ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q83GR4 | MITKVSGFLFRTFREDPATTESRGYGFLLRAGYIRQTGSGIFSWMPLGLKVRHKIENIIRYEMGQVNAIEVLFPALFSADLFKQSGRWSEYGDDIFRLKDRRQGDYLLAPTHEEAFTQMMKEICTSYRDLPRTVYQIQDKYRDELRPRAGLLRSREFSMKDAYSFDLDEKGLRQSYEAQKRAYKKIFDRLKIDYVIVKANAGAMGGSVSEEFLHPTEMGDDTFVVTADGSAFNAEVYVTPPGPAIDYSNAPEAEDCETPGVISIPDLVNHMNSSGRFIGRVIESSDCLKCLLFRIEYAEVQNGNPSNLVVKKILERGFEY... | 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... |
B5ZBT9 | MAKKLEKIITRNENFADWYTSIVNNAKLIQYTDIKGMMVFQPNAWAIWEAIKNQIDLEFKKHGVRNLAMPTLIPLSEFQKEKDHIEGFAPELFMVNQIGDKKLDNPYAIRPTSEILFCNYFKNIVNSYNDLPIKNNQWCSVMRAEKTTRPFLRNAEFHWQELHAIFASEHEADEFAKTILDVYTDFVQNYLCIPVIKGLKTPWERFAGAQKTYTIEAMMQDGQALQSATSHYLGQFFAKAYDIKFQGQDNQMHYVHQMSAGLSTRIIGALIMVHADDQGLILPPDIAFNQIAILSIFANKNPQLLTISEQIRNELSDYRL... | 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: ... |
Q81R81 | MDYKTQFAESLSNIFTNELTQQQILDLIETPKQDEFGDAAFPCFSLAKQYKKSPAIIAKEVAEKLSDPFFTKVEAVGPYVNVFFNRDTVSDAVLKTILAEKEEYGKNYFGCEKTVVIDYSSPNIAKPFSMGHLRSTMIGNSLKHIAEKCGYEVVGINYIGDWGTQFGKLITAYKKWGNEAVVKEDPIRELFKLYVQFHEEVKDDEELEEEGRAWFKKLEEGDEEAVELWNWFRHESLKEFSRIYELLGVEFTNFQGEAFYNNLMEDFIGILEEHDLLEESEGALVVNLEEEGMPPCLIRKSDGATIYATRDLTAALYRQN... | 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 | MLAQMISEELARILSLKEDEVERLLEIPPQETLGDLAFPCFTLAKTKRKAPPFIAAELEAAFLEHKEVTAKATGGYVNFFFHRETVAGQLFQEMKSNQYWQPNSGDGKRVVIDMSSPNIAKPFGIGHLRSTIIGHALYHLLKKTGYDPIRVNHLGDWGTQFGKQIAAYQRWGGDVDLKQNPIASFLELYVRFHEEAEKDESLEDEGREWFKKLEEGDEEADRLWTYFVKESLNEFDRMYNRLGVEFDYVLGESFYNDQMAPVVKELQEKGLLTCSEGALVVPLEDADLPPCLIVKSDGTSIYATRDLATAIYRHHVQKGE... | 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 | MPITNTDESLSAASAPLKPGAFLHEIFSDRARQFPERTAVSDAARTLSYAQLDALSTKLAARLRDEGVTYGTRVGMYLPRSVDLVTSLLGILKAGGTYVPVDPQYPGKRVEHIVRDSELSLIIGDAANLPKISSLRVLALDELLSAPALQPAAQDTRIDPNNSTAYIIYTSGSTGEPKGVQVSHGNVSRLLESTQRAYGFNAQDVWSMFHSIGFDFSVWEIWGALAHGGQVAVVPYDISRSPAALRQWLADQRITVLSQTPSAFRGLDEADRGNTAPLALRYVVLGGEALPASVLRPWVERHGDQKPALINMYGITEATV... | 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:... |
Q3J281 | MNLFTEIRTLVTAELGAMTEAGDLPAGLDLSAVAVEPPRDPAHGDMSTNAAMVLAKPSGKPPRTIAEALATRLAADPRISSAEVAGPGFLNLRLRPAVWQGMVATILQAGDTYGRSTIGAGQKVNVEFVSANPTGPMHVGHVRGAVVGDALARLLAYAGWNVTREYYINDGGAQVDVLARSAFERYREAHGLEPEIREGLYPGDYLIPVGEALKAKYGDSLLDKGEQHWLTEVREFATEMMMQMIREDLAALGVEMDVYSSEKALYGTGKIEAALDRLKEMDLIYEGVLEPPKGKTPEDWEPREQTLFRSTAHGDDVDRP... | 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 | MRYALERFISDIQAAIVATGKVPADLIEITTPKPNIPADRTFVTFKAAKALGVDPVRLAADLATAIVPPPDSLIGEVTATGAFLNFTLHPQRLAAAVMAEIETYGDAYGSVADGANRTVVIDYSSPNIAKRMHVGHIRSTIIGQALVHIFRALGYRVIGDNHLGDWGTQFGIILAAMQRYGRPQNEGEAAMAELEALYARYNAEMKDNPPLEDEARRWSLALEQGDPTARELWQWCVDLTMRAAQRNYDRLGVRFDYAYGESFYEAMLPGVIEEALQSGAAFRDVDGAVVAELDKLPRFIVQRSDGGTVYITRDIATIKF... | 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 | MNIENYLSETLAKVFQKLGYAESFAKVVTSTREDVGHFQCNGAMPLAKFAKKPPLAIAEEIVEHIDAEDIFAKLEVAKPGFINITLAPKFLADTTNRFLNSNKFGVQNNLPNRKVVLDFGGPNVAKPMHVGHIRSALLGDALQRIHRFCGDTVVSDVHLGDWGTQMGMLIEEIKLQSPQLVYFDENYTGEYPTESPVTVQELAEIYPRASKRCKSDINEMEKARLATFELQQGRRGYVALWQHFVRISIDAVKKDFDSLDVHFDLWLGESDANKFIDEMISYFQANNFIYEDEGAWVIDTNKDGVPPLIVIKKDGGVMYG... | 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 | MKITSRELTDIFQKHVENLFPNKELKPVEITVATNENFGDYQCNFAMINSKIIGDNPRKIAEEVKNNFPYGDVIEKLEVAGPGFINIFLSDKYISNSIKKIGEDYDFSFLNRKGKVIIDFSSPNIAKRMHIGHLRSTIIGESISRIYRFLGYDVVADNHIGDWGTQFGKLIVGYRNWLDKKAYKKNAIEELERVYVKFSDEAEKDPSLEDLARAELKKVQDGEEENTKLWKEFITESLKEYNKLYKRLDVHFDTYYGESFYNDMMADVVKELVDKKIAVDDDGAKVVFFDEKDNLFPCIVQKKDGAYLYSTSDIATVKFR... | 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 | MKDAVRDLVREALERSFADGTLASGHVPDIVVEKPALEEHGDFACTAAMLMAKAEKKAPRAIAEIIITHLNDRESLVESVEIAGPGFINFRMRTSAWCRVLRRIEREGGDYGKSEAGAGKKVQVEFVSANPTGPLHIGHGRGAAIGDTICRLLAAIGWDVTREFYYNDAGQQIANLALSVQARCLGVEPGGPLWPTDGYQGEYIKDVARSYLNRETVDAGDQHVTAAGDPHDVEAIRRFAVAYLRREQDQDLRAFDVGFDVYFLESSLYAEGRVDDVVQRIIAKGHAYEQDGALWLRTTEFGDDKDRVMRKSDGSYTYFV... | 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 | MTALSLQQQLAESIYTALGTAFEAGQLGQLTQLPPRQSVVVEKPKVPEHGDYATPVAMSLAKPCRLAPLAIAEAIASYLASDEIGVEVAKPGFINLRLGHRFVAVELQNILELKGDYGRTVPQQPERILLEFVSANPTGPLHLGHGRWAALGSSLERILQFAGYTVDSEFYINDAGNQMQLLGLSLKQRYLQVLGEAVELPDGGYKGSYLKELAEQLVADKGDSLGGEPVEWFSAYAEGRLLEQQKITLQQFRTEFDRWYSERSLHCAGAIEAALADLEARGMLYRAARSRQEQSGEITGRSKKVQAPAAFEEEDGGGEA... | 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 | MFLELKAQATSILKEAIRKAGFEVEDSELQFETSPHADLASRAAFRLAGIHRQNPKDLASRIVSAVEIPEGSFIGKVSAAGPYINFFAGKHYLNGTVNAVLKEKEKFGCGAPKDRILLEHTSANPNGPLHVGHIRNSIIGDTLARILRRAGYDVEVQYYVNDMGRQIAVVSWACERFELDLSRKSDSAIADVYIKANVELDKNPGYIKEIDALMEKVEAGDVRTIEHFDKAVSLAVAGIKETLLRLNVAHDKFVSESTFLKSGAVHDIVERIKATGRTKTDKGALVVDLSDYGFEKTLVIQRSNGTSLYTTRDLAYHEWK... | 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 | MFRYIEKEARDSITAALEKLGIKVPPEIKLEEPPNPQLGDLASTVSFELAGKLRRAPIEITADIMSVIETPEIFETIESKGPYINFFVDYGRFSSRLLESIQDDYGSHPPRDERVILEHTSANPNGPLHIGHIRNAIIGDSLARILRMAGYDVETQYYVNDMGRQIAMIVWGLLNLDGDLEDYPGDKMDHRVGKLYFEVNQRLKENPGIRDEVDELIRKYEAGENEELFRKVVEYCLSGMEETMKRLHVHHDRFVWEGQFVRDGTVDRVIESLRKTGYTGENDVLYLDLEEFGLEKELVLTRSDGTSLYSTRDIAYHLQK... | 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 | MKDTIRQLIQQALDQLTADGTLPAGLTPDIQVENTKDRSHGDFASNIAMMLAKPAGMKPRDLAARLVEAIPAHEQLAKVEIAGPGFLNFFQDHVWLAASLDRALADERLGVRKAGPAQRVVIDLSSPNLAKEMHVGHLRSTIIGDAVARVLEFLGDTVIRQNHVGDWGTQFGMLLAYLEEQPVDAEAELHDLEVFYRAAKKRFDESPEFADRARELVVKLQAGDPDCLRLWTRFNEISLSHCQKVYDRLGVKLSMADVMGESAYNDDLAQVVADLTAKGLLTEDNGALCVFLEEFKNAEGNPLPVIVQKAGGGYLYATTD... | 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 | MTPEELSLAISACLKDAVAAGEIALAESAVPEDVRVERPKNRDHGDWATNIALQLAKQAGTNPREFATILSARLKTISGVSAVDIAGPGFLNITVDAAAAGALAKAIVEAGTQYGTNTALAGHTVNMEFVSANPTGPLHIGHTRWAALGDAIARVLRASGADVTAEYYINDAGSQMNTFANSVYSRLHGLPVPEGGYPGQYIADLGHEVLTAHPDIRELTEVAALPVIRAAAYEAQMKDIKATLADFGVAFDVFFSEQELHDAGAIESAVARLREQGHVFDDGGAVWLRTTDFGDDKDRVMIRANGEPTYFAADAAYYLS... | 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 | MNIRTILVEKAIAAMTTVGLPADTNPAVTQSTRPQFGDYQINAAMGAAKKMKSNPRELAQKIIDNLDVSDIAEKTEIAGPGFINIHLKPEFLAQSVKAANSDAKLAVNEHANPQKVVVDYSSPNLAKEMHVGHLRSTIIGDAIVRALEFRGDSVVRQNHMGDWGTQFGMLIAHLEDQISQGVDLDTVALADLETFYRDAKKRFDDEEGFADKARNYVVKLQGGDAHCEKLWKLFIATSVKHSEEVYKRLNVTLTQADIMAESAYNAELNDIISLLKDKNIAVESQGAQVVFLDELANKDGEPSAFIVQKSGGGFLYATTD... | 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 | MASVTSLSDSVQQHLASALTATRPEAAGADPLLRRSDRADYQANGILALAKKTKANPRELAAEVVARITTGDELIEDVEVSGPGFLNITVADRAITANLAARLADGERLGVPLKQDAGTTVVDYAQPNVAKEMHVGHLRSAVIGDALRSMLDFTGEKTIGRHHIGDWGTQFGMLIQYLFEHPGELAPAGDIDGEQAMSNLNRVYKASRAVFDTDEEFKERARRRVVALQSGDKETLDLWQQFVDESKVYFYSVFEKLDMEIRDEEIVGESAYNDGMPETARLLEEMGVAVRSEGALVVFFDEIRGKDDQPVPLIVQKADG... | 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 | MIDPVLLREHPDVLRRSQEARGDSVQLVDEALQVDIERRAAITAFEELRAEQNAFGKRVAQAPKQEKKELVAQAQQLAGRVKEAQQVAAAAEARFESVLRKIGNPVVAGVPSGGEDDYAVLKEVGGIPAFGFEPRDHLALGELLGAIDMARGAKVSGARFSFLRGLGARLEIALMNLALDKALANGFVPLITPTLVKPEVMQGTGFLGEHSDEVYHLETDDLYLTGTSEVALAGYHADEILDVTEPLRYAGWSTCYRREAGSAGKDTRGIIRVHQFTKLEMFVYTLPEHAEAEHARLLAWQEEMMQALGLSYRVIDTAAG... | 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... |
