ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8KES6 | MLDITYIRQNPDDVKEMLRRRQQQGDAPKVDRLLERDAERKAMVQRTDDLKALRNRVSKEIANIKRTGQGSADELIGQMKQVSDEIADLDLALSALEAEIEELLLTLPNKLHKSVPEGRSAEENVLYKGPVSFEHNLDFPVKNHLELGKSLGILDFERGAKISGAGFPVYTGKGARLERALINFMLDTHSANHGYTEVFPPFMVNQESLRGTGQWPKFADQVYHMPEDGLYAIPTAEVPVTNLHRGEILDADKLPIAYAAYSACFRREAGSYGKDTRGFLRVHQFNKVEMVRFTRPEASYEALEEILGHAEAILVALKIPYRVITLCSGDISANAAKCYDIEVWSPAENKYLEASSVSNFEDYQARRSNIRFKPDSKSKPEFVHTLNGSGLATSRLMVSLLEHYQTADGKLMVPEALKPYTGFEIIE | 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)
Sequence Mass (Da): 47991
Sequence Length: 427
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
B2VC55 | MLDPNLLRNEPDAVAEKLARRGYKLDVDTLRAHEERRKVLQVETENLQAERNSRSKSIGQAKARGEDIEPLRQEVNALGERLDAAKAELDALLTCINDFSMAIPNIPADVVPLGKDDSENQEISRWGEPRQFDFTVRDHVELGEMAAGLDFAAAVKLTGSRFIVMKGQIALMHRALSQFMLDLHTEQHGYQETYVPYLVNHASLYGTGQLPKFGEDLFHTRPLDEEASSSNYALIPTSEVPLTNLVRDEILEEETLPLKMTAHTPCFRSEAGAYGRDTRGLIRMHQFDKVEMVHITRPEDSMDALEELVGHAEKVLQLLNLPYRKVLLCTGDMGFGAQKTYDLEVWLPAQDTYREISSCSNMGDFQARRMKARCRPRGESKTRLVHTLNGSGLAVGRTLVAVLENYQQADGRIEVPEVLRPYMKGLHFIG | 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)
Sequence Mass (Da): 48442
Sequence Length: 430
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
Q8RH11 | MLELKFMRENVEMLKEMLKNRNSNVDMDAFVELDSKRREVLSEVENLKRERNNASAEIANLKKEKKNADHIIEKMGEVSTKIKDLDAELVEIDEKIKDIQLNIPNVYHPSTPIGPDEDYNLEIRKWGIPKKFDFEPKSHWDIGEDLGILDFERGAKLSGSRFVLYRGAAARLERAIINFMLDVHTLEEGYTEHITPFMVKAEVCEGTGQLPKFEEDMYKTTDDMYLISTSEITMTNIHRKEILEQAELPKYYTAYSPCFRREAGSYGKDVKGLIRLHQFNKVEMVKITDAESSYDELEKMVNNAETILQRLELPYRVIQLCSGDLGFSAAKTYDLEVWLPSQNKYREISSCSNCEAFQARRMGLKYRVPNGSEFCHTLNGSGLAVGRTLVAIMENYQQEDGSFLVPKVLIPYMGGVDVIKK | 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)
Sequence Mass (Da): 48389
Sequence Length: 421
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
C1A8M5 | MHDIRLLRDQLDVLREGMRRRGKLTELGDVLDRAESLEQARRTAITELEAQQARRNKVTQEVAQRRKAGEDATALIAEGRAIGEQITALEQRRNEADAAVQAMLYELPNIPLADVPEGDETANTVVRTWGTPRTPDASIVPHWDKGEALGMLDLARGAKISGSGFIVYRNRGARLVRALMNMMLDIHTEEHGYEETWVPLVVNRASMTGTGNFPKFEEDAYAITEDELFLIPTAEVPVTNLYRDEILDAEELPKRFCAFSACFRREAGAAGKDTRGLLRVHEFDKVELVRYANPETSLEELELLTSQAETILKRLELPYRVLLLAAGDTGFSSAKTYDLEVFAPGVGKWLEVSSCSLFTDFQARRANIRYRPAAGEKPRFVHTLNGSALAFSRIIASLLEHHQQPDGSVRIPEALQPYFGRAVLA | 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)
Sequence Mass (Da): 47513
Sequence Length: 425
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
Q5L3Y0 | MLDVKILRTQFEEVKEKLMQRGGDLTNIDRFEQLDKDRRRLIAEVEELKSKRNDVSQQIAVLKREKKDAEPLIAQMREVGDRIKRMDEQIRQLEAELDDLLLSIPNVPHESVPIGQSEEDNVEVRRWGEPRSFSFEPKPHWEIADRLGLLDFERAAKVAGSRFVFYKGLGARLERALINFMLDIHLDEFGYEEVLPPYLVNRASMIGTGQLPKFAEDAFHLDSEDYFLIPTAEVPVTNLHRDEILAADDLPIYYAAYSACFRAEAGSAGRDTRGLIRQHQFNKVELVKFVKPEDSYDELEKLTRQAETILQRLGLPYRVVALCTGDLGFSAAKTYDIEVWLPSYGTYREISSCSNFEAFQARRANIRFRRDPKAKPEYVHTLNGSGLAIGRTVAAILENYQQEDGSVIVPEALRPYMGNRDVIR | 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)
Sequence Mass (Da): 48668
Sequence Length: 424
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
Q6F2A0 | MLDINFIESNLVKVKEQLNKRSGDYSLIIDEAVELNVQRKSILKEVENLKANKNNLSKQVGELMRNKQSDEANKIKEEVTLINSKIEKLDDSLKLVQEQLTSKLQNIPNIPNDNMPIGNDDNDNVEVRQWGNELIKKHNTPHWDIADKLKLVDFEAGPKLSGSRFVVYTGLGAKLVRSLSNILLNLHTSKGYTEITVPLLVNPQAMYGTGQLPKFKEDAYITTNDQYLIPTGEVPLTNLHAGEILDLNQLPIHYTTYSQCFRQEAGSAGRDTKGLIRLHQFNKVELVKITNQESSEAELQAMVNDAEAVLQLFNLPYRVVELCTGDVGFSSSKTYDLEVWFPEQNKYREISSCSNCTDFQARNMQTRYRDANGEVKLAHTLNGSGVAIDRLIAAILENYWDGEKLILPTALKPYFDNKEYID | 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)
Sequence Mass (Da): 47794
Sequence Length: 422
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
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Q6KIJ8 | MLDIKLILKNKDFVISKLKQRSNFNVSEIEKLYTLGTERANILISLSELQSKRNEISSKIGEAKRNKTDALFFMDEVENIKKELSILEEKSTKIENKIQELISFIPNIPLDDVPFGKDDTDNVILKEFPKIGRGLVKAKKPHYEIGVEKDLIDFSRGAKLSGSRFIVYKNAGAKLIRALESFMLDTHEKNGYSEIMPPFLVNSKMMYGTGQLPKFKEDLFKIEGHDLYLIPTAEVPVTNLFNNEIIDLEKNSKFSSFTNCFRSEAGSAGRDTKGIIRLHQFNKVELVEFASEQKSLRAFNSVLKNAKYLLELLEIPYREVLLCTGDLGFSSRKTIDLELWLPSEQRYREVSSVSYFGDFQSRRSMIRYRDENKNTQYVHTINGSGLAIDRVLAAILEQYQNDDGSISVPKVLIPYLNVEKI | 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)
Sequence Mass (Da): 48180
Sequence Length: 421
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
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Q46F20 | MLDLKFVRSSPDIVRHALINRNMSTELIDSLLEYDIAWRKCLTEGDELKHKRNVVTREIAKLKKENKDTLSKIEEMQGINSRIKEIDDIIRDYKSKIHEIMLRIPNIPSSTTPVGKDENDNPVVRIVGEPRKFTFTPKPHWEIGEALDILDFEKGAKISGQGFTVYKGMGAKLERALVNFMLEVHARQGYLEVFPPVLINEKAMTGTGQLPKFKDDMYLCTDGYYLAPTAEVPVTNLFMDDYIEKLPVFLTAYTACFRREAGKHGQDTRGIIRQHQFNKVELVKFVKPETSYDELEKLTNDAEEILKLLKLPYRVVNLCTGDIGFSAAKTYDLEVWVPTQEKYREISSCSNFENFQARRANIRFRTPDGPQFVHTLNGSGLAVGRTVVAILENYQREDGSVEIPEVLRPYLGGAKEISNEVKT | 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)
Sequence Mass (Da): 48312
Sequence Length: 423
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
Q1H290 | MLDIQQLRNDLDNVVARLSSRGFAFDINAFIALENERKTVQTRTQDLQAKRNATSKQIGIAKSRGEDVASIMAEVAGLGAQLKEGEERLAAIQAELQQLLLSVPNLPHESVPVGKSEEDNVEVRRVGTPRRFDFDVKDHTDIGTPLGLDFDTGAKLAGARFTLMRGQIARLHRALAQFMLDTQTEQHGYTECYTPYIVNADSLRGTGQLPKFEADLFAAQKGGQEGESNEAFYLIPTSEVTLTNTVRDEIVPLDSLPIKLTAHTPCFRSEAGSYGRDTRGMIRQHQFDKVEMVQITHPERSYDALEEMVGHAEHVLQALGLPYRVVLLCTGDMGFGAAKTYDLEVWLPAQNTYREISSVSNCEAFQARRLQARFRNENGKPELLHTLNGSGLAVGRTLVAVLENNQQADGSVVVPEVLRPYMGGLTVISAQQ | 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)
Sequence Mass (Da): 47737
Sequence Length: 432
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
Q2FS27 | MLDIRFVRANPDAIREDLKKRNDMEKLAWIDDLLVQDIRHRELIGQTNELRRRRNSISYDINRAKKAGEDASALIAEAAGLPGRIKENEAEMEEISKKIRYYLMRIPNILHESVPVGADDTQNVEVKRYGTPRTFTFELKNHGQLAADNDWADFERATKTSGAGFYFLKGNLVLLDLALQRFSLDILMEKGYTPIIPPYMINRKSYEEVTDLDDFEKVMYKIEDDDAYLIATSEHPMAAMYQDEIFEEKDLPLRLAGLSPCFRREIGSHGLDTKGLFRVHQFHKVEQFVYCHPDDSWTIHEELRENAEEIFQKLEIPYRVVNICTGDIGTVAAKKYDIEAWMPRENEYREVVSCSNCTTYQAVRLNIRVRDKEDFESKQFVHTLNSTAIATSRAMRAILENNQQEDGSVVIPKVLRPYMNDKEFL | 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)
Sequence Mass (Da): 49346
Sequence Length: 425
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
B3DX68 | MLDIQLIRHNLAQTKQKLALRSKGLETLLDHIFELDFKKRSLQSEIEKYRALRNKQSKEIGLKKIKGENVEGQFSELKKMGSRIEEMEKELIQFENQINTLLLSLPNIPHDSVPTGGPEANKVVKTWGEPRQANFPLKTHWELGRELGILDLERGAKLSGSGFSLFTGNGAKLQRALIQFMLTIHTEEHGYKELWPPYLVTEDCMRGTGHLPKFALDMYATDKDNLYLIPTGEVPLTNFHRDEILAESSLPLRYVAYTPCFRREAGSAGKDTRGLLRLHQFDKVELVQITKPENSYTALEEMVSHAENILRSLNLCYRVVLLASQDMGFGAAKCYDLEVWSPGIQSWLEVSSVSNMENFQSRRMNLRYKSSSGKNILCHTLNGSGTALPRLVAAILENYQKEDGRVLIPEKIRTYFKEEYL | 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)
Sequence Mass (Da): 48046
Sequence Length: 421
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
A3CTP4 | MLELKFVRAHPEIVRADLTKRGDTEKLAWVDEVLEMDRRARELTVAIGDLRNRRNVISREISQARKAGNDITELLAEAAGLPERIKEVETERETLTEAVRYRLMRLPNILHESVPVGKDDSENVEIRRWGEPEIPAFDLENHGALAVEHGWADFERAAKIAGSGFYFLKGRLALLDMALQRFAMDILVEHGYTPIIPPYMMNRAAYEGVTDLADFENVMYRIDGEDEYLIATSEHPMAAMYCDEIFEEKDLPLRLAGLSPCFRREIGAHGLDTKGLFRVHQFHKVEQFIYATPEQSWDLHEELMANAEEVFQRLGLPYRIVSICTGDIGTVAAKKYDLEVWMPREERYREAVSCSNCTAYQAVRLNIKVRNPTEFTEKRYVHTLNSTAIATSRAIRAILENNQNEDGSVTIPKALRPYLYGSETL | 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)
Sequence Mass (Da): 48635
Sequence Length: 425
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
Q2S1G4 | MLDLDTVRNDPRRVKEALRAKGIGSPDLVDTLLEIDETRRSAITELQDVQSRQNELSQQIGALKREGKDEEAEAIIEKTGRMKEKINRLKEEVQEAEARQEELVLELPNIPHPSVPVGADEDDNEVEATVGEMPAFDFDPAPHWELADRHNLVDLERGAKVAGSGFPFYLGKGARLQRALLNFFLDRARERGYTEMQAPLFVNPESAKGTGQIPDKDALMYEIPRDDFYPIPTAEVPVTNFHRDEILAADDLPRRYCTYSPCWRREAGSYGSDVRGLNRLHQFDKVELVRIVPPDESYRALDALLEDAESALDALDLPYRRLLMCTGDMGFTQAKVYDLEVWSAAQERWLEVSSVSNFEAFQARRAQIRYRLEPEAKPELVHTLNGSGLAFPRIVAALLENNQQPDGSIELPEALHPYTGFARIGAEA | 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)
Sequence Mass (Da): 48295
Sequence Length: 428
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.1.1.11
|
Q920N7 | MAVDVTEYHLSVIKSPPGWEVGVYAAGALALLGIAAVSLWKLWTSGSFPSPSPFPNYDYRYLQQKYGEAYVEAKLKRVPPWNDQRTTTRGPPSRKGSLSIEDTFESISELGPLELMGRELDLAPYGTLRKSQSADSLNSISSVSNTFGQDFTLGQVEVSMDYDGASHTLHVAVLQGKDLLEREEATFESCFMRVSLLPDEQIVGISRIQRNAYSIFFDEKFSVPLDPTALEEKSLRFSVFGIDEDERNVSTGVVELKLSVLDLPLQPFSGWLYLQDQNKAADAVGEILLSLSYLPTAERLTVVVVKAKNLIWTNEKSTADPFVKVYLLQDGRKMSKKKTAVKRDDPNPVFNEAMIFSVPAIVLQDLSLRVTVAESSSDGRGDNVGHVIIGPGVSGMGTTHWNQMLATLRRPVSMWHPVRRN | 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 .
