ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q3SWL7 | MSLIVKICGLSTPSTLDVALQAGADMVGFVFFPPSPRHLELARAQELGAQVRGRAAKVALTADADDETLCGIIEALRPDLLQLHGKETVPRIREIKRRFGLPVMKAIGVEIAADLADLPRYAAVADRLLFDARPPKHATRPGGLGVPFDWRLLTNLSVDIPFMLSGGLAAGNVDDAVRITRAGGVDVSSGVESAPGVKDAGMVRDFIRAARAAETSLREATSHVP | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 23863
Sequence Length: 225
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q8ESU3 | MFVKICGITSIDTAQAVVDANADMIGFVFAPSKRQLSTSLAEEIANTLPQTIQKVGVFVDEPLENILSIIERVNLDIVQLHGDESIDYQKRIPIPIIKAFPATTEGLNQANQSSAKYILIDSPPLQSSRGGNGVTFNWNILKDQPFTSKLILAGGLNTENIREAIKTVNPAGVDVSSGVETNGKKDAKKIQQFITNVQRKDVLR | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22232
Sequence Length: 204
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
A6L9J9 | MIIKVCGMREPQNIREVAALAINWIGFIFYERSKRFVERCPTEQQATDSEQLSPKKVGVFVNATIESMMEKASTYKLDYLQLHGNESPEDCHTLQKRGYSLIKAFPIATKEDFEKTREYEGRVDYFLFDTRCEGYGGSGKRFDWSILTGYKGETPFLLSGGIRPENAEAIRNFRHPRFAGIDLNSGFEIEPGLKDIDKLKNFIQQILHPAVETGRAPSPTV | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 25196
Sequence Length: 221
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q7TU07 | MQANDRPRTFHLTVAYDGTEYCGWQVQPEQRSIQSELERVIRPLAGRPVRVLGSGRTDAGVHAIGQVARCVLPVWKADTVALQRAINSKLPNDIRVKAVRETRERFHPIADATGKQYQYLVQVGGSRDPFANRFVNRVGGPIDHSAMQSAAAKFVGRHDFKAFQGTGAERPSTVRTIHSARWIPRVATGPTGAELEGEHWCFEIDGEGFLYNMVRNLMGTMLEVGRGKKSPNWIDEVLASRDRKMAGPTAPPQGLFLCRVDYPDEVFQVEEPDVIE | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30792
Sequence Length: 276
EC: 5.4.99.12
|
Q2RNZ9 | MVRYRLTVEYDGRGYCGWQRQDNGPTIQQSLEEAAFRLCGVATRVHGSGRTDSGVHALGQVAHLDLPRAYGAATVMKALNAHLRPQPIAVIDAAEVAEDFHARFSAEERSYRYRILNRIAPPTLDQGRVWWVARPMEAAIMDEAAQVLVGRHDFSSFRAAECQADSPVKTLSELRVTRVGDEIHVFARARSFLHHQVRNMVGTLALVGDGRWTADRLRAALEACDRSAAGPTAPPDGLYFLRVRFPGETAAPAKAGPLEAAPLGEAPLKEATLKEDWR | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30619
Sequence Length: 278
EC: 5.4.99.12
|
Q9ZCA3 | MYRYKITIEYLGTHFAGWQRQAGVLSVQQILEEAIYKFSSEQVTLFGSGRTDAGVHAIGQVAHFDLSKYLEPYKIIKAINYFVRPYDVGVWNCELVSNNFHARFSAISRHYIYRIINRTYPSVIDFNRAWWISSPLDILAMQKAAAYLLGKHDFTSFRSSSCQSKSPIKTLTEINIIKEYEEIKLYISAPSFLHYMVRNIVGSLVLVGKNIWQAEQIKNVLDARDRKIAGPTAPAFGLYFIKAEY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 28170
Sequence Length: 245
EC: 5.4.99.12
|