Q72LS1 | MLDLRYITENTEDLKKVLELRGFKEIGIIDELKSIIQRKREFQKEADILREERNKASKEVGKIKQSGGDITKISASVKLVGEKIKEIESKLEQEENALLNINLGLPNILDPKVPPGKSEHDNIVQYEVGKIPTFQFVPKTHFEIGEALHWIDFEKGVKLSGARAYTYWKDGARLERALMNFMLDVHTKEHDYTEVWVPSMVNDESMMATGQYPKFKDEFYRIDKDELNLIPTAEVPLTNLYRDEIIPEDQLPISVTAHTSCFRREAGSYGKDTRGLVRVHQFQKVELVKFCKPEDSEEEHKKMLSHAENILKKLELPYRV... | 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... |
Q8ZTP4 | MSYSVLEALRNSPDVVRKVLTARRMDASLVDKFLELDEKWRRLKKEVDELRHEYNKLSKEGAKAPPERRREIADKARELAARLERAEKELEETERAREEVLWSFPNLIHESVPICPEGVDSIPVRHWGVVKTTKDVVDKLDKGVDYLVVEKAPVGHADMAEVVLKMADTLKAGEVAGSRFYYLFDDLVWLDFALAMYALDYLAQKGFRPVIPPYMLKYDLIRRVLDFDTFKDAIYKIDGEDLYLIATAEHGIAAYLYKRELLEEELPQLYVGWSPCFRKEAGAGSRDIKGIFRVHIFHKVEQFVFSLPEDSWKWHEEITK... | 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... |
O58441 | MLDIKLIRENPELVKNDLIKRGELEKVKWVDEILKLDTEWRTKLKEINRLRHERNKIAVEIGKRRKKGEPVDELLAKSREIVKRIGELENEVEELKKKIDYYLWRLPNITHPSVPVGKDENDNVPIRFWGKARVWKGHLERFLEQSQGKMEYEILEWKPKLHVDLLEILGGADFARAAKVSGSRFYYLLNEIVILDLALIRFALDRLIEKGFTPVIPPYMVRRFVEEGSTSFEDFEDVIYKVEDEDLYLIPTAEHPLAGMHANEILDGKDLPLLYVGVSPCFRKEAGTAGKDTKGIFRVHQFHKVEQFVYSRPEESWEWH... | 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... |
Q98LC8 | MLDIKWIRDNPKALVEALAKRSWSAGEAQSTVDDLIARDEARREHVTELQTKQERRNAASKEIGNAMRSGDAALAEKLKAEVGDIKTFIQNGEARERELDKALTDALAVLPNVPLDDVPVGKDEHDNVVKHIVGKVPTRSNWVKEHFEIGEALGMMDFERAAKLSGSRFTVLKSGLARMERAIGQFMLDLHTTEHGYEEVIPPLMVRDEVLFGTNQLPKFEEDLFFTPHGEGRLGLIPTAEVPLTNLVREEITAHEKLPLRFTALTPCFRSEAGSAGRDTRGMLRQHQFYKVELVSITDQDSSLAEHERMTQCAEEVLKR... | 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... |
Q7UXX6 | MLDRKFILQNAQLVAENSAKRGVSVDVDAICRLEAERMDALKQAEELNRQANEVSKQIKSAKDNDERQELIAKGRSLREQKDAAGAAQDRLEAEILELQTILPNMTHPDVPEGGEHDANEIGRGKTPVPEMDFQPLDHLQLGEKHDLFDFEGGARVAGSGFYFLRNAAVRLDLALQQFAISHLAGKGFTPVSTPDLALTSVLQGTGFNPRGPETQIYSIENTELNLVATAEIPLGGMLSGQILASEELPLRYCGLSHCFRTEAGAAGRASKGLYRVHQFTKVEMFAFTLPDQSTAMHEEMRELECEIFDALEVPYRVIDT... | 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... |
Q7MLV2 | MLDSKLLRTELDETAAKLARRGFKLDVETIGKLEEQRKSIQVEVENLQSTRNSISKQIGQLMSAGDKEGAEKIKQQIGSLGSDLDVKKIELDAVMAQLDDIILSVPNIPADEVPNGKDENDNLEISRWGEPKSYDFELKDHVDLGEMGDGLDFASAVKITGARFIVMKGQFARLHRAIAQFMLDLHTEEHGYTEMYVPYLVNADSLFGTGQLPKFGKDLFHTEPLTEKASDEEPRKLSLIPTAEVPVTNLVRDTISDEADLPLKMTAHTPCFRSEAGSYGRDTRGLIRMHQFDKVELVQITKPEDSMNALEELTGHAEKV... | 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... |
Q8D265 | MIDHKLIIKNIEEVCKKLILRNFYLDKKKILLQDQKRKILQIEVEKLQNKRNLQSKIISKIKINNKNIDIYKNKSNKINILLNEKKQKLKKIKKEIDNYLSTIPNILDEKVPIGKDQKNNIEVKKWGSPKIYNFKIKSHVEIGEKIKYLDFSRSAKISGSRFVVMKNKISYMHRALSQFMLNLHTNQHGYEEYYVPYLVNKNMLYGTGQLPKFYNDFFYAKSFFEDIQSCYALIPTAEVPLTNLMRNEIIDENYLPIKMTSHTPCFRSEAGSYGKDTKGLIRMHQFDKVEIVQIVSPENSIKALEEITHHAERVLQLLDL... | 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... |