PTM: Phosphorylation of Ser-97 is required for mossy-fiber long-term potentiation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 46680
Sequence Length: 421
Subcellular Location: Cytoplasmic vesicle
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P97610 | MAVDVTEYHLSVIKSPPGWEVGVYAAGALALLGIAAVSLWKLWTSGSFPSPSPFPNYDYRYLQQKYGEAYVEAKLKRVPPWNAQRTTTRGPPSRKGSLSIEDTFESISELGPLELMGRELDLAPYGTLRKSQSADSLNSISSVSNTFGQDFTLGQVEVSMDYDGASHTLHVAVLQGKDLLEREEATFESCFMRVSLLPDEQIVGISRIQRNAYSIFFDEKFSVPLDPTALEEKSLRFSVFGIDEDERNVSTGVVELKLSVLDLPLQPFSGWLYLQDQNKAADAVGEILLSLSYLPTAERLTVVVVKAKNLIWTNDKTTADPFVKVYLLQDGRKMSKKKTAVKRDDPNPVFNEAMIFSVPAIVLQDLSLRVTVAESSSDGRGDNVGHVIIGPGASGMGTTHWNQMLATLRRPVSMWHPVRRN | 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: Phosphorylation of Ser-97 is required for mossy-fiber long-term potentiation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 46608
Sequence Length: 421
Subcellular Location: Cytoplasmic vesicle
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Q7L8C5 | MVLSVPVIALGATLGTATSILALCGVTCLCRHMHPKKGLLPRDQDPDLEKAKPSLLGSAQQFNVKKSTEPVQPRALLKFPDIYGPRPAVTAPEVINYADYSLRSTEEPTAPASPQPPNDSRLKRQVTEELFILPQNGVVEDVCVMETWNPEKAASWNQAPKLHYCLDYDCQKAELFVTRLEAVTSNHDGGCDCYVQGSVANRTGSVEAQTALKKRQLHTTWEEGLVLPLAEEELPTATLTLTLRTCDRFSRHSVAGELRLGLDGTSVPLGAAQWGELKTSAKEPSAGAGEVLLSISYLPAANRLLVVLIKAKNLHSNQSKELLGKDVSVKVTLKHQARKLKKKQTKRAKHKINPVWNEMIMFELPDDLLQASSVELEVLGQDDSGQSCALGHCSLGLHTSGSERSHWEEMLKNPRRQIAMWHQLHL | 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 | MVLSVPVIALGATLGTATSILALCGVTCLCRHMHPKKGLLPRDREPDPEKARPGVLQAAQQFNIKKSTEPVQPRPLLKFPDIYGPRPAVTAPEVINYADYTLETTEESAAPASPQAQSDSRLKRQVTEELSIRPQNGVVEDVCVMETWNPEKAASWNQAPKLHFRLDYDQKKAELFVTSLEAVTSDHEGGCDCYIQGSVAVKTGSVEAQTALKKRQLHTTWEEGLALPLGEEELPTATLTLTLRTCDRFSRHSVIGELRLGLDGASVPLGAAQWGELKTTAKEPSAGAGEVLLSISYLPAANRLLVVLIKAKNLHSNQSKELLGKDVSVKVTLKHQAQKLKKKQTKRAKHKINPVWNEMIMFELPDDLLRASSVELEVLGQGEEGPSCELGHCSLGLHASGSERSHWEEMLKNPRRQIAMWHQLHL | 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 | MAIEGGERTCGVHELICIRKVSPEAVGFLSAVGVFIILMLLLFLYINKKFCFENVGGFPDLGSEYSTRKNSQDKIYNSYMDKDEHGSSSESEDEALGKYHEALSRTHNSRLPLADSRQRNYAWETRQKYSPLSAEYDGYSSEASIDEGNCIQRMRRTPPLDELQPPPYQDDSGSPHLSCTPSEIGDSKCEFSHCSNSPRCSYNKCPSEGSTGHEIESFHNKGYEEDVPSDSTAVLSPEDMSAQGSSSQLPKPFDPEPEAKYGTLDVTFDYDSQEQKLLVTVTAVTDIPTYNRTGGNSWQVHLVLLPIKKQRAKTSIQRGPCPVFTETFKFNHVESEMIGNYAVRFRLYGVHRMKKEKIVGEKIFYLTKLNLQGKMSLPVILEPSYNHSGCDSQMSVSEMSCSESTSSCQSLEHGSVPEILIGLLYNATTGRLSAEVIKGSHFKNLAANRPPNTYVKLTLLNSMGQEMSKCKTSIRRGQPNPVYKETFVFQVALFQLSDVTLILSVYNKRSMKRKEMIGWISLGLNSSGEEELNHWTEMKESKGQQVCRWHALLES | 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 | MAIEGGERTCGVHELICIRKVSPEAVGFLSAVGVFIVLMLLLFLYINKKFCFENVGGFPDLGSGYNTRTNSQDKMYNSYMDRDEPGSSSESEDEALGKYHEALSRTHNSRWPLVDSRQKSYAWETRQKYSPLSAEYDGYSTEASMEDGNCIQRMRRTPPLDELQPPPYQDDSGSPHLSCTPSEIGDAKCEISHCSNSPRCSFNKCPSEGSTGHEAESYHNKGYEDDVPSDSTAVLSPEDMSAQGSSSQLPKPFDPEPEAKYGTLDVTFDYDSERQKLLVTVTAVTDIPTYNRTGGNSWQVHLVLLPIKKQRAKTSIQRGPCPVFTETFKFNHVESEMIGNYAVRFRLYGVHRMKKEKIVGEKIFYLTKLNLQGKMSLPVILEPSYNPSGCDSQVSLSEASCGDSTSSCQSLQHGSVPEILIGLLYNATTGRLSAEVIKGSHFKNLAANRPPNTYVKLTLLNSMGQEMSKCKTSTRRGQPNPVYKETFVFQVALFQLSDVTLILSVYNRRSMKRKEMIGWISLGLNSSGEEELRHWTAMKESKGQQVCRWHALLES | 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 | MAEQLALVIGGTIGGLLLLLLIGASCCLWRRFCATLTYEELPGTPAMATTAASSGQRDRPCQPHARTQLSRPPAVPFVVPPTLQGRDWVPLHSGEWADAPWDPCPASELLPHTSSGGLGDACMVGAINPELYKFPEDKSETDFPDGCLGRLWFSVEYEQEAERLLVGLIKAQHLQAPSETCSPLVKLYLLPDERRFLQSKTKRKTSNPQFDEHFIFQVSSKTITQRVLKFSVYHVDRQRKHQLLGQVLFPLKNETLVGDCRRVIWRDLEAESLEPPSEFGDLQFCLSYNDYLSRLTVVVLRAKGLRLQEDRGIVSVFVKVSLMNHNKFVKCKKTSAVLGSINPVYNETFSFKADATELDTASLSLTVVQNMEGDKSQQLGRVVVGPYMYTRGRELEHWDEMLSKPKELVKRWHALCRTTEP | 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 Location: Cell membrane
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Q9BSW7 | MAYIQLEPLNEGFLSRISGLLLCRWTCRHCCQKCYESSCCQSSEDEVEILGPFPAQTPPWLMASRSSDKDGDSVHTASEVPLTPRTNSPDGRRSSSDTSKSTYSLTRRISSLESRRPSSPLIDIKPIEFGVLSAKKEPIQPSVLRRTYNPDDYFRKFEPHLYSLDSNSDDVDSLTDEEILSKYQLGMLHFSTQYDLLHNHLTVRVIEARDLPPPISHDGSRQDMAHSNPYVKICLLPDQKNSKQTGVKRKTQKPVFEERYTFEIPFLEAQRRTLLLTVVDFDKFSRHCVIGKVSVPLCEVDLVKGGHWWKALIPSSQNEVELGELLLSLNYLPSAGRLNVDVIRAKQLLQTDVSQGSDPFVKIQLVHGLKLVKTKKTSFLRGTIDPFYNESFSFKVPQEELENASLVFTVFGHNMKSSNDFIGRIVIGQYSSGPSETNHWRRMLNTHRTAVEQWHSLRSRAECDRVSPASLEVT | 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 | MLEPLNEGLLSRISDVLLCGWTCQHCCQRCYESSCCQSSEDEVEILGPFPAQTPPWLMASRSNDKDGDSVHTASDVPLTPRTNSPDGRRSSSDTSKSTYSLTRRISSLDSRRPSSPLIDIKPVEFGVLSAKKESIQPSVLRRTYTPDDYFRKFEPRLYSLDSNLDDVDSLTDEEIMSKYQLGMLHFSTQYDLLHNHLTVRVIEARDLPPPISHDGSRQDMAHSNPYVKICLLPDQKNSKQTGVKRKTQKPVFEERYTFEIPFLEAQRRTLLLTVVDFDKFSRHCVIGKVAVPLCEVDLVKGGHWWKALIPSSQNEVELGELLLSLNYLPSAGRLNVDIIRAKQLLQTDVSQGSDPFVKIQLVHGLKLVKTKKTSFLRGTIDPFYNESFSFKVPQEELENASLVFTVFGHNMKSSNDFIGRIVIGQYSSGPSESNHWRRMLNTHRTAVEQWHSLRSRAECDRVSPASLEVT | 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 | MAYIQLEPLNEGFLSRISDLLLCRWTCRHCCQKCYESSCCQSSEDEVEILGPFPAQTPPWLMASRSSDKDGDSVHTASEVPLTPRTNSPDGRRSSSDTSKSTYSLTRRISSLESRRPSSPLIDIKPIEFGVLSAKKEPIQPSVLRRTYTPDDYFRKFEPHLYSLDPNSDDVDSLTDEEILSKYQLGMLHFSTQYDLLHNHLTVRVIEARDLPPPISHDGSRQDMAHSNPYVKICLLPDQKNSKQTGVKRKTQKPVFEERYTFEIPFLEAQRRTLLLTVVDFDKFSRHCVIGKVSVPLCEVDLVKGGHWWKALIPSSQNEVELGELLLSLNYLPSAGRLNVDVIRAKQLLQTDVSQGSDPFVKIQLVHGLKLVKTKKTSFLRGTIDPFYNESFSFKVPQEELENASLVFTVFGHNMKSSNDFIGRIVIGQYSSGPSESNHWRRMLNTHRTAVEQWHSLRSRAECDRVSPASLEVT | 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 | MVSESHHEALAAPPATTVAAAPPSNVTEPASPGGGGGKEDAFSKLKEKFMNELNKIPLPPWALIAIAIVAVLLILTCCFCLCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQDDDAETGLTDGEEKEEPKEVEKLGKIQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEYKVAMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQIVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQPEEEVDAMLAVKK | 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 synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. May play a role in dendrite formation by melanocytes (By similarity). May play a role in regulating the secretion of hormones relevant to the reproduction and egg-laying of female geese .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47208
Sequence Length: 421
Domain: The first C2 domain mediates Ca(2+)-dependent phospholipid binding.
Subcellular Location: Cytoplasmic vesicle
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A1RY76 | MKTLLIHAKHFEYEAREKALDAAESIDGNRSGSFENALVVFVTVEKGDGSSQDVVEEAAADVLDVFRRVGASRVVVYPYAHLSDDLADPEEAKRVLSQLAERISSAGVPVSRAPFGWYKRFSVECYGHPLSELSRTIKPGRRVRPGYADFAVMFPDGRIVGIEELRAEELPEDFVALLEAEVFKKKREGGEPKYLEYCRKFGFEWEPMSDLGHMRYGPEATIMLDAVAEYAWQCARSLGIPVYKVRGTNTFNLSFKPVAQHAQLFGDRLYQMEVDEKKLILRYAACHQQFAMVKDWEISYRDLPFGAFEVADSYRLEQPGELLLCFRLRKFYMPDLHVFCKDLAEAMEVSFRIHSKIYEEIRKLGRDYVSIYNLTRSFLEQHRDYLKRLVEMEGKPVLLHFVPEGKYYWVINVEYNIIDELGRPREIGTFQIDVGNAERFGITYVDENNTRRYPVIIHTAIIGSLERYVFAVLDTAAKKARAGEVPSLPLWLSPVQVRVIPHSSEYLKLADSIADKLEEQGIRVDVDDREESLAKRIRDAEVKWIPYVVVVGKREAESGKLTVRVRGQGQYEMSLEELVGRLVSELKGYPRVSAALPRYVSARPRYSP | 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-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
Sequence Mass (Da): 69661
Sequence Length: 608
Domain: The N-terminal domain is an archaea-specific tRNA-editing domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis of tRNA editing is performed by the charged tRNA itself.
