ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q2G3C3 | MTENTPGTSAPERFDPATADTRWQRVWDEKQSFRADDSSTKPRSYVLEMFPYPSGRIHIGHVRNYTMGDVLARYKRMRGFEVLHPMGWDAFGMPAENAAMEKGVHPGGWTRDNIANMKAQLKRLGFALDWSREIATCEPEYYGQEQALFLDLYAAGLVYRKESTVNWDPVDMTVLANEQVIDGRGWRSGALVEKRKLNQWFLKITDFADELLEGLSTLDKWPEKVRVMQENWIGKSQGLQFRFDLSNGETVEVYTTRPDTIFGASFVAVAPDHPIAQGVAAINCEAANFIALCKKGGTTAAELETAEKLGFDTGIGARHP... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 94260
Sequence Length: 848
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
Q04FL2 | MSYDHKAIEKRWQTYWDEHKTFKTAPETSGKPKYYVMNMFPYPSGQGLHVGHPESYTATDIMARFNRMRGFNVLQPMGWDAFGLPAEQYAIKTGHNPADFTNENIKHFKKQVKSLGFSYDWDREINTTDPEYYKWTQWIFEQLYKKGLAYEDEIMVNWAPDFPGGGIVVANEEVIDGKTERGSYPVYRVPMKQWVLRITKYAERLLSDLDDLDWPEAIKEQQRNWIGKSTGAAVFFKVDGKSDYQVEVYTTRPDTLFGASYMVLAPEHDLVDKITTSECRADVDAYKAKIASKSDLERTDLNREKTGAFTGAYGINPVNG... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 93102
Sequence Length: 810
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
Q30YL0 | MKYNPQAIEEKWQHIWEEKEMFRSEHGSDKPKYYVLEMFPYPSGNIHMGHVRNYSIGDVVARFKRMQGFNVLHPMGWDAFGLPAENAAIKHDTHPAKWTYSNIDNMRSQLKRLGYSYDWRRELATCDAEYYRWEQLFFLKFMEKGLIYRKKAPQNWCPKCNTVLANEQVIDGLCWRCDSVVEQRDLAQWFLRITSYAEELLADLEKLTGGWPDRVLTMQHNWIGKSVGAEIEFAVDGSDETVKVFTTRPDTVFGSTFMSIAPEHPLVEKLITGTGQEETVRAFVTRIRNMDRIERTADTLEKEGVFTGAYCINPLSGRRM... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 93741
Sequence Length: 829
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
A1B5Q5 | MPYDPAISEPRWQEAWEQADTFRAVRDERPKYYVLEMFPYPSGRIHMGHVRNYTMGDVVARFKRAQGFSVLHPMGWDAFGMPAENAAMEQGGHPRDWTYGNIATMRGQLKPLGLSIDWSREFATCDDAYVAQQQALFLDMLEAGLITRKSAQVNWDPVDMTVLANEQVIDGKGWRSGATVERKELTQWFFKISDYSDELLSALDGLEGWPEKVRLMQANWIGKSRGLQFRFHTVDLPDFPTIEVYTTRPDTLMGASFVALSPDHPLVKALAASDPKVAAFVEECRRIGTTEEAIETAPKMGFDTGLTVRHPLDADWRLPI... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 93879
Sequence Length: 844
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
A7HSL7 | MSTRYNARAAEPKWQKIWEERGDFLMRDDADGKPKYYVLEMFPYPSGRIHMGHVRNYTMGDVIARYKKARGFNVLHPMGWDAFGMPAENAAMEKNVHPKGWTYDNIAAMREQLKAIGLAIDWSREFATCDPEYYGHEQALFLDMLEAGLVSRKKSMVNWDPVDNTVLANEQVIDGRGWRSGALVERRELTQWFLKISDFADELLEGLDTLDRWPEKVRLMQKNWIGRSEGARVFFELENAPDGNTKLEIFTTRPDTLYGASFCALSPHHPLTQSLAKDNPALTDFIRECDRIGTSEEAIETADKMGFDTGLKARHPFIEG... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 97257
Sequence Length: 870
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
Q6MCC8 | MKYDHQQIEAKWQKFWQDNQTYRSDDNFQKPKYYVLDMFPYPSGAGLHVGHVVGYTATDIIARYMRTKGYNVMHPMGWDSFGLPAEQYAIRTGTHPAESTQENINNYRRQLRALGFSYDWNRELATSDPNYYKWTQWIFTKLYEKGLAYEAEMLVNYCPALGTVLANEEIENGKTKDGGHPVERRPLKQWILKITAYADRLLQDLDLLDWPESLKKLQINWIGKSEGAYVQFIEKTTQEAFSVFTTRPDTLFGVSYLVLAPEHPLVSHITASSQQQAVRAYQAQIASKSDLDRTELNRDKTGVFTGAYAVNPVNHKEIPI... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 97641
Sequence Length: 845
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
A1APS3 | MEQKYNPAAVEQKWQQQWETGASFAVNEQSDRPKYYLLEMFPYPSGRIHMGHVRNYSIGDVIGRFKRMRGFNVLHPMGWDAFGMPAENAAIQNKSHPAKWTYENIDYMRGQLKKMGLSYDWGRELATCDLEYYRWEQKIFLEMFAKGLAYKKTSYVNWCPTCETVLANEQVEDGACWRCDSPVQQKELDQWFFRITQYAEELLSYTEKLPGWPERVLVMQKNWIGKSHGCEVDFPLEGGTGSVRVFTTRPDTLFGATFMSLAPEHPQARELTTPDRRDEVERFIEKVRNTDRSKRTADDYEKEGVFTGSYCINPLTQVRM... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 93197
Sequence Length: 823
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
Q3AXV7 | MYGTIAAKPHAGPVNAASSSASANNSPQENRYDPSALEQRWRARWKDQGLDTTETESSKPGFFALSMFPYPSGSLHMGHVRNYVITDVIARVQRMRGDSVLHPMGWDAFGLPAENAAIERNIDPGEWTDRNIDQMRNQLDRLGLSIDWDREQATCHSDYYRWTQWLFLELLEGGLAYRKNATVNWDPVDQTVLANEQVDADGRSWRSGALVEQRQLNQWFLRITDYAEALLNDLDKLKGWPERVRTMQANWIGRSEGAEITFQVTGSSQQSITVFTTRPDTLSGASYVVLAPEHQLVDGLTTEEHLASVDQFRKQVARLS... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 97885
Sequence Length: 884
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
Q0AWK4 | MDRKYDFKSIEAKWQAYWENKQLFKVEEDPEKPKYYNLEMFPYPSGHLHMGHVRNYAIGDVVARFKSMNGFNVLHPMGWDAFGLPAENAAIKNAIHPATWTYSNIENMKRQLKTMGISYDWDRELATCKPDYYKFTQWMFLKLYENKLAYKKKSAVNWCPSCQTVLANEQVVDGACERCEAVIEKKQLEQWFFKITDYAQRLLDDLALLPGWPEKVKTMQKNWIGRSEGCEFSLHIEDSDEVLTVFTTRPDTVFGVTYMVLAPEHPLVEKICHPEQEKEVKAFVNKMKYLNEMARTSTEAEKEGVFTGAYAINPMDGSRI... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 94728
Sequence Length: 824
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
Q9WY15 | MKEYRPQEIEKKWQEVWEEKKVFYTPQRSEKPKYYALVMFPYPSGTLHVGHVKNYVIGDIVARYKRMRGYNVLHPFGYDAFGLPAENAAIEKGIHPEEWTRKNIATIRQQVKKLGISYDWSREIATCDEEYYKWTQWIFLQLYKNGLAYKKKAAVNWCPKCKTVLANEQVKDGKCERCGTSVTIRHLEQWFFKITDYAERLLNDLDKLTGWPEHVKTMQRNWIGKSTGAEIDFPVEGSDTKIRVFTTRPDTLWGVTFMALAPESPLVEELVPEEKKEELQEFLERVKQQDRFRRTSVEAEKEGFFLGRYAINPVTGERIP... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 95625
Sequence Length: 824
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
Q97AN8 | MDYSRCCGSTNSRVIYMNIDEKWQNAWERDHVFEPKIDERKKFMITVPWPYTNGSLHVGHGRTYTLGDIIARYKRSRNYNVLFPMGFHQSGTPILAFSERIRAGDASTIALYRSYLSEYGEKDIDGWLEKFKDPRNIADYFSNAIINDFKHLGYSIDWTRKFTSADEFYQNVVKWQFHKLNEKGLIKQDKYPILYSIDDDNAVGEDDIKDGDTDKVSVEEYTAVFFESNSYSLIAASLRPETLFGVTNIWINPTGEYVKIKIGDKIAVVSKEAVDKLKYQRNDVSVIGPISAESIQRKKFTTPFGKEVPVYKADFVDTDN... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 104994
Sequence Length: 910
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
O83595 | MGYPFRALEKKWQAYWRDKRVFCVSEDERFPPERRAYVLDMFPYPSAQGLHVGHPEGYTATDIYCRYLRMGGYNVLHPMGFDAFGLPAENFALKTGTHPRVSTSANCDTFRRQIQSFGFSYDWEREISTADPEYYRWTQWLFLKLYEKGLAYEATAPINWCPSCKTGLANEEVRDACCERCGAEVTRRGVRQWMVRITAYAERLLSDLDELDWPESVKQMQRNWIGKSCGAEIDFPVDAPACSVHDKLPQTIRVYTTRADTLFGVTYLVLAPEHEAVTALTTHAQRAAVQAYVQRAAKKNDLERTDLAKEKTGVFTGAYV... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Sequence Mass (Da): 98991
Sequence Length: 878
Subcellular Location: Cytoplasm
EC: 6.1.1.4
|
Q2T087 | MSASDLHPVQAGAPQGRRQILVTSALPYANGQIHIGHLVEYIQTDIWARTMRMHGHEIYYIGADDTHGTPVMLRAEQEGVSPKQLIERVWREHKRDFDSFGVSFDNFYTTDSDENRVLSEKIYLALKEAGFIAEREIEQAYDPVKQMFLPDRFIKGECPKCHAKDQYGDSCEVCGTTYQPTDLVNPYSVVSGATPVRKTSTHHFFRLSDPRCEAFLREWVSGLAQPEATNKMREWLGDAGEAKLADWDISRDAPYFGFEIPGAPGKYFYVWLDAPVGYYASFKNLCERRGLDFDAWISKDSTTEQYHFIGKDILYFHTLF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Sequence Mass (Da): 7... |
