ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8KES6 | MLDITYIRQNPDDVKEMLRRRQQQGDAPKVDRLLERDAERKAMVQRTDDLKALRNRVSKEIANIKRTGQGSADELIGQMKQVSDEIADLDLALSALEAEIEELLLTLPNKLHKSVPEGRSAEENVLYKGPVSFEHNLDFPVKNHLELGKSLGILDFERGAKISGAGFPVYTGKGARLERALINFMLDTHSANHGYTEVFPPFMVNQESLRGTGQWPKFADQVYHMPEDGLYAIPTAEVPVTNLHRGEILDADKLPIAYAAYSACFRREAGSYGKDTRGFLRVHQFNKVEMVRFTRPEASYEALEEILGHAEAILVALKIP... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
B2VC55 | MLDPNLLRNEPDAVAEKLARRGYKLDVDTLRAHEERRKVLQVETENLQAERNSRSKSIGQAKARGEDIEPLRQEVNALGERLDAAKAELDALLTCINDFSMAIPNIPADVVPLGKDDSENQEISRWGEPRQFDFTVRDHVELGEMAAGLDFAAAVKLTGSRFIVMKGQIALMHRALSQFMLDLHTEQHGYQETYVPYLVNHASLYGTGQLPKFGEDLFHTRPLDEEASSSNYALIPTSEVPLTNLVRDEILEEETLPLKMTAHTPCFRSEAGAYGRDTRGLIRMHQFDKVEMVHITRPEDSMDALEELVGHAEKVLQLLN... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q8RH11 | MLELKFMRENVEMLKEMLKNRNSNVDMDAFVELDSKRREVLSEVENLKRERNNASAEIANLKKEKKNADHIIEKMGEVSTKIKDLDAELVEIDEKIKDIQLNIPNVYHPSTPIGPDEDYNLEIRKWGIPKKFDFEPKSHWDIGEDLGILDFERGAKLSGSRFVLYRGAAARLERAIINFMLDVHTLEEGYTEHITPFMVKAEVCEGTGQLPKFEEDMYKTTDDMYLISTSEITMTNIHRKEILEQAELPKYYTAYSPCFRREAGSYGKDVKGLIRLHQFNKVEMVKITDAESSYDELEKMVNNAETILQRLELPYRVIQL... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
C1A8M5 | MHDIRLLRDQLDVLREGMRRRGKLTELGDVLDRAESLEQARRTAITELEAQQARRNKVTQEVAQRRKAGEDATALIAEGRAIGEQITALEQRRNEADAAVQAMLYELPNIPLADVPEGDETANTVVRTWGTPRTPDASIVPHWDKGEALGMLDLARGAKISGSGFIVYRNRGARLVRALMNMMLDIHTEEHGYEETWVPLVVNRASMTGTGNFPKFEEDAYAITEDELFLIPTAEVPVTNLYRDEILDAEELPKRFCAFSACFRREAGAAGKDTRGLLRVHEFDKVELVRYANPETSLEELELLTSQAETILKRLELPYR... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q5L3Y0 | MLDVKILRTQFEEVKEKLMQRGGDLTNIDRFEQLDKDRRRLIAEVEELKSKRNDVSQQIAVLKREKKDAEPLIAQMREVGDRIKRMDEQIRQLEAELDDLLLSIPNVPHESVPIGQSEEDNVEVRRWGEPRSFSFEPKPHWEIADRLGLLDFERAAKVAGSRFVFYKGLGARLERALINFMLDIHLDEFGYEEVLPPYLVNRASMIGTGQLPKFAEDAFHLDSEDYFLIPTAEVPVTNLHRDEILAADDLPIYYAAYSACFRAEAGSAGRDTRGLIRQHQFNKVELVKFVKPEDSYDELEKLTRQAETILQRLGLPYRVV... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q6F2A0 | MLDINFIESNLVKVKEQLNKRSGDYSLIIDEAVELNVQRKSILKEVENLKANKNNLSKQVGELMRNKQSDEANKIKEEVTLINSKIEKLDDSLKLVQEQLTSKLQNIPNIPNDNMPIGNDDNDNVEVRQWGNELIKKHNTPHWDIADKLKLVDFEAGPKLSGSRFVVYTGLGAKLVRSLSNILLNLHTSKGYTEITVPLLVNPQAMYGTGQLPKFKEDAYITTNDQYLIPTGEVPLTNLHAGEILDLNQLPIHYTTYSQCFRQEAGSAGRDTKGLIRLHQFNKVELVKITNQESSEAELQAMVNDAEAVLQLFNLPYRVV... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q6KIJ8 | MLDIKLILKNKDFVISKLKQRSNFNVSEIEKLYTLGTERANILISLSELQSKRNEISSKIGEAKRNKTDALFFMDEVENIKKELSILEEKSTKIENKIQELISFIPNIPLDDVPFGKDDTDNVILKEFPKIGRGLVKAKKPHYEIGVEKDLIDFSRGAKLSGSRFIVYKNAGAKLIRALESFMLDTHEKNGYSEIMPPFLVNSKMMYGTGQLPKFKEDLFKIEGHDLYLIPTAEVPVTNLFNNEIIDLEKNSKFSSFTNCFRSEAGSAGRDTKGIIRLHQFNKVELVEFASEQKSLRAFNSVLKNAKYLLELLEIPYREV... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q46F20 | MLDLKFVRSSPDIVRHALINRNMSTELIDSLLEYDIAWRKCLTEGDELKHKRNVVTREIAKLKKENKDTLSKIEEMQGINSRIKEIDDIIRDYKSKIHEIMLRIPNIPSSTTPVGKDENDNPVVRIVGEPRKFTFTPKPHWEIGEALDILDFEKGAKISGQGFTVYKGMGAKLERALVNFMLEVHARQGYLEVFPPVLINEKAMTGTGQLPKFKDDMYLCTDGYYLAPTAEVPVTNLFMDDYIEKLPVFLTAYTACFRREAGKHGQDTRGIIRQHQFNKVELVKFVKPETSYDELEKLTNDAEEILKLLKLPYRVVNLCT... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q1H290 | MLDIQQLRNDLDNVVARLSSRGFAFDINAFIALENERKTVQTRTQDLQAKRNATSKQIGIAKSRGEDVASIMAEVAGLGAQLKEGEERLAAIQAELQQLLLSVPNLPHESVPVGKSEEDNVEVRRVGTPRRFDFDVKDHTDIGTPLGLDFDTGAKLAGARFTLMRGQIARLHRALAQFMLDTQTEQHGYTECYTPYIVNADSLRGTGQLPKFEADLFAAQKGGQEGESNEAFYLIPTSEVTLTNTVRDEIVPLDSLPIKLTAHTPCFRSEAGSYGRDTRGMIRQHQFDKVEMVQITHPERSYDALEEMVGHAEHVLQALG... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q2FS27 | MLDIRFVRANPDAIREDLKKRNDMEKLAWIDDLLVQDIRHRELIGQTNELRRRRNSISYDINRAKKAGEDASALIAEAAGLPGRIKENEAEMEEISKKIRYYLMRIPNILHESVPVGADDTQNVEVKRYGTPRTFTFELKNHGQLAADNDWADFERATKTSGAGFYFLKGNLVLLDLALQRFSLDILMEKGYTPIIPPYMINRKSYEEVTDLDDFEKVMYKIEDDDAYLIATSEHPMAAMYQDEIFEEKDLPLRLAGLSPCFRREIGSHGLDTKGLFRVHQFHKVEQFVYCHPDDSWTIHEELRENAEEIFQKLEIPYRV... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
B3DX68 | MLDIQLIRHNLAQTKQKLALRSKGLETLLDHIFELDFKKRSLQSEIEKYRALRNKQSKEIGLKKIKGENVEGQFSELKKMGSRIEEMEKELIQFENQINTLLLSLPNIPHDSVPTGGPEANKVVKTWGEPRQANFPLKTHWELGRELGILDLERGAKLSGSGFSLFTGNGAKLQRALIQFMLTIHTEEHGYKELWPPYLVTEDCMRGTGHLPKFALDMYATDKDNLYLIPTGEVPLTNFHRDEILAESSLPLRYVAYTPCFRREAGSAGKDTRGLLRLHQFDKVELVQITKPENSYTALEEMVSHAENILRSLNLCYRVV... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
A3CTP4 | MLELKFVRAHPEIVRADLTKRGDTEKLAWVDEVLEMDRRARELTVAIGDLRNRRNVISREISQARKAGNDITELLAEAAGLPERIKEVETERETLTEAVRYRLMRLPNILHESVPVGKDDSENVEIRRWGEPEIPAFDLENHGALAVEHGWADFERAAKIAGSGFYFLKGRLALLDMALQRFAMDILVEHGYTPIIPPYMMNRAAYEGVTDLADFENVMYRIDGEDEYLIATSEHPMAAMYCDEIFEEKDLPLRLAGLSPCFRREIGAHGLDTKGLFRVHQFHKVEQFIYATPEQSWDLHEELMANAEEVFQRLGLPYRI... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q2S1G4 | MLDLDTVRNDPRRVKEALRAKGIGSPDLVDTLLEIDETRRSAITELQDVQSRQNELSQQIGALKREGKDEEAEAIIEKTGRMKEKINRLKEEVQEAEARQEELVLELPNIPHPSVPVGADEDDNEVEATVGEMPAFDFDPAPHWELADRHNLVDLERGAKVAGSGFPFYLGKGARLQRALLNFFLDRARERGYTEMQAPLFVNPESAKGTGQIPDKDALMYEIPRDDFYPIPTAEVPVTNFHRDEILAADDLPRRYCTYSPCWRREAGSYGSDVRGLNRLHQFDKVELVRIVPPDESYRALDALLEDAESALDALDLPYR... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q920N7 | MAVDVTEYHLSVIKSPPGWEVGVYAAGALALLGIAAVSLWKLWTSGSFPSPSPFPNYDYRYLQQKYGEAYVEAKLKRVPPWNDQRTTTRGPPSRKGSLSIEDTFESISELGPLELMGRELDLAPYGTLRKSQSADSLNSISSVSNTFGQDFTLGQVEVSMDYDGASHTLHVAVLQGKDLLEREEATFESCFMRVSLLPDEQIVGISRIQRNAYSIFFDEKFSVPLDPTALEEKSLRFSVFGIDEDERNVSTGVVELKLSVLDLPLQPFSGWLYLQDQNKAADAVGEILLSLSYLPTAERLTVVVVKAKNLIWTNEKSTAD... | Function: Synaptic vesicle phosphoprotein that enhances spontaneous neurotransmitter release but does not effect induced neurotransmitter release (By similarity). Unlike other synaptotagmins, it does not bind Ca(2+) or phospholipids (By similarity). Essential for mossy-fiber long-term potentiation in the hippocampus .