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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C6A1R1 | MRILLIHSDYLEYEVKDKALKKPEEISENQKKGRLDEVLAVFMSVEKVDEQNPEEIVKKAVKEIEEVVSQVKTNNIFVYPFAHLSSELGSPDVALRILKEIENELKNKGYNVRRAPFGYYKAFKLSCKGHPLAELSRTIVPGEAKKEEEVPEALKKEEELVSYWYILTPEGELVEVDKFDFSGYENLKKFANYEINKSRLVTEEPPHVKIMLEQELVDYEEGSDPGNLRYYPKGRLIKSLLENYVTDKVIEYGAMEVETPIMYDFEHPALEKYLNRFPARQYVVKSGDKRFFLRFAACFGQFLIKKDATISYRHLPLRMYELTRYSFRREKRGELSGLRRLRAFTMPDMHTVAKNLQQAMEEFKKQYKLSMEVLKGVGLTPEDYEVAIRFTEDFWNENKDFIVDLAGIIGKPVLIEMWKQRFFYFILKFEFNFVDNLDKAAALSTVQIDVENSQRFGITYYDEEGQEKYPLLLHCSPSGAIERVMYAILEKQAKIMKKGKKPMYPLWLSPIQVRIIPVSEKYLDYALYIAGKLEGAKIRADVDDRNERLNKKIREAEKEWIPYIIVVGENEKRMGVITVRKREDNKQYEIQVEDLIKEIRQKTEGFPYKPRPLPPLVSMRPKFRG | 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-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
Sequence Mass (Da): 73363
Sequence Length: 625
Domain: The N-terminal domain is an archaea-specific tRNA-editing domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis of tRNA editing is performed by the charged tRNA itself.
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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P56881 | MTVYLPDGKPLELPEGATAKDVARALGEGWERRAVGAIVDGELYDLLKPLPQGAKVRLLTEKDPEFQTLFRHTLAHVLAQAVKEFFREKGYDPESVRLGVGPVIEKGFYYDIEAPEPLSDEDLPAIEAKMREILKRDLPLRRFVLSREEALARYRGKDPYKTELVLEIPEGEEISFYQQGDEAYGFTDLCRGPHVPSTGRIPPHFKLTHVAGAYWRGDENRPMLQRVYGVAFRTAEELKEYLWQLEEAKKRDHRRLGRELELFLIDPLVGKGLVLWLPKGNVVREELMAFMREEQVRRGYQLVTTPHIGSLELYKTSGHYPYYAESQFPPISFKERGEEEEYLLKPMNCPHHIRIYAYRKRSYRELPLRLAEFGTVYRYEKAGELLGLTRVRGFTQDDAHIFCTPEEVKGEFLGVLDLVLKVFATLGLKDYRARIGVRDPKSDKYVGDEAKWALAERQIEEAAAEAGLRYTVEEGDAAFYGPKLDFVVKDALGREWQLGTIQVDYNLPERFGLTYVGKDGEEHRPVMLHRAPFGSLERFIGILIEHFAGDFPLWLAPVQAVVVPVSEKQEDYAREVAGRLKEAGLRAEADTRPERMQARIRDAEVQKVPYILVVGEREKAEGAVSVRRRKKGNLGTMPLAAFLEGALREYRERRLEPVF | 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-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
Sequence Mass (Da): 75537
Sequence Length: 659
Domain: The C-terminal domain recognizes the anticodon bases.
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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Q3SK34 | MVTVTLPDGSVRPFEGPVTVAEVASSIGAGLAKAALAGKVDGKLVDTSYVIDADAQLAIVTAKDAEALDLIRHDAAHVMAQAVQELYPGTQVTIGPAIEDGFYYDFAREQPFTPEDLEKIEKRMDEIVKRDLPIRREVWSRDEAMKVFGDLGETYKVQIIDEVIPKGEELSIYRQGEWFDVCRGPHLPSTGKLPRAFKLMKLAGAYWRGDSKNAMLQRIYGTAWAKKEDLEAYLHRLEEAEKRDHRRLAKQLDLLHMQDEAPGMVFWHPKGWIVWQQIEQYMREKFVEYGYQEVRTPAVMDRSMWEKSGHWENYRDNMFTTASENRDYAVKPMNCPGHVQIFNSGLHSYRDLPLRLAEFGSCHRNEPSGALHGIMRVRGFTQDDAHIFCMEEQVEQEVADFIVMLQKVYADFGFNDVLVKLSTRPDKRVGSDESWDKAESALAAALEKNGLSFDLQPGEGAFYGPKIEFTLKDTLGRLWQCGTIQLDFNLPVRLGAEFVAEDNTRKIPVMLHRAILGSMERFIGILIEHHAGNFPLWLAPVQVMVMNISERQAAYAEAVAEALRRAGIRAALDLSNNKINYKIREHSLQKLPYQLVVGDKEMEARVVAVRARGNQDMGQLGLDDLIARLRAEVLARQ | 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-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
Sequence Mass (Da): 72180
Sequence Length: 637
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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B8GRI1 | MPLITLPDGSERRFDAPVTVRDVAADIGAGLAKAALAGRVNGRLVDTSHLIEDDASLAIITDRDPEGLEVIRHSTAHLLAQAVKDLFPSAQVTIGPVIDNGFYYDFAFERPFHPDDLEKIEARMKELAKADLPVSRSVMDRDEAVDFFRDQGEEYKAQIIADIPAGETISLYKQGEFIDLCRGPHVPSTGKLKAFKLTKVAGAYWRGDSSNEMLQRIYGTAWPNKQQLDDYLHRLAEAERRDHRRIGTELNLFSIQEDAGGGLVFWHPKGARIRRAIEQFWFDMHERAGYQFLYTPHIANLDLWKTSGHADFYSESMYEPMEDDNQAFQLKPMNCPFHVLVYKDRLHSYRDLPLRWAEMGTVYRREMSGALHGLMRVRGFTQDDAHIFCREDQIEAEILRILDLTLEVLQAFGFDDFDVNLSTRPDKAVGSDQIWEHATAALKAALEKKGLDYSVDEGGGAFYGPKIDIKIRDAIGREWQCSTVQLDFNLPERFEMEYVAEDNSRRRPIMIHRALLGSVERFFGVLIEHYAGSFPLWLAPVQVQVLTITDRQDDYAREVADRLRNRGIRADADLRNEKIGFKIREHTLQRVPYLLVLGDREMETNTVAVRTRSGEDLGSMDLNQLSERLAGEIASRGRSHLED | 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-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
Sequence Mass (Da): 73259
Sequence Length: 643
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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O83809 | MGLCVEENITMLQKRSDTLDRLRHSLAHVMAEAVQALFPGTKLAVGPPIDYGFYYDFSPPRPLCDADLAPIEEKMRAILRAGCPFVKEVVSRPDALARFKDEPFKQELIERISADDTLSLYHSGAFTDLCRGPHVQSMRDINPHAFKLTSIAGAYWRGNERGPQLTRIYGTAWESEEDLHTYLRMQDEAKRRDHRKLGPALGLFHLDEENPGQVFWHPEGWTLYVAIQQYLRRVMHEDGYAEVHTPFVMPQSLWERSGHWDKYRANMYLTEGEKRSFALKPMNCPGHVEIFKQKTRSYRDLPLRLSEFGSCTRNEPSGSLHGVMRVRGFVQDDAHIFCTEAQIASEVTRFCRLLARVYADFGFAQEQIRVKFSTRPEQRIGDDATWDRAERALAEACEAAGLSYEHAPGEGAFYGPKLEFALIDTLEREWQCGTIQVDYQLPSCERLNAEYVGEDNQRHMPVILHRTVIGSLERFIGILIEHYGGAFPPWLAPVQAVVIPVAPAFLEYAQHVARELCARSLRVQADVSAERMNAKIRTAQTQKVPYLLIVGERELRAQQVAVRPRTGPQHSMGLSAFSTFLLAKLETRALHA | 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-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
Sequence Mass (Da): 67399
Sequence Length: 592
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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Q83GK5 | MDGFEFFSGRSDVVAMICDDRLLDLSESIPSGKVPEPIELDSPHGLDILRHSCAHVLAQAVQSIYGDAKLGIGPFTENGFYYDFSVNEPFSSDSLRVIEDKMREIVHSDQKFVRKVVDRQSAHSQFRDEPFKLEIINATDDTLSIYYNIDADSGSVRWMDFCRGPHLPSTRFIGDAFALTHVSSVYWRGNSDNPQMQRVYGTAWGSAKDLKGYLDRVELAKLVDHRKLGKELDLFSLPDEIGPGLALFHVKGGIIRSEMEQYARLRHLEEGYNFVYSPHITKRDLFERSGHLQWYGQSMFPPMRLDKDSCSQGFDYYLKPMNCPFHSLVFSSQPRSYRQLPLRLAEFGTVYRYEQSGAIHGLARVRGLTQDDAHIYATRESFEDEVSKALQFTISLLGDYGLDQFYIEISTRDASGKFLGSDEDWAYATHILQKVAQDSGLQTRDDPGGAAFYGPKISVQAKDAIGRYWQMSTIQLDFNLPERFGLFYTDRAGERKRPIMVHRALFGSFERFFAVLTEHYAGAFPPWLSPEQVVALPVTSAHIPYLEEFVSRFSSRLIRARVDYMQDRLPKKIRSYVKEKIPFVLVAGDRDLTNRTVAIRFRDGTQISDLPIQKCFDGICASIDRKKQIQTRIDFDSVLE | 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-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
Sequence Mass (Da): 73126
Sequence Length: 640
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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B5ZC42 | MYKFDPKLNHSAAHVLAMALTKFYPNLSLAIGPAIDEGFYYDFNLNDPNTSITPIDLLKIEKEMKKIAAQALTFDYEQVSYEQAKDLFKNNKYKLDIIEENKNKPLSIYHSGKWFDLCKGPHVENTKEIKAIKLLNIAGSYWRGDANNDQLIRIYGVAFNDQAQLDAYLVDLQERKERDHRKIGKDLNLFTFNNLAGQGLPIWLPNGTIIKSQVQKFINEVEFQFNFDTVITPILGSIDLYKTSGHWDHYKDNIFSPVQIDNEVLILRPMTCPHHTLVYSNELRSYRSLPIRLSEHSILHRYESSGGLTGFERVREMILEDCHVFCRPDQIEHEVINAFKMIQEAQEGLGIKTFEIHLSLNDPNDKEKYYDDPQMWEHSQNALRKMLKDHKIPYKEMVGEAAFYGPKIDFQVKTVLNRIITVSTIQLDFLLPNRFNLSYINENNEQSTPVMIHIGIIGTYERLLAILLEQTKGVLPLWLSPVQVVIIPVNENLHADYAKELNAKLRKHLVRSSLDLRNERLSKKIREAQIQKIPYQIVVGDEEIKNDKMVTYRRYGSEETTTVSVDDFIKVLENDIRSKK | 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-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
Sequence Mass (Da): 67307
Sequence Length: 580
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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Q6AMA0 | MAQDSLLSKGYEFADVEEKWLSRWHKQNAFATKMEDGKDAFSIVIPPPNVTGVLHVGHALNNTLQDILVRYHRMCGDNTMWIPGTDHAGIATQNVVERQLATEGKGRHDLGREAFIERVWKWREDKGGTIVNQLKKIGSSCDWERERFTMDEGLSTSVREVFVRLYKEGLIYKGDYIVNWCPRCQTALADDEVEHEDSKGKLYHIRYPFADGSGSVVIATTRPETMPGDTAIAVHPDDERYAHLGEIGIKLPLTDRILPVVFDHHVEKDFGTGALKVTPSHDRNDYEIGIRHGLDLCKVIDEKGMMNDNAGKYAGLDRFECRKQIVEDLREQGYLVEIEDYDHAVGHCYRCKTVIEPTTSLQWFVSVKPLAAKAVDAVRDGQINIYPKTWYNTFYSWMDNIRDWCISRQIWWGHRIPAWSCADCGELIVETEDPTSCPKCGSSKLSQETDVLDTWFSSALWPFSTMGWPENTKELQTFYPTSVLITSFDILFFWVARMMMMGLHLMDEVPFKDVYLHALVRDKHGKKMSKSTGNVIDPLEIMAQYGTDSMRFTLTAFAAQGREIKLDEDRIEGYRHFINKIWNAARFAQMHIGDCDDSIRVAVETPKDLALGHRWILSRTAKLVEGIHRSLRGYLFNEVASLNYQFIWKEFCDWYLEWIKSDLFSDDLVARDQARGCLMVVLETILKTLHPITPFVTEEIWSVLPGERGFLATSAFPEVREEWKDEEAEAEMELLMGIITGIRNIRSEAEVHPSTKINATVICHDSKRADIIRSYTSGISDMTRLEGFTVVAEAEKPADAATYIYNDIEIFVPLAGLVDIEAELEKLSRERKKVEAKLKQINGKLGNAKFLAGAPEAVVAKVTGEKEELDAKLAKIDEASDRLKKLS | 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 + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Sequence Mass (Da): 101010
Sequence Length: 887
Domain: ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Subcellular Location: Cytoplasm
EC: 6.1.1.9