P32732 | MVNGVLLLHKPVGMTSHDCVMKIRKLLKTKKVGHTGTLDPEVSGVLPICVGRATKIVEYLTEKSKTYDAEITLGFSTTTEDQTGETVETKPVNHDIDKADVEKVLNSLKGKQEQIPPMYSAVKVNGKKLYEYARAGIEVERPKRMITIEDIALTTEIKHHGETASFRFTVTCSKGTYVRTLAVMIGEKLGYPAHMSHLIRTASGDFSLDECFTFDELEAQAQSGTVEEHTVPIERALNHLPKWIISDTLAKKVENGALLETPEQFSEMTSGDRIAVFTESGTCLAIYFPHPAKKGLLKPAKVLMQKSEQ | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 34204
Sequence Length: 309
EC: 5.4.99.25
|
Q8A2U2 | MNFKKGEVLFFNKPLGWTSFKVVGHVRYHICRRIGVKKLKVGHAGTLDPLATGVMILCTGKATKRIEEFQYHTKEYVATLRLGATTPSYDLEHEIDATYPTGHITRELVEETLTHFLGAIEQVPPAFSACMVDGKRAYELARKGEEVELKAKQLVIDEIELLECRLDDPEPTIRIRVVCSKGTYIRALARDIGEALQSGAHLTELIRTRVGDVRLEDCLDPEHFKEWIDRQEIENDEDNN | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 27290
Sequence Length: 240
EC: 5.4.99.25
|
Q6G0P4 | MVRQRKKRGRPVSGWVIFDKPKGMRSTEAVSQIKWLFHAQKAGHAGTLDPLASGLLPIALGEATKTVPYVMQGTKTYRFQIAWGEERSTDDLEGEITHISSKRPTQEEILALLPQYTGVILQTPPQFSAIKITGNRAYDLAREGKVVEIPPRQVEIETFKLIETPTRERSVFEITCGKGTYVRSLARDMGRDLGCYGHIADLRRTTVAPFCEDDLITWEELKAVALDKIAINENGIPSERNFTKIDELLIETGAALKCLSHYTLSETRAQ | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 30257
Sequence Length: 270
EC: 5.4.99.25
|
Q1LSL0 | MCFSLNINSHNINGIILLDKQEGLSSNYLLHKVKRLFRVQKAGHTGALDPLASGMLPICLGEATKFSKYLLDADKRYIVSAKLGEKTNTYDATGIIINTRPVTINQAMIEHIMEQFYGDIYQIPPMFSSIKYQGRALYKYARKGINIPRSARLVHIYNLQILDWDNTHIELQIHCSKGTYIRTIIDDIGELLGCGAHVTMLRRLAVAHYHTARMITLESLQTAITLALRQTPNTLVQLNKLLLPIDSAVANFPAIKLSKDSVARVRKGQMVAVDQCWQSGLVRMCENKGETTYFFGIGEITQPGVLKPKRLLAEKYV | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 35647
Sequence Length: 317
EC: 5.4.99.25
|
Q6MMS4 | MTNKNQFNGLLLVDKPSGISSHDVVARLRRILSTRAVGHSGTLDPMASGLMACLVNEGTKLSQYILEGDKGYRLRAQFGIRTDTLDTTGETLETRPTDHLTRELILSEALKLQGEMEVEVPIYSAIKVQGKKLYEYARGEQEVTIPKKVMKFWDIEPVEIGSDWAEFDIKCSKGSYIRTWIDLLGKALGCGAAMSGLRRTWSSPYKIDQAQTLEQIEASVKGGSLGPAFVPMELALPQVKRIRIKGQDKVLLGNGQISHDLRSQLISAFNPDVDQYIQVLAQEGGELLAVIGLEPGRGFVLRRVFKYS | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 34110
Sequence Length: 308
EC: 5.4.99.25
|
Q8CY45 | MLHTTPSGLLIIDKPQGVTSFDAVAAVRGALHIKKVGHAGTLDPMATGTLVIAFGHATRLLNAIVAHDKTYEATIRLGLRTTTDDAEGEVLVDGEARSRWQTLSAQLTEGGQSGEPTALPTASWQDLLTRTIATNFTGDIEQVPNTFSAIKINGQRAYDLAREGKDVELKPRPVTISEFTVLDIRSGFVAGEQAAEPLREDANTGAIPALDVDVRISCSSGTYIRALARDLGKELGVGGYLTRLRRTRVGRFALPDDASGLIAPEAMLDTRTHTVTAHTDQKTFTNREGQTVTRNKCVLDTPEGLAGDERRNWLLDHALT... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 41719
