ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q83GR4 | MITKVSGFLFRTFREDPATTESRGYGFLLRAGYIRQTGSGIFSWMPLGLKVRHKIENIIRYEMGQVNAIEVLFPALFSADLFKQSGRWSEYGDDIFRLKDRRQGDYLLAPTHEEAFTQMMKEICTSYRDLPRTVYQIQDKYRDELRPRAGLLRSREFSMKDAYSFDLDEKGLRQSYEAQKRAYKKIFDRLKIDYVIVKANAGAMGGSVSEEFLHPTEMGDDTFVVTADGSAFNAEVYVTPPGPAIDYSNAPEAEDCETPGVISIPDLVNHMNSSGRFIGRVIESSDCLKCLLFRIEYAEVQNGNPSNLVVKKILERGFEYIGFLVPGDRNVDLKRAQVALSPLTIEPADNRVFECNPSFVRGSIGPGLSGVFYCADPRVSLGSSWIIGANRPGVHRIGAIAGRDFSFDCTLDVSSIKTGDKSEWGPVTVKRGIEIGHLFQLGLKYSNALGLKVLDKDGYNKAVFMGSYGIGVSRLFALIAEKNCDERGLKWPAVLAPFDLHVVLLSSARAELIDSLTDCGLDVLVDDRRVSPGVKFTDAQLIGVPKIIVIGDKTRGEDVEVWDRANDQRTVLPLKEMIQGVIQGVIQGVIQGVIQGGDTGGDTGGDTGGCTER | 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 two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Catalytic Activity: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
Sequence Mass (Da): 67793
Sequence Length: 613
Domain: Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.
Subcellular Location: Cytoplasm
EC: 6.1.1.15
|
B5ZBT9 | MAKKLEKIITRNENFADWYTSIVNNAKLIQYTDIKGMMVFQPNAWAIWEAIKNQIDLEFKKHGVRNLAMPTLIPLSEFQKEKDHIEGFAPELFMVNQIGDKKLDNPYAIRPTSEILFCNYFKNIVNSYNDLPIKNNQWCSVMRAEKTTRPFLRNAEFHWQELHAIFASEHEADEFAKTILDVYTDFVQNYLCIPVIKGLKTPWERFAGAQKTYTIEAMMQDGQALQSATSHYLGQFFAKAYDIKFQGQDNQMHYVHQMSAGLSTRIIGALIMVHADDQGLILPPDIAFNQIAILSIFANKNPQLLTISEQIRNELSDYRLFEDHSDKGVGYKLAQQEIEGTPICILVGVKELANQQVVLVRRDTHEKINVNLIDLKSTIKKLLLDIKTNIYQKAKKQLDESIVFVNSIEELKQVIAQNKMAKAFFDGSKEDDEQIKLLTNASTRCIFDETQSGQCFYTNKKTNKLTLFARAY | 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): 54320
Sequence Length: 472
Domain: Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension.
Subcellular Location: Cytoplasm
EC: 6.1.1.15
|
Q81R81 | MDYKTQFAESLSNIFTNELTQQQILDLIETPKQDEFGDAAFPCFSLAKQYKKSPAIIAKEVAEKLSDPFFTKVEAVGPYVNVFFNRDTVSDAVLKTILAEKEEYGKNYFGCEKTVVIDYSSPNIAKPFSMGHLRSTMIGNSLKHIAEKCGYEVVGINYIGDWGTQFGKLITAYKKWGNEAVVKEDPIRELFKLYVQFHEEVKDDEELEEEGRAWFKKLEEGDEEAVELWNWFRHESLKEFSRIYELLGVEFTNFQGEAFYNNLMEDFIGILEEHDLLEESEGALVVNLEEEGMPPCLIRKSDGATIYATRDLTAALYRQNTFGFDKALYVVGPEQSLHFNQFFTVLKKLGYTWVDGMEHVPFGFILKDGKKMSTRKGRVILLEEVLEEAIELAKQNIEEKNPNLKQKEEVAKQVGAGAVIFHDLKNERMHNIEFSLENMLKFEGETGPYVQYTHARACSILRKESVEFETCTFALKDDHSWSVVKLLNKFPQVIEIAFNKNEPSVISKYVLDVAQSFNKYYGNVRILEESEEKDSRLALVYAVTVVLKEGLRLLGVEAPEEM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 64470
Sequence Length: 562
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q9KEL8 | MLAQMISEELARILSLKEDEVERLLEIPPQETLGDLAFPCFTLAKTKRKAPPFIAAELEAAFLEHKEVTAKATGGYVNFFFHRETVAGQLFQEMKSNQYWQPNSGDGKRVVIDMSSPNIAKPFGIGHLRSTIIGHALYHLLKKTGYDPIRVNHLGDWGTQFGKQIAAYQRWGGDVDLKQNPIASFLELYVRFHEEAEKDESLEDEGREWFKKLEEGDEEADRLWTYFVKESLNEFDRMYNRLGVEFDYVLGESFYNDQMAPVVKELQEKGLLTCSEGALVVPLEDADLPPCLIVKSDGTSIYATRDLATAIYRHHVQKGEKLLYVVGGEQTLHFKQVFHVLKKMGYKWADQCEHITFGLLRLDGKKMSTRRGRVVMLEDVLNDVVAHAKAKIKEKHPNHPHLHEVAEAVGVGAVIFGDLKQDRRLDVNFRLEDALSFEGETGPYVQYTYARIQSILRKGDKLNDSRHMDWQHVTKDEGWSLLKVLIQYPNVLIKATEAREPHQLARYVLTVSKKFNQFYHKYVILADDETVRQARLILAERTGEVIADAMAVLGVKTPEEL | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 64133
Sequence Length: 561
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q52400 | MPITNTDESLSAASAPLKPGAFLHEIFSDRARQFPERTAVSDAARTLSYAQLDALSTKLAARLRDEGVTYGTRVGMYLPRSVDLVTSLLGILKAGGTYVPVDPQYPGKRVEHIVRDSELSLIIGDAANLPKISSLRVLALDELLSAPALQPAAQDTRIDPNNSTAYIIYTSGSTGEPKGVQVSHGNVSRLLESTQRAYGFNAQDVWSMFHSIGFDFSVWEIWGALAHGGQVAVVPYDISRSPAALRQWLADQRITVLSQTPSAFRGLDEADRGNTAPLALRYVVLGGEALPASVLRPWVERHGDQKPALINMYGITEATVHTTFKRVLAQDLETAAMVSLGKPLDGWRLHLLDANQAPVAAGTTGELYIEGAGVAQGYLNREALNVERFVELPGAVRAYRTGDLMTLESNGEYRYAGRCDEQLKISGFRIEPGEIEASLQTSPSVAAAHVGVHDYGDGDLRLVAYVVPGQGVDAWTEQARSEVAALMAENLPGYMRPSVYVPLAELPVTHHGKIDKQQLPSPAAGTALSGAADVKGLSEQEHFVLKVWSEDLGLKNIGVNDDFFDSGGTSLALIRSLSKLKTHYKINLDPGILADGATAKVLADHITRSLVQAH | Function: Involved in the biosynthesis of syringomycin E, a cyclic lipodepsinonapeptide toxin with phytotoxic activity . Specifically adenylates L-threonine and loads it onto its peptidyl carrier domain, via a thioester linkage to the phosphopanthetheine moiety . Is highly specific for L-threonine .
Catalytic Activity: ATP + holo-[peptidyl-carrier protein] + L-threonine = AMP + diphosphate + L-threonyl-[peptidyl-carrier protein]
Sequence Mass (Da): 66144
Sequence Length: 614
EC: 6.2.1.70
|
Q3J281 | MNLFTEIRTLVTAELGAMTEAGDLPAGLDLSAVAVEPPRDPAHGDMSTNAAMVLAKPSGKPPRTIAEALATRLAADPRISSAEVAGPGFLNLRLRPAVWQGMVATILQAGDTYGRSTIGAGQKVNVEFVSANPTGPMHVGHVRGAVVGDALARLLAYAGWNVTREYYINDGGAQVDVLARSAFERYREAHGLEPEIREGLYPGDYLIPVGEALKAKYGDSLLDKGEQHWLTEVREFATEMMMQMIREDLAALGVEMDVYSSEKALYGTGKIEAALDRLKEMDLIYEGVLEPPKGKTPEDWEPREQTLFRSTAHGDDVDRPVKKSDGSWTYFAPDIAYHYDKVTRGFDQLIDIFGADHGGYVKRMKAAVAALSAGRVPLDIKLIQLVKLWKNGEPFKMSKRAGTYVTLRDVVEQVGTDVTRFVMLTRKNDATLDFDFDKVLEQSKENPVFYVQYANARINSVLRKAREQGMDVSDATLATADLDRLDHPAEIALIAKLAEWPRLVEIAARTNEPHRVAFYLHELASELHGLWNRGNDEAGLRFLQDDPVVSQAKIALARAVGVVICAGLGILGVTPVEEMR | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 63685
Sequence Length: 580
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
A9WEH7 | MRYALERFISDIQAAIVATGKVPADLIEITTPKPNIPADRTFVTFKAAKALGVDPVRLAADLATAIVPPPDSLIGEVTATGAFLNFTLHPQRLAAAVMAEIETYGDAYGSVADGANRTVVIDYSSPNIAKRMHVGHIRSTIIGQALVHIFRALGYRVIGDNHLGDWGTQFGIILAAMQRYGRPQNEGEAAMAELEALYARYNAEMKDNPPLEDEARRWSLALEQGDPTARELWQWCVDLTMRAAQRNYDRLGVRFDYAYGESFYEAMLPGVIEEALQSGAAFRDVDGAVVAELDKLPRFIVQRSDGGTVYITRDIATIKFRLQEFNPSHIIYVVDARQELHFRQLFAIVRAMGYALDVELIHVPFGVITTPDGQPLSTKKGNMVYLESLLDDAVARARALVDAKSPTLSPEERAQIAEAVGIGAVIYNDLYQDPRRNITLDWDRMLSIEGNSAAYLQYSHARCRSILRRAAEEGMLSTEVDPGLLTHPSEQRLVRHLARLPEAVREAGARYAPFVIADWCYTTAREFGIFFEQCPVLRAETPALRAARLQLVSATANALRNGLALLGIQAPERM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 63529
Sequence Length: 574
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
A0Q5D7 | MNIENYLSETLAKVFQKLGYAESFAKVVTSTREDVGHFQCNGAMPLAKFAKKPPLAIAEEIVEHIDAEDIFAKLEVAKPGFINITLAPKFLADTTNRFLNSNKFGVQNNLPNRKVVLDFGGPNVAKPMHVGHIRSALLGDALQRIHRFCGDTVVSDVHLGDWGTQMGMLIEEIKLQSPQLVYFDENYTGEYPTESPVTVQELAEIYPRASKRCKSDINEMEKARLATFELQQGRRGYVALWQHFVRISIDAVKKDFDSLDVHFDLWLGESDANKFIDEMISYFQANNFIYEDEGAWVIDTNKDGVPPLIVIKKDGGVMYGTTDLATLWQRSKDLDPDEIIYVVDKRQSLHFKQVFSVAERTKVVSEKCKLKHVAFGTVNGKDGRPFKTREGGVMHLADLISQAKEYAKNRMPDENDDSIIDQIAMATIKFGDLINNYANDYFFDLEKFAQHEGKTGPYLLYTAVRAKSILRKIFGDNYDIKSLAKDYKVVNAHNEYEEKLQLQLIQFPIAVQRAYENSQPHHICEYAYSLANSFNKFYVNCPITNLDDESLKKARIALCMATVKAMTIASDLIGISIPERM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 65856
Sequence Length: 581
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q8RG14 | MKITSRELTDIFQKHVENLFPNKELKPVEITVATNENFGDYQCNFAMINSKIIGDNPRKIAEEVKNNFPYGDVIEKLEVAGPGFINIFLSDKYISNSIKKIGEDYDFSFLNRKGKVIIDFSSPNIAKRMHIGHLRSTIIGESISRIYRFLGYDVVADNHIGDWGTQFGKLIVGYRNWLDKKAYKKNAIEELERVYVKFSDEAEKDPSLEDLARAELKKVQDGEEENTKLWKEFITESLKEYNKLYKRLDVHFDTYYGESFYNDMMADVVKELVDKKIAVDDDGAKVVFFDEKDNLFPCIVQKKDGAYLYSTSDIATVKFRKNTYDVNRMIYLTDARQQDHFKQFFKITDMLGWNIEKYHIWFGIIRFADGILSTRKGNVIKLEELLDEAHSRAYDVVNEKNPNLSEGEKQNIAEVVGVSSVKYADLSQNKQSDIIFEWDKMLSFEGNTAPYLLYTYARIQSILRKVAELNIGLNENIEIKTENKIEKSLATYLLAFPISVLKAGETFKPNLIADYLYELSKKLNSFYNNCPILNQDIETLKSRALLIKKTGEVLKEGLELLGIPILNKM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 65719
Sequence Length: 569
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q74C63 | MKDAVRDLVREALERSFADGTLASGHVPDIVVEKPALEEHGDFACTAAMLMAKAEKKAPRAIAEIIITHLNDRESLVESVEIAGPGFINFRMRTSAWCRVLRRIEREGGDYGKSEAGAGKKVQVEFVSANPTGPLHIGHGRGAAIGDTICRLLAAIGWDVTREFYYNDAGQQIANLALSVQARCLGVEPGGPLWPTDGYQGEYIKDVARSYLNRETVDAGDQHVTAAGDPHDVEAIRRFAVAYLRREQDQDLRAFDVGFDVYFLESSLYAEGRVDDVVQRIIAKGHAYEQDGALWLRTTEFGDDKDRVMRKSDGSYTYFVPDVAYHLNKWERGFIRVVNEQGADHHSTITRVRAGLQALDAGIPKGWPEYVLHQMVTVMRGGEEVKISKRAGSYVTLRDLVDEVGRDATRFFFLMRKPDSQLVFDIDLAKQQTLENPVYYVQYAHARICSIFENAADKGVVPPTVDQASLESLGTPEELTLVKLLSSFPEIVEGSALNFEPHRITYYLQELAGAFHSFYNKNRVITEDADLTGARLLLLHSTATVIRNGLGLLGVSAPEKM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 62308
Sequence Length: 561
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q7NDF6 | MTALSLQQQLAESIYTALGTAFEAGQLGQLTQLPPRQSVVVEKPKVPEHGDYATPVAMSLAKPCRLAPLAIAEAIASYLASDEIGVEVAKPGFINLRLGHRFVAVELQNILELKGDYGRTVPQQPERILLEFVSANPTGPLHLGHGRWAALGSSLERILQFAGYTVDSEFYINDAGNQMQLLGLSLKQRYLQVLGEAVELPDGGYKGSYLKELAEQLVADKGDSLGGEPVEWFSAYAEGRLLEQQKITLQQFRTEFDRWYSERSLHCAGAIEAALADLEARGMLYRAARSRQEQSGEITGRSKKVQAPAAFEEEDGGGEALFFKAADFGDEMDRVVKRADGNTTYLAADIAYHWDKYQRGYGRLINIWGADHHGYVPRMKAVAQALGHPADSLEILIGQMVRLFKTNPETGQKEEMRMSKRRGELVSVDDLIEEVGVDAGRWFLLSQSLNTTVNFDLDLAQSEKFDNPVFYVQYNHARCCSILRKAPERGMPILERFEFLKPDGGLWLETPQERTLALRLLAAPDEYRFAAVDRTPQRLTQYAYDLASDVSQFYEHCPILPPLAENLEPALRYARLGLVVATRQVLATTLTLLGIEPRESM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 66957