Q9PP85 | MRYITTPIYYVNDVPHLGHAYTTIIADTLARFYRLQGHETRFLTGTDEHGQKIEEAAKLRNSTPQEYADKISFEFKKLWDEFEITYDIYARTTDTRHIEFIKAMFLKMWQKGDIYKDEYEGHYCISCESFFTQSQLINDCSCPDCGKQTRILKEESYFFKLSKYQDKILQWYEEKDPILPKNKKNELINFVQNGLKDLSITRTSFDWGIKLPQEINDDKHIIYVWLDALFIYVSSLDFQNKGENAKFWPAHVHLVGKDILRFHAIYWPAFLMSVDLPLPKFIGAHGWWTKEGEKMSKSKGNVVKPKEVVDAYGSEAFRYF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Sequence Mass (Da): 7... |
Q8Z068 | MNLVNKAEKTFALTTPLYYVNDVPHIGSAYTTMAADAVARFQKLLGRDVLLITGTDEHGQKIQRSAESLGKAPQEFCDEIVPSFMSLWRLLNIQYDRFSRTTAVRHKAIVDEFFARVWEAGDIYQGQQKGWYCVSCEEFKEERELLEGNRCPIHVNKEVEWRDEQNYFFRLSKYQTQLEEFYQSHPDFIQPESRRNEVLNFVSQGLQDFSISRVNLDWGFPVPNDPKHTLYVWFDALLAYVTALLDPEDEPTLENALGKWWPINLHLIGKDILRFHAVYWPAMLLSAGLPLPDRVFGHGFLTKDGQKMGKSLGNTVDPVG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Sequence Mass (Da): 6... |
Q9ZTS1 | MASPPPPPKLPVPGRRNILVTSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNVIYICGTDEYGTATETKAMEEKCSPKEICDKYHAVHSEVYKWFDIKFDKFGRTSSPQQTEVCQAIFQKLMENNWLTENTMQQLYCDTCQRFLADRLVEGKCPTEGCNYEAARGDQCENCSKLLNPTELIDPKCKVCKNTPRVRDTDHLFLELPLLSDKLVNYINETSVAGMWSQNAIQATNAWLKEGLKPRCITRDLKWGVPVPHEKYKDKVFYVWFDAPIGYVSITASYTPDWEKWWKDPDNVELFQFMGKDNVPFHTVMFPS... | Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Sequence Mass (Da): 89453
Sequence Length: 801
Subcellular Location: Cytoplasm
EC: 6.1.1.10
|
A6LFP0 | MEKHFKRTLITTALPYANGPVHIGHLAGVYVPADIYARYLRLKGEEVLMIGGSDEHGVPITLRAKKEGITPQDVVDRYHGIIKKSFEEFGITFDIYSRTTSATHHQMASDFFRTLYDKGEFIEKTSEQYYDEEAKQFLADRYIMGTCPHCGNEKAYGDQCEACGTSLSPTDLIDPKSAISGSKPVMRETKHWYLPLDKWEPFLRKWILEDHKEWKPNVYGQCKSWLDMGLQPRAVSRDLDWGIPVPVEGAEGKVLYVWFDAPIGYISNTKELLPDSWETWWKDPETKMVHFIGKDNIVFHCIVFPSMLKAEGSYNLPENV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Sequence Mass (Da): 7... |
Q6MDG0 | MFKNLCDKIMTQKILITSALPYANGPLHFGHIAGAYLPADCYARFQRLMKKDVLYICGSDEYGIAITLSADLAGRTPQEHVDLFHHINQSFFEQLQISFDHYSRTTWKGHVEPTHQFFNDLLQNGYIEERTTDQLYSEKDQKFLADRYVVGTCPRCGFENARGDECPCCGASYEATELKNPRSKLTDASLILRPTKHWFLLLEKFKKPLMEWLETKNWKPNVINFIRGYIDHLHARAITRDMKWGISVPLPDSEGKVLYVWFDAPIGYISATKEWALLRGEEKLWEKYWLDPETKLVNFIGKDNIPFHASIFPAMIMGQN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Sequence Mass (Da): 7... |
Q6L1M5 | MSERILVNCALPYANGPLHLGHIAGAYLAADIFVRFNRLNGNEVLFVSGSDEYGTPITITAEKNKTSPQNVADIYHREHEQTFKNLDIVFDIFTRTTDPEHVKDVDEFFINLLNKNYLEKRYMVSPYCKSTGKFMPDRYIHGTCPYCGFNDARGDQCDECGRTLDPIELINPRCTSSNEEPLFIATEHFFLRLDLLSDELLNYLNTRENWKPNVINFTRSIINEGLRPRPITRDIDWGVPIPLNGFEGKRIYVWFEALIGYITGARVYSKNIKDDDYWKKFWLDKNVKSYYFIGKDNIPFHTIIWPAMLIAHGDYNLPYN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Sequence Mass (Da): 7... |
Q64332 | MMNFLRRRLSDSSFIANLPNGYMTDLQRPEPQQPPPAPGPGAATASAATSAASPGPERRPPPAQAPAPQPAPQPAPTPSVGSSFFSSLSQAVKQTAASAGLVDAPAPSAASRKAKVLLVVDEPHTDWAKCFRGKKILGDYDIKVEQAEFSELNLVAHADGTYAVDMQVLRNGTKVVRSFRPDFVLIRQHAFGMAENEDFRHLVIGMQYAGLPSINSLESIYNFCDKPWVFAQMVAIFKTLGGEKFPLIEQTYYPNHREMLTLPTFPVVVKIGHAHSGMGKVKVENHYDFQDIASVVALTQTYATAEPFIDAKYDIRVQKI... | Function: Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. May play a role in noradrenaline secretion by sympathetic neurons.
PTM: Phosphorylation at Ser-10 dissociates synapsins from synaptic vesicles (By similar... |
O14994 | MNFLRRRLSDSSFMANLPNGYMTDLQRPDSSTSSPASPAMERRHPQPLAASFSSPGSSLFSSLSSAMKQAPQATSGLMEPPGPSTPIVQRPRILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVSRSFKPDFILVRQHAYSMALGEDYRSLVIGLQYGGLPAVNSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITSVVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGS... | Function: May be involved in the regulation of neurotransmitter release and synaptogenesis.
PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63303
Sequence Length: 580
Domain: The A region binds phospholipids with a preference... |
Q8BI41 | MTGFWVLCFVLFPSSLSYPESWMPLVNLTHHILRDTNSSLFSNCWVCLSTQTQRSLAVPAPLSIWTDTPMKLHLTYSVRPFSGSFSISDIERRLRLFRPLTASYSFHNPDRRAIAFLQLVSSTGIFRIITRITSVIYPHKDRFFESAQRPLWGPLFTETVLRSQAPLCISRFFKVSAYATFVGNLSASLCNYTMHISPSTSHENLDLSTTHTFKQAMKRPDAKWKNPLRFSGPPSLIFSKPAYYPCPTDIKHCHTSPATPWMHCPQAPFGTCYNLTLFEPDNSTHPVTMSVNPTHFKVKLQGHRDPYPLSHYQPLTGAAL... | Function: This endogenous retroviral envelope protein has retained its original fusogenic properties . Together with Syna, participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis . Synb is specifically involved in formation of syncytiotrophoblast layer II (SynT-II) . Promotes m... |
Q9SW96 | MADEIVPPATQLAAVSLENDGSTVQRAQFSNRVLIRTILDRPDGGAGLAGQTVRIGGWVKSGRDQGKRTFSFLAVNDGSCPANLQVMVDPSLYDVSNLVATGTCVTVDGVLKVPPKGKGTQQQIELNVVKVIDVGTVDASKYPLPKTKLTLETLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEGAGEMFQATTLINYTERLEQDLIDNPPPTEADVEAARLIVIERGNVVAELKAAKASKEAITAAVAELKIAKETFAHIDERSRLRPGLPKKDGNIDYSKDFFGRQAFLTVSGQLQVE... | Catalytic Activity: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn)
Sequence Mass (Da): 63783
Sequence Length: 572
Subcellular Location: Cytoplasm
EC: 6.1.1.22
|
Q9SW95 | MESHGKTHQKEHDNDLSPKPITLSKYSKRVELKTLLDRSDRGAGLAGKRVVIGGWVKSARAVKKNSPPPPLPVVAAPSPSSGGDQAHTTANIRCTEIIQSKMNIFKRFFDVLSGGGKTYPIFDKTELAGQKAVPPPEYVFYFLISDGSSISSLQVVVDSALSTVPATQLMALGTCIVAEGVLRLPLAASAKHVIELEAEKLLHVGTVDPEKYPLSKKQLPLHMLRDFSHFRPRTTTVGSVTRVHSALTLASHTFLQYHGFQYVQVPVITTTTGFGEMFRVTTLLGKTDDKEEKKPPVQEKDGFSIDTVKAVIKEKTRLID... | Catalytic Activity: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn)
Sequence Mass (Da): 71364
Sequence Length: 638
Subcellular Location: Cytoplasm
EC: 6.1.1.22
|
P10723 | MTVYICPETGDDGNDGSELKPLRTLYQAMIITKSSKGDFLIRTKKDGKQIWEAASKTALKKSWKHYEQEMLKNEKVAAKMLEKDATEVGVKAALEEAKKVQIELDTSLSYITGVKIRDLVKHRNERVCIKGWIHRMRRQGKSLMFFILRDGTGFLQVLLMDKLCQTYDALTVNTECTVEIYGAIKEVPEGKEAPNGHELIADFWKIIGNAPPGGIDNVLNEEASVDKMLDNRHLVIRGENAAALLRLRAAATRAMREHFYNAGYLEVAPPTLVQTQVEGGSTLFNLDYFGEQSFLTQSSQLYLETCIPTLGDVFLHCSVL... | Function: Potentially protective antigen in lymphatic filariasis.