... |
P97610 | MAVDVTEYHLSVIKSPPGWEVGVYAAGALALLGIAAVSLWKLWTSGSFPSPSPFPNYDYRYLQQKYGEAYVEAKLKRVPPWNAQRTTTRGPPSRKGSLSIEDTFESISELGPLELMGRELDLAPYGTLRKSQSADSLNSISSVSNTFGQDFTLGQVEVSMDYDGASHTLHVAVLQGKDLLEREEATFESCFMRVSLLPDEQIVGISRIQRNAYSIFFDEKFSVPLDPTALEEKSLRFSVFGIDEDERNVSTGVVELKLSVLDLPLQPFSGWLYLQDQNKAADAVGEILLSLSYLPTAERLTVVVVKAKNLIWTNDKTTAD... | Function: Synaptic vesicle phosphoprotein that enhances spontaneous neurotransmitter release but does not effect induced neurotransmitter release . Unlike other synaptotagmins, it does not bind Ca(2+) or phospholipids . Essential for mossy-fiber long-term potentiation in the hippocampus (By similarity).
PTM: Phosphoryl... |
Q7L8C5 | MVLSVPVIALGATLGTATSILALCGVTCLCRHMHPKKGLLPRDQDPDLEKAKPSLLGSAQQFNVKKSTEPVQPRALLKFPDIYGPRPAVTAPEVINYADYSLRSTEEPTAPASPQPPNDSRLKRQVTEELFILPQNGVVEDVCVMETWNPEKAASWNQAPKLHYCLDYDCQKAELFVTRLEAVTSNHDGGCDCYVQGSVANRTGSVEAQTALKKRQLHTTWEEGLVLPLAEEELPTATLTLTLRTCDRFSRHSVAGELRLGLDGTSVPLGAAQWGELKTSAKEPSAGAGEVLLSISYLPAANRLLVVLIKAKNLHSNQSK... | Function: May be involved in transport vesicle docking to the plasma membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 46885
Sequence Length: 426
Domain: The first C2 domain/C2A does not mediate Ca(2+)-dependent phospholipid binding.
Subcellular Location: Membrane
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Q9EQT6 | MVLSVPVIALGATLGTATSILALCGVTCLCRHMHPKKGLLPRDREPDPEKARPGVLQAAQQFNIKKSTEPVQPRPLLKFPDIYGPRPAVTAPEVINYADYTLETTEESAAPASPQAQSDSRLKRQVTEELSIRPQNGVVEDVCVMETWNPEKAASWNQAPKLHFRLDYDQKKAELFVTSLEAVTSDHEGGCDCYIQGSVAVKTGSVEAQTALKKRQLHTTWEEGLALPLGEEELPTATLTLTLRTCDRFSRHSVIGELRLGLDGASVPLGAAQWGELKTTAKEPSAGAGEVLLSISYLPAANRLLVVLIKAKNLHSNQSK... | Function: May be involved in transport vesicle docking to the plasma membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 46870
Sequence Length: 426
Domain: The first C2 domain/C2A does not mediate Ca(2+)-dependent phospholipid binding.
Subcellular Location: Cytoplasmic vesicle membrane
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Q8NB59 | MAIEGGERTCGVHELICIRKVSPEAVGFLSAVGVFIILMLLLFLYINKKFCFENVGGFPDLGSEYSTRKNSQDKIYNSYMDKDEHGSSSESEDEALGKYHEALSRTHNSRLPLADSRQRNYAWETRQKYSPLSAEYDGYSSEASIDEGNCIQRMRRTPPLDELQPPPYQDDSGSPHLSCTPSEIGDSKCEFSHCSNSPRCSYNKCPSEGSTGHEIESFHNKGYEEDVPSDSTAVLSPEDMSAQGSSSQLPKPFDPEPEAKYGTLDVTFDYDSQEQKLLVTVTAVTDIPTYNRTGGNSWQVHLVLLPIKKQRAKTSIQRGP... | Function: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 62287
Sequence Length: 555
Subcellular Location: Membrane
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Q7TN84 | MAIEGGERTCGVHELICIRKVSPEAVGFLSAVGVFIVLMLLLFLYINKKFCFENVGGFPDLGSGYNTRTNSQDKMYNSYMDRDEPGSSSESEDEALGKYHEALSRTHNSRWPLVDSRQKSYAWETRQKYSPLSAEYDGYSTEASMEDGNCIQRMRRTPPLDELQPPPYQDDSGSPHLSCTPSEIGDAKCEISHCSNSPRCSFNKCPSEGSTGHEAESYHNKGYEDDVPSDSTAVLSPEDMSAQGSSSQLPKPFDPEPEAKYGTLDVTFDYDSERQKLLVTVTAVTDIPTYNRTGGNSWQVHLVLLPIKKQRAKTSIQRGP... | Function: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 62044
Sequence Length: 555
Subcellular Location: Membrane
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Q9BQS2 | MAEQLALVIGGTIGGLLLLLLIGASCCLWRRFCATLTYEELPGTPAMATTAASSGQRDRPCQPHARTQLSRPPAVPFVVPPTLQGRDWVPLHSGEWADAPWDPCPASELLPHTSSGGLGDACMVGAINPELYKFPEDKSETDFPDGCLGRLWFSVEYEQEAERLLVGLIKAQHLQAPSETCSPLVKLYLLPDERRFLQSKTKRKTSNPQFDEHFIFQVSSKTITQRVLKFSVYHVDRQRKHQLLGQVLFPLKNETLVGDCRRVIWRDLEAESLEPPSEFGDLQFCLSYNDYLSRLTVVVLRAKGLRLQEDRGIVSVFVKV... | Function: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 47375
Sequence Length: 421
Domain: Neither C2 domains mediates Ca(2+)-dependent or -independent phospholipid binding.
Subcellular Locati... |
Q9BSW7 | MAYIQLEPLNEGFLSRISGLLLCRWTCRHCCQKCYESSCCQSSEDEVEILGPFPAQTPPWLMASRSSDKDGDSVHTASEVPLTPRTNSPDGRRSSSDTSKSTYSLTRRISSLESRRPSSPLIDIKPIEFGVLSAKKEPIQPSVLRRTYNPDDYFRKFEPHLYSLDSNSDDVDSLTDEEILSKYQLGMLHFSTQYDLLHNHLTVRVIEARDLPPPISHDGSRQDMAHSNPYVKICLLPDQKNSKQTGVKRKTQKPVFEERYTFEIPFLEAQRRTLLLTVVDFDKFSRHCVIGKVSVPLCEVDLVKGGHWWKALIPSSQNEV... | Function: Plays a role in dendrite formation by melanocytes .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53849
Sequence Length: 474
Subcellular Location: Membrane
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Q920M7 | MLEPLNEGLLSRISDVLLCGWTCQHCCQRCYESSCCQSSEDEVEILGPFPAQTPPWLMASRSNDKDGDSVHTASDVPLTPRTNSPDGRRSSSDTSKSTYSLTRRISSLDSRRPSSPLIDIKPVEFGVLSAKKESIQPSVLRRTYTPDDYFRKFEPRLYSLDSNLDDVDSLTDEEIMSKYQLGMLHFSTQYDLLHNHLTVRVIEARDLPPPISHDGSRQDMAHSNPYVKICLLPDQKNSKQTGVKRKTQKPVFEERYTFEIPFLEAQRRTLLLTVVDFDKFSRHCVIGKVAVPLCEVDLVKGGHWWKALIPSSQNEVELGE... | Function: Plays a role in dendrite formation by melanocytes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53293
Sequence Length: 470
Subcellular Location: Membrane
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Q5R8Q5 | MAYIQLEPLNEGFLSRISDLLLCRWTCRHCCQKCYESSCCQSSEDEVEILGPFPAQTPPWLMASRSSDKDGDSVHTASEVPLTPRTNSPDGRRSSSDTSKSTYSLTRRISSLESRRPSSPLIDIKPIEFGVLSAKKEPIQPSVLRRTYTPDDYFRKFEPHLYSLDPNSDDVDSLTDEEILSKYQLGMLHFSTQYDLLHNHLTVRVIEARDLPPPISHDGSRQDMAHSNPYVKICLLPDQKNSKQTGVKRKTQKPVFEERYTFEIPFLEAQRRTLLLTVVDFDKFSRHCVIGKVSVPLCEVDLVKGGHWWKALIPSSQNEV... | Function: Plays a role in dendrite formation by melanocytes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53890
Sequence Length: 474
Subcellular Location: Membrane
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A0A075F932 | MVSESHHEALAAPPATTVAAAPPSNVTEPASPGGGGGKEDAFSKLKEKFMNELNKIPLPPWALIAIAIVAVLLILTCCFCLCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQDDDAETGLTDGEEKEEPKEVEKLGKIQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEYKVAMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNG... | Cofactor: Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains.