Q7M9J5 | MIDLKLLMNDFEEVAERLAKRHLEADFLEQARLLAGQYKAKKRESEELQAEQNAKSKLFGQYKKEGKEIDSLKAELDTLKIRLSEILPEVSVLERELESLALIIPNLPDEKTPIGRDEHDNIEIRRVLEPKMFDFRPKEHWELAEQNGWIEFDRGVKLAKSRFSVLRKEGARMSRALISYMLDFNHSRGFEEVVTPVIVNRETLLGTGQLPKFENDLFKISEVIEEEQGGEKGRGHELYLIPTAEVTLTNLYRDEIIPHDELPLLLTAHTPCFRKEAGSAGRDTRGIIRQHQFDKVELVALTKPEESDAIQQKMIDCASD... | 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... |
O67583 | MEKIKVKIKGKEYEVEKGTPLGKIFELAGIKDALGGVINGKIIDLQTPVRESGEIKPVYRGSKESLEIMRHSLAHIMAQALKELYGAKKVHLGVGPTTEEGFYYDVEVEGHKITEEDLPKIEQKMKEIIERDYPILRRELSREEAIKLFDKLKEKYKIDIIKEIPEEEVISVYEQGDFIDLCKGPHLPSTGKAGAFKLTSISGAYWKGRSDQPQLTRIYGIAYWSDKEVKERLKFYEEVKKRDHRRLGKELEFFTIDDNVGAGLILWLPRGAIYRKVLEDYLREEHLKRGYQLVYTPHVGKSKLWETSGHLECYKQNMFP... | 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... |
Q5P7X5 | MPNITLPDGSVRSFDHPVTVSEVASSIGAGLAKAALAGKVDGRLVDLSYRIEADTPLAIVTEKGDEGLDVIRHSTAHLLAHAVKELFPEAQVTIGPVIENGFYYDFAYKRPFTPEDLEKIEKRMAELARREIPVSREVWPRDKAVEFFKSQGEHYKAEIIASIPQAEDVSLYRQGDFIDLCRGPHVPSTGKLKVFKLTKVAGAYWRGDSKNEMLQRIYGTAWAKKDDLENYLHMLEEAEKRDHRKLGRLLDLFHIQEEAPGMVFWHAKGWTLWQQVEQYMRRTILDNGYQEVKTPQIVDRSLWEKSGHWDMYSELMFTTQ... | 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... |
A0JXC7 | MSDAQQITLIVDGEETKVTTGTTGAELFFERRDVVVARVNGELKDLDQPLPEGADIEGVTIDSPDGLNVLRHSTAHVMAQAVQQLRPDAKLGIGPYITDGFYFDFDVAEPFTPEDLKALEKMMLKIINQNQKFVRRVVSEDEAREAMKNEPYKLELLGKKNNAADAGEGVNVEVGAGDITIYDNVDRKSGDSVWCDLCRGPHLPNTKLISNAFALTRSSAAYWLGNQNNQQLQRIYGTAWPTKDALKAYQERIAEAERRDHRKLGAELDLFSFPDELGSGLPVFHPKGGIIRKAMEDYSRQRHVDAGYDFVYTPHITKGH... | 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... |
B6YQ95 | MIKITFPNTSARNYAIGTTPMQIAESISCRLAEEILSANVNGEMWDLSRPINENASVKLYKWEDFEGKRTFWHSSAHLLAESLQELYPNIHFGMGPAIENGFYYDVDLGDGVVIKDVDLVTIEKKMQELASKKLSISRQNVTKQNALELFGKKGETYKIELISKLEDGKITVYTQGNFTDLCRGPHLPNTSYIKAIKLTSVARAYWKGDESRKQLTRIYGISFPKKEELSEYLALMEKAKKRDHRRIGKEMELFTFSHKVGRGLPLWLPKGTQLRLRLEDFLKRIQKKYGYQQVITPHIGNKTLYIASGHYAKYGKDSFQ... | 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... |
Q8AAP2 | MIKITFPDGSVREYNEGVNGLQIAESISSRLAQDVLACGVNGETYDLGRPINEDADFVLYKWDDEEGKHAFWHTSAHLLAEALQELYPGIQFGIGPAIENGFYYDVDPGEAVIKESDLPAIEAKMLELSAKKDAVVRESISKTDALKMFGDRGETYKCELISELEDGHITTYTQGAFTDLCRGPHLMTTAPIKAIKLTTVAGAYWRGHEDRKMLTRIYGITFPKKKMLDEYLVLLEEAKKRDHRKIGKEMQLFMFSETVGKGLPMWLPKGTALRLRLQEFLRRIQTRYDYQEVITPPIGNKLLYVTSGHYAKYGKDAFQP... | 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... |
Q728R5 | MNVSIEGQMLEVASGASCGDALKGALSGKKFKNVLACRLDGGLVDITATVPDGTTTIEPVYADSPEGLDLIRHSTAHIMACAVKRLFPAAKVTIGPSIDNGFYYDFDAERPFSPEDFEAIEREMQKIVDAATPFERSEMPRDEAVALFEGMGETYKVEIIRDLPNDTVSLYRCGEFVDLCRGPHIPHAGFAKAFKLMSVAGAYWRGDEKNPMLSRIYGTAFADAKTLKEHLHRIEEAKRRDHRKLGQQLDLFAFHEDVAPGMVFWHPKGMLVRTIIEDFLRKEHLKRRYDIVQGPQLLRRELWEKSGHYDNYRENMYFTE... | 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... |
Q8XE27 | MPVITLPDGSQRHYDHAVSPMDVALDIGPGLAKACIAGRVNGELVDACDLIENDAQLSIITAKDEEGLEIIRHSCAHLLGHAIKQLWPHTKMAIGPVIDNGFYYDVDLDRTLTQEDVEALEKRMHELAEKNYDVIKKKVSWHEARETFANRGESYKVSILDENIAHDDKPGLYFHEEYVDMCRGPHVPNMRFCHHFKLMKTAGAYWRGDSNNKMLQRIYGTAWADKKALNAYLQRLEEAAKRDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQEVKGPFMMDRVLWEKTGHWDNYKDAMFTT... | 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... |
Q58597 | MKMLLIHSDYLEFEAKEKTKIAEETENLKGKLDECLACFIAVEREDENNPEGTAIGAVEEIEKVANQLKVNNIVVYPYAHLSSDLSSPETAVKVLKDIESILKERGYNVLRAPFGWYKAFKISCKGHPLSELSRKIVAKEEKKEEGEESKFYLLNPETEEIIELNENNINIIKDEELLALAKHELGIREHKEHDEPPHVKFIKEKDICSYEEASDPGHFRWYPKGKLMRDLLADYVYNLVVNMGAMPVETPIMYDLGNPAIREHADKFGERQYRFRQGNKELMLRFAACFGQFMMKKDMYLLPRYLPLKLYELSTYSFRY... | 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 inc... |