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Q72E47 | MAENALPKGYEPRDVEERWRRHWEDNRTFTPDMDAPGEPYSIVIPPPNVTGALHIGHALNHVLIDVLCRNARQQGKKVLWLPGTDHAGIATQNVVERALAKEGLSRHDLGREAFIERVWQWKEEYGNRILNQIRMLGDSVDWTRERFTMDEGLSKAVRKVFVDLYNGGYIYRGNYIINWCNRCHTALADDEVDHMPEQGHLYHVRYDFEDGSGSVVIATTRPETIMADTGVCVHPEDERYAGLIGKKILVPVIGRAVPLFADTYVDREFGTGALKVTPCHDPNDWTLGERHGLAFIQCIDEDGNMTAEAGPYAGLTKEECRKRIVADLEASGQLVRVEELNHSVGHCYRCKTVVEPHMSEQWFVASTKLAPRARAAVPQMTQIFPESWMKTYFNWLDNIRDWCISRQIWWGHRIPAWTCGKCGKLIVSEQDPTACPDCGCTDLTQDPDVLDTWFSSALWPFSTMGWPDKTKDLATFYPTSVLVTGFDILFFWVARMMMLGMHFMDEVPFKHVYLHALVRDGEGRKMSKSTGNVIDPLAMIDKYGTDSLRFTLAAFAAMGRDIKLSEDRIEGYRHFVNKVWNAARFSLMNLPEEAPAALDLDNVKGMHHKWILHRLEELKASQAAGIDGYRFNEVAQGLYRFWWNEFCDWYLELIKPDMQAGGERQATAQYVLWTVLREALLLLHPFMPFVTAEVWQALPGHAGDDIATKLYPAARPGCRDVKDAEHMELVQATISAVRTIRAELNIAPSYRLTTLVRPASAEDAATLEEGREMLMTLARLDGLTVAVDVEAPKASASSVVAGNEVIVPLTGAVDFEAELARLDKELGKIEKDFVQVNKKLANESFVSKAPADVVAKERARAEELSDAKAKLEALQQRFRDAIGK | 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 + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Sequence Mass (Da): 99823
Sequence Length: 884
Domain: ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Subcellular Location: Cytoplasm
EC: 6.1.1.9
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P07118 | MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESQESFCIMIPPPNVTGSLHMGHAFQQTIMDTMIRYQRMQGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTRHDYGREAFIDKIWEWKAESGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLRTAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETLLGDTGVAVNPEDPRYKDLIGKYVILPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHALPMINILTFDGDIRESAQVFDTKGNESDVYSSEIPAEFQKLERFAARKAVVAAVDALGLLEEIKPHDLTVPYGDRGGVVIEPMLTDQWYVRADVLAKPAVEAVENGDIQFVPKQYENMYFSWMRDIQDWCISRQLWWGHRIPAWYDEAGNVYVGRNEDEVRKENNLGADVVLRQDEDVLDTWFSSALWTFSTLGWPENTDALRQFHPTSVMVSGFDIIFFWIARMIMMTMHFIKDENGKPQVPFHTVYMTGLIRDDEGQKMSKSKGNVIDPLDMVDGISLPELLEKRTGNMMQPQLADKIRKRTEKQFPNGIEPHGTDALRFTLAALASTGRDINWDMKRLEGYRNFCNKLWNASRFVLMNTEGQDCGFNGGEMTLSLADRWILAEFNQTIKAYREALDSFRFDIAAGILYEFTWNQFCDWYLELTKPVMNGGTEAELRGTRHTLVTVLEGLLRLAHPIIPFITETIWQRVKVLCGITADTIMLQPFPQYDASQVDEAALADTEWLKQAIVAVRNIRAEMNIAPGKPLELLLRGCSADAERRVNENRGFLQTLARLESITVLPADDKGPVSVTKIIDGAELLIPMAGLINKEDELARLAKEVAKIEGEISRIENKLANEGFVARAPEAVIAKEREKLEGYAEAKAKLIEQQAVIAAL | 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 + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Sequence Mass (Da): 108192
Sequence Length: 951
Domain: ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Subcellular Location: Cytoplasm
EC: 6.1.1.9
|
Q5HC99 | MQSLFSNKYKFKDTEEKLNAYWDKIKLYKWKNLQGKQFIIDTPPPTISGQLHIGHVFSYCHTDFIARYQRMLGKDVLYPIGFDDNGLPTERLVEKIKKVRAADIDRKEFKALCNEVSAKFRMEFKILFQSLGISYDWDLEYHTISEEIQKLSQMSFIALYNMGKIYRKLQPIFWDCADRTAIARVEVEEKEMSSFMSTIAFSTEAGELINIATTRPELMPACVALFFNPLDIRYQHLQGQYAIVPIFGNKVPILSDEQVKIDKGTGLVMCCTFGDELDVYWWNKHNLNTQIIISKSGTLDLKHNIAETDTLSGKLHGVSIVEARKLVLETLSKCNLLIKKEEILHNVKCAERSGMPIEILLSNQWFIKVVEIKHELLEQVRKINWYPQSMRKQIEMWIDGLNWDWCISRQRYFGIPFPVWYSKRDNEEIIIPDVNELPIDPTETLPQGYSKEEVEADVDVMDTWATSSLSPQFNSIHTGINSIPLIPASLRAQSHEIIRSWAFYTILQAYYHHNSIPWENIMVSGWCLAADKSKMSKSKGNALIPNQLLQEYGADVIRYWAANSRLGSDTVFSDEVLQLGKRLVTKLWNASKFVSMFVSQCQIPDLNCVTETMDKWVLTKLYKVIVKATESFNVFEYCVALDYIESFFWKDFCDNYLELVKKRAYGESVTNKENLSAVNTLSFVLMALLKMLAPFMPYITEEIYSTLYNNGSIHDHDNWPVVNTSLCNEMDEQLGEDFIEILNQVRKIKANAQLSVKCKIYKLIINSENYDFPTSWENDLKAVCNAEHIVQDKRTSYYNDKFLISVQFAN | 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 + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Sequence Mass (Da): 93855
Sequence Length: 810
Domain: ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Subcellular Location: Cytoplasm
EC: 6.1.1.9
|
A7HJX5 | MEIGTRYDPKNIEMKWYKHWLEKKYFTPRGAGPKYSIVIPPPNITGKIHMGHALNITIQDILSRYKRMKGFDVLWLPGEDHAGIATQTAVERYLSTQGKSRRDFSRDEFLNIVWNWANKYRQEIKNQIMSIGASVDWTRERFTLDEGLSKAVRKVFVDMYKKGLIYKGKYIVNWCHRCGTVLSDEEVDYHEEEGALYHIKYPIKGEDDYIIIATTRPETMLGDTAVAVHPSDERYRKYVGKIAILPLVGREIPVIADNYVDPSFGTGALKVTPAHDTNDYLIGQRHNLPFVDIFDENIVINENGGKFKGMTAEQARKAVVEELEAQGYLVKIEKMKHSVGRCYRCDTVVEPRLMDQWFVSMKPLAKRAIEAVENGEVTFIPDRWKKVYLNWMYEIRDWCISRQLWWGHRIPVWQCQDCGHYNVSENEPVKCEKCGSTNLKQDEDVLDTWFSSALWPFSTMGWPEKTPDLERYYPTDVLVTGFDIIFFWVARMIMMGYEFMDEKPFKEVYIHQLVRDKYGRKMSKSLGNGIDPLEVIDEYGADPMRFTLAILAAQGRDLKLDVRFFDTYKKFANKIWNATRFVLMNLEDFEKVDIKLSKLKLSDKWILSRLQKTIQKISEALDSYDFNIAANEIYNFFWDELCDWYIEAVKNRLKTEERKVVQNVLVYVLDMSLRLLHPFMPFLTEELWTKLPTSGESIVVAQWPEIEENFIDENSEKRFMQLMNIIRGIRNIRAEVNVPQSTKVKTFVKGTLTDEEQEYIKFLGNVESIEFVEKRPELSATAYISLENEVYVSLGTLIDVKSEVERLRKKVEKLKSDMEKFAKKLEDENFLKNAPEDIVEETKEKQRLFQEQIARIEQIISDLEAKA | 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 + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Sequence Mass (Da): 101498
Sequence Length: 867
Domain: ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Subcellular Location: Cytoplasm
EC: 6.1.1.9
|
Q5NHZ4 | MTQEINKNYNPKEIEQANYQNWEASGKFACGNTDSKDTYTIMLPPPNVTGTLHMGHGFQMSLMDILIRYNRMSGKDTLWQPGTDHAGIATQMVVERQLNAQGISRHDLGRENFVSKVWEWKELSGGTITSQMRRIGASPDWDRERFTMDKGLSDAVKKCFIKLYEDGLAYRGERLVNWDPKLKTAVSDLEVAQVDKQGSLWHFIYPVADSDEKIIIATTRPETMLGDMAVAVHPEDERYTHLVGKMINLPLTDRQIPIIADDYVEKDFGTGCVKITPAHDFNDYEMGKRHNLPMLNILTDDATLNTNVPSKYQGLDRFEARKQVVADMEALGLLDKIEPHALKVPTGDRTGEILEPYLTKQWFVKADVLAKPAIEAVEKGDVRFVPDNWKNTYFAWMRDIQDWCVSRQLWWGHRIPAWYDEAGNAYVGEDEADVRAKYNLADDIAIKQDEDVFDTWFSSALWPFSTLGWPEQTPELAKYYPTSVLVTGFDIIFFWVARMMMFGMYFMNDVPFRDIYITGLIRDSEGQKMSKSKGNVLDPVDLIDGISLDELLKKRTTGLMQPQMKAKIEKATKKEFPEGISAYGADAVRFTYAALASTSRDISFDTARVEGYRNFCNKLWNASRFVMMNLDDYKVCDNYELGVADKWIWSVLNTATADVHRHLANYRFDLVTNTIYDLVWNNYCDWYVEFAKVALKDDSLSEQQKNGVKYTLTKVLENILALAHPLIPFITESIYQQLKAHLNDAKDTIMDVSYPVATQALEAPEAEKAIVWLQNVVTTLRNMRSEVGIKPSLEISLIVKDVADKDREYLAQTEGFIKALARINNIEFNDNPPTSLSQIVEGLELNIPLAGLVDIEAEKARLDKELDKLKDEVDRVQKKLSNERFVSNAPEAVVAAEQEKLAKYQELYAKTLEKKEALG | 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 + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Sequence Mass (Da): 104790
Sequence Length: 919
Domain: ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Subcellular Location: Cytoplasm
EC: 6.1.1.9
|
Q8RHK3 | MNELDKNYSPNEIEEKWYKIWEDSKYFAASLSSEKENYSIVIPPPNVTGILHMGHVLNNSIQDTLIRYNRMTGKNTLWMPGCDHAGIATQNKVERKLAEDGLKKEDIGREKFLEMTWDWKEKYGGIITKQLRKLGASLDWDRERFTMDEGLSYAVRKIFNDLYHDGLIYQGEYMVNWCPSCGTALADDEVDHEEKDGHLWQIKYPVKDSDEYIIIATSRPETMLADVAVAVHPEDERYKHLIGKTLILPLVNREIPVIADEYVDKEFGTGALKITPAHDPNDYNLGKKYNLPIINMLTPDGKIVEDYPKYAGLDRFEARKKIVEDLKAQDLFIKTEHLHHAVGQCYRCQTVIEPRVSPQWFVKMKPLAEKALEVVRNGEVKILPKRMEKIYYNWLENIRDWCISRQIWWGHRIPAWYGPDRHVFVAMDEAEAKEQAKKHYGHDVELSQEEDVLDTWFSSALWPFSTMGWPEKTKELDLFYPTNTLVTGADIIFFWVARMIMFGMYELKKIPFKNVFFHGIVRDEIGRKMSKSLGNSPDPLDLIKEYGVDAIRFSMIYNTSQGQDVHFSTDLLGMGRNFANKIWNATRFVIMNLKGFDVKSVDKTKLDYELVDKWIISRLNETAKDVKDCLEKFELDNAAKAVYEFLRGDFCDWYVEIAKIRLYNDDEDKKISKLTAQYMLWTILEQGLRLLHPFMPFITEEIWQKIKVDGDTIMLQQYPVADDSLIDVKIEKSFEYIKEVVSSLRNIRAEKGISPAKPAKVVVSTSNSEELETLEKNELFIKKLANLEELTCGTDLEAPSQSSLRVAGNSSVYMILTGLLNNEAEIKKINEQLAKLEKELEPVNRKLSDEKFTSKAPQHIIDRELRIQKEYQDKIKKLKESLKSFEE | 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 + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Sequence Mass (Da): 103049
Sequence Length: 887
Domain: ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Subcellular Location: Cytoplasm
EC: 6.1.1.9
|
P11931 | MAQHEVSMPPKYDHRAVEAGRYEWWLKGKFFEATGDPNKRPFTIVIPPPNVTGKLHLGHAWDTTLQDIITRMKRMQGYDVLWLPGMDHAGIATQAKVEEKLRQQGLSRYDLGREKFLEETWKWKEEYAGHIRSQWAKLGLGLDYTRERFTLDEGLSKAVREVFVSLYRKGLIYRGEYIINWDPVTKTALSDIEVVYKEVKGALYHMRYPLADGSGFIEVATTRPETMLGDTAVAVHPDDERYKHLIGKMVKLPIVGREIPIIADEYVDMEFGSGAVKITPAHDPNDFEIGNRHNLPRILVMNEDGTMNENAMQYQGLDRFECRKQIVRDLQEQGVLFKIEEHVHSVGHSERSGAVIEPYLSTQWFVKMKPLAEAAIKLQQTDGKVQFVPERFEKTYLHWLENIRHWCISRQLWWGHRIPAWYHKETGEIYVDHEPPKDIENWEQDPDVLDTWFSSALWPFSTMGWPDTDSPDYKRYYPTDVLVTGYDIIFFWVSRMIFQGLEFTGKRPFKDVLIHGLVRDAQGRKMSKSLGNGVDPMDVIDQYGADALRYFLATGSSPGQDLRFSTEKVEATWNFANKIWNASRFALMNMGGMTYEELDLSGEKTVADHWILTRLNETIETVTKLAEKYEFGERGRTLYNFIWDDLCDWYIEMAKLPLYGDDEAAKKTTRSVLAYVLDNTMRLLHPFMPFITEEIWQNLPHEGESITVAPWPQVRPELSNEEAAEEMRMLVDIIRAVRNVRAEVNTPPSKPIALYIKTKDEHVRAALLKNRAYLERFCNPSELLIDTNVPAPDKAMTAVVTGAELIMPLEGLINIEEEIKRLEKELDKWNKEVERVEKKLANEGFLAKAPAHVVEEERRKRQDYIEKREAVKARLAELKR | 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 + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Sequence Mass (Da): 102048
Sequence Length: 880
Domain: ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Subcellular Location: Cytoplasm
EC: 6.1.1.9
|