Sequence Length: 387
EC: 5.4.99.25
|
Q493T5 | MKRYKNVRNRDINGILLLDKPKGISSGLFLNKIKKLFNAKKIGHTGTLDPLATGMLPVCFGKATKLAKYLLHSDKRYKVSAQLGVSTDTFDSDGTIISVSPVQSNDYILEQCLESFIGIRNQIPPMFSSLKYRGVPLYKYARKGIYFPRKPRSIHIYNLSLIKKTENIIELDVHCSTGTYIRSIVNDIGEYLGCGAHVIELRRLSVGQYISSSMINPATLEAIFYNDSFDDVQVFCKLDAFLTPMNMIMLELANISNEKC | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 29277
Sequence Length: 260
EC: 5.4.99.25
|
Q2KXZ0 | MAKRRGQPLDGVLLLDKPVGLSSNHALQRAKRTLDAAKAGHTGTLDPFATGLLLCCMGRATKISGAMLNADKTYRATLQFGEETDSGDLTGNIVARAPEDFPGVEEANLREVLSRFQGSIEQIPPMYSALKRDGKPLYEYARAGIELERPPRRVMIYRIELLSFTGHQAEIDVACSKGTYIRTLAQDIGRALGCYAHLFALRRTQVGPFSLDRAVTLDALQAMTDPKAALLALNELPAGLLPAT | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 26479
Sequence Length: 244
EC: 5.4.99.25
|
O51743 | MENGFLLINKEQGKTSFETLFPIKKYFNTNRVGHAGTLDKFASGILVCLVGKYTKLSGYFTSLDKEYVAEFRFGLETDTLDPNGRIVSKTDYIPNVEDIDLKLKDFVGEIYQSPPRFSSVHIDGSRAYKLALNGKFFEIKKRKVTVYNIQRLSYDFSSSLLSLKISCSKGTYIRSIARDLAYSLNSCAYVSNLKRTKVGMFRLKDSTLCENLSKASLISLESLKSFEKVYIDSNKINLVKNGVYFEIEININEFKILKSREEKILAVIQGVGLNKYKYVIIF | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 32145
Sequence Length: 282
EC: 5.4.99.25
|
Q8TRR5 | MSSAGKLPSEIERTLVRKSGAWTNPVYGCAPEKRPILEYIEKGVVNIDKPSGPTSHEVAAWVKAILGVNTAGHAGSLDPKVTGLLPTLLGKATKAVPALRLSGKEYVCHLKLHRAMPPKLVRKVCEEFTGPIYQMPPIKSAVKRVIRVRTIYYIEVLEIEGMSVLFRVGCEAGTYIRKLCHDIGLALGCGGHMQALRRTKAGPFTEKTLVTLHELKDAYVFWKEDGDESELRRVIRPMESAVSHLPKIILRDSAVDAVCSGASLAVPGITSLDSSLAEGELAALFTLKGELVALAKAEMNTEEILKASAGIAASPIRVLM... | Function: Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 36647
Sequence Length: 338
EC: 5.4.99.25
|
Q609C2 | MGAISTATLSGVLLLDKGSGMTSNSALQRARKLLDMRKAGHTGSLDPLASGILPLCFNEATKLSSYLLDSDKRYRVLARLGVTTDTGDADGEVRLRTPVPALDEPALLTVLAGFTGPILQVPPMFSALKHRGKRLYELARKGVEVERPPRPVTVFEIELAGRGADYLELDVHCSKGTYQAVEKVSIEAAMYPFAWVRGRRKPFFSAPTAAWAPPLGAARPFWAH | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 24287
Sequence Length: 224
EC: 5.4.99.25
|
Q57612 | MILLEKTQEKKINDKEELIVKEEVETNWDYGCNPYERKIEDLIKYGVVVVDKPRGPTSHEVSTWVKKILNLDKAGHGGTLDPKVTGVLPVALERATKTIPMWHIPPKEYVCLMHLHRDASEEDILRVFKEFTGRIYQRPPLKAAVKRRLRIRKIHELELLDKDGKDVLFRVKCQSGTYIRKLCEDIGEALGTSAHMQELRRTKSGCFEEKDAVYLQDLLDAYVFWKEDGDEEELRRVIKPMEYGLRHLKKVVVKDSAVDAICHGADVYVRGIAKLSKGIGKGETVLVETLKGEAVAVGKALMNTKEILNADKGVAVDVER... | Function: Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 38483