Q7UJ52 | MSADSPSSPASSQAAEVQVRLPDGSLKTQPADATAMDVAKEISEGLARSVVAAEVDGTIVDSFRPLGEIADDENVVPLRLLTTRDESALDVLRHSAAHVMARAIMRIYKGVSLAFGPTTSGGFYYDFDMPEKISEDDFPKIEAEIKKIIKAKEPFERFVLERDEARKLCDDLDQDLKVEHIETGLGDQATVSFYRQGEFVDLCRGPHIPHAGMIKAIKLLSVAGAYWKGDASGRQLQRVYGTAFFDKKELASYLEQIEEAKRRDHRVLGKQHGLFAINPEVGQGLCLWLPKGARVRVTLEDFLRRELLSRGYDPVYSPHI... | 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... |
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 s... |
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 s... |
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 abo... |
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. Activat... |
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. Activat... |
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 ... |
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 ... |
Q6MAM1 | MTELPKAYEAKKIDEKWYQFWDAKRYFTANPLSNKPTYCIVIPPPNVTGVLHMGHALVNTVQDILIRWKRMLGFETLWVPGTDHAGIATQMVVERHLIKTEGKKRTDYTREEFLKHVWTWKEKSENRIIEQLKRLGNSCDWTRLRFTMDENNSLAVRTMFKKLFDDGLIYRGDYLVNWDPHTQTALADDEVEYEDKQSFLWYFKYPLRDESEFISIATTRPETMLGDTAVAVSPNDERFKHLIGKEIRLPLMNRLIPIIADHHVDPSFGTGVVKITPAHDPNDYQIGLSHRLPFINIMTPDGKINENGGHFQGLSMTEAR... | 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 + ... |
Q4FM20 | MSNDKYIHTDVEDKIYSYWEKNNLFKPTKNKKQFSVVIPPPNVTGSLHMGHALNNSIQDLLVRYHRMNNYETLWQPGTDHAGIATQALVEKKLTADGIDKNEIGREKFIEKVWEWKEEHGDIILNQLKKLGCSCDWSRNAFTMDENLSKSVLKVFVELHKKGLIYKDKKLVNWDTVLKTAISDLEVDQREVNSKIYYIQYPIEASSDFITIATTRPETMLGDTAIAVNPKDDRFKHLVGKFVTVPIVGKKIKIIEDEYADPEMGTGALKITPAHDFNDYEVGQRNNLEIINIFTEGGKVNENAPKEYIGLDRFEARKRII... | 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 + ... |
Q6LUW1 | MEKTYNPQSIEQALYQRWEEAGYFKPHGDTSKDAYSIMIPPPNVTGSLHMGHAFQDTIMDTLIRAERMKGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTKHDYGRDAFIDKIWEWKAESGGTITKQLRRLGASVDWDRERFTMDDGLSAATQEVFVRLFEEDLIYRGKRLVNWDPKLHTAISDLEVESKDKKGFMWHFRYPLADGVKTADGKDYIVVATTRPETMLGDTGVAVNPEDPRYKDLIGKQIKLPIVGRLIPIVGDEHADMDKGTGCVKITPAHDFNDYEVGKRHSLPMINILTFNADIRDAAEVFDTNGEA... | 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 + ... |
A6L3G7 | MELASKYNPADVEGKWYQYWLDNKLFSSKPDGREPYTVVIPPPNVTGVLHMGHMLNNTIQDILVRRARMEGKNACWVPGTDHASIATEAKVVNKLAGQGIKKTDLSRDEFLKHAWAWTEEHGGIILKQLRKLGASCDWDRTAFTMDEERSESVIKVFVDLYNKGLIYRGVRMVNWDPKALTALSDEEVIYKEEHSKLYYLRYKVEGDAEGRYAVVATTRPETIMGDTAMCINPNDPKNQWLKGKKVIVPLVNRIIPVIEDDYVDIEFGTGCLKVTPAHDVNDYMLGEKYNLPSIDIFNDNGTLSEAAGLYVGMDRFDVRK... | 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 + ... |
B2RK53 | MEIASKYNPEEVESKWYNYWMEYGCFISVPDGRKPYTVVIPPPNVTGVLHMGHMLNNTIQDILVRRARMKGYNACWVPGTDHASIATEAKVVGRLAAQGISKQDLGREEFLRHAWDWTHEHGGIILEQLKRLGASCDWTRTAFTMDESRSESVIKVFVDLYNKGLIYRGIRVVNWDPKALTALSDEEVIYKETNGKLYYLRYFVENEPDKYIIVATTRPETIMGDTAVCVNPNDERYRWLRGKRVIVPTVGRAVPIIEDEYVDMEFGTGCLKVTPAHDVNDYMLGQKHRLESIDIFHDNGILNEHGGPYAGMDRFDVRKK... | 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 + ... |