Catalytic Activity: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn)
Sequence Mass (Da): 62339
Sequence Length: 548
Subcellular Location: Cytoplasm
EC: 6.1.1.22
|
Q19722 | MSKLYIDTDAGSDQHPGTEAQPLATLVQAMLISKNSGEFLMKKKSEEGESWEPAAKAAIKKAVKKYEAEVKKLEKAGCREKEAEEAQHAALEEAKKITFSLDKSLPEAKVIKIGESVQHRDQRVSIKAWVHRLRRQGKSLMFLVLRDGYGFLQCVLNDKLCQSYDAVTLSTETSVQVYGIIKALPDGKSAPDGHELTVDYWEVIGKAPAGGIDNVLNESAGVDVMLDNRHLVIRGENASRILRIRAAATRAMRDHFFAAGYTEVAPPTLVQTQVEGGSTLFGLDYYGEPAYLTQSSQLYLETCNAALGDVYCISQSYRAE... | Function: Involved in protein synthesis . Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Catalytic Activity: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate... |
Q6BU46 | MSQVYVNEKTGADSTDVSGSEQQPFQTPAFALFKNEDAKILVYKQLEDSEEFGYGEISASALKKAKKGAEGLKKKQEKQAKLQEEQRKHQDDAAKKFAEMDLISIKEDESLPQAKKIKLRTVQDNIGTRVVVQGWIHRLRLQKGLGFITLRDGTGFIQCILTGDLAKCKTTHELTLESTVTIKGVINKLPEGKSAPGGVELKVDYYEVVGLAPSGEEAFSNKVQENADPSLLLDQRHLALRGESLSAVMKVRSTLLQAIRRFFAEEGLLEVTPPCMVQTQVEGGSTLFKMDYYGEEAYLTQSSQLYLETCLPALGDVFCV... | Catalytic Activity: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn)
Sequence Mass (Da): 62236
Sequence Length: 552
Subcellular Location: Cytoplasm
EC: 6.1.1.22
|
Q554D9 | MSTEEDQKLFLSIGLDEKRAKDTLKNKDLTALLKTIIEEASVSKGCDKSIGNLLYSLATCQQVNSPIRSNVSKAIGEEKIKTTIQFQAATQYLKDNKEFNQDTFNDFCGVGVVITPEQIQKAIDDLFTKKATEISEKKWHIPIGDLLNPLKESLKWADLKEVKIMLDKKLETTLGPKVVEAKEKKVAATTTAPVKKIEEQLAAITLKQDASLPTPKRLKIRECSPKFANQRVEVHAWAHHVRNQKKIVFLELRDGTGFLQCVLSGDLVHPSIIDKLLREATVKIVGTLVIPPADKKCPGGVELQADYWELLGPSNADLEG... | Catalytic Activity: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn)
Sequence Mass (Da): 74555
Sequence Length: 653
Subcellular Location: Cytoplasm
EC: 6.1.1.22
|
O43776 | MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISKSQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGALEGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQS... | Function: Catalyzes the attachment of asparagine to tRNA(Asn) in a two-step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn) . In addition to its essential role in protein synthesis, acts as a signaling molecule that induced migration of CCR3-expressin... |
Q6KHD7 | MTSIKHLLINAKKYDQKEFEIKAWVASNRGNTNIRFVEINDGSTIKNLQVVIKKEIMSFLEVDKIRLGAAIHVKGVLKYTPGMAQEIELNADKFILLKNTDEDFPIQKKETSLEALREIPHLRHRTTTLRAIMLIRSTLALEIHKFYNERGYLWVSSPIITGNDGEGAGESFVVDDESKDFFFNKKATLGVTGQLHAEAYALGFSKVYTFAPTFRAENSNTTKHAAEFWMMEPEVAFFDLKDLIKMSDDMLRQVIKRTVEAHPHEFEFFEKNKPGLLKNLNLFLNNKLSILEYREAIKILEKVKDRFEDKNIFFGKDLAT... | Catalytic Activity: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn)
Sequence Mass (Da): 51588
Sequence Length: 447
Subcellular Location: Cytoplasm
EC: 6.1.1.22
|
B0JN99 | MTTRIKEIFQTGQPDQSVTVQGWVRTKRELKEFTFLEVNDGSSLANLQVILEPTLPDYENVLKTISTGAAIAVSGNLVPSPGKGQNIELKAAEITLYGDCPPDYPLQKKRHSFEFLRTIAHLRARTNTLGAVMRVRNACATAIHSFFQEKGFIWVHTPIITANDCEGAGELFTVTSLDLKKPANFAEDFFGKRAYLTVSGQLQAEVMAMALSNVYTFGPTFRAENSNTSRHLAEFWMVEPEMAFCDLEGDQDLAEAFLKYIFKFVLENCPEDLQFFNERIDKTVLSTAENIVNSEFGRITYSEAIELLEKADRQFEFPVE... | Catalytic Activity: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn)
Sequence Mass (Da): 51586
Sequence Length: 454
Subcellular Location: Cytoplasm
EC: 6.1.1.22
|
P47359 | MKSVTVKQLLQTPRKFNNKQIKLSGWVKNKRASANIIFLAISDGSSINTLQAVVKQEDNPQVFSLLQTVNLASAVMVWGEIILTPKAKQPLELKLKQVSLLAQAESDYPLQKKEHSQEFFRSNAHLRVRAKTYFAVMKIRSVLSHAIFEYFFKNDFILVQSPILTSNDCEGAGETFVIKDSETFFNKTTFLTVSGQFGAEAFAQAFKKVFTFGPTFRAEKSHTNRHLSEFWMIEPEIAFANLKDLMQLIQNLIKFLIKKVMENASDELNVLAKQFSNDIISNLKTIISTKKFPIIEYSKALAILKESSDTKKTNFELNDF... | Catalytic Activity: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn)
Sequence Mass (Da): 52086
Sequence Length: 456
Subcellular Location: Cytoplasm
EC: 6.1.1.22
|
Q04EX6 | MGETKVIRIEDVSKFVGQTVKIGVWLRQKRGSGKIAFLQLRDGTGFMQGVVSVGDVDEATFKLAEHLKQESSFYVTGEIHQDSRSEFGFEMAVSDIEIVGESEDYPITPKEHGTDFLFDERHLYLRHQKPFATMKIRDEIIRAIYDFFHKDGFLKLDSPIITDSAPEGTTELFPVKYFDKDAYLSQTGQLYAEAGAMAFGKVYDFGPTFRAEKSSTRRHLTEFWMIDAEMAWMHQEDSLKVQERFIAYLIERVVDNCQVELKMLGRDVEKLRAYTKLPYPRISYDDAVKLLQDNDFKIEWGVDFGSPEETFLAKRFNSPF... | Catalytic Activity: ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn)
Sequence Mass (Da): 50118
Sequence Length: 434
Subcellular Location: Cytoplasm
EC: 6.1.1.22
|
Q18CD2 | MKMSKMFMPTLKEIPADAEITSHQLMVRSGMIKKMTSGVYNQLPMGLRVFKKIEQIIREELNKKDCQEILCAALLPSELWKESGRWTAMGEEMFRLKDRTEREYCLGPTHEEAFTDIIRQEITSYKQLPLNLYQIQVKYRDERRPRFGVMRTKTFTMKDAYSFDVDDKGLDKSYQDMFDAYVSIFDRCGLENSPVQADSGAIGGSTSAEFMVKSEVGEDEVVFCSGCDYAANVERAESCNLASQKEEMKELEEVHTPGAATIKELEEFLKTSPDKFAKTLVYEADGKTVVVVVRGDREVNEIKVSNAIGSVIEFALATDD... | Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has... |
Q39233 | MSFQDLEAGTRSPAPNRFTGGRQQRPSSRGDPSQEVAAGIFRISTAVNSFFRLVNSIGTPKDTLELRDKLQKTRLQISELVKNTSAKLKEASEADLHGSASQIKKIADAKLAKDFQSVLKEFQKAQRLAAEREITYTPVVTKEIPTSYNAPELDTESLRISQQQALLLQSRRQEVVFLDNEITFNEAIIEEREQGIREIEDQIRDVNGMFKDLALMVNHQGNIVDDISSNLDNSHAATTQATVQLRKAAKTQRSNSSLTCLLILIFGIVLLIVIIVVLV | Function: May function in the docking or fusion of transport vesicles with the prevacuolar membrane.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 31061
Sequence Length: 279
Subcellular Location: Prevacuolar compartment membrane
|
P93654 | MSFQDLESGRGRSTRKFNGGRQDSTQAVASGIFQINTGVSTFQRLVNTLGTPKDTPELREKLHKTRLHIGQLVKDTSAKLKEASETDHQSGVNPSKKIADAKLARDFQAVLKEFQKAQQTAAERETTYTPFVPQSALPSSYTAGEVDKVPEQRAQLQESKRQELVLLDNEIAFNEAVIEEREQGIQEIHQQIGEVNEIFKDLAVLVNDQGVMIDDIGTHIDNSRAATSQGKSQLVQAAKTQKSNSSLTCLLLVIFGIVLLIVIIVLAA | Function: May provide the t-SNARE function in the vacuolar assembly. Promotes the formation of vacuolar membrane 'bulbs'. Required for inflorescence stem gravitropism.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 29481