Function: Calcium sensor that participates in triggering neurotransmitter release at the synapse (By similarity). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the syn... |
A1RY76 | MKTLLIHAKHFEYEAREKALDAAESIDGNRSGSFENALVVFVTVEKGDGSSQDVVEEAAADVLDVFRRVGASRVVVYPYAHLSDDLADPEEAKRVLSQLAERISSAGVPVSRAPFGWYKRFSVECYGHPLSELSRTIKPGRRVRPGYADFAVMFPDGRIVGIEELRAEELPEDFVALLEAEVFKKKREGGEPKYLEYCRKFGFEWEPMSDLGHMRYGPEATIMLDAVAEYAWQCARSLGIPVYKVRGTNTFNLSFKPVAQHAQLFGDRLYQMEVDEKKLILRYAACHQQFAMVKDWEISYRDLPFGAFEVADSYRLEQPG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
C6A1R1 | MRILLIHSDYLEYEVKDKALKKPEEISENQKKGRLDEVLAVFMSVEKVDEQNPEEIVKKAVKEIEEVVSQVKTNNIFVYPFAHLSSELGSPDVALRILKEIENELKNKGYNVRRAPFGYYKAFKLSCKGHPLAELSRTIVPGEAKKEEEVPEALKKEEELVSYWYILTPEGELVEVDKFDFSGYENLKKFANYEINKSRLVTEEPPHVKIMLEQELVDYEEGSDPGNLRYYPKGRLIKSLLENYVTDKVIEYGAMEVETPIMYDFEHPALEKYLNRFPARQYVVKSGDKRFFLRFAACFGQFLIKKDATISYRHLPLRMY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
P56881 | MTVYLPDGKPLELPEGATAKDVARALGEGWERRAVGAIVDGELYDLLKPLPQGAKVRLLTEKDPEFQTLFRHTLAHVLAQAVKEFFREKGYDPESVRLGVGPVIEKGFYYDIEAPEPLSDEDLPAIEAKMREILKRDLPLRRFVLSREEALARYRGKDPYKTELVLEIPEGEEISFYQQGDEAYGFTDLCRGPHVPSTGRIPPHFKLTHVAGAYWRGDENRPMLQRVYGVAFRTAEELKEYLWQLEEAKKRDHRRLGRELELFLIDPLVGKGLVLWLPKGNVVREELMAFMREEQVRRGYQLVTTPHIGSLELYKTSGHY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q3SK34 | MVTVTLPDGSVRPFEGPVTVAEVASSIGAGLAKAALAGKVDGKLVDTSYVIDADAQLAIVTAKDAEALDLIRHDAAHVMAQAVQELYPGTQVTIGPAIEDGFYYDFAREQPFTPEDLEKIEKRMDEIVKRDLPIRREVWSRDEAMKVFGDLGETYKVQIIDEVIPKGEELSIYRQGEWFDVCRGPHLPSTGKLPRAFKLMKLAGAYWRGDSKNAMLQRIYGTAWAKKEDLEAYLHRLEEAEKRDHRRLAKQLDLLHMQDEAPGMVFWHPKGWIVWQQIEQYMREKFVEYGYQEVRTPAVMDRSMWEKSGHWENYRDNMFT... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
B8GRI1 | MPLITLPDGSERRFDAPVTVRDVAADIGAGLAKAALAGRVNGRLVDTSHLIEDDASLAIITDRDPEGLEVIRHSTAHLLAQAVKDLFPSAQVTIGPVIDNGFYYDFAFERPFHPDDLEKIEARMKELAKADLPVSRSVMDRDEAVDFFRDQGEEYKAQIIADIPAGETISLYKQGEFIDLCRGPHVPSTGKLKAFKLTKVAGAYWRGDSSNEMLQRIYGTAWPNKQQLDDYLHRLAEAERRDHRRIGTELNLFSIQEDAGGGLVFWHPKGARIRRAIEQFWFDMHERAGYQFLYTPHIANLDLWKTSGHADFYSESMYEP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
O83809 | MGLCVEENITMLQKRSDTLDRLRHSLAHVMAEAVQALFPGTKLAVGPPIDYGFYYDFSPPRPLCDADLAPIEEKMRAILRAGCPFVKEVVSRPDALARFKDEPFKQELIERISADDTLSLYHSGAFTDLCRGPHVQSMRDINPHAFKLTSIAGAYWRGNERGPQLTRIYGTAWESEEDLHTYLRMQDEAKRRDHRKLGPALGLFHLDEENPGQVFWHPEGWTLYVAIQQYLRRVMHEDGYAEVHTPFVMPQSLWERSGHWDKYRANMYLTEGEKRSFALKPMNCPGHVEIFKQKTRSYRDLPLRLSEFGSCTRNEPSGSL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q83GK5 | MDGFEFFSGRSDVVAMICDDRLLDLSESIPSGKVPEPIELDSPHGLDILRHSCAHVLAQAVQSIYGDAKLGIGPFTENGFYYDFSVNEPFSSDSLRVIEDKMREIVHSDQKFVRKVVDRQSAHSQFRDEPFKLEIINATDDTLSIYYNIDADSGSVRWMDFCRGPHLPSTRFIGDAFALTHVSSVYWRGNSDNPQMQRVYGTAWGSAKDLKGYLDRVELAKLVDHRKLGKELDLFSLPDEIGPGLALFHVKGGIIRSEMEQYARLRHLEEGYNFVYSPHITKRDLFERSGHLQWYGQSMFPPMRLDKDSCSQGFDYYLKP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
B5ZC42 | MYKFDPKLNHSAAHVLAMALTKFYPNLSLAIGPAIDEGFYYDFNLNDPNTSITPIDLLKIEKEMKKIAAQALTFDYEQVSYEQAKDLFKNNKYKLDIIEENKNKPLSIYHSGKWFDLCKGPHVENTKEIKAIKLLNIAGSYWRGDANNDQLIRIYGVAFNDQAQLDAYLVDLQERKERDHRKIGKDLNLFTFNNLAGQGLPIWLPNGTIIKSQVQKFINEVEFQFNFDTVITPILGSIDLYKTSGHWDHYKDNIFSPVQIDNEVLILRPMTCPHHTLVYSNELRSYRSLPIRLSEHSILHRYESSGGLTGFERVREMILE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q6AMA0 | MAQDSLLSKGYEFADVEEKWLSRWHKQNAFATKMEDGKDAFSIVIPPPNVTGVLHVGHALNNTLQDILVRYHRMCGDNTMWIPGTDHAGIATQNVVERQLATEGKGRHDLGREAFIERVWKWREDKGGTIVNQLKKIGSSCDWERERFTMDEGLSTSVREVFVRLYKEGLIYKGDYIVNWCPRCQTALADDEVEHEDSKGKLYHIRYPFADGSGSVVIATTRPETMPGDTAIAVHPDDERYAHLGEIGIKLPLTDRILPVVFDHHVEKDFGTGALKVTPSHDRNDYEIGIRHGLDLCKVIDEKGMMNDNAGKYAGLDRFE... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
Q72E47 | MAENALPKGYEPRDVEERWRRHWEDNRTFTPDMDAPGEPYSIVIPPPNVTGALHIGHALNHVLIDVLCRNARQQGKKVLWLPGTDHAGIATQNVVERALAKEGLSRHDLGREAFIERVWQWKEEYGNRILNQIRMLGDSVDWTRERFTMDEGLSKAVRKVFVDLYNGGYIYRGNYIINWCNRCHTALADDEVDHMPEQGHLYHVRYDFEDGSGSVVIATTRPETIMADTGVCVHPEDERYAGLIGKKILVPVIGRAVPLFADTYVDREFGTGALKVTPCHDPNDWTLGERHGLAFIQCIDEDGNMTAEAGPYAGLTKEEC... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
P07118 | MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESQESFCIMIPPPNVTGSLHMGHAFQQTIMDTMIRYQRMQGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTRHDYGREAFIDKIWEWKAESGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLRTAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETLLGDTGVAVNPEDPRYKDLIGKYVILPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHALPMINILTFDGDIRESAQVFDTKGNE... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
Q5HC99 | MQSLFSNKYKFKDTEEKLNAYWDKIKLYKWKNLQGKQFIIDTPPPTISGQLHIGHVFSYCHTDFIARYQRMLGKDVLYPIGFDDNGLPTERLVEKIKKVRAADIDRKEFKALCNEVSAKFRMEFKILFQSLGISYDWDLEYHTISEEIQKLSQMSFIALYNMGKIYRKLQPIFWDCADRTAIARVEVEEKEMSSFMSTIAFSTEAGELINIATTRPELMPACVALFFNPLDIRYQHLQGQYAIVPIFGNKVPILSDEQVKIDKGTGLVMCCTFGDELDVYWWNKHNLNTQIIISKSGTLDLKHNIAETDTLSGKLHGVSI... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
A7HJX5 | MEIGTRYDPKNIEMKWYKHWLEKKYFTPRGAGPKYSIVIPPPNITGKIHMGHALNITIQDILSRYKRMKGFDVLWLPGEDHAGIATQTAVERYLSTQGKSRRDFSRDEFLNIVWNWANKYRQEIKNQIMSIGASVDWTRERFTLDEGLSKAVRKVFVDMYKKGLIYKGKYIVNWCHRCGTVLSDEEVDYHEEEGALYHIKYPIKGEDDYIIIATTRPETMLGDTAVAVHPSDERYRKYVGKIAILPLVGREIPVIADNYVDPSFGTGALKVTPAHDTNDYLIGQRHNLPFVDIFDENIVINENGGKFKGMTAEQARKAVV... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
Q5NHZ4 | MTQEINKNYNPKEIEQANYQNWEASGKFACGNTDSKDTYTIMLPPPNVTGTLHMGHGFQMSLMDILIRYNRMSGKDTLWQPGTDHAGIATQMVVERQLNAQGISRHDLGRENFVSKVWEWKELSGGTITSQMRRIGASPDWDRERFTMDKGLSDAVKKCFIKLYEDGLAYRGERLVNWDPKLKTAVSDLEVAQVDKQGSLWHFIYPVADSDEKIIIATTRPETMLGDMAVAVHPEDERYTHLVGKMINLPLTDRQIPIIADDYVEKDFGTGCVKITPAHDFNDYEMGKRHNLPMLNILTDDATLNTNVPSKYQGLDRFEA... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
Q8RHK3 | MNELDKNYSPNEIEEKWYKIWEDSKYFAASLSSEKENYSIVIPPPNVTGILHMGHVLNNSIQDTLIRYNRMTGKNTLWMPGCDHAGIATQNKVERKLAEDGLKKEDIGREKFLEMTWDWKEKYGGIITKQLRKLGASLDWDRERFTMDEGLSYAVRKIFNDLYHDGLIYQGEYMVNWCPSCGTALADDEVDHEEKDGHLWQIKYPVKDSDEYIIIATSRPETMLADVAVAVHPEDERYKHLIGKTLILPLVNREIPVIADEYVDKEFGTGALKITPAHDPNDYNLGKKYNLPIINMLTPDGKIVEDYPKYAGLDRFEARK... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