Q74BJ6 | MAEKELAKVYEPTAVERKWYETWEQEGYFRANPDSGKPSYSIVIPPPNVTGALHMGHALNNTLQDILCRWKRMNGYEVLWMPGTDHAGIATQNVVERQLAGEGTSRHELGREAFIERVWKWKAESGGQIIGQLKRLGASCDWGRERFTMDEGLSRAVREVFVRLYEEGLIYRDNRLINWCPRCHTALSDIEVEHEDKAGNLWHIRYPVVGEPGRFVVVATTRPETMLGDTAVAVHPEDERYADLVGKKVLLPLVNREIPVVADGYVDREFGTGVVKITPAHDFNDFEVGRRHNLDLLNVFDESAVVNSAGHQYEGMERFAARKRVVEDLEALGLLEKIDDHAHAVGGCYRCKTVVEPYLSLQWYVKVGPLAERALAAVKDGRTRIVPQQWENTYYDWMENIKDWCISRQIWWGHRIPAWYCDHCGETTVAKIDPTVCAACGSDEIRQETDVLDTWFSSALWPFSTMGWPDRTPELAAFYPTSCLVTGFDILFFWVARMMMMGLHFMNEVPFSDVYIHALVRDAQGQKMSKSKGNVIDPLVVIDQYGTDAFRFTLAAFAAQGRDIKLAEERIAGYRNFVNKIWNASRFALMNLEGFEPDTVDPATLDLSNADRWILHRLNSAAAETAEALEAYRFNDAAGTLYRFTWSEFCDWYIELAKDDLYRGDDARKETARYVLWLVLENLLRLLHPFMPFITEEIWQTLPGARPAPSIMVAGYPRSVPERDFPDGAAEMELVMEVIRGIRNIRGEMDVAPSREIAAILSCGSAESLHLLKRNEVYVMSLARLSDLAIGQQLERPADAAIQVAGDVEIAVPLKGLVNVEEEEKRLLKEIGKLDKEIEMFGRKLENPSFVERAPADVVAKEREKLAEVTQKKDVLLASLEKIRKLA | 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 + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Sequence Mass (Da): 100798
Sequence Length: 887
Domain: ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Subcellular Location: Cytoplasm
EC: 6.1.1.9
|
Q9PH12 | MSQFTSSYDPTSFEARLYAAWEAAGHFKPSGTGQPYTILLPPPNVTGTLHMGHAFQQTLMDALVRYHRMCGDDTLWQVGTDHAGIATEMVVSRNVVLEGHGETRDSLGRDGFINKVWEWKQQSGDTIERQMRRLGVSADWSRSTFTMDPQPSAAVTEAFVRWYEAGLIYRGQRLVNWDPVLKTAISDLEVENVAEEGMLWSIRYPLSDGVTYEHVEHDAAGNEILRETRDSLIVATTRPETLLGDTAVMVHPEDRRYTALIGKTVTLPLTGRHIPVIGDAYVDPTFGTGVVKVTPAHDFNDYQIGLRHRLPMIQVLDDAACIVSKTSIQSGMPSGATSDTTNTPSDPEASSAANQHDTLVMPAHLAGLDRYAARKQILADLDAQGLLVAAIPHTLQVPRGDRTGQVIEPYLTAQWFVKMETLAARGLALVERGAVTFVPPNWINTYRHWMENIQDWCISRQLWWGHRIPAWFDTQGGVYVGRSEAEVRAKHALGPEVTLTQDNDVLETWFSSQLWPFSTLGWPDPTAMAEHGYARYLPSSVLVTGFDIIFFWVARMIMATDHFTGNVPFHDVYITGLIRDAQGQKMSKSKGNVLDPLDIIDGITLDDLVAKRTTGLMQPKLAEKIAKATRKEFPEGIAPHGADALRFTIAALATHGRDIKFDLGRAEGYKNFCNKLWNATRFVLMNTADDTAHSPAQHQAGQDGQDAPRTPQPRTDAEQWILSRLTAITAEAHAQFAAYRFDLLAQALYEFAWNEFCDWFVELAKPALNSDDTQAAASTRHTLLYVLETLLRLLHPLIPFITEELWRQVAPRLGIQATTLMLRPYPQPQQLETAAFANAAADVEWLKIMVSALRRIRSTLNVPPSRRVSLLLQGDQEVDRRRITHFATALHFLLKLEHIDWLGADSAAPPSATAIVGTLKLLVPLEGLIDVDAERVRLDKEIKRVESEIDKSNGKLSNAVFVQNAPAAVVEQERSRLTEWTTQLNGLRERRATL | 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 + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Sequence Mass (Da): 110954
Sequence Length: 994
Domain: ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Subcellular Location: Cytoplasm
EC: 6.1.1.9
|
Q9HN83 | MTSDDTDDTAGADDVALDPWGSATISDYRALFDEFGIEAFEDVLDGVPTPHSLMRRAIIFGHRDYRRVAAAMRNDEPFAALSGFMPTGDPHIGHKMVFDELIWHQQQGGDAYALIADLEAHSARGLDWAEIDEHAEDYLLSLLALGFDADEGELYRQSTNRELQDLAFELGIEANTSEFEAIYGFGGDTDVSHMQSVVTQMADILYPQLDAPKPTVIPVGPDQDPHVRFARDLAERTRYFKVTEAFASVAFDDDERPLVRAAYDARSQYAADTDQPRCTEAADWLAAEPAAADGVDAATAESVVQKLENAGMEPLRPRVRFFDRQATDEAFTALIDEIAGEKRVFEGHVDAFELSAETARDLALAVEVDHGGYGFVPPSSVYHRFMTGLTGGKMSSSEPASHISLLDDPETGADKVAAATTGGRDTAAEQRERGGEPDDCPVYELYAYLLAGDDDALAEEVYAECANGDRLCGGCKEQAADLMAQFLETHQENREAARDVLAELDIDLDSARV | 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
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Q82E91 | MKRIFSGVKPTGHLTLGNYLGAVRRWVDVDQHGADALFCVVDLHALTVDHDPARVRRLSRQAATLMLAAGLDPELCTVFVQSHVDEHARLSYLMECVATDGEMRRMIQYREKAAREQQRGGSVRLSLLTYPVLMAADILAYGTDEVPVGDDQTQHVELTRDLAVRFNQRYGHTFVVPRATRPEVAARVMNLQEPTSKMGKSDDVGPGIVYLLDEPEAVRKKVMRAVTDSGRDVVYDRESRPGVSNLLEILAACEGGSPEALSGAYASYGALKKDTAEAVVELLRPLQERHKALCAEPGYVEGVLRDGARRARELARPRVDAAYRAIGLLEA | 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 | MTRVFSGVKPTGHLTLGNYLGAMRRWAAVDQHRSDALFCVVDLHALTVDHDPARVRRLSRQAASLLLAAGLDPELCTVFVQSHVDEHARLSYVLECVATDGEMRRMIQYKEKAARERVRGGSVRLSLLTYPVLMAADILAYGTDEVPVGEDQTQHVELARDLAVRFNQRYGHTFVVPRATSPAVAARVMNLQEPASKMGKSDDTGPGIVYLLDEPDVVRKKVMRAVTDSGRDVVYDPEERAGLANLLEILAACTDGEPAELAGGYDSYGALKKDTAEAVVEMLRPVRERHMELSADPGYVDGVLREGAEKARAMARPTVDDAYRAIGLLPPVNAAR | 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
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Q9RVD6 | MPFVDLEVPTMTTPTPAATPARPRVLTGDRPTGALHLGHLAGSLQNRVRLQDEAELFVLLADVQALTDHFDRPEQVRENVLAVALDYLAAGLDPQKTTCVVQSAVPELAELTVYFLNLVTVSHLRQNPTVKAEIAQKGYGERVPAGFFVYPVSQAADIAAFGATLVPVGDDQLPMLEQTREIVRRFNALYAPVLAEPQAQLSRVPRLPGLDGQAKMSKSLGNAIALGDSADEVARKVMGMYTDPGHLRASDPGRVEGNPVFTFLDAFDPDPARVQALKDQYRAGGLGDVKVKKHLIDVLNGVLAPIRTRRAEYERDPDAVLRFVTEGTARGREVAAQTLGQVRRAMRLFGH | 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 regioselective nitration of tryptophan at the 4-position.
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 38180
Sequence Length: 351
EC: 6.1.1.2
|
Q9HN66 | MTADGNDVTPYAVESDDLDYEKLLARFGADELTDDQRARFPDHPLVNRGLFYAGRDVDDFLTAGEQSIVTGVGPSGPMHLGHAMVFYFARRLQDEFGARVYVPLSDDEKYWFKDQTPAETGDYLRANLRDLLAVGFDPELTRIVVDTRDADVLYPLATAFAGDVRHATLQNVYGEPDNVGQAFYPAVQTAHLLLPQLVHGEHETLVPIAVDQDPHVRVSRDVAAKARYPVGKPGALLMQFLPSLAGPGKMSSSAGVSIRLTDSPDTVREKVRTHAYTGGRASVEEHRAKGGVPAEDVPFQYLSAFFEPDDAELARIEREYRAGDLLSGELKDLAADRITEFLAAHQRRRAALGDVTEALDAFRLTDDERQRARDAVGFGY | 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 | MSMANERPRVLSGIQPTSGSFHLGNYLGAVRQWVDMQDTHDAFYMVVDLHAITVPQDPKELRENTRVAAAQLLAAGLDPDRCTLFVQSHVPEHAQLGWLMNCITGFGEASRMTQFKDKSAKQGNDRTTVGLFTYPMLMVADILLYQADQVPVGEDQRQHLELTRDLADRFNQTYGDAFTVPTAYILKETAKIYDLQDPTAKMSKSAATPKGLINLLDEPKATAKKVKSAVTDTDTVVRFDRETKPGVSNLLTIYSTLTGAEIAELERKYEGKGYGALKTDLADVVVEFVTPFRERTRQYLDDPETLDAILAKGAEKARSVAAETLARAYDEVGFLPAKH | 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 | MEVDKKDEREAESSEQVVNPWEVSAKDGGKIDYDKLIDKFGCQRLDESLIDRVQRLTSRQPHVFLRRSVFFAHRDFNEILDAYERGDKFYLYTGRGPSSEALHLGHLIPFMFTKYLQEAFKVPLVIQLTDDEKSIWKNLSVEESQRLARENAKDIIACGFDVTKTFIFSDFDYVGGAFYKNMVKVGKCVTLNKAMGIFGFSGEDPIAKLSFPPVQAVPSFPSSFPHLFPGKDNLRCLIPCAIDQDPYFRMTRDVAPRLGYSKPALIESTFFPALQGENGKMSASDPNSAIYVTDSAKDIKNKINRYAFSGGQDSIEKHRELGANLEVDIPVKYLSFFLEDDSELEHIKKEYGEGRMLTGEVKKRLTEVLTEIVERHRRARAAVTDEMVDAFMAVRPLPSMFE | 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
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Q55DZ8 | MTETTPTTNETKEQVITPWEVEAAPGGSVDYMKLVDQFGSTVISEELIARFEKVTGKRAHHFLRRGIFFSHRDLKEILDHHESGKKWFLYTGRGPSSGSLHFGHLLPFTFTKYLQDAFNVPLVVQMTNDEKFLWKDMTLEESIKFTHNNVKDIIALGFDIQKTFIFSNLEYIHHLYPNVLKIARCVNLNQIQNIFGFKESDAIGKFTFPPVQAAPCFPDSFPHIFPLNDPEIKNIRCLIPCAIDQDPYFRMTRDIAHRIGHQKPALIHSKFFPALQGHNTKMSASDTNSAVYLSDTPDQVKDKIKKHAFSGGGATKEEQEKNGADLSVDITYEYLTFMLEDDEQLKDIAHRYSTGKMMTGEIKQILIDLMNKIIIRHKEARAKITDEVLSTFMSIRKLNF | 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
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P23381 | MPNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGMSSGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDRTDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKLSFDFQ | 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 are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression.
PTM: Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-TrpRS.
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 53165
Sequence Length: 471
Subcellular Location: Cytoplasm
EC: 6.1.1.2
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P32921 | MADMPSGESCTSPLELFNSIATQGELVRSLKAGNAPKDEIDSAVKMLLSLKMSYKAAMGEEYKAGCPPGNPTAGRNCDSDATKASEDFVDPWTVRTSSAKGIDYDKLIVQFGSSKIDKELINRIERATGQRPHRFLRRGIFFSHRDMNQILDAYENKKPFYLYTGRGPSSEAMHLGHLVPFIFTKWLQDVFNVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDINKTFIFSDLEYMGQSPGFYRNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAAPSFSNSFPKIFRDRTDIQCLIPCAIDQDPYFRMTRDVAPRIGHPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGRDTVEEHRQFGGNCEVDVSFMYLTFFLEDDDRLEQIRKDYTSGAMLTGELKKTLIDVLQPLIAEHQARRKAVTEETVKEFMTPRQLSFHFQCFCFDT | 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 and shear stress-responsive gene expression (By similarity).
PTM: Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-TrpRS.
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 54358
Sequence Length: 481
Subcellular Location: Cytoplasm
EC: 6.1.1.2
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Q5ZJ08 | METASGPQEKYQLITRNLQEVLGEDKLMAILKEREVKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRTRYYEHVIKAMLESIGVPLEKLKFIRGTDYQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPSLGYAKRIHLMNPMVPGLTGSKMSSSEEDSKIDLLDRKEDVKKKLKKAFCEPGNIENNGVLSFIKHVLFPLKSEFVILREEKWGGNKTYTAYETLEKDFAEQVVHPGDLKNSVEAALNKLLDPIREKFNSPELKKLTNAAYPNPSKAKPAEKGTKNSEPETIVPSRLDIRVGKVVSVEKHPDADSLYVEKIDVGEPEPRTVVSGLVQFVPKEQLQDRLVVLLCNLKPQKMRGVESQGMVLCASSVGEPRQVEPLDPPAECCAGERVYVEGYEDGEPDDELKPKKKVFEKLQADFRISEDCIAQWKERNFLTKLGSISCKSLKGGSIS | 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
Sequence Length: 527
Domain: The nuclear localization signal, which mediates localization to the nucleus, is also important for interacting with tRNA(Tyr), suggesting that it is sterically blocked when tRNA(Tyr) is bound.