Sequence Length: 268
Subcellular Location: Prevacuolar compartment mem... |
A0R9A0 | MAKEQVQAITKMEEDFAQWYTDIVKKAELVDYSSVKGCMILRPYGYALWENMQKVMDEKLKATSHENVYMPMFIPESLLQKEKDHVEGFAPEVAWVTHGGDEKLAERLCVRPTSETLFCEHFSKIVQSYNDLPKLYNQWCSVVRWEKTTRPFLRTTEFLWQEGHTIHETAEESQAETLNILNLYASFCEDYLAIPVIKGQKTEKEKFAGAKATYTIESLMHDGKALQTGTSHNFGTNFSEAFDIKFLDRNGKWQYVHQTSWGVSTRMIGGLIMVHSDNNGLVMPPKVAPVQVVIVPIAQHKEGVLAKATELQGHIQKVAR... | Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Catalytic Activity: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
Sequence Mass (Da): 54685
Sequence Length: ... |
Q0SAY4 | MARDERGVTAQSEDFAAWYNEVVFKAGLVDRGPAKGTMVIRPYGYRLWELLQSELDRRIKDTGHENAYFPLLIPESYLGREAEHVEGFSPELAVVTHVGGKVLEEPLVVRPTSETIIGEMMAKWISSHRDLPLLLNQWANVVRWELRPRMFLRTTEFLWQEGHTAHVDEASARRETMLALDIYHEVARELAAIPVVPGEKTPGERFAGAVATYTIEGMMRDGRALQSGTSHYMGIKFASAFDIRFTSETGREELCHTTSWGMSTRMIGGIVMTHGDDKGLVFPPRLAPHQVVIVPITRGGNVAVEGAADELAHRLRSVGV... | Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Catalytic Activity: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
Sequence Mass (Da): 52973
Sequence Length: ... |
B8DNM5 | MRWSNCYIPTLKEAPADAEVVSHKLLTRAGMIRKLTSGIYIYMPLGLKAIEKTAAIVREEMNRAGALELSMPMVQPADLWQESGRWEFYGKELLRFQDRNGRDYCLGPTHEEVITDLVRGEVRSYRQLPINLYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFDRDEAGADKSYWAMYEAYQNVFKRLGLRFRAVEADSGSIGGSFSHEFMVLADTGEDTIAACTGCQYAANVERAEVAPPAVPATLPAVGAIEEVPTPGKHTVEEVCAFLGVPQSALVKTLILVADGKPVAALVRGDRELNDVKLKNLLKCDELELAAP... | Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has... |
Q99XY4 | MKQSKLLIPTLREMPSDAQVISHALMVRAGYVRQVSAGIYAYLPLANRTIEKFKTIMREEFEKIGAVEMLAPALLTADLWRESGRYETYGEDLYKLKNRDNSDFILGPTHEETFTTLVRDAVKSYKQLPLNLYQIQSKYRDEKRPRNGLLRTREFIMKDGYSFHHNYEDLDVTYEDYRQAYEAIFTRAGLDFKGIIGDGGAMGGKDSQEFMAITPARTDLDRWVVLDKSIASMDDIPKEVLEDIKAELAAWMISGEDTIAYSTESSYAANLEMATNEYKPSSKVAAEDALAEVETPHCKTIDEVAAFLSVDETQTIKTLL... | Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has... |
Q87YQ1 | MSKDPMSKPTPEPAAHSKAGPAVPTNFLRPIVQADLDSGKHSKIITRFPPEPNGYLHIGHAKSICVNFGLAKEFGGDTHLRFDDTNPAKEDQEYIDAIMNDVKWLGFEWAGEVRYASQYFDQLHDWAVELIKAGKAYVDDLTPEQAREYRGTLTEPGKNSPFRERSVEENIDLFARMKAGEFEDGARVLRAKIDMASPNMNLRDPILYRIRHAHHHQTGDKWCIYPIYDFTHGQSDAIEGITHSICTLEFESHRPLYDWFLDNLPVPCKPRQYEFSRLNLNYTITSKRKLKQLVDEKHVNGWDDPRMSTLSGFRRRGYTP... | Catalytic Activity: ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)
Sequence Mass (Da): 65197
Sequence Length: 569
Subcellular Location: Cytoplasm
EC: 6.1.1.18
|
A1SS83 | MTQVDTAPSNFIRNIIDSDLQSGKHQVIHTRFPPEPNGYLHIGHAKSICLNFGLAEDYPNALCNLRFDDTNPVKEDADYVAAIEKDVRWLGFKWAGDIHYSSDYFEQLYDFAIELIKKDKAYVCALDAQQTREYRGSLMTVGKDSPFRNRPISESLDLFARMRAGEFAEGSMMLRAKIDMASPNMKMRDPVLYRIRFAHHHQTGDKWCIYPMYDFTHCISDALEGITHSLCTLEFEDHRPLYDWVLANISIACKPRQIEFSRLNLQYTLTSKRKLHTLIEEKIISAWDDPRMPTISGMRRRGYPAASIREFCKRIGVTKQ... | Catalytic Activity: ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)
Sequence Mass (Da): 63197
Sequence Length: 553
Subcellular Location: Cytoplasm
EC: 6.1.1.18
|
Q8Y199 | MSQDNATGAAAASTSNFLRQIIDTDLEQGTYAGRQDTAGHALPPIITRFPPEPNGYLHIGHAKSIWVNFGLAKEYGGRCHLRFDDTNPVKEDTEYVDSIIDAVHWLGYSWQNGTGEHLYYASDYFEQLYGFAEVLIQRGAAYIDSQSAEQIAANRGDFTRPGTPSPFRDRSVEENLALFRDMRAGKYQDGQHVLRARIDMAAPNIVMRDPVLYRIRHAHHHRTGDAWCIYPMYDFTHCISDALENITHSLCTLEFENNRPLYDWVLDHLRDAGALPAPLPHQYEFARLHLTYAITSKRKLLQLVNEKRVDGWDDPRMPTL... | Catalytic Activity: ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)
Sequence Mass (Da): 65607
Sequence Length: 580
Subcellular Location: Cytoplasm
EC: 6.1.1.18
|
Q7UX42 | MARANRGEHSTLSTFWQSRHNAASFDPLYRRIDVNAPEPSDSATPEKTPSKHFIRQAIDADLASGRFDGVATRFPPEPNGYLHIGHAKSICLNFGLAKDMGGTCNLRFDDTNPIKEDTEYVDSIQEDVRWLGFEWDNLHFASDYFDQLYDWAEQLVKDGKAYVCDLTAEETREYRGTLTEPGKNSPHRDRTPEKNLELLRAMKAGKFKDGEKTLRAKIDMASPNINLRDPVMYRIAHVPHHRTGDKWCIYPMYDWAHGQSDSLEKITFSICTLEFEHHRPLYNWYCENLGIHHPRQIEFARLNMTFTVMSKRKLLQLVKE... | Catalytic Activity: ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)
Sequence Mass (Da): 68668
Sequence Length: 601
Subcellular Location: Cytoplasm
EC: 6.1.1.18
|
Q7W0K0 | MLLEQQKQLISLIQAAVAQCLPEAQAQVQLERPKVAAHGDIATNVAMQLAKPARRNPRELAQGIVDALMAQPQARELIQDAEIAGPGFINFRLTPAARQAVVQAVASQADAYGRAPRNGEKVLVEFVSANPTGPLHVGHARQAALGDAICRLYDASGWDVTREFYYNDAGNQIDNLAISVQARGRGIAPDAPDYPADGYKGDYIVEIARDFAARKSVQASDGQPVTATGDLDSLDDIRAFAVAYLRREQDLDLQAFGLAFDNYFLESSLYASGRVQETVDTLVAKGHTYEEGGALWLRTTELGTGDDKDRVMRKSEGGYT... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 61387
Sequence Length: 560
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
C0R2B0 | MESRRMLKKIISNILKEALKEYLKDTDVKDIESYIEIGYAVDDKFGDYACPVAMRLAKVLKKNPLEIANSITEKIDKKYFDKIEVAKPGFINLTLSYNYINECINDLINNDDYGKNTVEDKKKILVEYVSANPTGPLHIGHGRWAAIGSALSNILKYAGHEVYQEFYVNDAGEQITKLNESVKAVQEGREIPEDGYHGEYIKDVAKQDGVPKDIILESQKKLLERFGTHMDNYASELKIREGGELEKTMDFLDKEGLLFEEDNAVWFKSTKYGDDKDRVVKKSNGTYTYFAPDITYHKNKIDRGYHYLIDILGADHHGYV... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 61484
Sequence Length: 534
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q5FH87 | MSVACTIRRHIIEKLHVLNIDNFVVTNESILAKLIVDYPNNPDHGDLYTNAALILSKYIKKNPMDIAKILVDEFSSIKEISDINVVKPGFINFNISLDVWYEIIISINRLKEKFGHVNFGNGKRVNIEFVSANPTGPMHIGHARGAIFGDVLANLLERVGYEVVREYYINDAGAQVDVLVESVYLRYKEVLGENIVIGSGLYPGLYLKDIGKLLYQEYGSGLLGMDYSQRRRIIRDVSLMYLMKLIKEDLALLGIKHDIFTSESQLQKDNIVQKCVELLQEKQLIYYGTLDQPKGTEGINWKPRTQMLFKSTDFGDDVDR... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 65365
Sequence Length: 576
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
B2KD56 | MLDNLKKDIETKLFNAEVFEGAVLPPVDLTPAPPHTGADISLTWAMSAAKTLKKNPLEIAKAAVKVISEVTFVASASYAAPGFINIILEDSFISSSALDRRLKNRKTAGENKERVLIEFVSANPTGPLHVASGRGASLGDSLVRIFNALGIQCDSEYYVNDSGNQAMLLGVSLKARVNGQEPPENGYHGSYLIEMADEIREMSKDWTEEQFSIYAIEYLIKTHQRDMQAFNVNFTRWFRESELYKESLPAKALDFLKEKGLAYEADGAVWFGTTKDNDDKDRVLVRADGRPTYFLADIAYHKNKYDRGFTTLVDILGADH... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 59933