P11931 | MAQHEVSMPPKYDHRAVEAGRYEWWLKGKFFEATGDPNKRPFTIVIPPPNVTGKLHLGHAWDTTLQDIITRMKRMQGYDVLWLPGMDHAGIATQAKVEEKLRQQGLSRYDLGREKFLEETWKWKEEYAGHIRSQWAKLGLGLDYTRERFTLDEGLSKAVREVFVSLYRKGLIYRGEYIINWDPVTKTALSDIEVVYKEVKGALYHMRYPLADGSGFIEVATTRPETMLGDTAVAVHPDDERYKHLIGKMVKLPIVGREIPIIADEYVDMEFGSGAVKITPAHDPNDFEIGNRHNLPRILVMNEDGTMNENAMQYQGLDRF... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
Q74BJ6 | MAEKELAKVYEPTAVERKWYETWEQEGYFRANPDSGKPSYSIVIPPPNVTGALHMGHALNNTLQDILCRWKRMNGYEVLWMPGTDHAGIATQNVVERQLAGEGTSRHELGREAFIERVWKWKAESGGQIIGQLKRLGASCDWGRERFTMDEGLSRAVREVFVRLYEEGLIYRDNRLINWCPRCHTALSDIEVEHEDKAGNLWHIRYPVVGEPGRFVVVATTRPETMLGDTAVAVHPEDERYADLVGKKVLLPLVNREIPVVADGYVDREFGTGVVKITPAHDFNDFEVGRRHNLDLLNVFDESAVVNSAGHQYEGMERFA... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
Q9PH12 | MSQFTSSYDPTSFEARLYAAWEAAGHFKPSGTGQPYTILLPPPNVTGTLHMGHAFQQTLMDALVRYHRMCGDDTLWQVGTDHAGIATEMVVSRNVVLEGHGETRDSLGRDGFINKVWEWKQQSGDTIERQMRRLGVSADWSRSTFTMDPQPSAAVTEAFVRWYEAGLIYRGQRLVNWDPVLKTAISDLEVENVAEEGMLWSIRYPLSDGVTYEHVEHDAAGNEILRETRDSLIVATTRPETLLGDTAVMVHPEDRRYTALIGKTVTLPLTGRHIPVIGDAYVDPTFGTGVVKVTPAHDFNDYQIGLRHRLPMIQVLDDAA... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
Q9HN83 | MTSDDTDDTAGADDVALDPWGSATISDYRALFDEFGIEAFEDVLDGVPTPHSLMRRAIIFGHRDYRRVAAAMRNDEPFAALSGFMPTGDPHIGHKMVFDELIWHQQQGGDAYALIADLEAHSARGLDWAEIDEHAEDYLLSLLALGFDADEGELYRQSTNRELQDLAFELGIEANTSEFEAIYGFGGDTDVSHMQSVVTQMADILYPQLDAPKPTVIPVGPDQDPHVRFARDLAERTRYFKVTEAFASVAFDDDERPLVRAAYDARSQYAADTDQPRCTEAADWLAAEPAAADGVDAATAESVVQKLENAGMEPLRPRVR... | Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 56055
Sequence Length: 513
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q82E91 | MKRIFSGVKPTGHLTLGNYLGAVRRWVDVDQHGADALFCVVDLHALTVDHDPARVRRLSRQAATLMLAAGLDPELCTVFVQSHVDEHARLSYLMECVATDGEMRRMIQYREKAAREQQRGGSVRLSLLTYPVLMAADILAYGTDEVPVGDDQTQHVELTRDLAVRFNQRYGHTFVVPRATRPEVAARVMNLQEPTSKMGKSDDVGPGIVYLLDEPEAVRKKVMRAVTDSGRDVVYDRESRPGVSNLLEILAACEGGSPEALSGAYASYGALKKDTAEAVVELLRPLQERHKALCAEPGYVEGVLRDGARRARELARPRVD... | Function: Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 36517
Sequence Length: 331
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q8CJX0 | MTRVFSGVKPTGHLTLGNYLGAMRRWAAVDQHRSDALFCVVDLHALTVDHDPARVRRLSRQAASLLLAAGLDPELCTVFVQSHVDEHARLSYVLECVATDGEMRRMIQYKEKAARERVRGGSVRLSLLTYPVLMAADILAYGTDEVPVGEDQTQHVELARDLAVRFNQRYGHTFVVPRATSPAVAARVMNLQEPASKMGKSDDTGPGIVYLLDEPDVVRKKVMRAVTDSGRDVVYDPEERAGLANLLEILAACTDGEPAELAGGYDSYGALKKDTAEAVVEMLRPVRERHMELSADPGYVDGVLREGAEKARAMARPTVD... | Function: Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 36804
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q9RVD6 | MPFVDLEVPTMTTPTPAATPARPRVLTGDRPTGALHLGHLAGSLQNRVRLQDEAELFVLLADVQALTDHFDRPEQVRENVLAVALDYLAAGLDPQKTTCVVQSAVPELAELTVYFLNLVTVSHLRQNPTVKAEIAQKGYGERVPAGFFVYPVSQAADIAAFGATLVPVGDDQLPMLEQTREIVRRFNALYAPVLAEPQAQLSRVPRLPGLDGQAKMSKSLGNAIALGDSADEVARKVMGMYTDPGHLRASDPGRVEGNPVFTFLDAFDPDPARVQALKDQYRAGGLGDVKVKKHLIDVLNGVLAPIRTRRAEYERDPDAV... | Function: Catalyzes the formation of 5'adenyl-Trp and tRNA(Trp) but with 5-fold less activity than TrpRS. Increases the solubility of the nitric oxide synthase oxygenase (nos), as well as its affinity for substrate L-arginine and its nitric-oxide synthase activity. The complex between trpS2 and nos catalyzes the regios... |
Q9HN66 | MTADGNDVTPYAVESDDLDYEKLLARFGADELTDDQRARFPDHPLVNRGLFYAGRDVDDFLTAGEQSIVTGVGPSGPMHLGHAMVFYFARRLQDEFGARVYVPLSDDEKYWFKDQTPAETGDYLRANLRDLLAVGFDPELTRIVVDTRDADVLYPLATAFAGDVRHATLQNVYGEPDNVGQAFYPAVQTAHLLLPQLVHGEHETLVPIAVDQDPHVRVSRDVAAKARYPVGKPGALLMQFLPSLAGPGKMSSSAGVSIRLTDSPDTVREKVRTHAYTGGRASVEEHRAKGGVPAEDVPFQYLSAFFEPDDAELARIEREY... | Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 41937
Sequence Length: 380
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q9KZA7 | MSMANERPRVLSGIQPTSGSFHLGNYLGAVRQWVDMQDTHDAFYMVVDLHAITVPQDPKELRENTRVAAAQLLAAGLDPDRCTLFVQSHVPEHAQLGWLMNCITGFGEASRMTQFKDKSAKQGNDRTTVGLFTYPMLMVADILLYQADQVPVGEDQRQHLELTRDLADRFNQTYGDAFTVPTAYILKETAKIYDLQDPTAKMSKSAATPKGLINLLDEPKATAKKVKSAVTDTDTVVRFDRETKPGVSNLLTIYSTLTGAEIAELERKYEGKGYGALKTDLADVVVEFVTPFRERTRQYLDDPETLDAILAKGAEKARSV... | Function: Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 37593
Sequence Length: 339
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q9SR15 | MEVDKKDEREAESSEQVVNPWEVSAKDGGKIDYDKLIDKFGCQRLDESLIDRVQRLTSRQPHVFLRRSVFFAHRDFNEILDAYERGDKFYLYTGRGPSSEALHLGHLIPFMFTKYLQEAFKVPLVIQLTDDEKSIWKNLSVEESQRLARENAKDIIACGFDVTKTFIFSDFDYVGGAFYKNMVKVGKCVTLNKAMGIFGFSGEDPIAKLSFPPVQAVPSFPSSFPHLFPGKDNLRCLIPCAIDQDPYFRMTRDVAPRLGYSKPALIESTFFPALQGENGKMSASDPNSAIYVTDSAKDIKNKINRYAFSGGQDSIEKHRE... | Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 45754
Sequence Length: 402
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q55DZ8 | MTETTPTTNETKEQVITPWEVEAAPGGSVDYMKLVDQFGSTVISEELIARFEKVTGKRAHHFLRRGIFFSHRDLKEILDHHESGKKWFLYTGRGPSSGSLHFGHLLPFTFTKYLQDAFNVPLVVQMTNDEKFLWKDMTLEESIKFTHNNVKDIIALGFDIQKTFIFSNLEYIHHLYPNVLKIARCVNLNQIQNIFGFKESDAIGKFTFPPVQAAPCFPDSFPHIFPLNDPEIKNIRCLIPCAIDQDPYFRMTRDIAHRIGHQKPALIHSKFFPALQGHNTKMSASDTNSAVYLSDTPDQVKDKIKKHAFSGGGATKEEQE... | Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 45850
Sequence Length: 400
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
P23381 | MPNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGMSSGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDRTDIQCLIPCAIDQDPYFRMT... | Function: Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that... |
P32921 | MADMPSGESCTSPLELFNSIATQGELVRSLKAGNAPKDEIDSAVKMLLSLKMSYKAAMGEEYKAGCPPGNPTAGRNCDSDATKASEDFVDPWTVRTSSAKGIDYDKLIVQFGSSKIDKELINRIERATGQRPHRFLRRGIFFSHRDMNQILDAYENKKPFYLYTGRGPSSEAMHLGHLVPFIFTKWLQDVFNVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDINKTFIFSDLEYMGQSPGFYRNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAAPSFSNSFPKIFRDRTDIQCLIPCAIDQDPY... | Function: T1-TrpRS has aminoacylation activity while T2-TrpRS lacks it. T1-TrpRS and T2-TrpRS possess angiostatic activity. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization a... |