Sequence Length: 601
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q8PX74 | MFLELKAQATSILKEAIRKAGFEVEDSELQFETSPHADLASRAAFRLAGIHRQNPKDLASRIVSAVEIPEGSFIGKVSAAGPYINFFAGKHYLNGTVNAVLKEKEKFGCGAPKDRILLEHTSANPNGPLHVGHIRNSIIGDTLARILRRAGYDVEVQYYVNDMGRQIAVVSWACERFELDLSRKSDSAIADVYIKANVELDKNPGYIKEIDALMEKVEAGDVRTIEHFDKAVSLAVAGIKETLLRLNVAHDKFVSESTFLKSGAVHDIVERIKATGRTKTDKGALVVDLSDYGFEKTLVIQRSNGTSLYTTRDLAYHEWKAGQADRIIDVFGADHKLISGQLRATLNAIGVKEPEVVIFEFVSLPEGSMSTRRGQFISADDLFDRVTGAAFEQVETRRPETSYEFKKQVAEAVGLGAVRYDIVRVSPEKSTVFNWKEALDFEKQGAPYIQYSHARACSILEKAKEEAAWNPDKEIDPSLLVEDSEIDLIKKMAMFDSVIDLGARELKPHVLAIYARELADAFNQFYRFVPVIAAEDENVRAARLALVDCARVVLANSLDTLGIIAPESM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 63055
Sequence Length: 569
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
O27496 | MFRYIEKEARDSITAALEKLGIKVPPEIKLEEPPNPQLGDLASTVSFELAGKLRRAPIEITADIMSVIETPEIFETIESKGPYINFFVDYGRFSSRLLESIQDDYGSHPPRDERVILEHTSANPNGPLHIGHIRNAIIGDSLARILRMAGYDVETQYYVNDMGRQIAMIVWGLLNLDGDLEDYPGDKMDHRVGKLYFEVNQRLKENPGIRDEVDELIRKYEAGENEELFRKVVEYCLSGMEETMKRLHVHHDRFVWEGQFVRDGTVDRVIESLRKTGYTGENDVLYLDLEEFGLEKELVLTRSDGTSLYSTRDIAYHLQKSEEGDVIIDVLGSDHKLAAEQVGIAVELLGGKRPEVIFYEFITLPEGSMSTRRGVFISVDELMDEAHSRALHEVKKRRDLPDDVADDIAESIGNGAIRYYIARLSPEKHIVFRWDDALSFERGCASIQYAHARACKLLEKASFTGEEDIEDGWKPEGDERELVRLLARFPVVVEESALARRVHPVAQYAQDLANTFNSFYRSTPVIGSDFEGARLRLVDSVRKTLRNALNLLGIHAPETM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 63648
Sequence Length: 560
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q9HUC8 | MKDTIRQLIQQALDQLTADGTLPAGLTPDIQVENTKDRSHGDFASNIAMMLAKPAGMKPRDLAARLVEAIPAHEQLAKVEIAGPGFLNFFQDHVWLAASLDRALADERLGVRKAGPAQRVVIDLSSPNLAKEMHVGHLRSTIIGDAVARVLEFLGDTVIRQNHVGDWGTQFGMLLAYLEEQPVDAEAELHDLEVFYRAAKKRFDESPEFADRARELVVKLQAGDPDCLRLWTRFNEISLSHCQKVYDRLGVKLSMADVMGESAYNDDLAQVVADLTAKGLLTEDNGALCVFLEEFKNAEGNPLPVIVQKAGGGYLYATTDLAAMRYRHNVLHADRVLYFVDQRQALHFQQVFEVARRAGFVPAGMELEHMGFGTMNGADGRPFKTRDGGTVKLIDLLEEAESRAYALVKERNEQRAERGEEPFDEVQLREIGRVVGIDSVKYADLSKHRTSDYSFNFELMLSFEGNTAPYLLYACTRVASVFRKLGQGREQLGGKIVLEQPQELALAAQLAQFGDLINNVALKGVPHLLCAYLYELAGLFSSFYEHCPILTAEDPAQKDSRLRLAALTGRTLEQGLELLGLKTLERM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 65199
Sequence Length: 587
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
B8HB09 | MTPEELSLAISACLKDAVAAGEIALAESAVPEDVRVERPKNRDHGDWATNIALQLAKQAGTNPREFATILSARLKTISGVSAVDIAGPGFLNITVDAAAAGALAKAIVEAGTQYGTNTALAGHTVNMEFVSANPTGPLHIGHTRWAALGDAIARVLRASGADVTAEYYINDAGSQMNTFANSVYSRLHGLPVPEGGYPGQYIADLGHEVLTAHPDIRELTEVAALPVIRAAAYEAQMKDIKATLADFGVAFDVFFSEQELHDAGAIESAVARLREQGHVFDDGGAVWLRTTDFGDDKDRVMIRANGEPTYFAADAAYYLSKKDRGYTEKIYLLGADHHGYIHRLKAIAAAAGDDPEVNIEVLIGQLVSVNGAKLSKRAGNIIELKDLIDWLGKDAVRYSLARFPADSPLTLDPELLKKNSNENPVFYVQYAHARSRGAARNAVAAGVERQVDGADSFDASLLDHATENELLSYLGSYPSIVAKAAELREPHRVARHLEAIAGAYHRWYDACRIAPMGEEAVTDVNRTRLWLNDATSQVLANGLDLLGVSAPERM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 59517
Sequence Length: 554
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q3IHI4 | MNIRTILVEKAIAAMTTVGLPADTNPAVTQSTRPQFGDYQINAAMGAAKKMKSNPRELAQKIIDNLDVSDIAEKTEIAGPGFINIHLKPEFLAQSVKAANSDAKLAVNEHANPQKVVVDYSSPNLAKEMHVGHLRSTIIGDAIVRALEFRGDSVVRQNHMGDWGTQFGMLIAHLEDQISQGVDLDTVALADLETFYRDAKKRFDDEEGFADKARNYVVKLQGGDAHCEKLWKLFIATSVKHSEEVYKRLNVTLTQADIMAESAYNAELNDIISLLKDKNIAVESQGAQVVFLDELANKDGEPSAFIVQKSGGGFLYATTDLAACDYRSNKLGADRILIFVDARQSLHFNQVELTARKAGFLRDETSYEFCPFGTMMGADNKPFKTRTGGTVKLADLLEESINRAAIKLAERESDLSEQERSEIARKVGIGAVKYADLSKHRTSDYIFNWDSMLSFEGATAPYLQYAYTRIRSIFRKSGVDAATLNSNVTIVEPQEKALALKLLQLEEVLDLMITEATPHVLCGYLYELASLYMTFYEACPVLKEGVEPNVRDSRLVLCNLVSKTLETGLDLLGIEVMEQM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 64218
Sequence Length: 580
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q9WX29 | MASVTSLSDSVQQHLASALTATRPEAAGADPLLRRSDRADYQANGILALAKKTKANPRELAAEVVARITTGDELIEDVEVSGPGFLNITVADRAITANLAARLADGERLGVPLKQDAGTTVVDYAQPNVAKEMHVGHLRSAVIGDALRSMLDFTGEKTIGRHHIGDWGTQFGMLIQYLFEHPGELAPAGDIDGEQAMSNLNRVYKASRAVFDTDEEFKERARRRVVALQSGDKETLDLWQQFVDESKVYFYSVFEKLDMEIRDEEIVGESAYNDGMPETARLLEEMGVAVRSEGALVVFFDEIRGKDDQPVPLIVQKADGGFGYAASDLTAIRNRVQDLHATTLLYVVDVRQSLHFRMVFETARRAGWLGDEVTAHNMGYGTVLGADGKPFKTRAGETVRLEDLLDEAVQRAAEVVREKARDLTEDEIQERAAQVGIGAVKYADLSTSPNRDYKFDLDQMVSLNGDTSVYLQYAYARIQSILRKAGEVRPAAHPELALHEAERALGLHLDAFGPTVFEAAAEYAPHKLAAYLYQLASLYTTFYDKCPVLKAETPEQVENRLFLCDLTARTLHRGMALLGIRTPERL | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Sequence Mass (Da): 64704
Sequence Length: 586
Subcellular Location: Cytoplasm
EC: 6.1.1.19
|
Q6AH61 | MIDPVLLREHPDVLRRSQEARGDSVQLVDEALQVDIERRAAITAFEELRAEQNAFGKRVAQAPKQEKKELVAQAQQLAGRVKEAQQVAAAAEARFESVLRKIGNPVVAGVPSGGEDDYAVLKEVGGIPAFGFEPRDHLALGELLGAIDMARGAKVSGARFSFLRGLGARLEIALMNLALDKALANGFVPLITPTLVKPEVMQGTGFLGEHSDEVYHLETDDLYLTGTSEVALAGYHADEILDVTEPLRYAGWSTCYRREAGSAGKDTRGIIRVHQFTKLEMFVYTLPEHAEAEHARLLAWQEEMMQALGLSYRVIDTAAGDLGSSAARKYDVEAWIPTQGRYRELTSTSNCGTFQARRLETRYRTESGKTAPVATLNGTLATTRWIVAILETHQREDGSVLVPETLRPYLGGLEILEPIGK | 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): 46163
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
|
Q72LS1 | MLDLRYITENTEDLKKVLELRGFKEIGIIDELKSIIQRKREFQKEADILREERNKASKEVGKIKQSGGDITKISASVKLVGEKIKEIESKLEQEENALLNINLGLPNILDPKVPPGKSEHDNIVQYEVGKIPTFQFVPKTHFEIGEALHWIDFEKGVKLSGARAYTYWKDGARLERALMNFMLDVHTKEHDYTEVWVPSMVNDESMMATGQYPKFKDEFYRIDKDELNLIPTAEVPLTNLYRDEIIPEDQLPISVTAHTSCFRREAGSYGKDTRGLVRVHQFQKVELVKFCKPEDSEEEHKKMLSHAENILKKLELPYRVIILCSGDISANSSITYDIEVWMPGLNRYMEISSVSNFRDFQARRGKIRYKSKDGKNQLVHTINGSGLALGRTYAAILENFQNEDGTLRIPEVLKSYF | 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): 48020
Sequence Length: 417
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
|
Q8ZTP4 | MSYSVLEALRNSPDVVRKVLTARRMDASLVDKFLELDEKWRRLKKEVDELRHEYNKLSKEGAKAPPERRREIADKARELAARLERAEKELEETERAREEVLWSFPNLIHESVPICPEGVDSIPVRHWGVVKTTKDVVDKLDKGVDYLVVEKAPVGHADMAEVVLKMADTLKAGEVAGSRFYYLFDDLVWLDFALAMYALDYLAQKGFRPVIPPYMLKYDLIRRVLDFDTFKDAIYKIDGEDLYLIATAEHGIAAYLYKRELLEEELPQLYVGWSPCFRKEAGAGSRDIKGIFRVHIFHKVEQFVFSLPEDSWKWHEEITKNTEELIRGLGLPYRVVNICAHDLGAPAAKKYDIEVWYPSQGMYRELASCSNVTDWQSYRLGIRVTRKGMKREYVHTLNCTGLATTRTITAILENFQREDGAVEIPKVLRQYLEPIKAAPKDYILPKAAKSP | 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): 52031
Sequence Length: 451
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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O58441 | MLDIKLIRENPELVKNDLIKRGELEKVKWVDEILKLDTEWRTKLKEINRLRHERNKIAVEIGKRRKKGEPVDELLAKSREIVKRIGELENEVEELKKKIDYYLWRLPNITHPSVPVGKDENDNVPIRFWGKARVWKGHLERFLEQSQGKMEYEILEWKPKLHVDLLEILGGADFARAAKVSGSRFYYLLNEIVILDLALIRFALDRLIEKGFTPVIPPYMVRRFVEEGSTSFEDFEDVIYKVEDEDLYLIPTAEHPLAGMHANEILDGKDLPLLYVGVSPCFRKEAGTAGKDTKGIFRVHQFHKVEQFVYSRPEESWEWHEKIIRNAEELFQELEIPYRVVNICTGDLGYVAAKKYDIEAWMPGQGKFREVVSASNCTDWQARRLNIRFRDRTDEKPRYVHTLNSTAIATSRAIVAILENHQEEDGTVRIPKVLWKYTGFKEIVPVEKKERCCAT | 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): 53255
Sequence Length: 455
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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Q98LC8 | MLDIKWIRDNPKALVEALAKRSWSAGEAQSTVDDLIARDEARREHVTELQTKQERRNAASKEIGNAMRSGDAALAEKLKAEVGDIKTFIQNGEARERELDKALTDALAVLPNVPLDDVPVGKDEHDNVVKHIVGKVPTRSNWVKEHFEIGEALGMMDFERAAKLSGSRFTVLKSGLARMERAIGQFMLDLHTTEHGYEEVIPPLMVRDEVLFGTNQLPKFEEDLFFTPHGEGRLGLIPTAEVPLTNLVREEITAHEKLPLRFTALTPCFRSEAGSAGRDTRGMLRQHQFYKVELVSITDQDSSLAEHERMTQCAEEVLKRLELPFRTMVLCTGDMGFGARKTYDIEVWLPGQNAYREISSCSVCGDFQARRMDARYKDKDGKGNRFVHTLNGSGTAVGRALIAVIENYQNEDGSVTIPEVLRPYMGGLAKIEAK | 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): 48549
Sequence Length: 434
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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Q7UXX6 | MLDRKFILQNAQLVAENSAKRGVSVDVDAICRLEAERMDALKQAEELNRQANEVSKQIKSAKDNDERQELIAKGRSLREQKDAAGAAQDRLEAEILELQTILPNMTHPDVPEGGEHDANEIGRGKTPVPEMDFQPLDHLQLGEKHDLFDFEGGARVAGSGFYFLRNAAVRLDLALQQFAISHLAGKGFTPVSTPDLALTSVLQGTGFNPRGPETQIYSIENTELNLVATAEIPLGGMLSGQILASEELPLRYCGLSHCFRTEAGAAGRASKGLYRVHQFTKVEMFAFTLPDQSTAMHEEMRELECEIFDALEVPYRVIDTATGDLGGPAYRKYDLEAWMPGRGESGDWGEVTSTSNCTDYQARRLNVRSKSNTQKGTDFVHTLNGTAIATGRAMIAILENHQRADGTINVPEILRPWVGCDVLKCE | 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): 46901