Sequence Length: 532
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
A6GZP8 | MSLQEILNPSIKTAIHQLFDLTIEKIEFQSTRKEFDGDITMVIFPLLKLIKTPQATPNGAKLNPADLGNKIGNYLVENVAQVEAFNVVSGFLNIVIANDYYINFFNTIKTDAQFGFVSPSEHDKAIMVEYSSPNTNKPLHLGHVRNNLLGYSVAEIIKASGKKVYKTQIINDRGIHICKSMLAWQKFGHSETPETSGLKGDKLVGKYYVAFDKAYKVEIAELMLQGKTEEEAKKQAPIIIEAQQMLLDWEAGKPAVMALWKTMNQWVYDGFATTYKNLGVNFDSYYYESNTYLLGKEVVQIGLDKGVFEKDPDGSVWIDL... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 67873
Sequence Length: 601
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q2J9H6 | MTAQTVRSLINQVEIAVSAAIDRVLPEAAGADPVVRPSEHADFQSNAALALAKRARTKPADLATAVADALRADGSTAVADVTVSGPGFLNLALADATVWTQVAARLADPRLGIDLPEQSRRTVIDYSGPNIAKEMHVGHLRTTIIGDALARVLGFLGAEVIRQNHLGDWGTQFGMLIQYLDEHPDATWHSDDLAPGTSTVSALDSLYRAARKEFDADPGFADRARARVVALQAGDEDTVARWREIVAESEVAFRQIYDRLGVLLEPSDSAGESFYNDRLLDIVDELTAAGIAQDSEGALVVLSQEVTGPDGDPATLMVRK... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 63622
Sequence Length: 588
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q73P28 | MEDIKTTWQKIIADTLNGIAPETCDKILPEQINIETPPNPEMGDVAFPLFTFAKSFKSSPAKIASDVCARLLENEDIKKYGMPKAIGPYLNVFLAKGDLASNVLDKVLKEKENYGKTSSLSGKRIMIEFSSPNTNKPLHLGHLRNDALGESISRILKFCGADVFKVNIINDRGVHICKSMIAYQKFGEGKTPESENIKSDRFVGDMYVAFHKYSQENPEKAEAEAKQMLLDWEAGENKELIGLWKKMNGWAIEGIKETYKRTGISFDKLYFESETYLKGKDQILKGLEAGVFYKEEDGSVWVDLAPIKLDKKVLLRSDGT... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 66634
Sequence Length: 590
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q83GE9 | MNVEDLKKSVTNIVHSMYNFDCSEIVSLTRPPKPEYGDWALSLPLKLASLLKSPAIDIAQSIASALLELDGVQDVYVAKPGFINLKLSREHTTGIISEVLEQGSSFGRNTTQSSKKINLEFVSGNPTGPLHLAHTRWAAVGDSIARILINCGADVTREYYINNVGNQIHLFSESVYARALSKSLPKDGYPGEYVKDIARRIQCEFPNIIDLSYEDAIKIFRKRSWQIQIEEIKKSCIAFRVNFDVWFSEESLHEPDRFGKSQIDKALARCKQNGYLFQKNGAFFIRTTEFGDDKDRAVLRSDTSYTYYAADCAYYLNKIN... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 62999
Sequence Length: 552
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
B1AIR8 | MITQKISEELNKALAKMGIHDTQETKILVDKTKNIKFGDFYTNIAMILSKKNNKSSLEIAKEIANNFEQDLFLEVNLQPPGFLNFKLKAKDHENLLKQIYYEKDRFGQFSKKNITYNIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYWINDAGNQIDKLAMSVLVRYLQLQNINIQLPADAYHGQEIHLVAQTLYQTYKNQFINVRLNEKYEIDDDIANQEIKNFAVKYLLNEIKNDLASINTFIDTYTSENWIRNSGRILEVLSKIKPYTYTLDGALWLKTTTFGDDKDRVLIKSDGSYTYFTPDIAY... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 63662
Sequence Length: 550
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q9KQC6 | MNIQALINDRVSQAIEAAGAPAGTPALVRQSAKAQFGDYQANGIMGAAKQLGTNPREFAQKVLDVLNLEGIASKTEIAGPGFINIFLSEEFLAAQAEAALADARLGVAQEAPKTIVADYSAPNVAKEMHVGHLRSTIIGDAVVRTLEFLGHKVIRANHIGDWGTQFGMLIANLERVQKASGEVSMELSDLEAFYRESKKLYDEDEQFAETARNYVVKLQGGDPFCLEMWKKLVDVTMIQNQRNYDRLNVSLTRENVMGESMYNDMLPQIVSDLKAKGLAVEDDGAQVVFLEEFKNKDGEPMGVIIQKRDGGFLYTTTDIA... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 63877
Sequence Length: 577
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q73HY6 | MNIFKQISSLIFSKLNELKQRGVISTSAANFIIEPPSNRVHGDIYTNVAMVLAKHEKKNPIEIAEVLAKEFELFDEVAKVEIAGSGFINMHLKIEVWHGILKQINELKTEFGTLDIGNNQAINVEFVSANPTGPLHIGHARGAVFGDVLANLLKKVGYKVTKEYYINDAGAQIDTLIRSVYLRYKEALGEKISIEKGLYPGEYLKPIGTGLAKKYGAELLEKQDNQVIRDYTLSSILEIIKEDMNLLGVNHDVFTSEYELQKSGKIEESIKILSDKGLVYEGYLEKPKGKESENWTSRKEMLFRSTKFGDDVDRALKKED... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 64167
Sequence Length: 568
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q6F8G5 | MIDPKLLRNNIEAVNLALAKRGVQLDPTEWASLEVRRKELQSKTESLQAERNAGAKQVGQIKKAGGDASEIMTRMQAIGDEIKAAEVALAELQAEIEQKALSIPNLPDESVPEGKDENDNVEISKWGTPRQFDFEIKDHTDLGEWMGGLEFETATKLTGSRFSVLKGPLARLQRALTQFMLDTHTLKNGYTEAYVPYLVNADSLRGTGQLPKFEEDLFKLQGEKEYYLIPTAEVPVTNFVRDEIIDAERLPLKYAAHTPCFRSEAGSYGRDTRGLIRQHQFDKVEMVQIVKPEDSMQALEELTGHAEGILQALGLPYRKI... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
C1F4G5 | MLDLAFVRANLELVEARLRARGQNPAELLGDFAAVDQHRRERITEAEQLKATRNKLSEEVARLRKAKEDASAVMEETRQLKTKIEDLERAATEAEEQLRERMARIPNLPYEDVPTGASAEDNVEVKRWGTPREFDFAPKPHWELGEQLGILDFERAAKLSGARFAVYWAEGARLERALAAFMLDLHTREHGYTEVLPPLMVNSRSLFGTGQLPKFAEDLFRCEDGEPYQAGKYRENDHWLIPTAEVPLTNLFRDETLDDSQLSTSLVAHTSCFRSEAGSYGKDVRGIIRQHQFQKVELVKFTRPEDSAAEHEALTRHAET... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q9ZCG5 | MLNIKWIRENQELFDEKLSQRFIEPMSSKIAMLDQEKRKITSLIQEFQHARKVKSKILGNMVSKSGEEFEELQRDVNHINEKLAELEQNLDNNNELNELLNMLPNIPDEEVPYGIDGSMNKLVRAYGKTNKNALNKQHFELGTKLNLMDFEQTAKISGSRFVTLKGDLAKLERALINFMIDIHTKEFDFFEISPPFLVRDRAMYNAGQLPKFSEESFITTNGYRLIPTAEVSLVNIVADTIIQREKLPMRYVAYTTCFRSEAGSSGRDTRGMIRLHQFGKVELVSITTPEESKNEHEYITNASETILKKLDLPYRVMLLC... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
Q9HKX5 | MIDVKLLRSNRELFEKNCEYRGVDKAPVEDFFRLDEEWRSINRELNGLRSQKNRETRKIAELIKNNGDASAEKKAVEDINARISDLENKLKKIEEERDRILWTIPNLVHESVPVCFGDENNQLVRYVGHAKVFRDDIEEFKKNSGNSQDYEVLDERPKSHVDLGLDLNVIDLESAARISGSRFYFIKNRLLKLEMALENYAVDFLSQRGFSIVEPPYMLNLESMRGATDLETFKDTLYKIEGEDLYLIATSEHSIAAMLSNQFLEEKDLPLRVAGISACFRREAGAHGKDTKGIFRVHQFNKIEQFVFCKPEDSWDFLEE... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
Seq... |
P34945 | MVDLKRLRQEPEVFHRAIREKGVALDLEALLALDREVQELKKRLQEVQTERNQVAKRVPKAPPEEKEALIARGKALGEEAKRLEEALREKEARLEALLLQVPLPPWPGAPVGGEEANREIKRVGGPPEFSFPPLDHVALMEKNGWWEPRISQVSGSRSYALKGDLALYELALLRFAMDFMARRGFLPMTLPSYAREKAFLGTGHFPAYRDQVWAIAETDLYLTGTAEVVLNALHSGEILPYEALPLRYAGYAPAFRSEAGSFGKDVRGLMRVHQFHKVEQYVLTEASLEASDRAFQELLENAEEILRLLELPYRLVEVAT... | Function: Catalyzes the attachment of serine to tRNA(Ser). Is also probably 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... |