Q5ZJ08 | METASGPQEKYQLITRNLQEVLGEDKLMAILKEREVKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRTRYYEHVIKAMLESIGVPLEKLKFIRGTDYQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPSLGYAKRIHLMNPMVPGLTGSKMSSSEEDSKIDLLDRKEDVKKKLKKAFCEPGNIENNGVLSFIKHVLFPLKSEFVILREEKWGGNKTYTAYETLEKDFAEQVVHPGDLKNSVEAALNKL... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 59284
Sequen... |
Q8SRV7 | MSVEQKLYLITRNLQEILGEEELKRIVSERELNVYWGTAITGKPHIAYLVPLMKIKDFVDAGCNVKILFADIHGFLDNLKAPIEKVQHRCAYYEKLIKSALKMLCVDLDRIQFVKGSEFQKSERYTMDLYRILSITSKHDAKKAGAEVVRQVENPMVSSLVYPSMQALDEVHLSVDAQFGGVDQRKIFTYARKYLPLLNYEKRIHLMSPMLPGLNSDKMSSSDDLSKIDLMDSKEAIWRKIRKCFCEEGNKDNGLMMIFSHIVFPILQLKGECVRITDRDGREMAFEKYQEFEEEFVRKSIHPGDLKSNAARLIDEIIRP... | Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 39143
Sequence Length: 337
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
B7XHC1 | MDETSIINENTDVFEKKITLIERNLQEITINDKEIIRKIIRKRNLKIYWGTAITGKPHIGYFLPILKIKDFVEAECEVTILFADIHGFLDNLKAPIELIENRYHYYEKIIKIMLMSVGCDINKIRFVKGSDYQKNSDYVFDLYKLCSYTTERDCKRAGSDVVKQRDNVLLSSLIYPNMQALDEEYLKVDAQFGGEDQRKIFMHAKTFLPKLGYKKRIHLMNPMMPGLNSDKMSSSDELSKIDLLDTEQQINKKINKCFCEEGNLQSGVLHVFEFVIFHYYTSISINKKSYTSIEDVKKDFEMKLIHPKDLKLACSNYINK... | Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 40043
Sequence Length: 342
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
P54577 | MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKL... | Function: Tyrosine--tRNA ligase that catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (Probable) . Also acts as a positive regulator of poly-ADP-ribosylation in the nucleus, independently of... |
C4V6W1 | MDTTEKLKLINRNLKEVIGGDIMEKIINKRDLNVYWGTATTGKPHIAYFLPILKIKDFVDAGCNVTILLADIHAFLDNLKAPIEKIECRSQYYKKIITLMLKSIKVDVSKISFIFGSEYQKSNKYFTDILRILNQTKKNDARRAGSEVVKQVKNSKLSSLVYPAMQALDEEYLNVDVQFGGIDQRKIFMYAREFLPLLKYKKRIHLMNPMIPGLNSDKMSSSDIDSKIDLLDTKLEIYKKIHNCSLENEGLIFLFKSIIYPYCSIFNLQIMISGKVYTFDKLYEDIKMKIIDETELKNIASDMIERLICPIRDEMLRDLK... | Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 38145
Sequence Length: 329
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
Q6DIJ1 | MGDGLTPEGKAQLITRNLQEVLGEDKMKEILKERPLRIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWDLLELRTRYYEQVIQAMLQSIGVPLERLRFIRGTEFQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYAKRIHLMNPMVPGLTGAKMSSSEEESKIDLLDSPADVKKKLKKAFCEPGNIENNGVLSFVRHVLFPLKSEFVVLRDEKFGGNKTYTDFETLEKDFTEQLVHPGDLKASVEKALNKL... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 58958
Sequen... |
P36421 | MSSAATVDPNEAFGLITKNLQEVLNPQIIKDVLEVQKRHLKLYWGTAPTGRPHCGYFVPMTKLADFLKAGCEVTVLLADLHAFLDNMKAPLEVVNYRAKYYELTIKAILRSINVPIEKLKFVVGSSYQLTPDYTMDIFRLSNIVSQNDAKRAGADVVKQVANPLLSGLIYPLMQALDEQFLDVDCQFGGVDQRKIFVLAEENLPSLGYKKRAHLMNPMVPGLAQGGKMSASDPNSKIDLLEEPKQVKKKINSAFCSPGNVEENGLLSFVQYVIAPIQELKFGTNHFEFFIDRPEKFGGPITYKSFEEMKLAFKEEKLSPP... | Function: Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-step reaction: L-tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) . The specificity determinants on tRNA(Tyr) are the base pair C1-G72, the discriminator residue A73, and the three anticodon ba... |
Q9M876 | MAYATGITFASRSILPICSRTFLSPLRVASLLVFPEKSSATFFRRVQVPHLFSTSTTTLFSSVKCSIHSTSSPETENQAVFRPNVVDILEERGLLESITSENLRSACSDPKVAPLRVYCGFDPTAESLHLGNLLGIIVLSWFQRCGHQAVGLIGGATGRVGDPSGKSLERPELDADTLEKNIAGITKIIIKILGSNPSPGGSYVIFNNYDWWKDMTMLDFLNKVGRFARVGTMMAKESVKKRLESEQGMSYTEFTYQLLQAYDFLHLFKNEGINVQIGGSDQWGNITAGTDLIRKILQAEEAAYGLTFPLLLKNDGTKFG... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 56619
Sequen... |
Q54WD9 | MIRNFTKGLLINNLNINKFGSTKIRPFCSTITKNDKNNVINILKKRGFIHQMTASDIEMIKMTSTNNNNNNDNNNNNNNNKVSLYAGFDPTADSLHIGNLLTLMVMLHFKRHGHNPIALMGGATALIGDPSGKSSDRVMLTEEFIEGNLKHIRENITAVLGEDTLVVNNIEWNKTMDVISFLREVGSYFRVGSMIKKDFIQNRLSDSNENGISFTEFCYSLFQANDFAHLFLKHGCSIQIGGSDQWGNITAGCDLIRKKLKGNAQGITIPLLTNSAGKKLGKSEGNSIWLSPHRTSPYKFYQYWIQVSDEDVERLLKLFT... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 54283
Sequen... |
Q9W107 | MLPLRRSLLKPLQDVLRHSHRQMSQKNLLELTDRGFFHGIFPDTAAPRMKQLFTRGQQSIYAGFDPTADSLHVGNLLVIMGLIHCQRAGHRPIALVGGATGLIGDPSGRKTERNQLGETVIETNLKAIEQQLRRVFENHENCLWDSKKQKLPLAPLIIVNNADWYADLQLIDFVANMGRHFRMGSMLSRSSVQSRLESEDGMSFTEFTYQIFQAYDWLHLLRRHNCCFQMGGSDQTGNLMTGHELISRVERKREVFGLTLPLVTTEEGDKFGKSAGNAVWLDGNKTSPFALYQFFLRMPDSEVEKLLKLFTFIPLPQVEQ... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 52575
Sequen... |
Q9Y2Z4 | MAAPILRSFSWGRWSGTLNLSVLLPLGLRKAHSGAQGLLAAQKARGLFKDFFPETGTKIELPELFDRGTASFPQTIYCGFDPTADSLHVGHLLALLGLFHLQRAGHNVIALVGGATARLGDPSGRTKEREALETERVRANARALRLGLEALAANHQQLFTDGRSWGSFTVLDNSAWYQKQHLVDFLAAVGGHFRMGTLLSRQSVQLRLKSPEGMSLAEFFYQVLQAYDFYYLFQRYGCRVQLGGSDQLGNIMSGYEFINKLTGEDVFGITVPLITSTTGAKLGKSAGNAVWLNRDKTSPFELYQFFVRQPDDSVERYLKL... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 53199
Sequen... |
P12063 | MLLRTKALIRSGGSIAKYAAANPSCFILQRRGLRREFGPKYTAKINEAEENWQARAEAIKKGKKQNTWDLFEERGYVKDTAGTKEHIAELMRTRRIGAYVGIDPTAPSLHVGHLLPLMPLFWMYLEGYKAFTLIGGSTAKIGDPTGRLKSRDHLSSSDATMNMTKIHYQLKKLWENVDTQMRARGYEADWARKRGIVNNNHWWNKQPMLEVLRRVGHALRIGPMLSRDTVKNKMTQGDGVSFAEFTYPIMQGWDWFELFYQQGVQMQIGGSDQYGNIISGLEVVKAARESEPDPQERKYVTPKTALDECVGFTVPLLTDS... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Has both an aminoacyl-tRNA synthetase activity and is involved in the splicing of group I introns. It acts in intron splicing by s... |
Q72RP6 | MDIQKQIEIIRRGTVDLISEEELKSKLQKKKTLKIKAGFDPTAPDLHLGHFVQLKKLKHFQDLGHEVSFLLGDFTAMIGDPTGKSETRKRLSREEVLENSKTYQNQVFKVLDPVKTKIVYNSNWCSKMNFEDVLVLSSKYNVARMLERDDFSKRYKAGQPISMIEFLYPLVQGYDSVAMECDVELGGTDQKFNLLVGRDLQREYGKEAQCVLTLPLLVGLDGSKKMSKSLGNYVGITETPIDMFGKLMSISDDLMWNYFELLTDLPLPEIENRKNGMAKKELHPKEIKTELAKLIMDQFSSPSENEEAIQEWKKIHNPKS... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 46319
Sequen... |
Q8EUX2 | MKNKNILEFLKKRGYIYQGSNFDLIEKELIKGTSFYIGFDPTADSLHVGHFLTMMAVKHLQKAGNNPVIVVGGGTGSVGDPSGRSEIRKILDRKTIDYNCECLKKQMSKFISFEGKNKAVMVNNADWLLKINWIEFLREFGVCFSVNKMLAAEAFKVRFEQESGLSFLEFNYMLMQAYDFYYLNQNYNVNIQLGGSDQWSNILAGVDLIRRKSSKEAFALTLNLLTKHDGTKMGKTATGAIWLDKNKTSPYEFYQYWLNIDDQDVERFLLLLTELDDKTISDLCKEKGKKIVEAKKVLASELTKMIHGQEELDKAIEQSK... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 46717
Sequen... |