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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Q8SRV7 | MSVEQKLYLITRNLQEILGEEELKRIVSERELNVYWGTAITGKPHIAYLVPLMKIKDFVDAGCNVKILFADIHGFLDNLKAPIEKVQHRCAYYEKLIKSALKMLCVDLDRIQFVKGSEFQKSERYTMDLYRILSITSKHDAKKAGAEVVRQVENPMVSSLVYPSMQALDEVHLSVDAQFGGVDQRKIFTYARKYLPLLNYEKRIHLMSPMLPGLNSDKMSSSDDLSKIDLMDSKEAIWRKIRKCFCEEGNKDNGLMMIFSHIVFPILQLKGECVRITDRDGREMAFEKYQEFEEEFVRKSIHPGDLKSNAARLIDEIIRPIREEMEKDLDMVREAYN | 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
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B7XHC1 | MDETSIINENTDVFEKKITLIERNLQEITINDKEIIRKIIRKRNLKIYWGTAITGKPHIGYFLPILKIKDFVEAECEVTILFADIHGFLDNLKAPIELIENRYHYYEKIIKIMLMSVGCDINKIRFVKGSDYQKNSDYVFDLYKLCSYTTERDCKRAGSDVVKQRDNVLLSSLIYPNMQALDEEYLKVDAQFGGEDQRKIFMHAKTFLPKLGYKKRIHLMNPMMPGLNSDKMSSSDELSKIDLLDTEQQINKKINKCFCEEGNLQSGVLHVFEFVIFHYYTSISINKKSYTSIEDVKKDFEMKLIHPKDLKLACSNYINKMVTPIRNEMLKDIDMIKKAYNN | 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
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P54577 | MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDEELKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS | 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 its tyrosine--tRNA ligase activity . Activity is switched upon resveratrol-binding: resveratrol strongly inhibits the tyrosine--tRNA ligase activity and promotes relocalization to the nucleus, where YARS1 specifically stimulates the poly-ADP-ribosyltransferase activity of PARP1 .
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 59143
Sequence Length: 528
Domain: The nuclear localization signal, which mediates localization to the nucleus, is also important for interacting with tRNA(Tyr), suggesting that it is sterically blocked when tRNA(Tyr) is bound.
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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C4V6W1 | MDTTEKLKLINRNLKEVIGGDIMEKIINKRDLNVYWGTATTGKPHIAYFLPILKIKDFVDAGCNVTILLADIHAFLDNLKAPIEKIECRSQYYKKIITLMLKSIKVDVSKISFIFGSEYQKSNKYFTDILRILNQTKKNDARRAGSEVVKQVKNSKLSSLVYPAMQALDEEYLNVDVQFGGIDQRKIFMYAREFLPLLKYKKRIHLMNPMIPGLNSDKMSSSDIDSKIDLLDTKLEIYKKIHNCSLENEGLIFLFKSIIYPYCSIFNLQIMISGKVYTFDKLYEDIKMKIIDETELKNIASDMIERLICPIRDEMLRDLKLIENAYGNK | 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
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Q6DIJ1 | MGDGLTPEGKAQLITRNLQEVLGEDKMKEILKERPLRIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWDLLELRTRYYEQVIQAMLQSIGVPLERLRFIRGTEFQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYAKRIHLMNPMVPGLTGAKMSSSEEESKIDLLDSPADVKKKLKKAFCEPGNIENNGVLSFVRHVLFPLKSEFVVLRDEKFGGNKTYTDFETLEKDFTEQLVHPGDLKASVEKALNKLLDPIREKFNSPEMKKLSNDAYPGASKQKTVPKGSTKNSGPEEIDPSLLDLRVGKILSVRQHPDADSLYVESVDVGEENPRCVVSGLVQYVPSDQLLGRSVVLLCNLKPQKMRGIESQGMLLCASTEGEQKQVEPLDPPTGSAPGERIYIEGYENGEPEGELKPKKKVFEKLQVDFRISDDLCAQWKGKNFLTKLGSVTCKTLRGGSIS | 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
Sequence Length: 528
Domain: The nuclear localization signal, which mediates localization to the nucleus, is also important for interacting with tRNA(Tyr), suggesting that it is sterically blocked when tRNA(Tyr) is bound.
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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P36421 | MSSAATVDPNEAFGLITKNLQEVLNPQIIKDVLEVQKRHLKLYWGTAPTGRPHCGYFVPMTKLADFLKAGCEVTVLLADLHAFLDNMKAPLEVVNYRAKYYELTIKAILRSINVPIEKLKFVVGSSYQLTPDYTMDIFRLSNIVSQNDAKRAGADVVKQVANPLLSGLIYPLMQALDEQFLDVDCQFGGVDQRKIFVLAEENLPSLGYKKRAHLMNPMVPGLAQGGKMSASDPNSKIDLLEEPKQVKKKINSAFCSPGNVEENGLLSFVQYVIAPIQELKFGTNHFEFFIDRPEKFGGPITYKSFEEMKLAFKEEKLSPPDLKIGVADAINELLEPIRQEFANNKEFQEASEKGYPVATPQKSKKAKKPKNKGTKYPGATKTNEIATKLEETKL | 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 bases G34, U35 and A36 . Also involved in nuclear tRNA export . Also attaches D-Tyr to tRNA(Tyr), this reaction is about 150-fold less efficient than attachment of L-Tyr .
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 44020
Sequence Length: 394
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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Q9M876 | MAYATGITFASRSILPICSRTFLSPLRVASLLVFPEKSSATFFRRVQVPHLFSTSTTTLFSSVKCSIHSTSSPETENQAVFRPNVVDILEERGLLESITSENLRSACSDPKVAPLRVYCGFDPTAESLHLGNLLGIIVLSWFQRCGHQAVGLIGGATGRVGDPSGKSLERPELDADTLEKNIAGITKIIIKILGSNPSPGGSYVIFNNYDWWKDMTMLDFLNKVGRFARVGTMMAKESVKKRLESEQGMSYTEFTYQLLQAYDFLHLFKNEGINVQIGGSDQWGNITAGTDLIRKILQAEEAAYGLTFPLLLKNDGTKFGKSEDGAIWLSPSMLSPYKFYQYFFSVPDVDVIRFLKTLTFLSLDEIKILEDQMSKPGYVPNTAQIKLAEEVTRFVHGEEGLKEAIKATEALRPGAETKLDWNLIERIAEDIPSCSLPIDRVSGLSIVDLSVSAGLFESKSAARRMLKQGGFYMNNERVDDENKRVDEEDIVEGRGLVLSAGKKNKVVVRIS | 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
Sequence Length: 511
Subcellular Location: Plastid
EC: 6.1.1.1
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Q54WD9 | MIRNFTKGLLINNLNINKFGSTKIRPFCSTITKNDKNNVINILKKRGFIHQMTASDIEMIKMTSTNNNNNNDNNNNNNNNKVSLYAGFDPTADSLHIGNLLTLMVMLHFKRHGHNPIALMGGATALIGDPSGKSSDRVMLTEEFIEGNLKHIRENITAVLGEDTLVVNNIEWNKTMDVISFLREVGSYFRVGSMIKKDFIQNRLSDSNENGISFTEFCYSLFQANDFAHLFLKHGCSIQIGGSDQWGNITAGCDLIRKKLKGNAQGITIPLLTNSAGKKLGKSEGNSIWLSPHRTSPYKFYQYWIQVSDEDVERLLKLFTLIPLEEISILVQKHNENPHLRLGQKTIAEHVTRLIHGQKGVEEALNTTELLFGESNKLLTPNASTTKIGDFDIGYLLSRVNFIELERSKFVDNQTEPILNLFAQISDASKSKVKQLLQSKSIYLNNIPVASNSQFIQSSDLIANDFIYLKSGKKIYYLIKFI | 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
Sequence Length: 482
Subcellular Location: Mitochondrion matrix
EC: 6.1.1.1
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Q9W107 | MLPLRRSLLKPLQDVLRHSHRQMSQKNLLELTDRGFFHGIFPDTAAPRMKQLFTRGQQSIYAGFDPTADSLHVGNLLVIMGLIHCQRAGHRPIALVGGATGLIGDPSGRKTERNQLGETVIETNLKAIEQQLRRVFENHENCLWDSKKQKLPLAPLIIVNNADWYADLQLIDFVANMGRHFRMGSMLSRSSVQSRLESEDGMSFTEFTYQIFQAYDWLHLLRRHNCCFQMGGSDQTGNLMTGHELISRVERKREVFGLTLPLVTTEEGDKFGKSAGNAVWLDGNKTSPFALYQFFLRMPDSEVEKLLKLFTFIPLPQVEQLMREHTKEPEKRKAQTLLAEDVTLLVHGESGLKQAERVTNALYKGNVEGLAELNLSEIQQTFQGATMVNLLTEPGMSILELAMKAKCFPTETDAVRIINAGGFYVNQKRVQNIAEVLTTGVHILRNGISLLRVGKRNFYIVRWQ | 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
Sequence Length: 464
Subcellular Location: Mitochondrion matrix
EC: 6.1.1.1
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Q9Y2Z4 | MAAPILRSFSWGRWSGTLNLSVLLPLGLRKAHSGAQGLLAAQKARGLFKDFFPETGTKIELPELFDRGTASFPQTIYCGFDPTADSLHVGHLLALLGLFHLQRAGHNVIALVGGATARLGDPSGRTKEREALETERVRANARALRLGLEALAANHQQLFTDGRSWGSFTVLDNSAWYQKQHLVDFLAAVGGHFRMGTLLSRQSVQLRLKSPEGMSLAEFFYQVLQAYDFYYLFQRYGCRVQLGGSDQLGNIMSGYEFINKLTGEDVFGITVPLITSTTGAKLGKSAGNAVWLNRDKTSPFELYQFFVRQPDDSVERYLKLFTFLPLPEIDHIMQLHVKEPERRGPQKRLAAEVTKLVHGREGLDSAKRCTQALYHSSIDALEVMSDQELKELFKEAPFSEFFLDPGTSVLDTCRKANAIPDGPRGYRMITEGGVSINHQQVTNPESVLIVGQHILKNGLSLLKIGKRNFYIIKWLQL | 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
Sequence Length: 477
Subcellular Location: Mitochondrion matrix
EC: 6.1.1.1
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P12063 | MLLRTKALIRSGGSIAKYAAANPSCFILQRRGLRREFGPKYTAKINEAEENWQARAEAIKKGKKQNTWDLFEERGYVKDTAGTKEHIAELMRTRRIGAYVGIDPTAPSLHVGHLLPLMPLFWMYLEGYKAFTLIGGSTAKIGDPTGRLKSRDHLSSSDATMNMTKIHYQLKKLWENVDTQMRARGYEADWARKRGIVNNNHWWNKQPMLEVLRRVGHALRIGPMLSRDTVKNKMTQGDGVSFAEFTYPIMQGWDWFELFYQQGVQMQIGGSDQYGNIISGLEVVKAARESEPDPQERKYVTPKTALDECVGFTVPLLTDSSGAKFGKSAGNAIWLDPYQTSVFDFYGYFVRRSDQEVENLLKLFTFMPISEITKTMEEHIKDPSKRVAQHTLAREVVTLVHGKQEASAAEDQHRMMYTGQMTIPQVSRAKDAATGGDQYKTISDQPVTLNNAPRIDMILPESLIMGKSIGRILYAAGLASSTTEGHKLAAAQGCYVGGAHRAGGENVTMNPDLISFMPVKLWFPGETQRYLINGNLLILRKGKHNVRVIQMVSDVEYAASGQTYPGQSFTGAVRKLNEIMKNLKEKKLTPEEAKNAVNELQKSSQEKQQGQQIIFPEEKSRQKKDMETKLKQEMIASVKTIDGMMDEKPSVRGDGVKKQTQDDRDPYKW | 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 stabilizing the catalytically active structure of the intron.