Q6MML0 | MLMSQITIILPDNSTKVFDHEPTALEVAMSIGPRLAKETLGAKLNGSTEISDLRTVLKDQTKVALVTTKSPESVEVVRHSCAHIMAQAIQDIWPEVKVTIGPVIDNGFYYDFDSPFAFTEEHFEKIEKKMSEIVSKDLPIHREDWPIQKAIETFKGMNERFKVELIEDLAKKGETTVGIYFNGTSWFDLCRGPHIQSTGQIKAFKLLSVAGAYWRGDEKNAQLQRVYATAFNDKKDLETYLHNIEEAKKRDHRKLGKELGMFYFNELAPGSPFFTGKGATVYNSLQTYLRELYFETGYQEVITPQIFDVNLFHTSGHYQN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q8G6C2 | MAQATISITVNGEAKEVEATTTGVELFAEDKNIIAVKINGENRDLYTPLNDGDTVDPIALDSEDGLAIMRHSATHVMAQAVQEVYPNAKLGVGPVIKDGFYYDFQVDQPFTPNDLKDIEKRMQRIIKSSQSFRRRSVTEEEALKEEADQPFKIELIEDKEAHLDPAAATEISEKELSFYDNVDRDGNVVWKDLCRGPHLPNTRYIKAFKIERSAAAYWRGSEKNPTMQRVYGTAWATKEDLKAYQTRLEEAAKRDHRKLGAEMDLFSFPDEIGPGLAVFHPKGAAVINAMEDYSREMHRKHHYSFVQTPHITKGGLYETS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
A1R0E4 | MSEKLDKEDVLYKKRHSIAHVMAEAVIELFPNTKIAIGPPIKDGFYYDFDFEKHIIEDDLLLIEQKMREILKTGSSFVKEVITKEQALMLFKDEPYKIDLIHELDIADEISIYKSHNFTDLCKGPHIDNMGKIDPKAFKLISIAGAYWRGDEKNKMLTRIYGTLWNNEKDLKAYLKLREEIKRRDHRKLGRELDLFSVHEEIGPGLIFFHPSGARIRALIEDFWREEHFKNGYDILFTPHVGKSWLWETSGHLDFYKESMFEKMEMDKSNYYVKPMNCPFHIAIYNTGRHSYRDLPFRWAELGTVYRYEKVGALHGTMRV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q0TMX8 | MIKITLKDGSIKEVEAGLSIFEIAQSISQGLARNACCGILNGKVEDLRFIVNEDSSLEICTFDSKEGQHAFNHTASHVLAAAVKRLFPQDKLAIGPSIDNGFYYDFDTEKPFSADQLNKLEEEMKKIIKENPEIKRFELPRNEALELMKDEPYKVELINDLPEGEVISFYQIGDFVDLCAGPHLMAVKPIKAVKLLRSTGAYWKGDEKNKMLSRVYGTAFPKKSELDAYLEALEEAKKRDHNKLGRELGIFTTDENVGQGLPLLMPKGARIIQTLQRWIEDEEQRRGYVLTKTPLMAKSDLYKISGHWDHYKDGMFVLGD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q8NPZ0 | MSARRSAIFVNTTDTAVANLVVFEVPAGTAIGAAMRELDLPNKGPEAIVCAKDAEGQLKDLSHVPETTATFTAVPANTDDGRAVIRHSCAHVLAQAVQAEFPGTKLGIGPAIENGFYYDFDAAEPFTPEDLKTIEKRMKKIIKTGQKFERRVYESAEAAAEELKNEPYKLELIQDKGNVDPNSDEATEVGAGELTAYDNVNPRTSEVEWSDLCRGPHIPTTRYIPAFALTRSSAAYWRGDQDNAGLQRIYGTAWEDKESLDAYQTMLAEAEKRDHRRLGTELDLFSFPDDLGSGLPVFHPNGGIVRNEMEDHSRRRHIAA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q83C10 | MPTIQLPDGSVKQFSKPVSVQAVAESIGTSLAKPALAGKIDDHLVDVSFIIDKDVSLRIITEKDPEGLEVIRHSAAHLLAHAVKELFPKAEVTIGPVVEDGFYYDFAFERSFTPEDLEKIEEKMRSLAKADLAVERRVLSRDEALTLFKKMGERYKVEIIRDIPKEEILTAYQQGDFIDLCRGPHVPRTGMLKAFKLTKLAGAYWRGDSNNEMLQRIYGTAWADTKALKAYLYRLEEAEKRDHRLLAKKMDLFHFQPESPGNVFWHPNGWSIILQMREYIRHITHKYGYQEVHTPQLIDASLWDKSGHLEKFGDDIFSLP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q3Z8G2 | MANQIDEAKPISDLEIMRHSAAHIMAEAVLSMFPEAKLGIGPAIDTGFYYDFDLPRTLTPEDLPEIETRMNQLVKANLPFRREEMSKDEARKLFADQPYKLELLDDIPDEIVSVYRQGNLCDLCRGPHVNYTSKVKAFKLLSIAGAYWRGDEKRPMLQRIYGAAFLDKASLAEYLNMLEESAKRDHRKLGKELELFSLHQEIGGGLVNWLPNGAIVRHLIEEFWKKEHLKRGYSLVYTPHIAKVDLWKTSGHWGFYRENMYSPMDIDGEEYVLKPMNCVYHILMFKNRTRSYKELPIRMAELGTVYRYERSGVLHGLSRV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
A0QWG2 | MTAVASSAPAAPIRVPAGTTAGAAVREADLPGRGAPDAIVVVRDAEGRLRDLSWTPDTDVEVTPVAADTEEGRSVIRHSCAHVLAQAVQELFPQAKLGIGPPITDGFYYDFDVEEPFTPEDLERLEKRMRQIIKDGQLFSRRVYESKDAAREELANEPYKLELVDDKSGDPDVMEVGGDELTAYDNLNARTKERVWGDLCRGPHIPTTRYIPAFKLTRSSAAYWRGDQNNASLQRIYGTAWESQEALDRHLELIEEAQRRDHRKLGVELDLFSFPDELGSGLPVFHPRGGVVRRELEDYSRRKHLEAGYEFVNTPHITKE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q1D6E3 | MSDIITVTLPDGSQKQTARGTTIADFVRESIGPGLAKAALFARVNGQDMDLARKLDEDVKLQIFTPKSPESLELIRHDAAHVVASAVQKLFPGTQVTIGPATEEGFYYDFFREKPFTPEDLEKIEAEANAELKRDMAFVRTEISMDEAVRLFEEKGEKFKVEIVKDIAAKGAKTLTLYTHGDWVDFCLGPHAPSTGKIGIIKILSSSGAYWRGDHRNPMLQRVYGTAFFDKKQLAEYLTRIEESKKRDHRKLGKELDLFHFHPYSPGSAFWTPKGTTLYTTLSNWMRQLTQNDGYVEIKTPLMFNKGLWETSGHWGKYKE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q74MP3 | MRALFLHSNRIKVIARQKALKEADQLEKPEFDVNKEHLAVFVAVEHGDNLSVAEQLVEEIKKVLEKIGIKEKVVVLYPYVHLTNNPSSPKLAKEVLDKAYDLLKSEGFEVYKAPFGWYKEFEIHVKGHPLAELSRTIKPKKVKKEEGNKVYLIYDGEKEYIIVGKKDKILVKDYKEIENKEKLHFELPKDGIELPIPINQDFEKMVLKEVFSEGEEIEKNPLNDVAKKFGFEWEPLSDYGHMRYKPYAALMVDLVNDYSIKIAKELPFPVFIVKGTNMFDLKQGPVAEHAKLFGERMYEVQSDKSVFVLRYAACFQQFAI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q3IRE7 | MSEIVVTLPDGSELEMESGSTVEDVAYEIGPGLGDDTVAGVVDGELVDKAEQLTDDCELVIVTDQSDEYLQVLRHSAAHVFAQALQRLHPEAKLAIGPPTEEGFYYDVTGVDLDADDLEAIEAEMETIIEADHDIERAERSREEAFEIYEDNPYKRDILETEAADEDPVSFYTQDDWQDLCQGPHVDSTGEIGAVELLNIAAAYWRGDEDNETLTRVYGTAFESESDLEGFLQRREEAKKRDHRKLGQELDLFSIPDVTGPGLPLYHPNGKAVLRELEDFVDQLNDDQGYEFVETPHLFRTELWKQSGHYENYVDDMFLL... | 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).
Catalytic Activity: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threo... |
Q9L278 | MSDVRVIIQRDSEREERVVTTGTTAAELFAGERSIIAARVSGDLKDLAYEVKDGETVEAVEISSEDGLDILRHSTAHVMAQAVQELFPEAKLGIGPPVKDGFYYDFDVEKPFHPDDLKAIEKKMQEIQKRGQRFSRRVVTDEAAREELADEPYKLELIGLKGSASSDDGADVEVGAGELTIYDNLDAKTGELCWKDLCRGPHLPTTRNIPAFKLMRNAAAYWRGSEKNPMLQRIYGTAWPTKDELKAHLEFLAEAEKRDHRKLGSELDLFSIPEQIGSGLAVFHPKGGIIRRVMEDYSRRRHEEEGYEFVYTPHATKGKL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
B2FN79 | MINITLPDGSRREFENPVSVMEVAQSIGAGLAKATIAGAVDGVLVDASDVIDHDASLRIITAKDEEGVEIIRHSCAHLVGHAVKQLYPDVKMVIGPVIAEGFYYDIYSERPFTPDDMAAIEKRMGELIAQDYDVIKKMTPRAEVIEIFKARGEDYKLRLIEDMSEDIQAMGMYYHQEYVDMCRGPHVPNTRFLKAFKLTRISGAYWRGDAQNEQLQRIYGTAWADKKQLEAYIKRIEEAEMRDHRRIGKQQDLFHLQEEAPGLVFWHPKGWALWQVVEQYMRKVYRNSGYGEVRCPQILDVSLWKKSGHWDNYQDNMFFT... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalytic Activity: ATP + L-threonin... |
Q05873 | METNEQTMPTKYDPAAVEKDRYDFWLKGKFFEAGSDQTKEPYSVVIPPPNVTGRLHLGHAWDTTLQDIVTRMKRMQGYDVLWLPGMDHAGIATQAKVEAKLREEGKSRYDLGREKFLEETWKWKEEYADFIRSQWAKLGLGLDYSRERFTLDEGLSKAVREVFVKLYEKGLIYRGEYIINWDPATKTALSDIEVIYKDVQGAFYHMSYPLADGSGSIEIATTRPETMLGDTAVAVHPEDERYKHLIGKTVILPIVNREIPIVGDDYVDMEFGSGAVKITPAHDPNDFELGNRHNLERILVMNEDGTMNENALQYQGMDRF... | Function: 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 (By similarity). Catalyzes the attachment of valine to tRNA(Val).