Sequence Length: 426
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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Q7MLV2 | MLDSKLLRTELDETAAKLARRGFKLDVETIGKLEEQRKSIQVEVENLQSTRNSISKQIGQLMSAGDKEGAEKIKQQIGSLGSDLDVKKIELDAVMAQLDDIILSVPNIPADEVPNGKDENDNLEISRWGEPKSYDFELKDHVDLGEMGDGLDFASAVKITGARFIVMKGQFARLHRAIAQFMLDLHTEEHGYTEMYVPYLVNADSLFGTGQLPKFGKDLFHTEPLTEKASDEEPRKLSLIPTAEVPVTNLVRDTISDEADLPLKMTAHTPCFRSEAGSYGRDTRGLIRMHQFDKVELVQITKPEDSMNALEELTGHAEKVLQLLELPYRKVLLCTGDMGFGSHKTYDLEVWVPAQNTYREISSCSNMWDFQARRMQARFRRKGEKKPELVHTLNGSGLAVGRTMVAILENNQEADGRIAIPTVLQKYMGGATHIG | 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): 48674
Sequence Length: 435
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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Q8D265 | MIDHKLIIKNIEEVCKKLILRNFYLDKKKILLQDQKRKILQIEVEKLQNKRNLQSKIISKIKINNKNIDIYKNKSNKINILLNEKKQKLKKIKKEIDNYLSTIPNILDEKVPIGKDQKNNIEVKKWGSPKIYNFKIKSHVEIGEKIKYLDFSRSAKISGSRFVVMKNKISYMHRALSQFMLNLHTNQHGYEEYYVPYLVNKNMLYGTGQLPKFYNDFFYAKSFFEDIQSCYALIPTAEVPLTNLMRNEIIDENYLPIKMTSHTPCFRSEAGSYGKDTKGLIRMHQFDKVEIVQIVSPENSIKALEEITHHAERVLQLLDLPYRKILLCSGDTGFSSCKTYDLEVWMPSRNKYIEVSSCSNTSDFQSRRTKIRYRKISNKEIHLTHILNGSALAISRTLASIIENYQTKEGNIKVPKILQPYMDGLKLIK | 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): 50213
Sequence Length: 429
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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Q7M9J5 | MIDLKLLMNDFEEVAERLAKRHLEADFLEQARLLAGQYKAKKRESEELQAEQNAKSKLFGQYKKEGKEIDSLKAELDTLKIRLSEILPEVSVLERELESLALIIPNLPDEKTPIGRDEHDNIEIRRVLEPKMFDFRPKEHWELAEQNGWIEFDRGVKLAKSRFSVLRKEGARMSRALISYMLDFNHSRGFEEVVTPVIVNRETLLGTGQLPKFENDLFKISEVIEEEQGGEKGRGHELYLIPTAEVTLTNLYRDEIIPHDELPLLLTAHTPCFRKEAGSAGRDTRGIIRQHQFDKVELVALTKPEESDAIQQKMIDCASDLLSSLGLPHRLVQLCGGDLGFGASNTVDIEVWLPGQNCYREISSISNTRDFQARRAMIRYKDEDKKNRLVHTLNGSSLAVGRTLVAIMENYQNADGTIEIPEVLRRYL | 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): 48948
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
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O67583 | MEKIKVKIKGKEYEVEKGTPLGKIFELAGIKDALGGVINGKIIDLQTPVRESGEIKPVYRGSKESLEIMRHSLAHIMAQALKELYGAKKVHLGVGPTTEEGFYYDVEVEGHKITEEDLPKIEQKMKEIIERDYPILRRELSREEAIKLFDKLKEKYKIDIIKEIPEEEVISVYEQGDFIDLCKGPHLPSTGKAGAFKLTSISGAYWKGRSDQPQLTRIYGIAYWSDKEVKERLKFYEEVKKRDHRRLGKELEFFTIDDNVGAGLILWLPRGAIYRKVLEDYLREEHLKRGYQLVYTPHVGKSKLWETSGHLECYKQNMFPSMKIDEEEYYVKPMNCPFHIAIYKSRTRSYKELPLKLFELGTVYRYELSGVLHGLLRVRGFTQDDAHIVCTPEQVNDVIRETLDFALSTLKDFGFNEFKIYLSTRPEYSIGSDEQWEVSQNALKKAIEDLGYEYEIDEGGGAFYGPKIDVKIRDAIGRMWQLSTIQFDFNLPERFDMTYVGPDNKKHRPYMIHRALLGSIERFTGILLEHYAGLLPIWLSPTQVMIIPIADRHHEYAKKVYEFLKENGIRAEMDLREERMNAKIRDAELKKIPVILVVGDREAQNNTVSVRTKKEGNLGSMELNKFLDWIKEKIKNKE | 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): 74097
Sequence Length: 638
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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Q5P7X5 | MPNITLPDGSVRSFDHPVTVSEVASSIGAGLAKAALAGKVDGRLVDLSYRIEADTPLAIVTEKGDEGLDVIRHSTAHLLAHAVKELFPEAQVTIGPVIENGFYYDFAYKRPFTPEDLEKIEKRMAELARREIPVSREVWPRDKAVEFFKSQGEHYKAEIIASIPQAEDVSLYRQGDFIDLCRGPHVPSTGKLKVFKLTKVAGAYWRGDSKNEMLQRIYGTAWAKKDDLENYLHMLEEAEKRDHRKLGRLLDLFHIQEEAPGMVFWHAKGWTLWQQVEQYMRRTILDNGYQEVKTPQIVDRSLWEKSGHWDMYSELMFTTQSEKRDYAVKPMNCPCHIQIFNQGLKSYRDLPLRMAEFGSCHRNEPSGALHGIMRVRNFVQDDAHIFCADEQVQTEAAAFIELLQKVYADFGFTEILIKLSTRPDKRVGTDDQWDAAEAALAAALDAQGLAYDLQPGEGAFYGPKIEFSLKDCLNRVWQCGTLQLDFNLPVRLGAEYVAEDNAKHYPVMLHRAILGSLERFIGILIEHYAGALPLWLAPVHAVVLNISEGQTDYATEVARRLKQAGFRVEADLRNEKINYKIREHSVHKLPYQIVIGEKEKAAGVVAVRARGGQDLGQMPLDTLIERWQREIEARSGSI | 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): 72346
Sequence Length: 638
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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A0JXC7 | MSDAQQITLIVDGEETKVTTGTTGAELFFERRDVVVARVNGELKDLDQPLPEGADIEGVTIDSPDGLNVLRHSTAHVMAQAVQQLRPDAKLGIGPYITDGFYFDFDVAEPFTPEDLKALEKMMLKIINQNQKFVRRVVSEDEAREAMKNEPYKLELLGKKNNAADAGEGVNVEVGAGDITIYDNVDRKSGDSVWCDLCRGPHLPNTKLISNAFALTRSSAAYWLGNQNNQQLQRIYGTAWPTKDALKAYQERIAEAERRDHRKLGAELDLFSFPDELGSGLPVFHPKGGIIRKAMEDYSRQRHVDAGYDFVYTPHITKGHLYEVSGHLDWYKEGMFPAMHIDAELNEDGTVRKPGQDYYLKPMNCPMHNLIFRSRGRSYRELPLRLFEFGSVYRYEKSGVVHGLTRVRGMTQDDAHIYCTREQMKDELTTTLNFVLGLLKDYGLDDFYLELSTKNEDKFVGDDATWDEATRTLAEVAEASGLELIPDPGGAAFYGPKISVQAKDALGRTWQMSTIQLDFNLPERFELEFQAADGTRQRPVMIHRALFGSVERFMGVLTEHYAGAFPAWLAPVQVVGIPVAEAFNDYMFDVVDQLKAVGIRAEVDISSDRFPKKIRTASKDKIPFVLIAGGEDAEAGAVSFRFRDGSQDNGVPVAEAVQRIVEAVRNRTS | 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): 74930
Sequence Length: 669
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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B6YQ95 | MIKITFPNTSARNYAIGTTPMQIAESISCRLAEEILSANVNGEMWDLSRPINENASVKLYKWEDFEGKRTFWHSSAHLLAESLQELYPNIHFGMGPAIENGFYYDVDLGDGVVIKDVDLVTIEKKMQELASKKLSISRQNVTKQNALELFGKKGETYKIELISKLEDGKITVYTQGNFTDLCRGPHLPNTSYIKAIKLTSVARAYWKGDESRKQLTRIYGISFPKKEELSEYLALMEKAKKRDHRRIGKEMELFTFSHKVGRGLPLWLPKGTQLRLRLEDFLKRIQKKYGYQQVITPHIGNKTLYIASGHYAKYGKDSFQPIHTPELGEEFLLKPMNCPHHCEIYKAFLRSYKELPLRLAEFGTVYRYERSGELQGLTRVRGFTQDDAHIFCSPEQVKEELIKVIDIVRVIFCALNFNDYEVQISLRDLNNRIKYIGSEENWKNSEGAIIEVCQEKKIKAKIKLGEAAFYGPKLDFMVKDALGRNWQLGTIQVDYNLPERFELEYVGADNQKHRPVMIHRAPFGSMERFVAVMIEHTGGKFPLWLVSDQVVILPVSENYNQYAEEIAKEFHKRDIRVTIDKRNEKVGRKIRDNELKKIPYLLIIGEKERRNSEISVRKHGKENIGIMKVTEFAEFLKKEVERQMSQWQ | 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): 75185
Sequence Length: 648
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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Q8AAP2 | MIKITFPDGSVREYNEGVNGLQIAESISSRLAQDVLACGVNGETYDLGRPINEDADFVLYKWDDEEGKHAFWHTSAHLLAEALQELYPGIQFGIGPAIENGFYYDVDPGEAVIKESDLPAIEAKMLELSAKKDAVVRESISKTDALKMFGDRGETYKCELISELEDGHITTYTQGAFTDLCRGPHLMTTAPIKAIKLTTVAGAYWRGHEDRKMLTRIYGITFPKKKMLDEYLVLLEEAKKRDHRKIGKEMQLFMFSETVGKGLPMWLPKGTALRLRLQEFLRRIQTRYDYQEVITPPIGNKLLYVTSGHYAKYGKDAFQPIHTPEEGEEYFLKPMNCPHHCEIYKNFPRSYKDLPLRIAEFGTVCRYEQSGELHGLTRVRSFTQDDAHIFCRPDQVKDEFLRVMDIISIVFRSMNFQNFEAQISLRDKVNREKYIGSDDNWEKAEQAIIEACEEKGLPAKIEYGEAAFYGPKLDFMVKDAIGRRWQLGTIQVDYNLPERFELEYMGSDNQKHRPVMIHRAPFGSMERFVAVLIEHTAGKFPLWLTPDQVAILPISEKFNEYAEQVKMYLKMHEIRAIVDDRNEKIGRKIRDNEMKRIPYMLIVGEKEAENGEVSVRRQGEGDKGTMKYEEFAKILNEEVQNMINKW | 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): 74553
Sequence Length: 646
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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Q728R5 | MNVSIEGQMLEVASGASCGDALKGALSGKKFKNVLACRLDGGLVDITATVPDGTTTIEPVYADSPEGLDLIRHSTAHIMACAVKRLFPAAKVTIGPSIDNGFYYDFDAERPFSPEDFEAIEREMQKIVDAATPFERSEMPRDEAVALFEGMGETYKVEIIRDLPNDTVSLYRCGEFVDLCRGPHIPHAGFAKAFKLMSVAGAYWRGDEKNPMLSRIYGTAFADAKTLKEHLHRIEEAKRRDHRKLGQQLDLFAFHEDVAPGMVFWHPKGMLVRTIIEDFLRKEHLKRRYDIVQGPQLLRRELWEKSGHYDNYRENMYFTEIDENAYGVKPMNCLAHMLIYRSAIRSYRDLPKRFFELGVVHRHEKSGVLHGLLRVRQFTQDDAHIICRPDQLEDEIIDVIALVRDLMNLFGFDYKVAVSTRPEKSIGSDEAWELATNALVKAVERAGIPYTINEGDGAFYGPKIDVRLMDCIGREWQCSTIQCDFTLPERFDLVYVGQDGERHRPVMVHRAILGSLERFIGVLIEQYAGAFPAWLAPVQARLLTVTDAQNEFVESARAALAKAGIRVEADVRNEKLGYKVREAQLEKIPYILVVGDKEVEAGGVNVRLRTGENLGLKSLDEVVSLLESDCQEPFKRGGMSYSFS | 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): 72664
Sequence Length: 644
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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Q8XE27 | MPVITLPDGSQRHYDHAVSPMDVALDIGPGLAKACIAGRVNGELVDACDLIENDAQLSIITAKDEEGLEIIRHSCAHLLGHAIKQLWPHTKMAIGPVIDNGFYYDVDLDRTLTQEDVEALEKRMHELAEKNYDVIKKKVSWHEARETFANRGESYKVSILDENIAHDDKPGLYFHEEYVDMCRGPHVPNMRFCHHFKLMKTAGAYWRGDSNNKMLQRIYGTAWADKKALNAYLQRLEEAAKRDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQEVKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIFNQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEEQIRDEVNGCIRLVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADLAVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPSRLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQVVIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVPYMLVCGDKEVESGKIAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLEE | 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): 74028
Sequence Length: 642
Domain: The C-terminal domain recognizes the anticodon bases but the N-terminal contributes also to the precise recognition of tRNA(Thr) by ThrRS.