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
Sequence Mass (Da): 75422
Sequence Length: 669
Subcellular Location: Mitochondrion matrix
EC: 6.1.1.1
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Q72RP6 | MDIQKQIEIIRRGTVDLISEEELKSKLQKKKTLKIKAGFDPTAPDLHLGHFVQLKKLKHFQDLGHEVSFLLGDFTAMIGDPTGKSETRKRLSREEVLENSKTYQNQVFKVLDPVKTKIVYNSNWCSKMNFEDVLVLSSKYNVARMLERDDFSKRYKAGQPISMIEFLYPLVQGYDSVAMECDVELGGTDQKFNLLVGRDLQREYGKEAQCVLTLPLLVGLDGSKKMSKSLGNYVGITETPIDMFGKLMSISDDLMWNYFELLTDLPLPEIENRKNGMAKKELHPKEIKTELAKLIMDQFSSPSENEEAIQEWKKIHNPKSRAVPDDVKEIKLGEEFFAETPEPLLVWVLSKLSFIPSVSEGRRLIKAGGLYLSEDKITDEKFPIQKGKEYLVRQGKKGKFLKIIS | 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
Sequence Length: 405
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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Q8EUX2 | MKNKNILEFLKKRGYIYQGSNFDLIEKELIKGTSFYIGFDPTADSLHVGHFLTMMAVKHLQKAGNNPVIVVGGGTGSVGDPSGRSEIRKILDRKTIDYNCECLKKQMSKFISFEGKNKAVMVNNADWLLKINWIEFLREFGVCFSVNKMLAAEAFKVRFEQESGLSFLEFNYMLMQAYDFYYLNQNYNVNIQLGGSDQWSNILAGVDLIRRKSSKEAFALTLNLLTKHDGTKMGKTATGAIWLDKNKTSPYEFYQYWLNIDDQDVERFLLLLTELDDKTISDLCKEKGKKIVEAKKVLASELTKMIHGQEELDKAIEQSKAAFENASDNLPTYELKASDLNNDYSIANILVVTKLSPSKAESRRLITSNAVSVNETKITDVNTKLEDLKIDQTNFTLHKGKKNHIKVIINK | 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
Sequence Length: 411
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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Q6F0M8 | MNIIKELEWRGLVKQITNEERLLKAQNDGAAVYCGFDPTADSLHVGHLMMIVTLKRFDKAGFQAIGLIGGGTGMIGDPSFKADERKLQTDEQVKFHATAIQNQLLRIIPDVTFANNVDWLGNMSLIDFLRDVGKDFNISYLLNKDSIATRISTGLSVTEFSYTMLQAYDFYNLYINHNCKVQIGGSDQWGNITSGTDYISTRVGSANTEAAGFTIPLLTKSDGQKFGKTESGAVWLDSNKTSVYDFYQFWINQDDNDCVKMLKYLTFLTKEEIDELEAKHKEAPHLRTMQKTLASEITKFVHGDKELNKAIKLTDAFFTGNILNLDDDLLELAIKSIPTIQLEKTTSAIDAIVNVNAASSKREAREFINAKAISFNDVAVQDENMLLSEIKTIKNNKIIVKKGKKKYYLLEIK | 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
Sequence Length: 413
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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B5ZAU9 | MHNLIKDLKARNLINNITNEEKLKKALAENKGIYVGFDPSADSLHLGNYIMIMLLKRFRLHNIKTFALVGGATGMIGDPSGKSAERNLLDKTILEHNITKIKYQLEKFTNSQVINNYDFYKNMTFLDFLRDVGKLININYLLEKEIISSRLDVGISYTEFSYNLLQGYDFLQLYKNDNIAIQAGGSDQWGNITTGIEIIRKSLGDDNIACGLTINLLTNSEGKKFGKSEKGAIYLDENKSSVYEMYQFLINQTDADVEKLLNFLTLIDVDEINKIMQAHKENPALRIAQKALAQAVVVDVHGQQKYEQALHISQVLFNGNINELNQEEFNIAIKSLPTTKLDKDEIKIIDLLNLANISSSNRVARDFLSTGSILVNDIKVNDENFLVKKQDAINQEFSIIKKGKRNYFLIVWNKD | 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
Sequence Length: 415
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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Q8D2L6 | MKDLIQELKNRKLISKLTDEINIKKILKEKKINLYCGFDPTADSLHIGHLIPLLFLKRFSNFGHIPIIVIGGATALLGDFNIKKNKSFLEKYKNVKNWSKTIENQILNIIKYENNNCNLIILNNYLWIKELKIINFLRDIGRFISINKILRKEIVKKKLKENQHISFMEFSYSLLQGYDYYFLNLNYDVYIQIGGSDQWSNIISGIDLVNKINKKKVYGITTPLLTRSNGSKLGKSDDKEKVIWLDKKKTSVYEFYQFWLNTPDEKIFRYLKLFTFISMSEINKLKCKFFNKEINPFQAQKILADEITKIVHGISQLRLAQKATNFLFYKKISELSIEDFYLLSTSGIKIYYPKSNENIKDILVNSKLSKSKNNAKSVILSSSIRINNKKQKSIDFMFKKEDKLFNLFTLIKKGKKDFCLLIWKNY | 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
Sequence Length: 426
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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Q3UFJ6 | MRNASGFLKTAGAPLVSATWLPPSPPPAMPTVAAGPQMERVDNGSQGAPQLFLTSALARGVSGVFVWTALLLTGHQIYSHLRSYTAPREQRFVIRLLFIVPIYAFDSWLSLLLLGGHPYYVYFDSVRDCYEAFVIYSFLTLCFQYLGGESAIMAEIRGKPIRSSCFYGTCCLRGMSYSITFLRFCKQATLQFCIVKPVMALITIILQAFDKYHDGDFNIHSGYLYVTLVYNASVSLALYALFLFYFATRDLLRPFEPVLKFLTIKAIIFLSFWQGMLLAILERCGVIPEVQAVDGTRVGAGTLAAGYQNFLICVEMLFASLALRYAFPSQVYSEKKNSPVPPAPMQSISSGLKETISPQDIVQDAIHNFSPAYQQYTQQSTHEAPGPGQGGHPAPSTHPGPASGSGGGKKSRNIEKRMLIPSEDL | 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 | MRNASGFLKTAGAPLVSATWLPPSPPPAMPMVAAGPQMERVDNGSQGAPQLFLTSALARGVSGVFVWTALLLTGHQIYSHLRSYTVPREQRFVIRLLFIVPIYAFDSWLSLLLLGGHPYYVYFDSVRDCYEAFVIYSFLTLCFQYLGGESAIMAEIRGKPIRSSCFYGTCCLRGMSYSITFLRFCKQATLQFCIVKPVMALITIILQAFDKYHDGDFNIHSGYLYVTLVYNASVSLALYALFLFYFATRDLLRPFEPVLKFLTIKAIIFLSFWQGMLLAILERCGVIPEVQAVDGTRVGAGTLAAGYQNFLICIEMLFASLALRYAFPSQVYSEKKNSPAPPAPMQSISSGLKETISPQDIVQDAIHNFSPAYQQYTQQSTHEAPGPGQGGHPSPSTHPGPASGSGGGKKSRNIEKRMLIPSEDL | 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 | MTVRGAALAPDPASPTTAAASPSISVIPEGSPTAMEQPVFLMTTAAQAISGFFVWTALLITCHQIYMHLRCYSCPNEQRYIVRILFIVPIYAFDSWLSLLFFTNDQYYVYFGTVRDCYEALVIYNFLSLCYEYLGGESSIMSEIRGKPIESSCMYGTCCLWGKTYSIGFLRFCKQATLQFCVVKPLMAVSTVVLQAFGKYRDGDFDVTSGYLYVTIIYNISVSLALYALFLFYFATRELLSPYSPVLKFFMVKSVIFLSFWQGMLLAILEKCGAIPKIHSARVSVGEGTVAAGYQDFIICVEMFFAALALRHAFTYKVYADKRVDAQGRCAPMKSISSSLKETMNPHDIVQDAIHNFSPAYQQYTQQSTLEPGPTWRGGAHGLSRSHSLSGARDNEKTLLLSSDDEF | 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 | MTVRGDVLAPDPASPTTAAASPSVSVIPEGSPTAMEQPVFLMTTAAQAISGFFVWTALLITCHQIYMHLRCYSCPNEQRYIVRILFIVPIYAFDSWLSLLFFTNDQYYVYFGTVRDCYEALVIYNFLSLCYEYLGGESSIMSEIRGKPIESSCMYGTCCLWGKTYSIGFLRFCKQATLQFCVVKPLMAVSTVVLQAFGKYRDGDFDVTSGYLYVTIIYNISVSLALYALFLFYFATRELLSPYSPVLKFFMVKSVIFLSFWQGMLLAILEKCGAIPKIHSARVSVGEGTVAAGYQDFIICVEMFFAALALRHAFTYKVYADKRLDAQGRCAPMKSISSSLKETMNPHDIVQDAIHNFSPAYQQYTQQSTLEPGPTWRGGAHGLSRSHSLSGARDNEKTLLLSSDDEF | 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 | MTVRGAALAPDPASPTTTTASPSVSATPEGSPTAMEHPVFLMTTAAQAISGFFVWTALLITCHQIYMHLRCYSRPNEQRHIVRILFIVPIYAFDSWLSLLFFTNDQYYVYFGTVRDCYEAFVIYNFLSLCYEYLGGESAIMSEIRGKAIESSCMYGTCCLWGKTYSIGFLRFCKQATLQFCVVKPLMAVSTVILQAFGKYRDGDFDVTSGYLYVTIIYNISVSLALYALFLFYFATRELLSPYSPVLKFFMVKSVIFLSFWQGMLLAILEKCGAIPKINSARVSVGEGTVAAGYQDFIICVEMFFAALALRHAFTYKVYADKRLDAQGRCAPMKSISSSLKETMNPHDIVQDAIHNFSPAYQQYTQQSTLEPGPTWRGGTHSLSRSHSLSGARDNEKTLLLSSDDEF | 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 | MPCTCGNWRRWIRPLVVLLYIVGLLVVVPLCVWELQKLEVGIHTKAWFIAGIFLLMTIPISLWGILQHLVHYTQPELQKPIIRILWMVPIYSLDSWIALKYPNIAIYVDTCRECYEAYVIYNFMVFLSNYLTNRYPNLVLIIEAKDQQRHLPPLCCCPSWAMGEVLLFRCKLGVLQYTVVRPFTTIIALICELVGVYDEGNFSFDNAWTYLVILNNMSQLFAMYCLVLFYKVLREELNPIQPVGKFLCVKMVVFVSFWQAVLIALLVKVGVISEKHTWEWQSVEAVATGLQDFIICVEMFLAAIAHHYSFSYKPYVQEAEEGSCFDSFLAMWDISDIRADISEQVRNVGRTVLGQPRKMFFAEDHEQNEHTSLLSSSTQDPISDASSMPSSPMGHYQGFGHTVTPLTTPTTVPVVDGIYNTSATRDTEESPELMHNSSEKALDRS | 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 | MPCTCTWRNWRQWIRPLVAVIYLVSIVVAVPLCVWELQKLEVGIHTKAWFIAGIFLLLTIPISLWVILQHLVHYTQPELQKPIIRILWMVPIYSLDSWIALKYPGIAIYVDTCRECYEAYVIYNFMGFLTNYLTNRYPNLVLILEAKDQQKHFPPLCCCPPWAMGEVLLFRCKLGVLQYTVVRPFTTIVALICELLGIYDEGNFSFSNAWTYLVIINNMSQLFAMYCLLLFYKVLKEELSPIQPVGKFLCVKLVVFVSFWQAVVIALLVKVGVISEKHTWEWQTVEAVATGLQDFIICIEMFLAAIAHHYTFSYKPYVQEAEEGSCFDSFLAMWDVSDIRDDISEQVRHVGRTVRGHPRKKLFPEDQDQNEHTSLLSSSSQDAISIASSMPPSPMGHYQGFGHTVTPQTTPTTAKISDEILSDTIGEKKEPSDKSVDS | 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 | MPCACNRSNWRRWIRPLLVLFYATTILVAVPICIWKFQKMKVGMHTKSWFIAGIFLLLTIPVSLWGILQHLVHYTQPELQKPIIRILWMVPIYSVDSWVALVYPKIAIYVDTWRECYEAYVIYNFMIFLTNYLTIRFPNLILHLEAKDQQNHILPLCCCPPWAMGEMLLFRCKLGVLQYTVVRPITTVTALVCEILDVYDEGNFGFSNAWTYLVILNNLSQLFAMYCLLLFYKVLKEELSPIQPVGKFLCVKLVVFVSFWQAVLIALLVKLGVISEKRTWEWQSAEAVATGLQDFIICIEMFFAAIAHHYTFSYKPYVHEAEEGSCFDSFLAMWDVSDIRDDISEQVRRVGRTMRGYPKKKCFPGDPDHNEHSSLLSSSSQDLTSGSSKVPSPGGLYQGFGHTISSQSPISIASIYEEIMNDIPEEQQKLLNPGQDVTINIPEEQQKLIDKRKDVMIDIPEQNAIPDNSQYQDQEQIVTLQALFPSTETSENSMIDTSESQQESSDLCTESSDSSTESSDLSTDP | 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 | MSCPYAGNGNDHDDSAVPLTTEVGKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRVVLILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKDPSLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVRRGDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSDRYKVFLDLFNLSTFLIPREAIPPLDETIRKKLINKSV | 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 potentially harmful free tryptophan in the hemolymph. In the adult the same reaction is the first step in the ommochrome biosynthetic pathway .
Catalytic Activity: L-tryptophan + O2 = N-formyl-L-kynurenine
Sequence Mass (Da): 44421
Sequence Length: 379
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
EC: 1.13.11.11
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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-kynurenine
Sequence Mass (Da): 30341
Sequence Length: 263
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
EC: 1.13.11.11
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P48775 | MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD | 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-kynurenine
Sequence Mass (Da): 47872
Sequence Length: 406
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
EC: 1.13.11.11
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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-kynurenine
Sequence Mass (Da): 32598
Sequence Length: 286
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
EC: 1.13.11.11
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P41895 | MSRRNPPGSRNGGGPTNASPFIKRDRMRRNFLRMRMGQNGSNSSSPGVPNGDNSRGSLVKKDDPEYAEEREKMLLQIGVEADAGRSNVKVKDEDPNEYNEFPLRAIPKEDLENMRTHLLKFQSKKKINPVTDFHLPVRLHRKDTRNLQFQLTRAEIVQRQKEISEYKKKAEQERSTPNSGGMNKSGTVSLNNTVKDGSQTPTVDSVTKDNTANGVNSSIPTVTGSSVPPASPTTVSAVESNGLSNGSTSAANGLDGNASTANLANGRPLVTKLEDAGPAEDPTKVGMVKYDGKEVTNEPEFEEGTMDPLADVAPDGGGRAKRGNLRRKTRQLKVLDENAKKLRFEEFYPWVMEDFDGYNTWVGSYEAGNSDSYVLLSVEDDGSFTMIPADKVYKFTARNKYATLTIDEAEKRMDKKSGEVPRWLMKHLDNIGTTTTRYDRTRRKLKAVADQQAMDEDDRDDNSEVELDYDEEFADDEEAPIIDGNEQENKESEQRIKKEMLQANAMGLRDEEAPSENEEDELFGEKKIDEDGERIKKALQKTELAALYSSDENEINPYLSESDIENKENESPVKKEEDSDTLSKSKRSSPKKQQKKATNAHVHKEPTLRVKSIKNCVIILKGDKKILKSFPEGEWNPQTTKAVDSSNNASNTVPSPIKQEEGLNSTVAEREETPAPTITEKDIIEAIGDGKVNIKEFGKFIRRKYPGAENKKLMFAIVKKLCRKVGNDHMELKKE | 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 TFIIH, and facilitating RNA polymerase II elongation.
PTM: Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases.