Catalytic ... |
Q89ZM4 | MELASKYNPADVEGKWYQYWLEHRLFSSKPDGREPYTIVIPPPNVTGVLHMGHMLNNTIQDILVRRARMEGKNACWVPGTDHASIATEAKVVNKLAAQGIKKTDLTRDEFLKHAWDWTEEHGGIILKQLRKLGASCDWDRTAFTMDEERSKSVLKVFVDLYNKGLIYRGVRMVNWDPKALTALSDEEVIYKEEHGKLFYLRYKVEGDPEGRYAVVATTRPETIMGDTAMCINPNDPKNAWLKGKKVIVPLVNRVIPVIEDDYVDIEFGTGCLKVTPAHDVNDYMLGEKYNLPSIDIFNDNGTLSEAAGLYIGMDRFDVRK... | 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 + ... |
Q6MQK8 | MKMSEQLSDRYNPADVESRTYEWWEKNGYFKAQDQSTKPPFSIILPPPNVTGFLHMGHALDHTIQDMMIRWKRMNGYNTMWLPGTDHAGIATQSVVERELKKDGVTRHDLGREKFVEKVWDWKHQYGNRIYGQMRRLGDSCDWDRAVFTLDEGVSKAVRKVFVSLHKKGLIYRGQRLVNWSGPLETAISDLEVEHKQIKGSLYHVKYPLEDGSGFLVVATTRPETMLGDSAVCVHPEDERYKHLIGKNVLLPLTNRKIKIIADTYVDKEFGSGVVKITPAHDFNDYKIGKTHNLEFINILTKKAEINENGGVYAGLKVQE... | 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 + ... |
Q8G777 | MTEGKSIINANLTPLPDKVGVDGLEDKWRTVWDEDGTYKFRNTRDRKAVYSIDTPPPTVSGSLHVGHVFSYTHTDVIARYKRMRGYDVFYPMGWDDNGLPTERRVQNYYGVRVDVSLPYDPDFKPPFEGTDGKKIDAKDQVPISRKNFIELCERLTAQDEKLFEALWRKLGLSIDWSQTYHTIGQHPQRVAQKAFLRNLARGEAYQQDAPGLWDVTFQTAVAQAELESREYPGFYHKVAFRFEDGTPIYIETTRPELLAACTSLIANPNDERYKQYFGQYVYSPLFKVKVPILAHPAAEMDKGAGIAMCCTFGDVTDVEW... | 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 + ... |
Q493Z9 | MSNYIVEKIYNPKNIEEPIYKFWEYGDYFSPHGNTSQESYCIMMPPPNITGQLHLGHAFQQTIMDVLIRYQRMQGKNTLWQTGTDHAGIATQMLVEHKIYNNTGKTRHDYTRDELIKNIWAWKSQSEQFITYQMKRLGNSVDWKRQRFTMDTEMSYAVTEAFIRLYRKNLIYRGKRLVNWDCKLQTAISDLEVINKKTKGSIWYIYYKLDNATISSNSHHLIVATTRPETMLGDTAVAVHPEDTRYKNYIGQYVIAPITNRRIPIISDKNVDMFKGTGCLKITPAHDFNDYIIGKRHGLPMINIFSLNGKILKKLEVFNS... | 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 + ... |
O51680 | MNCRPLEKYDPKAFEDEIYTKWLKNNVFLPDNSLFEKFSMVAPPPNVTGVLHMGHALNFVLQDVLVRYKRMKRHNTLWLFGTDHAGIATQAVFERHLKKIGKSKDDFEREELVQEIFKLKDRHRGIIVNQINKLGASYDHSRERFTLDENLCKAVNKVFKDLYFKGLIYRGEYLVNLDPGSGSVVSDEEIEYKEVDGKLYFVKYFIDNSSFIEVATTRPETMFGDTAIAVNPNDERYKSLVGKEVTIPLTTKKIKVIADFYVDSAFGTGALKVTPAHDPNDFEISKRHNISKVNILTQDGKLNKNVPLQYQGLSAKDARF... | 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 + ... |
A8F8Q3 | MNLGTRYSPEQIEKKWYERWVEKGYFAPKGSGIPFVIVIPPPNITGRIHMGHALNITLQDILVRYKRMRGFDTLWVPGEDHAGIATQNAVERYLESQGKSREQLGREKFIEIVWEWAKKYRKEIRQQIETLGASVDWSRERFTLDDGLSKAVRKVFVDLYNRGLIYRGKYMVNWCPRCQTVLSDEEVEHIEESAKLYYVKYPFSGSNEYIVIATTRPETMLGDVAVAVNPEDERYKNISGKTVVLPLMNREIPIITDSYVDPEFGTGAVKITPAHDPNDFDIAKRHSLQFIEIFDNEAKINENGGKYAGLDRYQARKAVL... | 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 + ... |
Q88P76 | MDKTYQPHAIETSWYNTWESENYFAPQGAGESYTIMIPPPNVTGSLHMGHGFNNAIMDALIRFRRMQGRDTLWQPGTDHAGIATQMLVERQLEAKGQNRHDLGREKFLEKVWEWKDQSGGNISRQIRRLGSSVDWSRERFTMDDGLSEAVKEAFVRLHEDGLIYRGKRLVNWDTKLHTAISDLEVENHDEKGHLWNLRYPLADGAKTAEGQDYLVVATTRPETLLGDAAVAVNPNDERYQALIGKFVELPLVGRRIPIIADDYCDPEFGTGCVKITPAHDFNDYEVGKRHNLPLLNIFDKNAFVLSSAQAFNLDGSVNEQ... | 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 + ... |
Q887M3 | MDKTYQPHAIETSWYQTWESENYFAPQGAGDSYTIMIPPPNVTGSLHMGHGFNNAIMDALIRFRRMQGRNTLWQPGTDHAGIATQMLVERRLEAQGVSRHELGREKFLDKIWEWKAESGGNISRQIRRLGSSVDWSRERFTMDDGLSDAVKEAFVRLHEDGLIYRGKRLVNWDTKLHTAISDLEVENHDEKGHLWNLRYPLADGAKTAEGLDYLIVATTRPETMLGDAAVAVNPQDERYKALIGKFVELPLVGRRIPIIADDYCDPEFGTGCVKITPAHDFNDYEVGKRHNLPLLNIFDKNANVLPAAQVFNLDGKLNES... | 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 + ... |
Q8ZVG2 | MAHRLPTRWDIKWEEELLKLWEKEGRFKTKISGSRPVFVIDTPPPYLSSNRPHIGQTASYAHFDMIARFLRMRGVDVIFPFYLDRNGLPIEVQVEKKYGVVAHEIPREKFIKMCKEELDSYEGEFVSSLRRWGLSFDYWPNGTDSPEYRRMTQKTFIELWHKGLVYEAERPTPWCPRCRTALAEPEIEYREEETYLNYIKFKVKETGEDIIIATTRPELLPATVAVIFHPDDSRYTRLNGMHAVVPPEGQVVPILPHKAANPNFGSGLVMISTFGDTRDLMIVNELKLPIRIIIDEGGRIKTGKYAGVSIREARAKIIED... | 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 (By similarity).
Catalytic ... |
O58052 | MLPKNYDPNEIEPKWQKYWLEEKIYKYRLDENKPSYAIDTPPPFTSGTLHLGHVLSHTWIDIIARYKRMRGYNVLFPQGFDNHGLPTELKVEKEFGITKDQPEEFLKKCVEWTWQAIEAMRKQFIRIGYSADWDLEYHTMDDWYKAAVQRSLLEFYKKGLIYREEHPVYWCPKCRTSLAKAEVGYVEEEGYLYYIKLPLADGSGYIPIATTRPELMPACVAVFVHPDDERYKHLVGKKVKLPIFEREVPILADEDVDPNFGTGAVYNCTYGDEQDIVWQKRYNLPVIIVINEDGTMNENAGPYAGLKIEEARKKIAEDLE... | 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 + ... |
Q92Q37 | MLDKTYDSAAVEPKIAKAWDEADAFRAGVNAKPDAETFTIVIPPPNVTGSLHMGHALNNTLQDIMVRFERMRGKDVLWQPGMDHAGIATQMVVERQLMERQLPSRRDMGREAFIERVWEWKAESGGLIFNQLKRLGASCDWSRERFTMDEGLSEAVIEVFVSLYKEGLIYRDTRLVNWDPKLQTAISDIEVEPVEVNGHLWHLRYPLEEGVTYQHPVAFDEDGNATEWETRNYLVVATTRPETMLGDTGVAVHPDDVRYKGIVGKHVILPIVGRRIPIVADEYPDPTTGTGAVKMTPAHDFNDFDVGKRQGLRQVNVLTA... | 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 + ... |
Q8XMQ5 | MEDKKKIIFSGIKPSGDLTLGNYLGAIKNWTKLQEEYDCYFCVVDLHAITVKQLPADLRRRTLEVLAIYIASGINPEENTLFIQSHVPAHSEASWLLTCNSYMGELSRMTQYKDKSKKMGDSIGAGLFNYPVLMAADILLYNADLVPVGKDQMQHLELARDIGTRFNNSYSKTFTIPEGYVPKEGAKIMDLQDPSKKMSKSDANPNGFILIMDEPNVIRKKISRAVTDSIGIVNYTDEQPGVKNLINILCAIKGYTPDEVVKMYDGKGYAEFKNDVAEAIVEELAPVQEKVKALLGDKKALEEIYKKGAEKANYAAMKTL... | 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): 37158
Sequence Length: 332
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q891C7 | MGGINMEDNKKTIFSGIQPSGNLTIGNYFGALKNWVKLQDEYNCFYCIVDLHAITVRQVPQELRKRTLEVLAVYIASGLDPEKNTLFIQSHVPAHTEAAWLLNCFTYLGELNRMTQFKDKSQNAGESISAGLLNYPVLMAADILLYNADLVPVGNDQKQHLELTRDIATRFNNLYSPTFKVPEPYIGKTGARIMDLQEPKKKMSKSAENKNGYILIMDPPNIIQNKINRAVTDNEGIVRYSDEQPGVKNLMNILSTATGKNVESIEKEYAGLGYSKFKKDVAEAIIAEVEPLQKEVKRYLEDKSYLEKVYKEGAQKASYV... | 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): 38118
Sequence Length: 338
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q9RWV7 | MSRVFSGIQPTGDPHIGNYFGAMQNYVRLGEQYGKQSLYCVVDLHAITNPGAFDPQTLAQKTFDMAVANFAIGLDPSKVVFFVQSHVPEHQELSWIFTCVTPVGELERMTQYKDKSAQFESVPSGLLMYPALMAADILLYKADIVPVGEDQTQHIELTREIARKFNHNFGETFTEPKAVYNKEALRIPGVDGQGKMSKSKGNTIGILEPFGDIWQKLRVAPTDPARVRRTDPGDPDKCLIGDYHKLFSPPETLETVYQGCRTAGIGCVDCKKMLMTHITEHLDPIQTRAAQLRADPDYVRDALRQGDQEARAIASEVMDE... | 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): 36866
Sequence Length: 330
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
P00954 | MTKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKSTIFVQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIAQRFNALYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDVQNKAGVSNLLDILSAVTGQSIPELEKQFEGKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKASAHASRT... | Function: Catalyzes the attachment of tryptophan to tRNA(Trp). Amino acylates tRNA(Trp) with both L- and D-tryptophan, although D-tryptophan is a poor substrate .