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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Q58597 | MKMLLIHSDYLEFEAKEKTKIAEETENLKGKLDECLACFIAVEREDENNPEGTAIGAVEEIEKVANQLKVNNIVVYPYAHLSSDLSSPETAVKVLKDIESILKERGYNVLRAPFGWYKAFKISCKGHPLSELSRKIVAKEEKKEEGEESKFYLLNPETEEIIELNENNINIIKDEELLALAKHELGIREHKEHDEPPHVKFIKEKDICSYEEASDPGHFRWYPKGKLMRDLLADYVYNLVVNMGAMPVETPIMYDLGNPAIREHADKFGERQYRFRQGNKELMLRFAACFGQFMMKKDMYLLPRYLPLKLYELSTYSFRYEQRGELVGLKRLRCFTMPDMHTVCLNLEQAMEEFEKQFWECLKTGDDLNLSYSVIFRFTKDFFDEHRDWFFKIAKEYKNKYGKDVILEILPKRKHYWVGKVDIAVIDSLGRPIENPTVQIDVESAKRFDIKVHTNEGEIYPIILHCSPTGSIERVLCGLLEKAAIEAEKGNAPMLPVWLSPIQVRVIPVAERHYDYALKVAEKLRENNIRADFDDREESVSKKIRNAGKEWVPYVVVIGDEEMESDKLTVTIREKSTLKKPYKEKMTLDELIERIKKETANYPYRPLPLPIRCSLQPKFH | 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 activates L-serine, but does not detectably transfer it to tRNA(Thr) . Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain . Has no activity on correctly acylated L-seryl-tRNA(Ser) or L-threonyl-tRNA(Thr) . Deacylates correctly charged glycyl-tRNA(Gly), but not glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA adenine 76 has been dehydroxylated) nor the 2'-fluoro tRNA derivative, strongly suggesting the editing function is tRNA catalyzed .
Catalytic Activity: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
Sequence Mass (Da): 72357
Sequence Length: 620
Domain: The N-terminal domain (about residues 1-140) is an archaea-specific tRNA-editing domain that has a highly similar structure to Dtd (D-aminoacyl-tRNA deacylase). Editing of incorrectly charged L-seryl-tRNA(Thr) by this domain is tRNA catalyzed .
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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Q7UJ52 | MSADSPSSPASSQAAEVQVRLPDGSLKTQPADATAMDVAKEISEGLARSVVAAEVDGTIVDSFRPLGEIADDENVVPLRLLTTRDESALDVLRHSAAHVMARAIMRIYKGVSLAFGPTTSGGFYYDFDMPEKISEDDFPKIEAEIKKIIKAKEPFERFVLERDEARKLCDDLDQDLKVEHIETGLGDQATVSFYRQGEFVDLCRGPHIPHAGMIKAIKLLSVAGAYWKGDASGRQLQRVYGTAFFDKKELASYLEQIEEAKRRDHRVLGKQHGLFAINPEVGQGLCLWLPKGARVRVTLEDFLRRELLSRGYDPVYSPHIGRVEMYETSGHFPYYRDSQFAPLFGSEVGGLLDAWSTRLDKDDLSKDDEDKLIAAAEVFGVKLPDYKPSASNDAKKDVLHRWQLNHERYLLKPMNCPHHCQIFGAQPRSYRQLPLRLFEFGTVYRHEQTGELNGMMRVRGLTQDDAHIFCTADQVEEEFRATIELTKFVLESVGLDDYRVQLSLRDPDSSKYVGSEENWDHAEGALRGVLEQSGLSFNEEPGEAAFYGPKADFMVRDCIGRSWQLGTVQLDYNLPERFKLEYKGNDNATHRPVMIHRAPFGSLERFTGMLIEHFAGAFPMWLSPEQIRVLPLSDKSVEYATAVAKQLDEAGFKVTVDASDGKVQAKIRNAQIDLVNYMAVVGPKEAESGQVALRDRIEGDLGSMPIKEAIARLQKEVETRQVRQAVKGSTVSIAETGGAATDY | 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): 83078
Sequence Length: 743
Subcellular Location: Cytoplasm
EC: 6.1.1.3
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O55042 | MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA | Function: Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By similarity). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (By similarity). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 . This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (By similarity).
PTM: Phosphorylated, predominantly on serine residues. Phosphorylated on Tyr-125 upon osmotic stress.
Sequence Mass (Da): 14485
Sequence Length: 140
Subcellular Location: Cytoplasm
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Q3I5G7 | MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGEAVVTGVTAVAQKTVEGAGSIAAATGFGKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA | Function: Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By similarity). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (By similarity). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (By similarity). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (By similarity).
PTM: Phosphorylated, predominantly on serine residues.
Sequence Mass (Da): 14520
Sequence Length: 140
Subcellular Location: Cytoplasm
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Q91448 | MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSRTKEGVVHGVTTVAEKTKEQVSNVGGAVVTGVTAVAQKTVEGAGNIAAATGLVKKDQLAKQNEEGFLQEGMVNNTGAAVDPDNEAYEMPPEEEYQDYEPEA | Function: May be involved in the regulation of dopamine release and transport.
PTM: Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
Sequence Mass (Da): 14874
Sequence Length: 143
Subcellular Location: Cytoplasm
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P33567 | MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTKEGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKKEEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEEQPQEEYQEYEPEA | Function: May be involved in neuronal plasticity.
PTM: Phosphorylated. Phosphorylation by G-protein coupled receptor kinases (GRK) is more efficient than phosphorylation by CK1, CK2 and CaM-kinase II (By similarity).
Sequence Mass (Da): 14277
Sequence Length: 134
Subcellular Location: Cytoplasm
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Q16143 | MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTREGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKREEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDPPQEEYQEYEPEA | Function: Non-amyloid component of senile plaques found in Alzheimer disease. Could act as a regulator of SNCA aggregation process. Protects neurons from staurosporine and 6-hydroxy dopamine (6OHDA)-stimulated caspase activation in a p53/TP53-dependent manner. Contributes to restore the SNCA anti-apoptotic function abolished by 6OHDA. Not found in the Lewy bodies associated with Parkinson disease.
PTM: Phosphorylated. Phosphorylation by G-protein coupled receptor kinases (GRK) is more efficient than phosphorylation by CK1, CK2 and CaM-kinase II.
Sequence Mass (Da): 14288
Sequence Length: 134
Subcellular Location: Cytoplasm
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Q91ZZ3 | MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTSGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKKEEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDSPQEEYQEYEPEA | Function: May be involved in neuronal plasticity.
PTM: Phosphorylated. Phosphorylation by G-protein coupled receptor kinases (GRK) is more efficient than phosphorylation by CK1, CK2 and CaM-kinase II (By similarity).
Sequence Mass (Da): 14052
Sequence Length: 133
Subcellular Location: Cytoplasm
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Q63754 | MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTKEGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKKEEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDSPQEEYQEYEPEAKGP | Function: May be involved in neuronal plasticity.
PTM: Phosphorylated. Phosphorylation by G-protein coupled receptor kinases (GRK) is more efficient than phosphorylation by CK1, CK2 and CaM-kinase II.
Sequence Mass (Da): 14504
Sequence Length: 137
Subcellular Location: Cytoplasm
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O76070 | MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGAKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVATKTVEEAENIAVTSGVVRKEDLRPSAPQQEGEASKEKEEVAEEAQSGGD | Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity).
PTM: Phosphorylated. Phosphorylation by GRK5 appears to occur on residues distinct from the residue phosphorylated by other kinases.
Sequence Mass (Da): 13331
Sequence Length: 127
Subcellular Location: Cytoplasm
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Q2PFW6 | MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGTKTKENVVHSVTSVAEKTKEQANAVSEAVVSSVNTVAAKTVEEAENIAVTSGVVRKEDLKPSAPQQEGEAAKEKEEVAEEAQSGGD | Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity).
PTM: Phosphorylated. Phosphorylation by GRK5 appears to occur on residues distinct from the residue phosphorylated by other kinases (By similarity).
Sequence Mass (Da): 13296
Sequence Length: 127
Subcellular Location: Cytoplasm
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Q9Z0F7 | MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGTKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVANKTVEEAENIVVTTGVVRKEDLEPPAQDQEAKEQEENEEAKSGED | Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases. May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity).
PTM: Phosphorylated. Phosphorylation by GRK5 appears to occur on residues distinct from the residue phosphorylated by other kinases (By similarity).
Sequence Mass (Da): 13160
Sequence Length: 123
Subcellular Location: Cytoplasm
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Q63544 | MDVFKKGFSIAREGVVGAVEKTKQGVTEAAEKTKEGVMYVGTKTKGERGTSVTSVAEKTKEQANAVSEAVVSSVNTVATKTVEEAENIVVTTGVVRKEDLEPPAQDQEAKEQEEGEEAKSGGD | Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases. May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity).
PTM: Phosphorylated. Phosphorylation by GRK5 appears to occur on residues distinct from the residue phosphorylated by other kinases (By similarity).