Sequence Mass (Da): 82194
Sequence Length: 735
Subcellular Location: Nucleus
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P43418 | MEKILMLNDDQIWIFKKHTNNIQLLIEVALYLKSNKSSVSKKDKDAMYDIFSESELYNPRESLRDKPLDTINHKLDGLSYFMFGYSDRINDENKFIFSPLGNLFLKYLHDKDKLSKIFSCMLISMQFPHPYSKPSECFLLYPFRLIFKLLLDKRLQGRLYHYEVYKIIIHTISIDEAKYEFLVKSILNSRKKSWNEKLNELSEIQHKVVKSVYEWQYYIVPLLGSLHIFKINNGDIEQKLYHPQKDGSKSPPTARKANNGYVEINDNLTNFIDKLLNKYSFLDTPILLSDSQRKSNDVTKEIYSFYPELLLAEIGETISFESHILNIPKLITEYSKNPDNSTSGKFEKILEEAFNLFIDVEAQWLAGAGRTDIECMYLPINEKFSIEAKSTKNKLSMINSGRLKRHRTLISANYTIVITPRYVPSVRYDIEAQDIVLITADTLAEYLYNNIISNNRDISYADIQAIIVANLGKDISTQISNLTLSKFG | 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 Mass (Da): 56737
Sequence Length: 488
EC: 3.1.21.4
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P25261 | AWGKNQFNNAFPIALACFMFSQQIKPIYIRLEKRNTEHNYIAVDQIFQINPLDPQAFFAFEHSYHPYTELIIGKTPAIDVVISNLQNSQIINAFEIKLTAIPDNTTAILSDHLQGCEIVIRPDTIVYLALSIAKIFQQNSSVLLDILDPICARISDWEDVTSIKPMIPVFCELLYTIFDRYQSAQIPILLQPIWKTQGKLSILHENCLDLFVWSNFALAKVFLDASIKPSEKSITRPERTTVWLIKMLYDFAQNGKIDYKRTLDRITFNLKNDKAFAASGMVTRKYMNSPELHNPRIKRHLIKHIIINGGQRYLSPERRLDSAIVSTPSLFEDGL | 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 | MQIYETYWEITNEYGYNTERFVETLKICVEYIDEIKLVNPNYTETDYSSVIYNELQMRLQSSPILQSTRKGFEGKPKNETSIRKSINQLVKSGFINPFLTGYHSLAKEYLQTKVNKKRNFLFSRIVYESSNFSYAITDKPDIKVRHINFLVNTLIENFEGKLSKNEIIALMLMDLRTYNGNYYPIDELRNFIRLNQNYISEFKERKYNQITYLWGLLSKLDEIYQKDEFICLEEDKKRVFGDLEDTQYLRKRDPYLHRLYKHQLQEESAEYCGGIKCMLEKLAYPVLIASHIKPFIQSDDNEAYDPNNGLLLSRTLDSLFDLKYISFDDNGNMLKSARLSDDVWQYWRNIKLDSVLLNEKRKQYLKFHRELMEKEDSKN | 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 fragments with terminal 5'-phosphates.
Sequence Mass (Da): 45321
Sequence Length: 379
EC: 3.1.21.4
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P36433 | MTEFFSGNRGEWSEPYALFKLLADGQLYLGDSQLNKLGIVMPILSILRQEKNYESSYILHNNSQNIIVTYNNEKFTVPISGFQEKAVLLLSEIKNASGNRAFSIPSIDDFLKKLGFTHLSASSSSKSDIHIVVHDLRTGITPTLGFSIKSQLGSPATLLNASKATNFTFKIYNLKDKQIEYINSLSGIKEKIKEIFSQDGKLEFVKVESCKFSNNLTLIDTKLPEILAEMILLYYSSKLNKIDDVTEHISRLNPLNYNLSCNHNYYEYKVKHFLNDVALGMRPDDVWLGQYDATGGYLVVKEDGELLCYHIYSKNSFEDYLYCNTKFDTPSSSRHDFGHIYQVNHDFFIKLNVQIRFL | 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) and inhibits channel inactivation.
Sequence Mass (Da): 4124
Sequence Length: 37
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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V5YXI5 | MKITRSLSTVEVHTGGEAFRIVTSGLPRAPGDTIVQRRAWLKENADEIRRALMFEPRGHADMYGGYLTEPVSPNADFGVIFVHNEGYSDHCGHGVIALSTAAVELGWVQRTVPETRVGIDAPCGFIEAFVKWDGEHAGPVRFVNVPSFIWQRDVSVETPSFGTVTGDIAYGGAFYFYVDGAPFDLPVREAAVEKLIRFGAEVKAAANAKYPVVHPEIPEINHIYGTIIANAPRHPGSTQANCCVFADREVDRSPTGSGTGGRVAQLYQRGLLAAGDTLVNESIVGTVFKGRVLRETTVGDIPAVIPEVEGSAHICGFANWIVDERDPLTYGFLVR | 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-pyrroline-2-carboxylate + H2O
Sequence Mass (Da): 36325
Sequence Length: 335
Pathway: Amino-acid degradation.
EC: 4.2.1.77
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Q6HMS9 | MKVSKVYTTIDAHVAGEPLRIITGGVPEIKGDTQLERRAYCMEHLDHLREVLMYEPRGHHGMYGCIITPPASAHADFGVLFMHNEGWSTMCGHGIIAVITVGIETGMFEVTGEKQNFIIDSPAGEVIAYAKYNGSEVESVSFENVPSFVYKKDVPIIIDDYEFQVDIAFGGAFYAVVDSKEFGLKVDFKDLSAIQMWGGKIKHYIESKMEVKHPLEEGLKGIYGVIFSDEPKGEDATLRNVTIFADGQVDRSPCGTGTSARIATLFEKDALQKGEIFVHECITDGKFEGEVLSVTAVDTYEAVVPKVTGHAFITGFHQFVVDPRDDLKRGFLLG | 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. Displays no proline racemase activity.
Catalytic Activity: trans-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O
Sequence Mass (Da): 36841
Sequence Length: 334
EC: 4.2.1.77
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Q3SX04 | MAGPLTVPWMPPHDPGTPALSVVDMHTGGEPLRIVLAGCPEVVGPTLLAKRRYMRQHLDHVRRRLMFEPRGHRDMYGAVLVPSELPDAHLGVLFLNNEGYSSMCGHAVLALGRFALDFGLVPAPPSDAQEALVNIHCPCGLVAAFVECEGCRSRGPVRFHSVPAFVLATDFLVDVPGRGKVVVDIAYGGAFYAFVSAEKLGLDVCSAKMGDLVAAASAVTEAVKAQFKISHPDSEDLAFLYGTILTDGKDTYNEEPTTNICVFADEQVDRSPTGSGVTARIALQYHKGLLELNQTRAFKSSATGSVFTGKAVREAKCGDFKAVIVEVSGQAHYTGTASFIVEDDDPLRDGFLLK | 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
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Q485S0 | MTKNIAQAAVKFEQWQPKIEQESYLTINSLECHTGGEPLRIITSGFPVLKGNTILAKANDCKQNYDQLRRALMFEPRGHADMYGAIITDAERDDSHFGAVFIHNEGYSSMCGHAVIALTKTAVESGVVARTGDVTQVVIDVPCGQIYAMAYSHNNVVKHVSFQCVPSFVYAKDQQVEVDGIGMVQFDIAYGGAFYAYVQASSLGLSLVPEQQEKLIAYGRKIKQAIIPQFEINHPTTAELSFLYGVIFIDDSPNQDVHSRNVCIFADGELDRSPTGSGVSGRIALHHAKQQIVLNETITIESILASSFSVRAIETVCFAGFDAVIPEVTGDAYVCGKGQWFINAEDPLKYGFLLR | 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
Sequence Length: 355
EC: 4.2.1.77
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Q96EM0 | MESALAVPRLPPHDPGTPVLSVVDMHTGGEPLRIVLAGCPEVSGPTLLAKRRYMRQHLDHVRRRLMFEPRGHRDMYGAVLVPSELPDAHLGVLFLHNEGYSSMCGHAVLALGRFALDFGLVPAPPAGTREARVNIHCPCGLVTAFVACEDGRSHGPVRFHSVPAFVLATDLMVDVPGHGKVMVDIAYGGAFYAFVTAEKLGLDICSAKTRDLVDAASAVTEAVKAQFKINHPDSEDLAFLYGTILTDGKDAYTKEPTTNICVFADEQVDRSPTGSGVTARIALQYHKGLLELNQMRAFKSSATGSVFTGKAVREAKCGDFKAVIVEVSGQAHYTGTASFIIEDDDPLRDGFLLK | 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-pyrroline-2-carboxylate + H2O
Sequence Mass (Da): 38138
Sequence Length: 354
EC: 4.2.1.77
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O14804 | MRAVFIQGAEEHPAAFCYQVNGSCPRTVHTLGIQLVIYLACAAGMLIIVLGNVFVAFAVSYFKALHTPTNFLLLSLALADMFLGLLVLPLSTIRSVESCWFFGDFLCRLHTYLDTLFCLTSIFHLCFISIDRHCAICDPLLYPSKFTVRVALRYILAGWGVPAAYTSLFLYTDVVETRLSQWLEEMPCVGSCQLLLNKFWGWLNFPLFFVPCLIMISLYVKIFVVATRQAQQITTLSKSLAGAAKHERKAAKTLGIAVGIYLLCWLPFTIDTMVDSLLHFITPPLVFDIFIWFAYFNSACNPIIYVFSYQWFRKALKLTLSQKVFSPQTRTVDLYQE | 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(s)-class of G-proteins which activate adenylate cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38242
Sequence Length: 337
Subcellular Location: Cell membrane
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Q96RI8 | MSSNSSLLVAVQLCYANVNGSCVKIPFSPGSRVILYIVFGFGAVLAVFGNLLVMISILHFKQLHSPTNFLVASLACADFLVGVTVMPFSMVRTVESCWYFGRSFCTFHTCCDVAFCYSSLFHLCFISIDRYIAVTDPLVYPTKFTVSVSGICISVSWILPLMYSGAVFYTGVYDDGLEELSDALNCIGGCQTVVNQNWVLTDFLSFFIPTFIMIILYGNIFLVARRQAKKIENTGSKTESSSESYKARVARRERKAAKTLGVTVVAFMISWLPYSIDSLIDAFMGFITPACIYEICCWCAYYNSAMNPLIYALFYPWFRKAIKVIVTGQVLKNSSATMNLFSEHI | 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 remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38451
Sequence Length: 345
Subcellular Location: Cell membrane
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Q5QD13 | MGSNSSPPTVLQLCYENVTGSCVKTPYSPGSRVILYAVFGFGAVLAVFGNLMVMISILHFKQLHSPTNFLIASLACADFGVGISVMPFSMVRSIESCWYFGRSFCTFHTCCDVAFCYSSLFHLSFISIDRYIAVTDPLVYPTKFTVSVSGICIGVSWILPLVYSGAVFYTGVYDDGLEELSSALNCVGGCQVVVNQNWVLIDFLSFLIPTLVMIILYGNIFLVARQQAKKIENIGSKTESSSESYKARVARRERKAAKTLGITVVAFMISWLPYSIDSLVDAFMGFITPAYIYEICVWCAYYNSAMNPLIYALFYPWFKKAIKVIMSGQVFKNSSATMNLFSEQI | 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 | MVNNFSQAEAVELCYKNVNESCIKTPYSPGPRSILYAVLGFGAVLAAFGNLLVMIAILHFKQLHTPTNFLIASLACADFLVGVTVMPFSTVRSVESCWYFGDSYCKFHTCFDTSFCFASLFHLCCISVDRYIAVTDPLTYPTKFTVSVSGICIVLSWFFSVTYSFSIFYTGANEEGIEELVVALTCVGGCQAPLNQNWVLLCFLLFFIPNVAMVFIYSKIFLVAKHQARKIESTASQAQSSSESYKERVAKRERKAAKTLGIAMAAFLVSWLPYLVDAVIDAYMNFITPPYVYEILVWCVYYNSAMNPLIYAFFYQWFGKAIKLIVSGKVLRTDSSTTNLFSEEVETD | 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 remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39016
Sequence Length: 348
Subcellular Location: Cell membrane
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Q9NYJ8 | MAQGSHQIDFQVLHDLRQKFPEVPEVVVSRCMLQNNNNLDACCAVLSQESTRYLYGEGDLNFSDDSGISGLRNHMTSLNLDLQSQNIYHHGREGSRMNGSRTLTHSISDGQLQGGQSNSELFQQEPQTAPAQVPQGFNVFGMSSSSGASNSAPHLGFHLGSKGTSSLSQQTPRFNPIMVTLAPNIQTGRNTPTSLHIHGVPPPVLNSPQGNSIYIRPYITTPGGTTRQTQQHSGWVSQFNPMNPQQVYQPSQPGPWTTCPASNPLSHTSSQQPNQQGHQTSHVYMPISSPTTSQPPTIHSSGSSQSSAHSQYNIQNISTGPRKNQIEIKLEPPQRNNSSKLRSSGPRTSSTSSSVNSQTLNRNQPTVYIAASPPNTDELMSRSQPKVYISANAATGDEQVMRNQPTLFISTNSGASAASRNMSGQVSMGPAFIHHHPPKSRAIGNNSATSPRVVVTQPNTKYTFKITVSPNKPPAVSPGVVSPTFELTNLLNHPDHYVETENIQHLTDPTLAHVDRISETRKLSMGSDDAAYTQALLVHQKARMERLQRELEIQKKKLDKLKSEVNEMENNLTRRRLKRSNSISQIPSLEEMQQLRSCNRQLQIDIDCLTKEIDLFQARGPHFNPSAIHNFYDNIGFVGPVPPKPKDQRSIIKTPKTQDTEDDEGAQWNCTACTFLNHPALIRCEQCEMPRHF | 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) specifically recognizes Lys-63'-linked polyubiquitin chains unanchored or anchored to the substrate proteins such as RIPK1/RIP1 and RIPK2: this acts as a scaffold to organize a large signaling complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1 . Regulates the IL1-mediated translocation of NCOR1 out of the nucleus (By similarity). Involved in heart development .
PTM: Degraded in a lysosome-dependent manner following interaction with TRIM38.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76494
Sequence Length: 693
Domain: The RanBP2-type zinc finger (NZF) mediates binding to two consecutive 'Lys-63'-linked ubiquitins.
Subcellular Location: Membrane
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