Sequence Length: 336
EC: 5.4.99.25
|
Q6LWM3 | MELIVKEESKTDYNYGSDPYNRDIKTLLNTGLVVIDKPSGPTSHEVAAWVRNMLNLVKAGHGGTLDPKVTGALPVALGNTTKCVPIWHIPPKEYVCLMHLHDDAELVDIENIFKEFTGRIHQRPPLKAAVKRSLRIRKIYEIEILEIDGRDILFRTKCQSGTYLRKLVDDMGEALGTSAHMQELRRTISGPFYENEAVYLQDLLDAYIFWKEDGNEEELRKIVKPLEYGLQHLKKIIIKDSAVDAVCHGATLYSSGISKIEKGLGTDEVVLIETLKGEAVAVGKPLMNTKDMLKTEEGEVVEITRVIMEPGIYPRIWKKR... | Function: Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 37662
Sequence Length: 333
EC: 5.4.99.25
|
B0JJJ5 | MFGFLNLNKPPDWTSHDCVAKVRKILKTKRVGHGGTLDPMATGVLPIAVGAATRLLAYLPENKAYRAKIQLGLSTDTDDITGKAIATCPWPDLTLEAVKPHLAEFIGNIAQIPPMYSAIHKDGRRLYELARKGEIIAVEPRQVKIDQITVLDWLEGEFPQIELDIHCGSGTYIRSLARDLGKVLAVGGTLASLTRTESCGFQLADSINLEALMVNSEGLISPRIALAHLDWISFTPERVIDWFHGRKINLTDTNVIIGSLVAVESLEAQFLGIGEIVVAEDEYYLQPKIVIQQ | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 32218
Sequence Length: 293
EC: 5.4.99.25
|
Q2RJM2 | MVMGFVNVLKPPGLTSHDVVQNLRRLLKVKRIGHGGTLDPLAAGVLPVAVGTATRLLEYLQGGDKAYRAEFILGLKTDTQDLGGRVLARKPCPPFTEKDLQAATRPFTGTIRQVPPMVSAVHYQGRRLYELAREGLEVERPARQVTIHEFRLIRAWPDGPYYRALIDITCSRGTYIRTLGADWGDYLGVGATLAFLLRTRAGSFRLTDAWTLEEIAGAIDRGERTFLLPPAAGLAHLPVIIVPGEFIRHVSNGVAIKGDVCRPLPSLREGDIVRLETGEGQLLALARVEPDTRGSFLLKPHKVLK | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 33505
Sequence Length: 305
EC: 5.4.99.25
|
Q6L1A0 | MSNLNGFIVVDKPKGPTSHQIDSWIRDITGEPRVGHIGTLDPGVSGVLVMALGKATKLIDIVHRESKEYVSVLRTYDKYDHDSIKSVFKEFTGKIYQIPPVRSAVSRELRIREIYNLELLEMDEKFVLFKVCCESGTYIRTLCTDIGYVLGSGGQMAELRRTRTGPFDESMCHTLQEVSDAFKLKSMGNEKLFKNIFIPMDFIFIKYPKVIVKETALKNIAHGSDIYPAGIHAITGSPKKGDVVAVYTEKNELVATGTMMVNADEIYDLKVIDIDNVLIETGDNDGKDSLVRKDNRWKDIPVQKPERKLHGNLQGSQEWK... | Function: Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 39148
Sequence Length: 349
EC: 5.4.99.25
|
A2BY54 | MEIKDGFIIINKEKGYTSHDCVQQIRKLLGTKKVGHTGTLDPGVTGTLPIAIGSATRFIQYLPQGKTYIGQIQLGIRTKTDDIQGEIINKKEWPILSNAQLDKFLNKFRGIIQQIPPKVSSVHVNGERAYKKFFKNEEFELKPREVKIEELVLKKWDQINGILEIKISCSTGTYIRSIARDLGGVLDSEGCLLNLKRISACGFHEKNSIKISDLVNLNKNCSTFIIPTIYALDHISTLILNNQEEINFWETGRLIKLDEENLIKSSKFDYKKPIKIINNQKMLLGIGFINEDKNKLHPKLVLNAK | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 34618
Sequence Length: 305
EC: 5.4.99.25
|
