEGATCQATNMFKALSGTPQAAPLGLLEEETHVPSLATMAQNLSRFLLEKIHNEYRTIPPISTALEQSLFNFPHPPTPDELVAKVLATSAVATIKCMNCRSETTRPGTTHVIDLLYPPPKTAGRGGRASKVTFSQVLKMGVERETTSKGWCSRCQRYQNLQMRKTIHSVPAVLVVNAGVSNQEHRKLWSTPGWLPEEIGIIVDQGQFFCFEGEDLKLHLQRGIHNITVYSLIGMVINIESHSPQKSHLVGIINVAHAEATPPGENKWHLFNDFSVRPVSAAEALTFNAAWKMPAVLLFQIKSANNKSNLDWKTNLDTSILYKDTNPNTEKKTYRTLDQERERPGPDTIVALDTEFVSLKQPEIQMNSDGERETIRPMSHALARVSVVRGQGENEGSAFIDDYIAIREPVVDYLTLYSGITASDLDPRTSKHNLVSLKTAYKKLWVLLNLGCKFLGHGLKQDFRVINIQVPRAQVIDTIEVFYLKSRLRKLSLAFLAWYLLKEDIQLETHDSIEDARTALKLYRKYLEFDDAGILEAMLEDIYKAGRATNFKPPRREDREKELQRQSTPPNSTAPNDCGAKPDGNGNENGGEPATPARKTGGITAPTFGAVNVFGTPSKASSPLPK
|
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24872509}.
|
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