Q9JYQ9 | MSKKRVLTGVTTTGIPHLGNYVGAIRPAVRAAQNLDTESFLFLADYHGIIKCHEPEMIHQSTQAVAATWLACGLDPERTTFYRQSDTPEVMELNWILTCITAKGLMNRAHAYKAAVQANAENGQEDPDFGVEMGLFSYPILMTADILMFNANEVPVGRDQIQHVEMARDIAGRFNHRFRELFTLPEVKIDENVELLVGLDGRKMSKSYGNTIPLWENDKKTQKSVNKIITNMKEPGEPKQPDESPLFEIYKAFSTPSETVEFTKMLADGLAWGEAKKLLAAKINAELAEPRERYNELTADPSQIEEILQAGAAKARKEAR... | 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 | METVVSGIRPTGNLHLGNYFGAIRSFLDMQHRYNCFFFIADWHSLTTHPHPDNIVRNVRTILAEYLACGIDPEKATIYVQSDVREVLELYLYLNMNAYLGELERTTSFKEKARKQPNNVNAGLLTYPTLMAADILIHRAVKVPVGKDQEQNMEMARKFARRFNTIYEVDFFPEPESFSPGATALKVPGLDGSGKMGKSEGNAIYLADDAKTISKKVMKAVTDAGPEVPNSVKPEPVENLFSMLRIVSSDEVYRHFDDLYNNCSIRYGDLKKQLAADIVAFTTPIRERILEIQADEAFLDRVVREGAERARESAARTLAEV... | 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 | MTTRILTGITPTGTPHLGNYAGAIRPAILASRRSDVDSFYFLADYHALIKCDDPARIQRSRLEIAATWLAGGLDVERATFYRQSDIPEIPELTWLLTCVSAKGLLNRAHAYKAAVDRNVEAGEDPDAGVTMGLYSYPVLMAADILMFNAHKIPVGRDQVQHVEMARDIGQRFNHLFGNGREFFVLPEAVIEENVATLPGLDGRKMSKSYDNTIPLFSPSRQLKDAIARIVTDSRAPGEPKDPDSSHLFLLYSAFASAEQVAAFRQELLEGLAWGEAKQRLFQLLDNELGEARERYQALIAKPDDIEDILLAGAAKARRIA... | 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 | MEEEFVVTPWEVRGRVDYEKLLKHFGAKPLTKDEVALLEKYAGEVHPLIRRGFFYAHRDFDFIMKWHGEGRPWALYTGRGPSGPVHIGHMVPWILLKWFSDKFGLEVYFQITDDEKFYDDPEMKLEEATNWAYENALDVIALGFSPERLHLIIDTKDIKPLYPIAVRVAKKLTWNTVKATFGFTDSTNIGLIFYPSLQIAVAFLPTELRREATPVLIPCAIDQDPYFRLARDIADALGYPKPSTLYSKFIMALTGESKMSASNPDSAIYTLDDEKTVRRKVMNAFTGGRPTAEEQRKYGGNPEVCPVFHYHMLFDPDDAS... | 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 | MTPEEQLRIIKEGTVEIIEEEELLKKLKEGRPLRVKAGFDPTAPDLHLGHVVLLQKLRQFQQLGHEVFFIIGDFTAMIGDPTGRSQTRPPLSREQVLENAKTYEHQVFKVLIPEKTTVVFNSTWLEELGTKGLIELCAKYTVARMLEREDFSKRFKEGIPIYIHEFIYPLLQAYDSVAIKADVEIGGTDQKFNLLIGRDIQREYGQEPQVCITLPLLVGTDGVRKMSKSYGNYVGITEDPKTMFAKIMSIPDEIMWDWFLLLTDYNKEEIEKMRREMHPMEAKKLLAFTIVKRFHSEEEARKAKEWWEKTFSQREFPEDA... | 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
Sequen... |
O29482 | MDITEKLRLITRNAEEVVTEEELRQLIETKEKPRAYVGYEPSGEIHLGHMMTVQKLMDLQEAGFEIIVLLADIHAYLNEKGTFEEIAEVADYNKKVFIALGLDESRAKFVLGSEYQLSRDYVLDVLKMARITTLNRARRSMDEVSRRKEDPMVSQMIYPLMQALDIAHLGVDLAVGGIDQRKIHMLARENLPRLGYSSPVCLHTPILVGLDGQKMSSSKGNYISVRDPPEEVERKIRKAYCPAGVVEENPILDIAKYHILPRFGKIVVERDAKFGGDVEYASFEELAEDFKSGQLHPLDLKIAVAKYLNMLLEDARKRLG... | 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
Sequen... |
Q2NJG7 | MSFYEELKWRNLIKDCNNEIQVKELLDNNQVKFYCGFDPTSHSLTVGHLIQITMILLMQRQGHLPVILVGGATGLIGDPKETEERKLLSLENSLQNAKSIESQLKTILLNKQVEFVNNYQWLSQIDIISFLRNYGKFFNINYMLSKHVVAKRLASGISFTEFSYMILQSLDFHHLYKNHKVRLQLGGSDQWGNITSGLEIIRKLEKKSDALGVSTPLLLNSDGTKFGKSEKRVLWLNPLMTSPYEIYQYFLNVSDKEVINYLKMLTLIPKKGILELEKKTLENPQKRLAQKALTQSIINLIHSSDILQECIKTNQILFSN... | 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
Sequen... |
Q8A2S5 | MNFVEELRWRGMLQDIMPGTEELLNKEQVTAYLGIDPTADSLHIGHLCGVMILRHLQRCGHKPLALIGGATGMIGDPSGKSAERNLLNEETLRHNQACIKKQLAKFLDFESDVPNRAELVNNYDWMKEFSFLDFVREVGKHITVNYMMAKDSVKRRLNGEARDGLSFTEFTYQLLQGYDFLHLYETKGCKLQMGGSDQWGNITTGAELIRRTNGGEVFALTCPLITKADGGKFGKTESGNIWLDPRYTSPYKFYQFWLNVSDSDAERYIKIFTSIEKEEIEALVAEHQQAPHLRALQKRLAKEVTIMVHSEEDYNAAVDA... | 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
Sequen... |
Q5UPJ7 | MENTDHTNNEHRLTQLLSIAEECETLDRLKQLVDSGRIFTAYNGFEPSGRIHIAQALITVMNTNNIIECGGQMIIYIADWFAKMNLKMNGDINKIRELGRYFIEVFKACGINLDGTRFIWASEFIASNPSYIERMLDIAEFSTISRVKRCCQIMGRNESDCLKASQIFYPCMQAADVFELVPEGIDICQLGIDQRKVNMLAIEYANDRGLKIPISLSHHMLMSLSGPKKKMSKSDPQGAIFMDDTEQEVSEKISRAYCTDETFDNPIFEYIKYLLLRWFGTLNLCGKIYTDIESIQEDFSSMNKRELKTDVANYINTIID... | 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
Sequen... |