Q6F0M8 | MNIIKELEWRGLVKQITNEERLLKAQNDGAAVYCGFDPTADSLHVGHLMMIVTLKRFDKAGFQAIGLIGGGTGMIGDPSFKADERKLQTDEQVKFHATAIQNQLLRIIPDVTFANNVDWLGNMSLIDFLRDVGKDFNISYLLNKDSIATRISTGLSVTEFSYTMLQAYDFYNLYINHNCKVQIGGSDQWGNITSGTDYISTRVGSANTEAAGFTIPLLTKSDGQKFGKTESGAVWLDSNKTSVYDFYQFWINQDDNDCVKMLKYLTFLTKEEIDELEAKHKEAPHLRTMQKTLASEITKFVHGDKELNKAIKLTDAFFTG... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 46375
Sequen... |
B5ZAU9 | MHNLIKDLKARNLINNITNEEKLKKALAENKGIYVGFDPSADSLHLGNYIMIMLLKRFRLHNIKTFALVGGATGMIGDPSGKSAERNLLDKTILEHNITKIKYQLEKFTNSQVINNYDFYKNMTFLDFLRDVGKLININYLLEKEIISSRLDVGISYTEFSYNLLQGYDFLQLYKNDNIAIQAGGSDQWGNITTGIEIIRKSLGDDNIACGLTINLLTNSEGKKFGKSEKGAIYLDENKSSVYEMYQFLINQTDADVEKLLNFLTLIDVDEINKIMQAHKENPALRIAQKALAQAVVVDVHGQQKYEQALHISQVLFNGN... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 47141
Sequen... |
Q8D2L6 | MKDLIQELKNRKLISKLTDEINIKKILKEKKINLYCGFDPTADSLHIGHLIPLLFLKRFSNFGHIPIIVIGGATALLGDFNIKKNKSFLEKYKNVKNWSKTIENQILNIIKYENNNCNLIILNNYLWIKELKIINFLRDIGRFISINKILRKEIVKKKLKENQHISFMEFSYSLLQGYDYYFLNLNYDVYIQIGGSDQWSNIISGIDLVNKINKKKVYGITTPLLTRSNGSKLGKSDDKEKVIWLDKKKTSVYEFYQFWLNTPDEKIFRYLKLFTFISMSEINKLKCKFFNKEINPFQAQKILADEITKIVHGISQLRLA... | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 50075
Sequen... |
Q3UFJ6 | MRNASGFLKTAGAPLVSATWLPPSPPPAMPTVAAGPQMERVDNGSQGAPQLFLTSALARGVSGVFVWTALLLTGHQIYSHLRSYTAPREQRFVIRLLFIVPIYAFDSWLSLLLLGGHPYYVYFDSVRDCYEAFVIYSFLTLCFQYLGGESAIMAEIRGKPIRSSCFYGTCCLRGMSYSITFLRFCKQATLQFCIVKPVMALITIILQAFDKYHDGDFNIHSGYLYVTLVYNASVSLALYALFLFYFATRDLLRPFEPVLKFLTIKAIIFLSFWQGMLLAILERCGVIPEVQAVDGTRVGAGTLAAGYQNFLICVEMLFAS... | Function: Acts as a heparin receptor in vascular cells (By similarity). May be involved in vesicle transport in exocrine cells and Sertoli cells .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46818
Sequence Length: 425
Subcellular Location: Cell membrane
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Q4QQS1 | MRNASGFLKTAGAPLVSATWLPPSPPPAMPMVAAGPQMERVDNGSQGAPQLFLTSALARGVSGVFVWTALLLTGHQIYSHLRSYTVPREQRFVIRLLFIVPIYAFDSWLSLLLLGGHPYYVYFDSVRDCYEAFVIYSFLTLCFQYLGGESAIMAEIRGKPIRSSCFYGTCCLRGMSYSITFLRFCKQATLQFCIVKPVMALITIILQAFDKYHDGDFNIHSGYLYVTLVYNASVSLALYALFLFYFATRDLLRPFEPVLKFLTIKAIIFLSFWQGMLLAILERCGVIPEVQAVDGTRVGAGTLAAGYQNFLICIEMLFAS... | Function: Acts as a heparin receptor in vascular cells . May be involved in vesicle transport in exocrine cells and Sertoli cells (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46878
Sequence Length: 425
Subcellular Location: Cell membrane
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A2VDL9 | MTVRGAALAPDPASPTTAAASPSISVIPEGSPTAMEQPVFLMTTAAQAISGFFVWTALLITCHQIYMHLRCYSCPNEQRYIVRILFIVPIYAFDSWLSLLFFTNDQYYVYFGTVRDCYEALVIYNFLSLCYEYLGGESSIMSEIRGKPIESSCMYGTCCLWGKTYSIGFLRFCKQATLQFCVVKPLMAVSTVVLQAFGKYRDGDFDVTSGYLYVTIIYNISVSLALYALFLFYFATRELLSPYSPVLKFFMVKSVIFLSFWQGMLLAILEKCGAIPKIHSARVSVGEGTVAAGYQDFIICVEMFFAALALRHAFTYKVYA... | Function: May activate the MAP kinase signaling pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45490
Sequence Length: 407
Subcellular Location: Membrane
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Q9Y519 | MTVRGDVLAPDPASPTTAAASPSVSVIPEGSPTAMEQPVFLMTTAAQAISGFFVWTALLITCHQIYMHLRCYSCPNEQRYIVRILFIVPIYAFDSWLSLLFFTNDQYYVYFGTVRDCYEALVIYNFLSLCYEYLGGESSIMSEIRGKPIESSCMYGTCCLWGKTYSIGFLRFCKQATLQFCVVKPLMAVSTVVLQAFGKYRDGDFDVTSGYLYVTIIYNISVSLALYALFLFYFATRELLSPYSPVLKFFMVKSVIFLSFWQGMLLAILEKCGAIPKIHSARVSVGEGTVAAGYQDFIICVEMFFAALALRHAFTYKVYA... | Function: May activate the MAP kinase signaling pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45562
Sequence Length: 407
Subcellular Location: Membrane
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Q8BG09 | MTVRGAALAPDPASPTTTTASPSVSATPEGSPTAMEHPVFLMTTAAQAISGFFVWTALLITCHQIYMHLRCYSRPNEQRHIVRILFIVPIYAFDSWLSLLFFTNDQYYVYFGTVRDCYEAFVIYNFLSLCYEYLGGESAIMSEIRGKAIESSCMYGTCCLWGKTYSIGFLRFCKQATLQFCVVKPLMAVSTVILQAFGKYRDGDFDVTSGYLYVTIIYNISVSLALYALFLFYFATRELLSPYSPVLKFFMVKSVIFLSFWQGMLLAILEKCGAIPKINSARVSVGEGTVAAGYQDFIICVEMFFAALALRHAFTYKVYA... | Function: May activate the MAP kinase signaling pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45589
Sequence Length: 407
Subcellular Location: Membrane
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Q5ZMP3 | MPCTCGNWRRWIRPLVVLLYIVGLLVVVPLCVWELQKLEVGIHTKAWFIAGIFLLMTIPISLWGILQHLVHYTQPELQKPIIRILWMVPIYSLDSWIALKYPNIAIYVDTCRECYEAYVIYNFMVFLSNYLTNRYPNLVLIIEAKDQQRHLPPLCCCPSWAMGEVLLFRCKLGVLQYTVVRPFTTIIALICELVGVYDEGNFSFDNAWTYLVILNNMSQLFAMYCLVLFYKVLREELNPIQPVGKFLCVKMVVFVSFWQAVLIALLVKVGVISEKHTWEWQSVEAVATGLQDFIICVEMFLAAIAHHYSFSYKPYVQEAE... | Function: May play a role in cell growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50930
Sequence Length: 445
Subcellular Location: Membrane
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Q9NVA4 | MPCTCTWRNWRQWIRPLVAVIYLVSIVVAVPLCVWELQKLEVGIHTKAWFIAGIFLLLTIPISLWVILQHLVHYTQPELQKPIIRILWMVPIYSLDSWIALKYPGIAIYVDTCRECYEAYVIYNFMGFLTNYLTNRYPNLVLILEAKDQQKHFPPLCCCPPWAMGEVLLFRCKLGVLQYTVVRPFTTIVALICELLGIYDEGNFSFSNAWTYLVIINNMSQLFAMYCLLLFYKVLKEELSPIQPVGKFLCVKLVVFVSFWQAVVIALLVKVGVISEKHTWEWQTVEAVATGLQDFIICIEMFLAAIAHHYTFSYKPYVQE... | Function: Possible tumor suppressor which may play a role in cell growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50142
Sequence Length: 438
Subcellular Location: Membrane
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Q3TPR7 | MPCACNRSNWRRWIRPLLVLFYATTILVAVPICIWKFQKMKVGMHTKSWFIAGIFLLLTIPVSLWGILQHLVHYTQPELQKPIIRILWMVPIYSVDSWVALVYPKIAIYVDTWRECYEAYVIYNFMIFLTNYLTIRFPNLILHLEAKDQQNHILPLCCCPPWAMGEMLLFRCKLGVLQYTVVRPITTVTALVCEILDVYDEGNFGFSNAWTYLVILNNLSQLFAMYCLLLFYKVLKEELSPIQPVGKFLCVKLVVFVSFWQAVLIALLVKLGVISEKRTWEWQSAEAVATGLQDFIICIEMFFAAIAHHYTFSYKPYVHE... | Function: Possible tumor suppressor which may play a role in cell growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60043
Sequence Length: 525
Subcellular Location: Membrane
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P20351 | MSCPYAGNGNDHDDSAVPLTTEVGKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRVVLILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKDPSLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVRRGDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMI... | Cofactor: Binds 1 heme group per subunit.