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 37438
Sequence Length: 334
Subce... |
Q830U2 | MKTIFSGIQPSGTPTIGNYIGAMKQFIELQNEYNCYFCIVDEHAITVPQEPQKLRQQIRSLAALYLAVGLDPQKATIFIQSEVSAHAEAGWIIQCNTSIGELERMTQFKDKSQKNGRAGVSAGLLTYPPLMVGDIVLYNADLVPVGDDQKQHLELTRDFVERFNKRYAQKNQEILTIPEVKIAEQGSRIMSLQEPTKKMSKSDTNVKGFISMLDEPAVIRKKIRSAVTDSTGVIEYNKEEKPGITNLLNIYSAATGQTVEELVQAYEGKGYGDFKADLAEAVVALLEPIQVRYQELLASEELDMILDEGAENARLVANKT... | 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): 37446
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q8RGA3 | MKRSLSGIQPSGILHIGNYFGAMKQFVDLQDSYDGFYFIADYHSLTSLTKAETLKENTYNIVLDYLAVGLDPSKSTIFLQSNVPEHTELTWLLSNITPVGLLERGHSYKDKIAKGIPSNTGLLTYPVLMAADILIYDSDVVPVGKDQKQHLEMTRDIAMKFNQQYGVEFFKLPEPLILDDSAIVPGTDGQKMSKSYNNTINMFATKKKLKEQVMSIVTDSTPLEEPKNPDNNIAKIYALFNNIDKQNELKDKFLAGNFGYGHAKTELLNSILEYFGTAREKREELEKNMDYVKDVLNEGSKKARTIAIEKIKKAKEIVGL... | 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): 36597
Sequence Length: 325
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
P00953 | MKTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQDPHELRQNIRRLAAKYLAVGIDPTQATLFIQSEVPAHAQAAWMLQCIVYIGELERMTQFKEKSAGKEAVSAGLLTYPPLMAADILLYNTDIVPVGEDQKQHIELTRDLAERFNKRYGELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNPKAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISNLLNIYSTLSGQSIEELERQYEGKGYGVFKADLAQVVIETLRPIQERYHHWMESEELDRVLDEGAEKANRVASEMVRKMEQ... | 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): 37193
Sequence Length: 328
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q9K8Y2 | MKKTVFSGIQPSGTLTLGNYLGAMKHFVSLQEDYNCYFCIVDQHAITVPQDRLKLRENIRSLAALYLAVGIDPSKATLFIQSEVPAHAQLGWMMQCVSYIGELERMTQFKDKSDGKEAVSASLLTYPPLMAADILLYHTNIVPVGEDQKQHLELTRDLAERFNKKYNDIFTIPEVQIPKVGARIMSLNDPSKKMSKSNPNPKSYISMLDDEKTITKKIKSAVTDSDGIVKFDKENKPAISNLLSIYSLCKGASIEEVEAQFVGKGYGEFKESLAQVVVDTLKPIQERYEQLIQSEELDHILDQGADKANRVARKTLEKAE... | 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): 37066
Sequence Length: 330
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
P56396 | MHKKRVFSGIQPTGQIHLGNYLGAIKHWVEMQDEYENLFCVVNSHAITLPIDPAFLKSQSYELVKLLLACGIDPKQSGLFIQSEVDEHPALAWLLNCQVSMGEMQRMTQFKDKSLKNPKSVNVGLFNYPILMASDILLYQSDLVPVGEDQKQHLELTRNIAEKFNRDFGNCFKVPEPLIAKVGARVMGLDDPKVKMSKSHQGANHAIFLLDEPDIIVKKIKKAATDSMGVIAFDEKREGIFNLLNIYMLLSNESPENIEERFKNKGYGDFKKELAEVMIQALKPIQERYKEISDDEVKAILNGGAEKARPLARATYQKAK... | 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): 36836
Sequence Length: 326
Subcellular Location: Cytoplasm
EC: 6.1.1.2
|
Q9A756 | MSAASSFKSEFLRTLEARGYIHQITHADELDTAAQGGPIVAYIGFDATAPSLHVGSLIQIMLLRRLQQAGHKPIVLMGGGTTKVGDPTGKDESRKLLSDADIQANIAGIKTVFSKFLTFGDGPTDAIMVDNDVWLSKFGYVQFLREYGVHFTVNRMLAFDSVKLRLEREQPMTFLEFNYMLMQAVDFLELNRAHGCVLQMGGSDQWGNILNGVELTRRVDQKSAFGLTTPLLATASGAKMGKTAAGAVWLNAEQLSPYDYWQFWRNTEDADVGRFLKLFTDLPLDRIAELEALEGAQINEAKKVLADEATRMAHGEEEAR... | 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): 45407
Sequen... |
Q3J3I3 | MTYHPKSDFLRVMQERGYLADCTDMQALDEALSKGVVPAYIGYDATAASLHVGHLLNIMMLRWLQKTGHKPITLMGGGTTKVGDPSFRSEERPLLTPDRIDENIEGMRKVFARYLSYGEGATDALMLNNAEWLDQLNYLDFLRDIGRHFSVNRMLSFESVKSRLDREQSLSFLEFNYMILQAYDFLELFRRTGCRLQMGGSDQWGNIVNGIDLTRRVLEGEIFGLTSPLLTTSDGRKMGKSAGGAVWLNGEMLAPYDFWQFWRNTTDADVGRFLKLYTELPVEECDRLGALQGSEINAAKILLANEVTTLLHGRDAAEAA... | 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): 45886
Sequen... |
Q9JXY5 | MSVIQDLQSRGLIAQTTDIEALDALLNEQKIALYCGFDPTADSLHIGHLLPVLALRRFQQAGHTPIALVGGATGMIGDPSFKAAERSLNSAETVAGWVESIRNQLTPFLSFEGGNAAIMANNADWFGSMNCLDFLRDIGKHFSVNAMLNKESVKQRIDRDGAGISFTEFAYSLLQGYDFAELNKRHGAVLEIGGSDQWGNITAGIDLTRRLHQKQVFGLTLPLVTKSDGTKFGKTEGGAVWLNAKKTSPYQFYQFWLKVADADVYKFLKYFTFLSIEEIDAIEAKDKASGSKPEAQRILAEEMTRLIHGEEALAAAQRIS... | 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): 47254
Sequen... |
B1ZUZ4 | MTILDDLQWRGLYADCTDLAALTQRLGQGPVTLYCGFDPTADSLHVGNLVPLLALRRFQLHGHHPIALAGGATGMVGDPSGRSAERNLLTPDQVAHNIASIKQQLGRFLDFDATTNPARMVDNSTWTAPISFLEFLRDVGKHFSVNAMLAKESVRARLESESGISYTEFSYMLLQAHDFLHLRETMNCELQVGATDQWGNITAGTDLIRKKLGAPAWGLTFPLLTKSDGTKYGKSTSGAVYLDPKRTTPYRFYQFFVQAEDADVIKLLKVLTFLSAEEITALDTDLKANPGARAAQKALARAVTTLVHGDTECANAIRAS... | 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): 45953
Sequen... |
Q8L617 | MGNCLSASTLPTEPNAPKSVEEGVKVFTVADLKKATNDFGNQMELGESLGYINPKTLSPAKKGVGMAVAVKKIYLANEQAFQDWLVDVEFLRHNSHPSLVKLIGYCYDRDMLFIVSEYFPNGSLGSYISRDSRPKSLPWETRLKISIGAAQCLAFLHSRKQAGLYRRYLTASKILLDSDFNARVSYFGKPKVSLDELVYTIGFSNVAPRYQYPPPEYILSGMSNMAGDVYSFGVILLKMLTGLGKDLTISAKREIKNKKYNIVEMIDPDLKNSYPLEAGRLMCELIKQCLEVDPKMRPTMQEVLDNLNAIAQI | Function: Together with BKN2/SZE2 and ZED1, required for effector-triggered immunity (e.g. Pseudomonas syringae effector type III HopZ1a) via the activation of ZAR1, thus being essential for resistance against P. syringae pv. tomato DC3000 expressing HopZ1a.
PTM: N-terminal myristoylation is critical for plasma membran... |
A0A411EW25 | MRHVQEARAVPAEHEARPAPVTMPANGSPYRLGAALLQSLAQEMNALAEQASALLSMPPESLSLDADAFAQIARRNVPRWHFAMLNDTERNTALMTALERGIPAGATVLDIGSGSGLLAMAAARAGAGRVFTCEMNPLLAEIARNVISAHGMSDVITVIGKPSTALDPVRDLGGPVDVLVSEIVDCGLIGEGLLPSVRHAREHLLKPDGIMLPSAARLHGRLVSSDEVLKLNQVTTAGGFDVSLMNTVATRGHFPVRLDTWPHRFLSEAAPLVEFDLARSALEPGERPLALTATADGEVQALAVWFELDMGSGITLSNPP... | Function: Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN) . Catalyzes the conversion of L-arginine to N(omega)-methyl-L-arginine (L-NMA), using S-adenosyl-L-methionine (SAM) as a methyl donor .
Catalytic Activity: L-arginine + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-... |
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