Q2RHS8 | MHDYFGGWFKLEQEVARQLRILRRGVAEIVPEEDLQAKLRKSLATGKPLKVKLGLDPTAPDIHLGHTVVLQKLRQFQELGHQVIIIIGDFTGRIGDPTGKSETRRQLTEAEILANAETYKEQIFKVLDPEQTRVTFNSHWLGKLTFAEVIELAARTTVARMLERDDFARRFQENRPISIHEFFYPLMQGYDSVALAADVELGGTDQKFNLLMGRHLQREYGQEPQVAMMMPILPGLDGVQKMSKSLGNYIGIKESPREMYGKTMSLPDELMLTYYELVTAVPLEELAAIRQGLASGSLHPRDAKMRLAREIVAMYHTPEA... | 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
Sequen... |
Q7NBH9 | MDFISELKKRNIIKQISNEEKLALALKNQKGVYVGFDPSGESLHLGNLIPIIVLRYLKKVGFKTYAILGGATGLIGDPSGKTSERKVQDYEKITANANKIKVQLERYTQAKIINNIDFYQNMNLLNFLRDTGKLINIGYLLDKEFIRSRIENGISYAEFSYNIIQGHDFLHLYEQYDVQVQCGGSDQWGNITTGIDMIKRKYGEEKTPYLCGLTFNLLLNPNGNKFGKSEQGALYLDENLTHPYLIWQYIYNQDDQFIIDLIHRYVLDQSLEQLQELIEAHLANKKTRIAQKFLADYLVKFIHSQEHLDTVHKMNKALFD... | 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
Sequen... |
P47693 | MLNNILQFLKERELYSQANFETELDNHLKEKKNNFYVGFDPTANSLHIGNYVLIHIAKLLKDMGHTPHIVLGSATALIGDPTGRIELRKILEEKEIVKNTKTIKKQIKQFLGDVIIHENKVWLEKLNYIEVIRELGAFFSVNKMLSTDAFSARWEKGLTLMELNYMILQAYDFYYLHKNHNVTLQIGGSDQWANILAGANLIKRKNNASVFGLTANLLVKANGEKMGKTSSGALWLDENKTSVFDFYQYWINLDDQSLKKTFLMLTMLDKKVIDELCNLKGPKIKQTKQMLAFLITELIHGTKKAKEAQQRSELIFSNQP... | 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
Sequen... |
Q98Q81 | MSQNKLKTLIEELKKRKVFNNITSEEKVDLITLDHGIYVGFDPTAISLHLGNYIQMVNLKRFQNVGFKTIAILGGATSMIGDPSFKDSERKLLSNETILENKKHIRKQLENFGFKVIDNLDFYKDMNILDYLRSVGKFFNVSTMMSRDSVANRIQSGLSFTEFSYQTLQAYDFKVLCEKENVMMQLGGSDQWGNLVSGLDFINKTLSKNLPTIGITMNLLVDSNGNKIGKSTGGASLWIDKTLTSPYVLYQYLLNTNDDDAYNLLLQLTFLQLSEIERIKNEHLKNPKLRLMQSRLSFEVVKDIHGKEEAQRALHISTSL... | 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
Sequen... |
Q4A5E2 | MHKVLTELRDREILKDISNEEKFLSLPKNSGVYVGFDPTADSLHLGNYVQIVNLIRFKKHNWNALAVLGGATGMIGDPSFRSTERVLLSTEELLKNKNKIKSQLESFGLKVFDNYEIYKDISFLDFLKNIGKLINVSYMLAKDSVKDRLAQGLSFTEFSYQIIQGYDFLHLYQNQDIFVQYGGSDQWGNITTGIEMISKVVGDNHKAIAITANLLTDSNGNKFGKSTGGGNLWLDAQKTKPFDMYQFLINQPDSEVEKLLKWLTFLEISEIKDLVNKHNKNPKDRLAQKALAYEVIKDIHGKSAAENCTFLSEMLFNLSL... | 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
Sequen... |
Q74MD3 | MDIEERINLIAQKPTEEILTIDRLKQYLEQGIDLNHYIGFEISGFVHLGTGIISMLKVRDFQKAKVKTTLFLADYHSWINKKLGGDLETIRKVAKGYFAEALKVSLKTVGGDPDEVKVVLGSELYEKLGIEYLENIIKISMNTTLNRIKKGITIMGRKQGESISFAQLLYVPMQVADIYSLNVNLAHGGIDQRKAHVIAIEVSDAFGYKPIAVHHHLLLGMHIDENIRQKLLEAKKTNNRELFEDSVIDIKMSKSKPETAIFIHDTPEDIRRKIRKAYCPIGEIELNPIIELVEYVIYPILKEPIVIENKKTHQTMEFDN... | 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
Sequen... |
Q67QD6 | MTMAFMSVDEQMKILMRGVVDLVSEEELRQKLERSVKTGRPLRVKLGIDPTGKDLTLGHTVPLRKLRDFVECGHQGVLIIGDYTAMVGDPTGRNEARPQLTHAETTANAQRYLEQAARVLDVSKLEIRRNSEWLAPMSFSDVIRLAAKSTVARMLEREDFKKRYEEGRPIFIHEFFYPLMQGTDSVAVQADVELGGTDQKFNLLAGRDLQRDAGQEPQVCLMTPIVEGLDGVQKMSKSLGNYIGLDHTPDEMFGRTMSIPDSLIITYFTYFTDVPQEEIERIEAAMAAGENPMTFKKQLGRAIITTYGGTEEEARLAEER... | 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
Sequen... |
Q2LR98 | MILKNVYDVFMERGFIEQVTDENAVRKALEAPLACYIGFDPTARSLHIGSLVPIMALIHLQRHGHTSIALVGGGTALIGDPSGKTEMRQILTREKIELNATCMRRQFARYLSFEDKKAMMINNADWLTKLNYISFLRDIGRHFSVNKMLAAESYKMRLEKGLNFIEFNYMLLQAYDFLYLFQNHNCVMQMGGNDQWGNMLAGVDLIRRVEGKVAHSMTFPLLTTATGQKMGKTEKGAVWLDRELTSPYEYYQYWINTGDIDVGKFLALFTFLPMEEIHQVKSLSDKELNMAKAILAFEATKITHGEDAALAAWNASAVAF... | 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
Sequen... |
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... |
Q24JP5 | MCARMAGRTTAAPRGPYGPWLCLLVALALDVVRVDCGQAPLDPVYLPAALELLDAPEHFRVQQVGHYPPANSSLSSRSETFLLLQPWPRAQPLLRASYPPFATQQVVPPRVTEPHQRPVPWDVRAVSVEAAVTPAEPYARVLFHLKGQDWPPGSGSLPCARLHATHPAGTAHQACRFQPSLGACVVELELPSHWFSQASTTRAELAYTLEPAAEGPGGCGSGEENDPGEQALPVGGVELRPADPPQYQEVPLDEAVTLRVPDMPVRPGQLFSATLLLRHNFTASLLTLRIKVKKGLHVTAARPAQPTLWTAKLDRFKGSR... | 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... |