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety . Required during larval growth to control the level of ... |
Q2N5X1 | MAQDVTYSSYLDLDRILAAQHPVSGAHDEMLFIIVHQASELWLKLCLHELFAARDCIAADNLRPSFKMLSRVARAQTQLIQSWDVLSTMTPHDYSQIRPHLGRSSGFQSPQYRMMEFLLGGRNPDMVAMHEPTPEIATALREELARTSLYDEAIRLLSRRGFAIPDEVLARKLDEVWVRSEEVEAAWAEIYRDPQQHWDLYELAEKLVDLEYHFQRWRFGHLKTVERIIGFKRGTGGTKGVPYLEGVLKQAFFPELLSVRTAI | Cofactor: Binds 1 heme group per subunit.
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Catalytic Activity: L-tryptophan + O2 = N-formyl-L-kynu... |
P48775 | MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDSL... | Cofactor: Binds 1 heme group per subunit.
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Catalytic Activity: L-tryptophan + O2 = N-formyl-L-kynu... |
A6W961 | MSGTAEENTREVEAGVVTDFTREMSYGEYLHLDELLAAQHPLSTPEHHDELLFIVQHQTSELWLKLVLHELRSAMRAIAADDLKTALKNIARVKHIQRTLTEQWSVLATLTPTEYAQFRGFLANSSGFQSQQYRAVEFALGNKNAKMLDVFAHDGPGHAQLTELLEAPSLYDEFLRHLARRGHDVPAELLERDVTKAHVHTPALVATFRVIYEDAQRYWTEYEACEELVDLEENFQLWRFRHLKTVERTIGFKRGTGGSSGVGFLARALDLTFFPELYAVRTEIGS | Cofactor: Binds 1 heme group per subunit.
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Catalytic Activity: L-tryptophan + O2 = N-formyl-L-kynu... |
P41895 | MSRRNPPGSRNGGGPTNASPFIKRDRMRRNFLRMRMGQNGSNSSSPGVPNGDNSRGSLVKKDDPEYAEEREKMLLQIGVEADAGRSNVKVKDEDPNEYNEFPLRAIPKEDLENMRTHLLKFQSKKKINPVTDFHLPVRLHRKDTRNLQFQLTRAEIVQRQKEISEYKKKAEQERSTPNSGGMNKSGTVSLNNTVKDGSQTPTVDSVTKDNTANGVNSSIPTVTGSSVPPASPTTVSAVESNGLSNGSTSAANGLDGNASTANLANGRPLVTKLEDAGPAEDPTKVGMVKYDGKEVTNEPEFEEGTMDPLADVAPDGGGRA... | Function: TFIIF is a general transcription initiation factor that binds to RNA polymerase II. Its functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TF... |
P43418 | MEKILMLNDDQIWIFKKHTNNIQLLIEVALYLKSNKSSVSKKDKDAMYDIFSESELYNPRESLRDKPLDTINHKLDGLSYFMFGYSDRINDENKFIFSPLGNLFLKYLHDKDKLSKIFSCMLISMQFPHPYSKPSECFLLYPFRLIFKLLLDKRLQGRLYHYEVYKIIIHTISIDEAKYEFLVKSILNSRKKSWNEKLNELSEIQHKVVKSVYEWQYYIVPLLGSLHIFKINNGDIEQKLYHPQKDGSKSPPTARKANNGYVEINDNLTNFIDKLLNKYSFLDTPILLSDSQRKSNDVTKEIYSFYPELLLAEIGETISF... | Function: An S subtype restriction enzyme that recognizes the double-stranded sequences 5'-GACGC-3' and 5'-GCGTC-3' and cleaves respectively 10 bases after G-1 and 10 bases before G'-1.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence M... |
P25261 | AWGKNQFNNAFPIALACFMFSQQIKPIYIRLEKRNTEHNYIAVDQIFQINPLDPQAFFAFEHSYHPYTELIIGKTPAIDVVISNLQNSQIINAFEIKLTAIPDNTTAILSDHLQGCEIVIRPDTIVYLALSIAKIFQQNSSVLLDILDPICARISDWEDVTSIKPMIPVFCELLYTIFDRYQSAQIPILLQPIWKTQGKLSILHENCLDLFVWSNFALAKVFLDASIKPSEKSITRPERTTVWLIKMLYDFAQNGKIDYKRTLDRITFNLKNDKAFAASGMVTRKYMNSPELHNPRIKRHLIKHIIINGGQRYLSPERRL... | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GRCGYC-3' and cleaves after R-2.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 38460
Sequence Length: 335
EC: 3.1.21.4
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P29537 | MKYEEINFKVPVESPYYPNYSQCVIERIYSILRNQKDMGDDRIIINTNLKKGLPLENINKIAGPMIEAWAEEVFSGIRDNRDNQYNLINVEAQERLGISDIILQFQVNNNVITGNVDVKATSNDIPDSGKSPNITSFSRIRTAYVKDPNFIFIILSIKHSVYVKRNEYTNLMDGIMQIIDFNVYDLKYISDSDISYNPALGTGQIQIKDIHYVSSQKRTTWQMCQLLDLKYLRSKKRTIEQFYNEAKRNKWIKD | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GTTAAC-3' and cleaves after T-3.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 29629
Sequence Length: 254
EC: 3.1.21.4
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P50191 | MQIYETYWEITNEYGYNTERFVETLKICVEYIDEIKLVNPNYTETDYSSVIYNELQMRLQSSPILQSTRKGFEGKPKNETSIRKSINQLVKSGFINPFLTGYHSLAKEYLQTKVNKKRNFLFSRIVYESSNFSYAITDKPDIKVRHINFLVNTLIENFEGKLSKNEIIALMLMDLRTYNGNYYPIDELRNFIRLNQNYISEFKERKYNQITYLWGLLSKLDEIYQKDEFICLEEDKKRVFGDLEDTQYLRKRDPYLHRLYKHQLQEESAEYCGGIKCMLEKLAYPVLIASHIKPFIQSDDNEAYDPNNGLLLSRTLDSLF... | Function: An S subtype restriction enzyme that recognizes the double-stranded sequences 5'-GGTGA-3' and 5'-TCACC-3' and cleaves respectively 13 bases after G-1 and 7 bases before T-1, leaving a single 3' protruding nucleotide.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragment... |
P36433 | MTEFFSGNRGEWSEPYALFKLLADGQLYLGDSQLNKLGIVMPILSILRQEKNYESSYILHNNSQNIIVTYNNEKFTVPISGFQEKAVLLLSEIKNASGNRAFSIPSIDDFLKKLGFTHLSASSSSKSDIHIVVHDLRTGITPTLGFSIKSQLGSPATLLNASKATNFTFKIYNLKDKQIEYINSLSGIKEKIKEIFSQDGKLEFVKVESCKFSNNLTLIDTKLPEILAEMILLYYSSKLNKIDDVTEHISRLNPLNYNLSCNHNYYEYKVKHFLNDVALGMRPDDVWLGQYDATGGYLVVKEDGELLCYHIYSKNSFEDY... | Function: An E and P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CCGG-3' and cleaves after C-1.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 40926
Sequence Length: 358
EC: 3.1.21.4
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P00643 | MSKISNALGRKDGNSGYTRVVGNAELGQLLSRVQATVISNGNELERLITQRCNLIENIDVFIEDTTRGNNVQNGVYLCLKKTFKKSKKYAESVKGIEPDMLIFIVESYRVCKVIELKDGDAFDTKKSQGEKEHLEKFATLFGAKIPFVTDYYICSFNQNDKKLIMAGFKGVFSLEHILTGKELCQILGISYQEILDIRRRDTEENFAYLIAEMMKIPEVREEVKKHF | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GANTC-3' and cleaves after G-1.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 25910
Sequence Length: 227
EC: 3.1.21.4
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O68584 | MSNKSNDNGRAYEFAFINELGRIATQNQNINIEKNSSYYVVEKSWSTLSDLEKEKYTKSAIAGINLITSLEPIIEDGNGVLNLKIQADNKGELGDIRDILIQRENINWEIGLSLKHNHFAVKHSRLSHKIDFSEKWFQLPSSQNYWDNILPIFEKLEIYKKDKIKWRELSNKEDCIYYPILKSFIAEIKEKYDKYNSIVPQRMVEYLLGYFDFYKIISQDNKKLTSIQSFNLRGTLNKPSKKRKADIFIPVANLPTRIIDIDFKPNSKNTVELYLDKGWQFSFRIHNASTIIEPSLKFDIKLIGVPATIICLETPWEE | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GGCC-3' and cleaves after G-2.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 37129
Sequence Length: 318
EC: 3.1.21.4
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P83257 | ACVGDGQRCASWSGPYCCDGYYCSCRSMPYCRCRNNS | Function: Insecticidal toxin. Lethal to lepidopteran larvae. No adverse affects when intracerebroventricularly injected in mice at a dose of 0.2 ug but causes reversible paralysis of legs when injected intracerebroventricularly in mice at a dose of 2.0 ug. Binds to site 4 of insect voltage-gated sodium channel (Nav) an... |
V5YXI5 | MKITRSLSTVEVHTGGEAFRIVTSGLPRAPGDTIVQRRAWLKENADEIRRALMFEPRGHADMYGGYLTEPVSPNADFGVIFVHNEGYSDHCGHGVIALSTAAVELGWVQRTVPETRVGIDAPCGFIEAFVKWDGEHAGPVRFVNVPSFIWQRDVSVETPSFGTVTGDIAYGGAFYFYVDGAPFDLPVREAAVEKLIRFGAEVKAAANAKYPVVHPEIPEINHIYGTIIANAPRHPGSTQANCCVFADREVDRSPTGSGTGGRVAQLYQRGLLAAGDTLVNESIVGTVFKGRVLRETTVGDIPAVIPEVEGSAHICGFANW... | Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Together with LhpI, is involved in a t3LHyp degradation pathway to L-proline, which allows A.brasilense to grow on t3LHyp as a sole carbon source.