Sequence Mass (Da): 12976
Sequence Length: 123
Subcellular Location: Cytoplasm
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Q6MAM1 | MTELPKAYEAKKIDEKWYQFWDAKRYFTANPLSNKPTYCIVIPPPNVTGVLHMGHALVNTVQDILIRWKRMLGFETLWVPGTDHAGIATQMVVERHLIKTEGKKRTDYTREEFLKHVWTWKEKSENRIIEQLKRLGNSCDWTRLRFTMDENNSLAVRTMFKKLFDDGLIYRGDYLVNWDPHTQTALADDEVEYEDKQSFLWYFKYPLRDESEFISIATTRPETMLGDTAVAVSPNDERFKHLIGKEIRLPLMNRLIPIIADHHVDPSFGTGVVKITPAHDPNDYQIGLSHRLPFINIMTPDGKINENGGHFQGLSMTEARHAVVSEMKEKGLLEKVEPHLNRVGISYRSKAIIEPYLSKQWFVKMDGFSKKLREVVQNGQVKLIPSHWESTYFHWIDNLRDWCISRQLWWGHRIPIWYHKEDSNRLICYAGSDLPDEVKNAPEEWIQDSDVLDTWFSSALWPFSTLGWPEQTSELAKFYPTSVLVTGHDILFFWVARMILMGDYALDQPPFPETYLLGLIYGKSYWRQESNGGILYVNEQERSDFDMGKPIPKEVFSKWEKMSKSKGNIIDPLEMIDQFGTDAVRMALCASATQARQIDLDRRRFEEFKNFTNKIWNGARFVLMNLDGNEQNRTMSLTSQGFSQGLDEALFTLEDRWILSVLNRTVESVNVHLNHYQFDQAAIEAYDFFWKEFCAYYVEIAKPILFGKIGTAQERTNKQKLLVIVLCQAIRLIHPMAPFITEELFHILKERLEGVEALTNADPYTKECIQALQSSACLVAPYPVRIGEKNQKVEAVFALMEQIVYTIRNIRGEMKLSPGTATDVYIIGQADDPEWQSAREHITMISALVKTRRILVETEEPKIGFACTGVYHALKIQLPLPEELLKQEKTRLNKEQEKLEISLEKLKNQLSNTDFVRRAPAHLTEKQNQQLSQTEQELREIKEKLMTLP | 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): 110265
Sequence Length: 949
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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Q4FM20 | MSNDKYIHTDVEDKIYSYWEKNNLFKPTKNKKQFSVVIPPPNVTGSLHMGHALNNSIQDLLVRYHRMNNYETLWQPGTDHAGIATQALVEKKLTADGIDKNEIGREKFIEKVWEWKEEHGDIILNQLKKLGCSCDWSRNAFTMDENLSKSVLKVFVELHKKGLIYKDKKLVNWDTVLKTAISDLEVDQREVNSKIYYIQYPIEASSDFITIATTRPETMLGDTAIAVNPKDDRFKHLVGKFVTVPIVGKKIKIIEDEYADPEMGTGALKITPAHDFNDYEVGQRNNLEIINIFTEGGKVNENAPKEYIGLDRFEARKRIIKELKEKEFFVKEENIKNKVPYGDRSNSIIEPFLTEQWFVDAKKLSIKAKDIVNSKKTNFFPANWSKTYFQWMNNIEPWCISRQLWWGHQIPAWYGPDKKIFVAINEEEAKLDAKKFYNKDVDLIRDPDVLDTWFSSGLWPFATLGWPDNKEYVDKFYPTSVLVTGFDIIFFWVARMIMFGMEFLDKEPFKDVYVHALVKDEKGQKMSKSKGNVINPLDLIEKYSADALRFTLLSMASPGTDVKLSEDRVKGYRNFLNKLWNANNFLITNNCDFSKIDEKPILSININKWIYAELIETKNKIEKNLKDYRFDEAAKNAYQFTWHSYCDWYLELSKTILFSEDEKAKDEVRQVSAYVFKQILILLHPFIPFVTEEIWLNNKFDNTGKDFLMLANWPSGEFERDTSINQVEKIISIVSELRSFKNELSVSPGSFIDISIETVSKKEQSFFTENEIILKKLGRIKNLYNKDLDKPTATLMVSGDLFKVYFDEDVDLELIKKNLTTRQNKYQEEMNKISQRLANKGFVDRAPKDIVDQEKTNYNNLKNDVERISITIKGL | 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): 101993
Sequence Length: 875
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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Q6LUW1 | MEKTYNPQSIEQALYQRWEEAGYFKPHGDTSKDAYSIMIPPPNVTGSLHMGHAFQDTIMDTLIRAERMKGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTKHDYGRDAFIDKIWEWKAESGGTITKQLRRLGASVDWDRERFTMDDGLSAATQEVFVRLFEEDLIYRGKRLVNWDPKLHTAISDLEVESKDKKGFMWHFRYPLADGVKTADGKDYIVVATTRPETMLGDTGVAVNPEDPRYKDLIGKQIKLPIVGRLIPIVGDEHADMDKGTGCVKITPAHDFNDYEVGKRHSLPMINILTFNADIRDAAEVFDTNGEANDAYNSELPAKYHGMERFAARKAIVAEFDELGLLEEVKDHDLTVPYGDRGGVAIEPMLTDQWYVRTAPLAAPAVKAVEDGQIQFVPKQYENMYFAWMRDVQDWCISRQLWWGHRIPAWYDNYGKVYVGRTEDEVREKNNLASVVVLRQDDDVLDTWFSSALWTFGTQGWPENTDALKTFHPSEVLVSGFDIIFFWVARMIMMTMHFVKDEEGNAQVPFKTVYMTGLIRDENGDKMSKSKGNVLDPIDMIDGIGLEELVEKRCGNMMQPKLAAKIEKQTRKAFEGGIEPYGTDALRFTLAAMASTGRDINWDMKRLEGYRNFCNKLWNASRYVLMNTEEHDCGMAEGAELEFSLADQWITSQFEVAAKEFNAHLDNYRLDMAANTLYEFIWNQFCDWYLELTKPVLWKGTEAQQRATRYTLITVLEKTLRLAHPILPYITESIWQSVKPLVDGVEGETIMTQALPQFNEDNFNADVVADLEWVKAFITSIRNLRAEYDIAPSKGLDVMIKVADEKDAARIQANEIVLTSLAKLDSIKVLAKNEETQACATSLVGKSELMIPMAGLIDKDAELARLDKEVAKTQGEIKRIEGKLNNQGFVAKAPEVVITKEREKLEGYQETLVKLEAQKETIAAL | 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): 108244
Sequence Length: 953
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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A6L3G7 | MELASKYNPADVEGKWYQYWLDNKLFSSKPDGREPYTVVIPPPNVTGVLHMGHMLNNTIQDILVRRARMEGKNACWVPGTDHASIATEAKVVNKLAGQGIKKTDLSRDEFLKHAWAWTEEHGGIILKQLRKLGASCDWDRTAFTMDEERSESVIKVFVDLYNKGLIYRGVRMVNWDPKALTALSDEEVIYKEEHSKLYYLRYKVEGDAEGRYAVVATTRPETIMGDTAMCINPNDPKNQWLKGKKVIVPLVNRIIPVIEDDYVDIEFGTGCLKVTPAHDVNDYMLGEKYNLPSIDIFNDNGTLSEAAGLYVGMDRFDVRKQIEQDLQAAGLLEKVEAYTNKVGFSERTNVAIEPKLSMQWFLKMQHFADMALPPVMNDELKFYPAKYKNTYKNWLENIKDWCISRQLWWGHRIPAYFLPEGGYVVAETAEEALKLAQEKTGNTNLKMEDLRQDDDCLDTWFSSWLWPISLFNGINNPNNEEINYYYPTSDLVTGPDIIFFWVARMIMAGYEYKGDMPFKNVYFTGIVRDKLGRKMSKSLGNSPDPLELIDKYGADGVRMGMMLAAPAGNDILFDDALCEQGRNFNNKIWNAFRLVKGWEVADIAQPEYARLATEWFESMLAKTAAEVADLFGKYRLSEALMAVYKLFWDEFSSWYLEMIKPAYGQPIDKATYEKTLGFFDNLLKLLHPFMPFITEELWQHIYDRKEGESLMVQQLNIPTACNEIIVKEFEVVKEVIGGIRTIRLQKNIAQKETLELQVVGVNPVATFNPVITKLCNLSSIEAVENKADGSGSFMVGTTEYAIPLGNLINTEEELAKLEADLKYQEGFLQSVLKKLSNEKFVSKAPANVIDMERKKQADAESKIASLKESIAALKK | 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): 99754
Sequence Length: 875
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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B2RK53 | MEIASKYNPEEVESKWYNYWMEYGCFISVPDGRKPYTVVIPPPNVTGVLHMGHMLNNTIQDILVRRARMKGYNACWVPGTDHASIATEAKVVGRLAAQGISKQDLGREEFLRHAWDWTHEHGGIILEQLKRLGASCDWTRTAFTMDESRSESVIKVFVDLYNKGLIYRGIRVVNWDPKALTALSDEEVIYKETNGKLYYLRYFVENEPDKYIIVATTRPETIMGDTAVCVNPNDERYRWLRGKRVIVPTVGRAVPIIEDEYVDMEFGTGCLKVTPAHDVNDYMLGQKHRLESIDIFHDNGILNEHGGPYAGMDRFDVRKKIEQDLIDAGLMERVENYVNKVGYSERTDVPIEPKLSMQWFLQMESLAKSALDAVMNDEIKLHPAKFKNTYRHWMENVKDWCISRQLWWGHRIPAYYLPDGSIVVAETAEKAVELARKQTGSDSLTAEDLRQDSDSLDTWFSSWLWPISVFGDVMDPENEELDYYYPTSDLVTAPDILFFWVARMIMAGYEYRGKKPFDNVYLTGIVRDGQGRKMSKSLGNSPDPIMLMEKYGADGVRMGLMMAAPAGNDVLFDESLSEQGRNFCNKIWNAFRLVKGWQQAETATQPEASALAVKWFGYRLDEVKTELDDLFSKYRLSEALTLVYKLFWDDFSSWYLEMVKPAYGQPMDAKTYGSTIGFFDQLLRLLHPFMPFITEELWHALASRHDGETIMLCLLPDAHETDRDFLQAFDRTREIIAAIRNIRTGKNVPFKEKLTLEAGNEHDASFDAVIIKMGNLEAINRVEEKTSGSTSFLIGTLEYAIPMGALIDVEEEIKKLSDELAYQEKFLASVMKKLGNESFVAKAPQAVIELEQKKKSDAEARIATLRDSLNQLQSTK | 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): 100258
Sequence Length: 876
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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Q9JYQ9 | MSKKRVLTGVTTTGIPHLGNYVGAIRPAVRAAQNLDTESFLFLADYHGIIKCHEPEMIHQSTQAVAATWLACGLDPERTTFYRQSDTPEVMELNWILTCITAKGLMNRAHAYKAAVQANAENGQEDPDFGVEMGLFSYPILMTADILMFNANEVPVGRDQIQHVEMARDIAGRFNHRFRELFTLPEVKIDENVELLVGLDGRKMSKSYGNTIPLWENDKKTQKSVNKIITNMKEPGEPKQPDESPLFEIYKAFSTPSETVEFTKMLADGLAWGEAKKLLAAKINAELAEPRERYNELTADPSQIEEILQAGAAKARKEARELLDKVRDAVGIRPLK | 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): 37616
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 6.1.1.2
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Q7MT94 | METVVSGIRPTGNLHLGNYFGAIRSFLDMQHRYNCFFFIADWHSLTTHPHPDNIVRNVRTILAEYLACGIDPEKATIYVQSDVREVLELYLYLNMNAYLGELERTTSFKEKARKQPNNVNAGLLTYPTLMAADILIHRAVKVPVGKDQEQNMEMARKFARRFNTIYEVDFFPEPESFSPGATALKVPGLDGSGKMGKSEGNAIYLADDAKTISKKVMKAVTDAGPEVPNSVKPEPVENLFSMLRIVSSDEVYRHFDDLYNNCSIRYGDLKKQLAADIVAFTTPIRERILEIQADEAFLDRVVREGAERARESAARTLAEVRHIIGFR | 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): 36969
Sequence Length: 327
Subcellular Location: Cytoplasm
EC: 6.1.1.2
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Q9HVX6 | MTTRILTGITPTGTPHLGNYAGAIRPAILASRRSDVDSFYFLADYHALIKCDDPARIQRSRLEIAATWLAGGLDVERATFYRQSDIPEIPELTWLLTCVSAKGLLNRAHAYKAAVDRNVEAGEDPDAGVTMGLYSYPVLMAADILMFNAHKIPVGRDQVQHVEMARDIGQRFNHLFGNGREFFVLPEAVIEENVATLPGLDGRKMSKSYDNTIPLFSPSRQLKDAIARIVTDSRAPGEPKDPDSSHLFLLYSAFASAEQVAAFRQELLEGLAWGEAKQRLFQLLDNELGEARERYQALIAKPDDIEDILLAGAAKARRIATPFIAELREAVGLRSLREPLKSAESGKKKAAKAARLVSFRDDDGSFRFRLLDAAGEQLLLSRAFADGKAAGAVSKRLLAGETADLRAEGNAFGLWLDGEAVAQSPAFADAAARDAAIERTREALAPQE | 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): 48962
Sequence Length: 448
Subcellular Location: Cytoplasm
EC: 6.1.1.2
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Q8ZTU5 | MEEEFVVTPWEVRGRVDYEKLLKHFGAKPLTKDEVALLEKYAGEVHPLIRRGFFYAHRDFDFIMKWHGEGRPWALYTGRGPSGPVHIGHMVPWILLKWFSDKFGLEVYFQITDDEKFYDDPEMKLEEATNWAYENALDVIALGFSPERLHLIIDTKDIKPLYPIAVRVAKKLTWNTVKATFGFTDSTNIGLIFYPSLQIAVAFLPTELRREATPVLIPCAIDQDPYFRLARDIADALGYPKPSTLYSKFIMALTGESKMSASNPDSAIYTLDDEKTVRRKVMNAFTGGRPTAEEQRKYGGNPEVCPVFHYHMLFDPDDASVEKIRQDCKSGALLCGECKLKLHEKITKFLKEHRERREKARGKVDEYRLSVKLSK | Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
Sequence Mass (Da): 43179
Sequence Length: 375
Subcellular Location: Cytoplasm
EC: 6.1.1.2