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-kynu... |
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-kynu... |
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-kynu... |
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
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Q58844 | MPLSKNVIEKISIETIRVLKSRFDTISDEDIKIRNMPFHMAFLRAFYGKIGINDDTEALKFLTLSQWFHGLSTTLGQSYFENIAHILSNGEKRTFKNYKIKRSVRDKISEIINDLKSGERLPNVEKENKELREATSKNSEYVNGLEFTADVYFEDKDKVVMIELKTVRPNAGEMRGEKQKILYGKAYMMETKPNKKVYYFIGFPYDPTENPENPCGYDKDRFMSSLIEFSKYFDKREVLIAEELWSFLSGEENTMKKILDIINSIAKPDFKEKFDFINTFPFINQDRLYTKDAIDEQKFKKYMDILQEWRLYSEIECAKA... | 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
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P23191 | MKNYVSNINLGNSSLKFIDERLQSENYRGIHLSQHNRYDLPKLIDILTLLNKHAPNQSLMQIRTTDISKRPQNIPEEQSYAEFCNEAKSLTNIGTQDAMRKNLFVDFARMGLINRYNDKKVLTDPFKRGVTKYVALSDMGVKLIDPKLDILSKNLIFSKSLNKLLTGFVEDVLSLLTNSDLKEISFDEFMLFVSAMNCNFNFSISTEQCESLIKEYRLLSRVQKNAVIDTLKSELIPDNFNGDKKDKRDYHNWANENQQIWTLFENIPFFIMEKDSRKLILITSDVDLSKYSKSKMKRSQQAKNDYFKHHKVNKIKGYEL... | 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 fr... |
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
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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
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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
Se... |
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
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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
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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
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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
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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
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O59646 | MKNPKFTENQKEIEKEEFEFLQKLNFIIKESLELFNTNLKNSMKFINYITLPIIMASIESKSFNPFSEIIEKHIAFILNSKMNSLGYKFLPLGYSSDLTYENDNSIIHIDIKTANLENPSDFKDTVPLGINQSSYPGVLDCKIRGKNIKADCKKIKVYPNIPTTYNNKLTITNALLFIYPDYKEIIDEIREDYIAIRELISINLKDILTPIEGSLEEFLNYKPSNEKKRLEPILDNIVRGYFIHDKLRHEFSENVEKDLEEFEKKIIGIAKKLKEREIKPVAILSISIPNGELAPHYDDEIVSGKSWGSSFRYHYKKSGN... | 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
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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
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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)... |
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
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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 | MGITIKKSTAEQVLRKAYEAAASDDVFLEDWIFLATSLREVDAPRTYTAALVTALLARACDDRVDPRSIKEKYDDRAFSLRTLCHGVVVPMSVELGFDLGATGREPINNQPFFRYDQYSEIVRVQTKARPYLDRVSSALARVDEEDYSTEESFRALVAVLAVCISVANKKQRVAVGSAIVEASLIAETQSFVVSGHDVPRKLQACVAAGLDMVYSEVVSRRINDPSRDFPGDVQVILDGDPLLTVEVRGKSVSWEGLEQFVSSATYAGFRRVALMVDAASHVSLMSADDLTSALERKYECIVKVNESVSSFLRDVFVWSP... | 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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