Catalytic Activity: trans-3-hydroxy-L-proline = 1-pyrr... |
Q6HMS9 | MKVSKVYTTIDAHVAGEPLRIITGGVPEIKGDTQLERRAYCMEHLDHLREVLMYEPRGHHGMYGCIITPPASAHADFGVLFMHNEGWSTMCGHGIIAVITVGIETGMFEVTGEKQNFIIDSPAGEVIAYAKYNGSEVESVSFENVPSFVYKKDVPIIIDDYEFQVDIAFGGAFYAVVDSKEFGLKVDFKDLSAIQMWGGKIKHYIESKMEVKHPLEEGLKGIYGVIFSDEPKGEDATLRNVTIFADGQVDRSPCGTGTSARIATLFEKDALQKGEIFVHECITDGKFEGEVLSVTAVDTYEAVVPKVTGHAFITGFHQFV... | Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts t3LHyp to L-proline. Can also catalyze the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp) in vitro. Di... |
Q3SX04 | MAGPLTVPWMPPHDPGTPALSVVDMHTGGEPLRIVLAGCPEVVGPTLLAKRRYMRQHLDHVRRRLMFEPRGHRDMYGAVLVPSELPDAHLGVLFLNNEGYSSMCGHAVLALGRFALDFGLVPAPPSDAQEALVNIHCPCGLVAAFVECEGCRSRGPVRFHSVPAFVLATDFLVDVPGRGKVVVDIAYGGAFYAFVSAEKLGLDVCSAKMGDLVAAASAVTEAVKAQFKISHPDSEDLAFLYGTILTDGKDTYNEEPTTNICVFADEQVDRSPTGSGVTARIALQYHKGLLELNQTRAFKSSATGSVFTGKAVREAKCGDF... | Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline to Delta(1)-pyrroline-2-carboxylate (Pyr2C).
Catalytic Activity: trans-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O
Sequence Mass (Da): 37957
Sequence Length: 354
EC: 4.2.1.77
|
Q485S0 | MTKNIAQAAVKFEQWQPKIEQESYLTINSLECHTGGEPLRIITSGFPVLKGNTILAKANDCKQNYDQLRRALMFEPRGHADMYGAIITDAERDDSHFGAVFIHNEGYSSMCGHAVIALTKTAVESGVVARTGDVTQVVIDVPCGQIYAMAYSHNNVVKHVSFQCVPSFVYAKDQQVEVDGIGMVQFDIAYGGAFYAYVQASSLGLSLVPEQQEKLIAYGRKIKQAIIPQFEINHPTTAELSFLYGVIFIDDSPNQDVHSRNVCIFADGELDRSPTGSGVSGRIALHHAKQQIVLNETITIESILASSFSVRAIETVCFAG... | Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Together with LhpI, is involved in a metabolic pathway that converts t3LHyp to L-proline.
Catalytic Activity: trans-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O
Sequence Mass (Da): 38956
Seque... |
Q96EM0 | MESALAVPRLPPHDPGTPVLSVVDMHTGGEPLRIVLAGCPEVSGPTLLAKRRYMRQHLDHVRRRLMFEPRGHRDMYGAVLVPSELPDAHLGVLFLHNEGYSSMCGHAVLALGRFALDFGLVPAPPAGTREARVNIHCPCGLVTAFVACEDGRSHGPVRFHSVPAFVLATDLMVDVPGHGKVMVDIAYGGAFYAFVTAEKLGLDICSAKTRDLVDAASAVTEAVKAQFKINHPDSEDLAFLYGTILTDGKDAYTKEPTTNICVFADEQVDRSPTGSGVTARIALQYHKGLLELNQMRAFKSSATGSVFTGKAVREAKCGDF... | Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline to Delta(1)-pyrroline-2-carboxylate (Pyr2C). May be required to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins such as collagen-IV that contain it.
Catalytic Activity: trans-3-hydroxy-L-proline = 1-pyrroli... |
O14804 | MRAVFIQGAEEHPAAFCYQVNGSCPRTVHTLGIQLVIYLACAAGMLIIVLGNVFVAFAVSYFKALHTPTNFLLLSLALADMFLGLLVLPLSTIRSVESCWFFGDFLCRLHTYLDTLFCLTSIFHLCFISIDRHCAICDPLLYPSKFTVRVALRYILAGWGVPAAYTSLFLYTDVVETRLSQWLEEMPCVGSCQLLLNKFWGWLNFPLFFVPCLIMISLYVKIFVVATRQAQQITTLSKSLAGAAKHERKAAKTLGIAVGIYLLCWLPFTIDTMVDSLLHFITPPLVFDIFIWFAYFNSACNPIIYVFSYQWFRKALKLTL... | Function: Olfactory receptor specific for trimethylamine, a trace amine. Also activated at lower level by dimethylethylamine. Trimethylamine is a bacterial metabolite found in some animal odors, and to humans it is a repulsive odor associated with bad breath and spoiled food. This receptor is probably mediated by the G... |
Q96RI8 | MSSNSSLLVAVQLCYANVNGSCVKIPFSPGSRVILYIVFGFGAVLAVFGNLLVMISILHFKQLHSPTNFLVASLACADFLVGVTVMPFSMVRTVESCWYFGRSFCTFHTCCDVAFCYSSLFHLCFISIDRYIAVTDPLVYPTKFTVSVSGICISVSWILPLMYSGAVFYTGVYDDGLEELSDALNCIGGCQTVVNQNWVLTDFLSFFIPTFIMIILYGNIFLVARRQAKKIENTGSKTESSSESYKARVARRERKAAKTLGVTVVAFMISWLPYSIDSLIDAFMGFITPACIYEICCWCAYYNSAMNPLIYALFYPWFRK... | Function: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has r... |
Q5QD13 | MGSNSSPPTVLQLCYENVTGSCVKTPYSPGSRVILYAVFGFGAVLAVFGNLMVMISILHFKQLHSPTNFLIASLACADFGVGISVMPFSMVRSIESCWYFGRSFCTFHTCCDVAFCYSSLFHLSFISIDRYIAVTDPLVYPTKFTVSVSGICIGVSWILPLVYSGAVFYTGVYDDGLEELSSALNCVGGCQVVVNQNWVLIDFLSFLIPTLVMIILYGNIFLVARQQAKKIENIGSKTESSSESYKARVARRERKAAKTLGITVVAFMISWLPYSIDSLVDAFMGFITPAYIYEICVWCAYYNSAMNPLIYALFYPWFKK... | Function: Orphan olfactory receptor specific for trace amines.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38279
Sequence Length: 345
Subcellular Location: Cell membrane
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Q96RI9 | MVNNFSQAEAVELCYKNVNESCIKTPYSPGPRSILYAVLGFGAVLAAFGNLLVMIAILHFKQLHTPTNFLIASLACADFLVGVTVMPFSTVRSVESCWYFGDSYCKFHTCFDTSFCFASLFHLCCISVDRYIAVTDPLTYPTKFTVSVSGICIVLSWFFSVTYSFSIFYTGANEEGIEELVVALTCVGGCQAPLNQNWVLLCFLLFFIPNVAMVFIYSKIFLVAKHQARKIESTASQAQSSSESYKERVAKRERKAAKTLGIAMAAFLVSWLPYLVDAVIDAYMNFITPPYVYEILVWCVYYNSAMNPLIYAFFYQWFGK... | Function: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has r... |
Q9NYJ8 | MAQGSHQIDFQVLHDLRQKFPEVPEVVVSRCMLQNNNNLDACCAVLSQESTRYLYGEGDLNFSDDSGISGLRNHMTSLNLDLQSQNIYHHGREGSRMNGSRTLTHSISDGQLQGGQSNSELFQQEPQTAPAQVPQGFNVFGMSSSSGASNSAPHLGFHLGSKGTSSLSQQTPRFNPIMVTLAPNIQTGRNTPTSLHIHGVPPPVLNSPQGNSIYIRPYITTPGGTTRQTQQHSGWVSQFNPMNPQQVYQPSQPGPWTTCPASNPLSHTSSQQPNQQGHQTSHVYMPISSPTTSQPPTIHSSGSSQSSAHSQYNIQNISTG... | Function: Adapter required to activate the JNK and NF-kappa-B signaling pathways through the specific recognition of 'Lys-63'-linked polyubiquitin chains by its RanBP2-type zinc finger (NZF) . Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin chains . The RanBP2-type zinc finger (NZF) sp... |
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