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O67632 | MTPEEQLRIIKEGTVEIIEEEELLKKLKEGRPLRVKAGFDPTAPDLHLGHVVLLQKLRQFQQLGHEVFFIIGDFTAMIGDPTGRSQTRPPLSREQVLENAKTYEHQVFKVLIPEKTTVVFNSTWLEELGTKGLIELCAKYTVARMLEREDFSKRFKEGIPIYIHEFIYPLLQAYDSVAIKADVEIGGTDQKFNLLIGRDIQREYGQEPQVCITLPLLVGTDGVRKMSKSYGNYVGITEDPKTMFAKIMSIPDEIMWDWFLLLTDYNKEEIEKMRREMHPMEAKKLLAFTIVKRFHSEEEARKAKEWWEKTFSQREFPEDAPLVKLNEKKLRAVDFLVKIGAVKSKNEARRVIQGGGLKINGEKVTDPNTEIEINGELKVKVGKKKFYRVVSG | 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): 45200
Sequence Length: 392
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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O29482 | MDITEKLRLITRNAEEVVTEEELRQLIETKEKPRAYVGYEPSGEIHLGHMMTVQKLMDLQEAGFEIIVLLADIHAYLNEKGTFEEIAEVADYNKKVFIALGLDESRAKFVLGSEYQLSRDYVLDVLKMARITTLNRARRSMDEVSRRKEDPMVSQMIYPLMQALDIAHLGVDLAVGGIDQRKIHMLARENLPRLGYSSPVCLHTPILVGLDGQKMSSSKGNYISVRDPPEEVERKIRKAYCPAGVVEENPILDIAKYHILPRFGKIVVERDAKFGGDVEYASFEELAEDFKSGQLHPLDLKIAVAKYLNMLLEDARKRLGVSV | 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): 36616
Sequence Length: 323
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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Q2NJG7 | MSFYEELKWRNLIKDCNNEIQVKELLDNNQVKFYCGFDPTSHSLTVGHLIQITMILLMQRQGHLPVILVGGATGLIGDPKETEERKLLSLENSLQNAKSIESQLKTILLNKQVEFVNNYQWLSQIDIISFLRNYGKFFNINYMLSKHVVAKRLASGISFTEFSYMILQSLDFHHLYKNHKVRLQLGGSDQWGNITSGLEIIRKLEKKSDALGVSTPLLLNSDGTKFGKSEKRVLWLNPLMTSPYEIYQYFLNVSDKEVINYLKMLTLIPKKGILELEKKTLENPQKRLAQKALTQSIINLIHSSDILQECIKTNQILFSNAKKESFQEKDFILLQKTLFCHSIKEDILLVDALVQTKLATSKSEAREFIKDNTIKLFNQKIKSLDFIITKENTLFGKYILLKKGKKNNALIVF | 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): 47600
Sequence Length: 413
Subcellular Location: Cytoplasm
EC: 6.1.1.1
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Q8A2S5 | MNFVEELRWRGMLQDIMPGTEELLNKEQVTAYLGIDPTADSLHIGHLCGVMILRHLQRCGHKPLALIGGATGMIGDPSGKSAERNLLNEETLRHNQACIKKQLAKFLDFESDVPNRAELVNNYDWMKEFSFLDFVREVGKHITVNYMMAKDSVKRRLNGEARDGLSFTEFTYQLLQGYDFLHLYETKGCKLQMGGSDQWGNITTGAELIRRTNGGEVFALTCPLITKADGGKFGKTESGNIWLDPRYTSPYKFYQFWLNVSDSDAERYIKIFTSIEKEEIEALVAEHQQAPHLRALQKRLAKEVTIMVHSEEDYNAAVDASNILFGNATSESLRKLDEDTLLAVFEGVPQFEISRDALAEGVKAVDLFVDNAAVFASKGEMRKLVQGGGVSLNKEKLEAFDQVITTADLLDGKYLLVQRGKKNYFLLIAK | 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): 48380
Sequence Length: 430
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
Q5UPJ7 | MENTDHTNNEHRLTQLLSIAEECETLDRLKQLVDSGRIFTAYNGFEPSGRIHIAQALITVMNTNNIIECGGQMIIYIADWFAKMNLKMNGDINKIRELGRYFIEVFKACGINLDGTRFIWASEFIASNPSYIERMLDIAEFSTISRVKRCCQIMGRNESDCLKASQIFYPCMQAADVFELVPEGIDICQLGIDQRKVNMLAIEYANDRGLKIPISLSHHMLMSLSGPKKKMSKSDPQGAIFMDDTEQEVSEKISRAYCTDETFDNPIFEYIKYLLLRWFGTLNLCGKIYTDIESIQEDFSSMNKRELKTDVANYINTIIDLVREHFKKPELSELLSNVKSYQQPSK | 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): 39723
Sequence Length: 346
EC: 6.1.1.1
|
Q2RHS8 | MHDYFGGWFKLEQEVARQLRILRRGVAEIVPEEDLQAKLRKSLATGKPLKVKLGLDPTAPDIHLGHTVVLQKLRQFQELGHQVIIIIGDFTGRIGDPTGKSETRRQLTEAEILANAETYKEQIFKVLDPEQTRVTFNSHWLGKLTFAEVIELAARTTVARMLERDDFARRFQENRPISIHEFFYPLMQGYDSVALAADVELGGTDQKFNLLMGRHLQREYGQEPQVAMMMPILPGLDGVQKMSKSLGNYIGIKESPREMYGKTMSLPDELMLTYYELVTAVPLEELAAIRQGLASGSLHPRDAKMRLAREIVAMYHTPEAALEAEREFRQVFQQHDLPDDMPELTIKEDRVWLPRLMVQAGLAPSTSEARRLIRQGAVKIDGERVTDPDTEVEVREGQVLQAGKRKFARLHTF | 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): 47023
Sequence Length: 413
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
Q7NBH9 | MDFISELKKRNIIKQISNEEKLALALKNQKGVYVGFDPSGESLHLGNLIPIIVLRYLKKVGFKTYAILGGATGLIGDPSGKTSERKVQDYEKITANANKIKVQLERYTQAKIINNIDFYQNMNLLNFLRDTGKLINIGYLLDKEFIRSRIENGISYAEFSYNIIQGHDFLHLYEQYDVQVQCGGSDQWGNITTGIDMIKRKYGEEKTPYLCGLTFNLLLNPNGNKFGKSEQGALYLDENLTHPYLIWQYIYNQDDQFIIDLIHRYVLDQSLEQLQELIEAHLANKKTRIAQKFLADYLVKFIHSQEHLDTVHKMNKALFDNQLDQLSDQEKLVVFASFDKVELDRNQSFMVIDFLLQAKVADSKRILRELIAQGSIQIDDLKITDPQAQLNVRKDQQLTVIKKGKKNYFIVVWKG | 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): 47914
Sequence Length: 415
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
P47693 | MLNNILQFLKERELYSQANFETELDNHLKEKKNNFYVGFDPTANSLHIGNYVLIHIAKLLKDMGHTPHIVLGSATALIGDPTGRIELRKILEEKEIVKNTKTIKKQIKQFLGDVIIHENKVWLEKLNYIEVIRELGAFFSVNKMLSTDAFSARWEKGLTLMELNYMILQAYDFYYLHKNHNVTLQIGGSDQWANILAGANLIKRKNNASVFGLTANLLVKANGEKMGKTSSGALWLDENKTSVFDFYQYWINLDDQSLKKTFLMLTMLDKKVIDELCNLKGPKIKQTKQMLAFLITELIHGTKKAKEAQQRSELIFSNQPDLDIKLVKTSTNLIDYLVETKFIKSKSEARRLISQKGLTINNKHVLDLNQIIEWKEELQIIRKGKKSFLTIKTVNS | 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): 45563
Sequence Length: 396
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
Q98Q81 | MSQNKLKTLIEELKKRKVFNNITSEEKVDLITLDHGIYVGFDPTAISLHLGNYIQMVNLKRFQNVGFKTIAILGGATSMIGDPSFKDSERKLLSNETILENKKHIRKQLENFGFKVIDNLDFYKDMNILDYLRSVGKFFNVSTMMSRDSVANRIQSGLSFTEFSYQTLQAYDFKVLCEKENVMMQLGGSDQWGNLVSGLDFINKTLSKNLPTIGITMNLLVDSNGNKIGKSTGGASLWIDKTLTSPYVLYQYLLNTNDDDAYNLLLQLTFLQLSEIERIKNEHLKNPKLRLMQSRLSFEVVKDIHGKEEAQRALHISTSLFKEKNSWFNLSLEDLIQLKGSVDFVPFKDDLFLTLVDSKIISSKREFNEFVRDKSLKINGQDVTGLDYDLPWENYDNKYLILKKGKKQYWVIYK | 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): 47699
Sequence Length: 414
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
Q4A5E2 | MHKVLTELRDREILKDISNEEKFLSLPKNSGVYVGFDPTADSLHLGNYVQIVNLIRFKKHNWNALAVLGGATGMIGDPSFRSTERVLLSTEELLKNKNKIKSQLESFGLKVFDNYEIYKDISFLDFLKNIGKLINVSYMLAKDSVKDRLAQGLSFTEFSYQIIQGYDFLHLYQNQDIFVQYGGSDQWGNITTGIEMISKVVGDNHKAIAITANLLTDSNGNKFGKSTGGGNLWLDAQKTKPFDMYQFLINQPDSEVEKLLKWLTFLEISEIKDLVNKHNKNPKDRLAQKALAYEVIKDIHGKSAAENCTFLSEMLFNLSLDLSKVTLENMEFAYNQIESFEVEKGVNLVNFLVENKILQSKRLAREFIASKSLKFNYEPIDEDFSVSSNYFEGKYATLHLGKKKILICKVK | 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): 46859
Sequence Length: 411
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
Q74MD3 | MDIEERINLIAQKPTEEILTIDRLKQYLEQGIDLNHYIGFEISGFVHLGTGIISMLKVRDFQKAKVKTTLFLADYHSWINKKLGGDLETIRKVAKGYFAEALKVSLKTVGGDPDEVKVVLGSELYEKLGIEYLENIIKISMNTTLNRIKKGITIMGRKQGESISFAQLLYVPMQVADIYSLNVNLAHGGIDQRKAHVIAIEVSDAFGYKPIAVHHHLLLGMHIDENIRQKLLEAKKTNNRELFEDSVIDIKMSKSKPETAIFIHDTPEDIRRKIRKAYCPIGEIELNPIIELVEYVIYPILKEPIVIENKKTHQTMEFDNVEQLKEAYAKKQIHPLDLKEYVAEKLIEILEPARKYFLEGKGNKYLEELKNLQITR | 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): 43178
Sequence Length: 376
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
Q67QD6 | MTMAFMSVDEQMKILMRGVVDLVSEEELRQKLERSVKTGRPLRVKLGIDPTGKDLTLGHTVPLRKLRDFVECGHQGVLIIGDYTAMVGDPTGRNEARPQLTHAETTANAQRYLEQAARVLDVSKLEIRRNSEWLAPMSFSDVIRLAAKSTVARMLEREDFKKRYEEGRPIFIHEFFYPLMQGTDSVAVQADVELGGTDQKFNLLAGRDLQRDAGQEPQVCLMTPIVEGLDGVQKMSKSLGNYIGLDHTPDEMFGRTMSIPDSLIITYFTYFTDVPQEEIERIEAAMAAGENPMTFKKQLGRAIITTYGGTEEEARLAEERWVAQFSRGEVPEDIPDVVLPAAELPMQAARVLFTAGLAPSLSEARRLIEQGGFTVDGEKVTDPRAELALRPGQVLKAGKRKYGRVVLK | 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): 45544
Sequence Length: 408
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
Q2LR98 | MILKNVYDVFMERGFIEQVTDENAVRKALEAPLACYIGFDPTARSLHIGSLVPIMALIHLQRHGHTSIALVGGGTALIGDPSGKTEMRQILTREKIELNATCMRRQFARYLSFEDKKAMMINNADWLTKLNYISFLRDIGRHFSVNKMLAAESYKMRLEKGLNFIEFNYMLLQAYDFLYLFQNHNCVMQMGGNDQWGNMLAGVDLIRRVEGKVAHSMTFPLLTTATGQKMGKTEKGAVWLDRELTSPYEYYQYWINTGDIDVGKFLALFTFLPMEEIHQVKSLSDKELNMAKAILAFEATKITHGEDAALAAWNASAVAFGVKLIDTSLMPSSTIPRGQLSQDASAIPFIKKSWNELAKGIPAYEIMHECGLCSSKSEARRLIAQGGGYVNENPIFAFDELITTEHLDRSGQIKLRKGKKKYMIIKVE | 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): 48282
Sequence Length: 428
Subcellular Location: Cytoplasm
EC: 6.1.1.1
|
Q8IUX1 | MVVFGYEAGTKPRDSGVVPVGTEEAPKVFKMAASMHGQPSPSLEDAKLRRPMVIEIIEKNFDYLRKEMTQNIYQMATFGTTAGFSGIFSNFLFRRCFKVKHDALKTYASLATLPFLSTVVTDKLFVIDALYSDNISKENCVFRSSLIGIVCGVFYPSSLAFTKNGRLATKYHTVPLPPKGRVLIHWMTLCQTQMKLMAIPLVFQIMFGILNGLYHYAVFEETLEKTIHEE | Function: As part of the MCIA complex, involved in the assembly of the mitochondrial complex I . Participates in constructing the membrane arm of complex I .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25943
Sequence Length: 230
Subcellular Location: Mitochondrion membrane
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P0DUU2 | CCTPFYFCCNN | Function: Probable toxin that inhibits ion channels.
PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or 'C1-C4, C2-C3', since these disulfide connectivities have been observed for conotoxins with cysteine framework V (for examples, see AC P0DQQ7 and AC P81755).
Sequence Mass (Da): 1315
Sequence Length: 11
Domain: The cysteine framework is V (CC-CC).
Subcellular Location: Secreted
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Q24JP5 | MCARMAGRTTAAPRGPYGPWLCLLVALALDVVRVDCGQAPLDPVYLPAALELLDAPEHFRVQQVGHYPPANSSLSSRSETFLLLQPWPRAQPLLRASYPPFATQQVVPPRVTEPHQRPVPWDVRAVSVEAAVTPAEPYARVLFHLKGQDWPPGSGSLPCARLHATHPAGTAHQACRFQPSLGACVVELELPSHWFSQASTTRAELAYTLEPAAEGPGGCGSGEENDPGEQALPVGGVELRPADPPQYQEVPLDEAVTLRVPDMPVRPGQLFSATLLLRHNFTASLLTLRIKVKKGLHVTAARPAQPTLWTAKLDRFKGSRHHTTLITCHRAGLTEPDSSPLELSEFLWVDFVVENSTGGGVAVTRPVTWQLEYPGQAPEAEKDKMVWEILVSERDIRALIPLAKAEELVNTAPLTGVPQHVPVRLVTVDGGGALVEVTEHVGCESANTQVLQVSEACDAVFVAGKESRGARGVRVDFWWRRLRASLRLTVWAPLLPLRIELTDTTLEQVRGWRVPGPAEGPAEPAAEASDEAERRARGCHLQYQRAGVRFLAPFAAHPLDGGRRLTHLLGPDWLLDVSHLVAPHARVLDSRVASLEGGRVVVGREPGVTSIEVRSPLSDSILGEQALAVTDDKVSVLELRVQPVMGISLTLSRGTAHPGEVTATCWAQSALPAPKQEVALSLWLSFSDHTVAPAELYDRRDLGLSVSAEEPGAILPAEEQGAQLGVVVSGAGAEGLPLHVALHPPEPCRRGRHRVPLASGTAWLGLPPASTPAPALPSSPAWSPPATEATMGGKRQVAGSVGGNTGVRGKFERAEEEARKEETEAREEEEEEEEEMVPAPQHVTELELGMYALLGVFCVAIFIFLVNGVVFVLRYQRKEPPDSATDPTSPQPHNWVWLGTDQEELSRQLDRQSPGPPKGEGSCPCESGGGGEAPTLAPGPPGGTTSSSSTLARKEAGGRRKRVEFVTFAPAPPAQSPEEPVGAPAVQSILVAGEEDIRWVCEDMGLKDPEELRNYMERIRGSS | Function: May play a role in embryonic and postnatal development of the brain. Increased resistance to cell death induced by serum starvation in cultured cells. Regulates cAMP-induced GFAP gene expression via STAT3 phosphorylation (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 110110
Sequence Length: 1023
Subcellular Location: Golgi apparatus membrane
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A1SG03 | MSDNFVSFGEQGAQLTYGSYLRLPQLLEAQHLESDPPAHDELLFITIHQVYELWFKQLLHEVSAARDAMLGGEAGGRLWWAQHLLTRVHVIERVLVQQIDVLETMTPQEFLEFRQRLAPASGFQSVQFRELEFLSGAKDPAYLERFRGITPAEKARLDARLSEPTLWDAFLAMLRSFGFAADSDAEVSAALRTAAHDRTRYAVVWALSEGLLQHDELAANWRARHVVMVERMIGSKSGTGGSSGSSYLRSRLPVQYYPLLWGLRSEL | 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): 30217
Sequence Length: 267
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
EC: 1.13.11.11
|
Q1GEF8 | MSDSAYNPGQDGAKMGFADAMSYGDYLHLDALLDQQHCKSDAHDEMLFIIQHQTSELWMKLALHELQAAREALQQGQTAEMFKMLARVSRIFEQLNSAWDVLRTMTPADYTRFREALGPSSGFQSYQYRLIEYVLGNRNPNMLRPHEHVPEVHALLSAELARPSFYDEVNRYLFQTLDGHTENLPAPRLDAPHALDETIQERWLKVYGDIDTYWTLYELAEKLVDLEDYFRRWRFNHVTTVERVIGFKRGTGGTSGVQYLRRMLSVELFPELWTLRGDL | 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): 32455
Sequence Length: 279
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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B1KJM2 | MVCPHNNPKQGNTREMEDSIHTDFNNDMSYGDYLCLEQVLSAQHPQSEVHDEMLFIIIHQTSELWLKLAGNELDTMIHNVQQGDFSHAFKVISRVKQILNQLTQSWNILSTLTPVDYLKFRDALGRSSGFQSYGYRKIEFLLGNKNADLIQVHESNEQVHSELQGILERPSLYDEVIRVLHKQGLPIDDSALNRDFTQPYQANESVLNAWLSVYRNADEHFELYELAEKLIDIEDAFQQWRFKHMYAVQRIIGNKMGTGGSSGVSFLKKALDISFFPELFELRTHL | 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): 33077
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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P25237 | MDVFDKVYSDDNNSYDQKTVSQRIEALFLNNLGKVVTRQQIIRAATDPKTGKQPENWHQRLSELRTDKGYTILSWRDMKVLAPQEYIMPHATRRPKAAKRVLPTKETWEQVLDRANYSCEWQEDGQHCGLVEGDIDPIGGGTVKLTPDHMTPHSIDPATDVNDPKMWQALCGRHQVMKKNYWDSNNGKINVIGILQSVNEKQKNDALEFLLNYYGLKR | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GGTACC-3' and cleaves after C-5.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 25112
Sequence Length: 218
EC: 3.1.21.4
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P50177 | MDFNNYIGLESDDRLNAFMATLSVTNRTPEYYVNWEKVERETRKFELELNTLNYLIGKEDIYSEALELFTNQPELLKAIPSLIASRDTSLDILNIDENDDMSFEQLNFLVIDENCIADYVDFINQAGLLDFLQNKAKRSLVDYVYGVEAGLDSNARKTRSGTTMEGILERTVSKIAQGKGLDWKPQATASFIKSQWDIEVPVDKSKRRFDAAVYSRALNKVWLIETNYYGGGGSKLKAVAGEFTELSQFVKTSKDNVEFVWVTDGQGWKFSRLPLAEAFGHIDNVFNLTMLKEGFLSDLFEKEI | Function: A P subtype restriction enzyme that recognizes the double-stranded unmethylated sequence 5'-GATC-3' and cleaves before G-1.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 34670
Sequence Length: 304
EC: 3.1.21.4
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Q58391 | MVKLMKKLEDKKGIIEITFEEEREILELPSKPELPKYASQLINLANIFSQGTRPKVVGQMSELIKEFRKTGGRTFEDWKKWYLQKYPNAIDEATEKIWNMLNNFKETLEQLERDDVRKWVEDLVLIKTYEGLMLQDAILKKVAEELGGNYRPSTIEEESKGIDGVIIIDDKEIPVSIKSKTYVNQEKHLSEELKGHLIIYEKKKNKIIVDYSDLLDLVENTK | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CTAG-3'; the cleavage site is unknown.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 25962
Sequence Length: 222
EC: 3.1.21.4
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P50189 | MQNAVSQAISQGIHVRREILGSLTYEQRVFLLEDLFVDLFGHQHVMLQRWAALTGQSAQVDTGYIAQFVASIVLGEPGQGFRGKGDDLADGSEVKSAANISGVDRPRWNHNLGSLDDDEHRRSRGLPTAGEEYLGVPYMFYLLVDRPHGVSDPAPIRIRAWCIDAQEDGDWRDLFETFLTSRRGRTYNFQLHPPVGYDDDVVVNTLGNLDFSNVLVFDARLSLADRDRPEIDWHVPLPTQVIPVTGRTRALRYGGRGARPTRLTNTADIVLGTNDLGALFPGVLAPRDSYDLATVSEIETEAEVEEYS | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GATNNNNATC-3' and cleaves after N-5.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 34293
Sequence Length: 308
EC: 3.1.21.4
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P34719 | MKLAFDDFLNSMSETNTTLDYFTDFDKVKKNVAQIEIHLNQLNYLLGKDDLKQAVYDLYAECPNAFSILEILIAVRKKEQKKSLDEKGQVVTLNSYFQSADKIIDFLNNTGLADVFRDKNIKNLVDYVFGIEVGLDTNARKNRGGDNMSKAVQLLFDNADIYYKKEVRNTIFTDIESLGADVKQFDFVIKTKRKTYVIETNYYNSGGSKLNEVARAYTDVAPKINQYSQYEFVWITDGQGWKTAKNKLQEAYTHIPSVYNLYTLHGFIEQLNSEGVIKDW | Function: A P subtype restriction enzyme that recognizes the double-stranded unmethylated sequence 5'-GATC-3' and cleaves before G-1.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 32248
Sequence Length: 280
EC: 3.1.21.4
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P11405 | MRTELLSKLYDDFGIDQLPHTQHGVTSDRLGKLYEKYILDIFKDIESLKKYNTNAFPQEKDISSKLLKALNLDLDNIIDVSSSDTDLGRTIAGGSPKTDATIRFTFHNQSSRLVPLNIKHSSKKKVSIAEYDVETICTGVGISDGELKELIRKHQNDQSAKLFTPVQKQRLTELLEPYRERFIRWCVTLRAEKSEGNILHPDLLIRFQVIDREYVDVTIKNIDDYVSDRIAEGSKARKPGFGTGLNWTYASGSKAKKMQFKG | Function: A 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): 29829
Sequence Length: 262
EC: 3.1.21.4
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Q9YAD8 | MPVEVIPVLHNVSSVQRVVDMARLSYSLGLDTLVVTKAYGGAAQSGVPEAMRLALKLGKSLVVLPELRDAVNLLSPTHVLAVTPSRAERLVGPGGLEGLEGRVLVVFSGGEPELDPSEAAGAIRVYIEGVEGKVGPIAEAALILYFLLRGGGDGRG | Function: A putative type II restriction enzyme, its methylase would be APE_2002.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 16177
Sequence Length: 156
EC: 3.1.21.4
|
Q58844 | MPLSKNVIEKISIETIRVLKSRFDTISDEDIKIRNMPFHMAFLRAFYGKIGINDDTEALKFLTLSQWFHGLSTTLGQSYFENIAHILSNGEKRTFKNYKIKRSVRDKISEIINDLKSGERLPNVEKENKELREATSKNSEYVNGLEFTADVYFEDKDKVVMIELKTVRPNAGEMRGEKQKILYGKAYMMETKPNKKVYYFIGFPYDPTENPENPCGYDKDRFMSSLIEFSKYFDKREVLIAEELWSFLSGEENTMKKILDIINSIAKPDFKEKFDFINTFPFINQDRLYTKDAIDEQKFKKYMDILQEWRLYSEIECAKAVKELSLLKLSSRDRRTFERLINNSMFSNNNKYNENRKMKILELYNKYMQK | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GGNCC-3'; the cleavage site is unknown.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 43911
Sequence Length: 370
EC: 3.1.21.4
|
P23191 | MKNYVSNINLGNSSLKFIDERLQSENYRGIHLSQHNRYDLPKLIDILTLLNKHAPNQSLMQIRTTDISKRPQNIPEEQSYAEFCNEAKSLTNIGTQDAMRKNLFVDFARMGLINRYNDKKVLTDPFKRGVTKYVALSDMGVKLIDPKLDILSKNLIFSKSLNKLLTGFVEDVLSLLTNSDLKEISFDEFMLFVSAMNCNFNFSISTEQCESLIKEYRLLSRVQKNAVIDTLKSELIPDNFNGDKKDKRDYHNWANENQQIWTLFENIPFFIMEKDSRKLILITSDVDLSKYSKSKMKRSQQAKNDYFKHHKVNKIKGYELDHIIPLLEAESVDEYRYLDNWLNLLYIDGKTHAIKSQSGSKYYIFTFDDNDYNQIYFLDTQGDKLSINNDDTALFDKNKVPKIYEYNQNFINAKTS | Function: An E and S subtype restriction enzyme that recognizes the double-stranded sequences 5'-GAAGA-3' and 5'-TCTTC-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): 48617
Sequence Length: 416
EC: 3.1.21.4
|
Q58017 | MNFEYIINSLLETIKTYNFFVDWEKIENNIKKIEKRLHILNYLIGKENFKEEFFELLKEYPEVITVFPILIAVRDNKITILNENMELETLEFKEKKYLTDEEIERYYKFFKETGLEDLLKNRKIKNLVDYVFGVEVGMDTNARKNRIGDLMENIVKKYIENLCKQNKNLDYIFQATKDKIKQKWGINLTLDKTNRKFDFAVFNKNTKKLYLIEVNFYSGGGSKLKATAGEYRSLNEFIKNNNNNVQFIWITDGKGWNTAKNPLKESFNSGVVILNLKMVKEGLLKEILTQ | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GATC-3'; the cleavage site is unknown.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 34392
Sequence Length: 290
EC: 3.1.21.4
|
Q58723 | MVVKLVNNELKILSGKLRDIFREIYNKIKNDENINDRNLDDKVLSLLKDYTISEENLKIKFSEPKDEIYSYEGRRTPYDLLCYGIINGKNFLIFINNKFGDLKSNTRNDVTTYNNLLRLYLGIKRQRLTSEITINGELVYNRISGNEIVSYGIFVVDKYRRGYKFFLLEEIKDDFYVNPRNNMFQIRYSPNLGDPIDYFAFVKKLIDAILESLEKSLNSIKTEILVLNSIKIQLINIKEGKHGED | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GTNNAC-3'; the cleavage site is unknown.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 28779
Sequence Length: 245
EC: 3.1.21.4
|
P31032 | MNPLFTQERRIFHKKLLDGNILATNNRGVVSNADGSNTRSFNIAKGIADLLHSETVSERLPGQTSGNAFEAICSEFVQSAFEKLQHIRPGDWNVKQVGSRNRLEIARYQQYAHLTALAKAAEENPELAAALGSDYTITPDIIVTRNLIADAEINRNEFLVDENIATYASLRAGNGNMPLLHASISCKWTIRSDRAQNARSEGLNLVRNRKGRLPHIVVVTAEPTPSRISSIALGTGEIDCVYHFALYELEQILQSLNYEDALDLFYIMVNGKRLKDISDLPLDLAV | Cofactor: Binds 2 magnesium ions per subunit.
Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GCCGGC-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): 31760
Sequence Length: 286
EC: 3.1.21.4
|
Q58895 | MDDKSYYEEIESILRQILQPIEKISFSTFIRVVSGYKIIPIDLSKKEDKELINDLAKACNEVIEEIKKTGGVKTKEGKTPKRVNEVGNHIEHYVKDVLNKYGYAITPKTKKGKQKSTGYPDIEFWYKGKKERDGRVVYIEIKTFNEKNINSSHRTFYASPSKDEEGVKIRYDAPHLCLSFKIEKLGRDYYATGFKIIDLSKLKGGIKREFNASNRELYKKDLIIYEKDLK | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GTAC-3'; the cleavage site is unknown.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 26764
Sequence Length: 230
EC: 3.1.21.4
|
P81326 | MLHFGGFIMEINHISKILEKEREEYIRNKVEEYLKQGFSKDDAVNKANQSWRTYIGHRIQDVIYNLLKKFLKDSGLKVTTDKALNNRNLPEELDKVKRLIAINYGEYLFLPDADVIVYKVENNDIKIIAIISVKNSFRERRFETTYWKLKLKESPVTSHIKVFLATPDKDNEISYKCPNGKPKKMRIILEYELDGIYFLKEDFEETEKAKHFGKIVEDIIEISKKL | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CCGG-3'; the cleavage site is unknown.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 26711
Sequence Length: 226
EC: 3.1.21.4
|
Q58599 | MRKMFICLHNTYSAKQVEEFGRIAYGFDINTIVVTKATASAAQSGIPTLHKMAYKLGKNVLFFEELDDAIEVLRPEKVFLIGNKSICDEKVDFNEVGENDLVVFCGASTGFTKLELEKGLGRYIVENEIGALGNLAIFLYEMSKKI | Function: A putative type II restriction enzyme, its methylase would be M.MjaORF1200P (AC Q58600).
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 16296
Sequence Length: 146
EC: 3.1.21.4
|
P29565 | MSNLLQAIMNIKSIQERNLGSYKGVQDSKNRMNQMGVTLEVFLKDAFCNTFDIENKDLVYSEYFSYLGNQNNPPDMILKGGDAVEVKKITGIKTSIQLNSSYPKSKLFVSDSRITEACKNCEDWEVKDIIYAIGTIPNRVLKLMFFVYGDCYAASPSIYQRIVEEVKGGLHSTGLEFSETNELGRINRVDPLGITDLRVRGMWIIKHPIKVFKNIIPPESIKNNNFNLIALMKAEKYKQFPKKDRKRIEAEDNIEVTDVKIKDPDNPAKLLDSVLVRYDEI | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GGCC-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): 32102
Sequence Length: 281
EC: 3.1.21.4
|
P43642 | MGKSELSGRLNWQALAGLKASGAEQNLYNVFNAVFEGTKYVLYEKPKHLKNLYAQVVLPDDVIKEIFNPLIDLSTTQWGVSPDFAIENTETHKILFGEIKRQDGWVEGKDPSAGRGNAHERSCKLFTPGLLKAYRTIGGINDEEILPFWVVFEGDITRDPKRVREITFWYDHYQDNYFMWRPNESGEKLVQHFNEKLKKYLD | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CAATTG-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): 23389
Sequence Length: 202
EC: 3.1.21.4
|
O59646 | MKNPKFTENQKEIEKEEFEFLQKLNFIIKESLELFNTNLKNSMKFINYITLPIIMASIESKSFNPFSEIIEKHIAFILNSKMNSLGYKFLPLGYSSDLTYENDNSIIHIDIKTANLENPSDFKDTVPLGINQSSYPGVLDCKIRGKNIKADCKKIKVYPNIPTTYNNKLTITNALLFIYPDYKEIIDEIREDYIAIRELISINLKDILTPIEGSLEEFLNYKPSNEKKRLEPILDNIVRGYFIHDKLRHEFSENVEKDLEEFEKKIIGIAKKLKEREIKPVAILSISIPNGELAPHYDDEIVSGKSWGSSFRYHYKKSGNSVFKGLDNKASRAVFLHINKEYLPVLKKYFDPITVYELTEKRL | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GCNNNNNNNGC-3' and cleaves after N-5.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 42214
Sequence Length: 363
EC: 3.1.21.4
|
P29566 | MIDNFKEIRLDFKDELKKITGKEVEFPKYTTQIINLANQNAQGTRPRVVGQMSDLIHECPDKSYEGWKKWYLEHYSDRIEKATKKISKMIENMKAAMELIDEEMIRKWVEDLVITKTAEGLIIQEIILKTIAEEAGLEWRLATSKEESKNIDGFIGSTPVSIKPMSYESMRPTVREEIDIQTIFYKKPKNSRYLYIYHNLNI | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CTAG-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): 23742
Sequence Length: 202
EC: 3.1.21.4
|
P59551 | MNGDHMVLGSSVTDKKAIILVTILLLLRLVAIAGNGFITAALGVEWVLRRMLLPCDKLLVSLGASRFCLQSVVMGKTIYVFLHPMAFPYNPVLQFLAFQWDFLNAATLWSSTWLSVFYCVKIATFTHPVFFWLKHKLSGWLPWMLFSSVGLSSFTTILFFIGNHRMYQNYLRNHLQPWNVTGDSIRSYCEKFYLFPLKMITWTMPTAVFFICMILLITSLGRHRKKALLTTSGFREPSVQAHIKALLALLSFAMLFISYFLSLVFSAAGIFPPLDFKFWVWESVIYLCAAVHPIILLFSNCRLRAVLKSRRSSRCGTP | Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36337
Sequence Length: 318
Subcellular Location: Membrane
|
O34104 | MNPNKERLIEIFRSNVKGRIPDISGRNIRHDGRWGHWLEERFGISANADNHADILGYELKNEATSGKTTFGDWSANEYIFKTPPYNSLFSGSTASEKQNAFCRMFGKPNEAKNGRFSWSGSPIPKIWQYNSFGQIMVIEENLDIVIYYSFSQDLRYNKFEIIPPQLQHDEIQIARWYGVANPLLSRRGKTLKDKLEDKFNDLGWFTCTTDSIGAYDKICFGRPITFENWINLVDSGIVYFDSGMYEGNKRPYSQWRADNSYWNSLITDCHQ | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CCNGG-3' and cleaves after C-2.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 31467
Sequence Length: 271
EC: 3.1.21.4
|
P09796 | MSEAVFFVENAEELAKQKMDNINPELSEKFQLLIKFLSRFPESCSNPRSKQVRKNFGKAEHIEYLAQNFNESRLPKKPTPPTTIPDEVVSLVLNVSFDIPQENLNRIKEEHRLSMASENIVGDLLERYLAEKLEPCGWIWCSGTSVKAVDFIHYDNEKDEWGLLQVKNRDNTENSSSSKIRDNTPIKKWFRTFSQRDATNWENFPDEVSSKDLNEDDFRAFVESYLRKIK | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GGWCC-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): 26870
Sequence Length: 230
EC: 3.1.21.4
|
O31074 | MGITIKKSTAEQVLRKAYEAAASDDVFLEDWIFLATSLREVDAPRTYTAALVTALLARACDDRVDPRSIKEKYDDRAFSLRTLCHGVVVPMSVELGFDLGATGREPINNQPFFRYDQYSEIVRVQTKARPYLDRVSSALARVDEEDYSTEESFRALVAVLAVCISVANKKQRVAVGSAIVEASLIAETQSFVVSGHDVPRKLQACVAAGLDMVYSEVVSRRINDPSRDFPGDVQVILDGDPLLTVEVRGKSVSWEGLEQFVSSATYAGFRRVALMVDAASHVSLMSADDLTSALERKYECIVKVNESVSSFLRDVFVWSPRDVHSILSAFPEAMYRRMIEIEVREPELDRWAEIFPET | Function: A subtype P restriction enzyme that recognizes the double-stranded sequence 5'-GAGCTC-3' and cleaves after T-5.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 39965
Sequence Length: 358
EC: 3.1.21.4
|
Q53608 | MINADKPHRWNDDVQASVRLYNQWFLDAAPKAYRDTRQLTIDEVEQAFQRTANMTSITPEVLKAHPKTLATLRMSTAPPIARDRLVGLSHGSKSLLDTMEKGKLPPRMKGDVLDTHLAKMCAVLTDLLDLDLFHWYPTGEPAEPRQRELAATVVADRLCGAIADPIVRNAQERRQLALIEEWLLARGYTKKTHSASLPLNTMQPGTFSFRQNVVVGSDLPVNIPVDAVIQPHTPHSHKLPILIEAKSAGDFTNTNKRRKEEATKIHQLQLKYGNEISLTLFLCGYFNTGYLGYSAAEGLDWVWEHRIDDLEAAGA | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GTCGAC-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): 35337
Sequence Length: 315
EC: 3.1.21.4
|
O52691 | MINDQLPRWVREARVGTRTGGPAMRPKTSDSPYFGWDSEDWPEVTRQLLSEQPLSGDTLVDAVLASWESIFESRLGSGFHIGTQIRPTPQVMGFLLHALIPLELANGDPSWRADLNSSEKDLVYQPDHKYSIEMKTSSHKDQIFGNRSFGVENPGKGKKAKDGYYVAVNFEKWSDAPGRLPRIRTIRYGWLDHTDWVAQKSQTGQQSSLPAVVSNTQLLAIHTGGQR | Function: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-AGTACT-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): 25464
Sequence Length: 227
EC: 3.1.21.4
|
O52512 | MHQDYRELSLDELESVEKQTLRTIVQALQQYSKEAKSIFETTAADSSGEVIVLAEDITQYALEVAETYPINRRFAGFIDYKRVRWLPSPHGLLPQVLLVDAKASTEKNRDTLQRSQLPMDAEFRNTSSGEVVTMEAGVIPHLMLQSANDGVLPAVTTSIFVHFYYRELKDVEGRYRELKSIYVLSLPHARLKQRYNPDPDTSFFGAGKHSPARGEVARIRVYFDRLKEACPWRLQELHYSADSEYTQPRWRDLNDAGHEVTKEFLFLER | Function: An F and P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GGCCN(5)GGCC-3' and cleaves before N-9.
Catalytic Activity: Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Sequence Mass (Da): 31044
Sequence Length: 269
EC: 3.1.21.4
|
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