P59880 | MNSIALGFLVINKPAGLTSHDCVNRLRRIYGIKRIGHGGTLDPAVTGVLPIAIGKATRLLSFLPSPKTYEGTIKLGISTNTDDLTGETISEHSWDQVKENSILNCLNKFQGEIKQCPPIFSSVHINGERAYKKARRGEFFELPPKLIKIYRIKLINWNKKDGTIDLEVHCSPGTYIRSLARDIGKKLGCGGALAKLNRTMALGFNIDQAIELPDLDKNNDLNKPMIIDPLKALSHLPSIKLMTIDELSSWRKGKHLILSKSRLKNPLYLIEDDKDIPKTFLTVINNENHLIGLARWHHEPFKIEPKIVFNADG | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 35025
Sequence Length: 313
EC: 5.4.99.25
|
P59881 | MTVPFGFVVIDKPAGITSHDCVSRMRRVFGIKRVGHGGTLDPAVTGVLPIALGHATRLLPYLPGAKSYRGSIQLGQRTSSDDQQGDLISKQAWPELNTAEIEAYLEPFRGRIQQRPPQVSAVHVQGERAHARARRGETMEIPARTITIDRLQLLNWNQQLGQIDFNVHCSSGTYIRSLARDLGELIGCGACLGWLKRTQALGFHEQQAVPLPDRDNPALTTPPAVLPPLTALAHLPRLQLNEEEQESWSCGRRITAHQDQCQPAPKPLASDQQESAPNQTDPSANKSMLVVIDCRGEVAGMAYWEDNATVKPKVVFNAQG | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 35093
Sequence Length: 320
EC: 5.4.99.25
|
P72154 | MAQVKRIRRSISGILVLDKPRGMSSNQALQKVRWLLNAEKAGHTGSLDPLATGVLPLCFGEATKFSQYLLDADKGYETVMRMGITTTTGDAEGELLAERDVTVGRDDLEQALPRFRGDIEQVPPMYSALKKDGQPLYKLARAGEVVEREARSVTITRLDLLSFEPPCATLAVSCSKGTYVRTLVEDLGQVLGCGAHVAALRRTQAGPFALAQAITLETLERVHAEGGPEALDQFLMPEDSGLLHWPVLQLSEHSAYYWLHGQPVRAPEAPKFGWLRVQDHTGRFIGIGEVTDDGRIAPRRLIRS | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs (By similarity). Osmoprotectant regulator of PLC.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 33410
Sequence Length: 304
EC: 5.4.99.25
|
Q58008 | MPLNMNKYLTDAYTGGIIKKYPEDFIVEEITPEGIILEVGKSIEFKDEENWKGNYIHFTLEKRNWTTLDAIREIANRVGKQRKHFGFAGNKDKYAVTTQRVGCFNVKLEDLMKVKIKGIILRDFQKTNRKIRLGDLWGNRFTIRVREPELKGKELEEALNKLCKLKYFLNYYGVQRFGTTRPITHIVGRFIIERDWEGAFHAYCGTPLPYDDKKSKLARELVDEENFKEAYKKFPKAFFYERRMIKAYIETGSYQKAFMILPPYLRCMFINAYQSYLFNEIINRRFEYGFEPMEGDILIDNVPSGALFGYKTRFASGIQG... | Function: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 46320
Sequence Length: 392
EC: 5.4.99.27
|
Q58759 | MKNISTKESFFKFKFNNRSLYCWGAFMKLRMKPEDFIVEEIIDFNKIAGDRCYLYKLTKRNIESLKAFSYIAKKFKIPLKDIGYCGLKDRHALTTQYISIPKKYGKLSLDEPNLKLELIGESKFLLLGDLEGNRFTITVRGLKKEDIPKIKENLKYLEFGAPNYFDSQRFGSVFDKKFIAKEVIKGNYEEAVKILLTKYKKSEKKLIKDLKRFIDKNWGDWDKIWEYIKENNIKSRLYVNMVKELKKSNDYKKALSYVDDRLKKIFVAAYQSYLWNECVKELLRKYVPEEDRVYYEYECGTLMFYKKMDEEVFNILKDKK... | Function: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 50180
Sequence Length: 422
EC: 5.4.99.27
|
Q6LZL0 | MPININKFILDMERFDGTLKKYPEDFIVEEITPEGTVLEVGKEIGFEDVEKWHGSFIHFTVEKTNWNTMDALKQIVRATKTKRKNFGFAGTKDKFAVTTQRFGCFGLKKEQLENINIKDIVIRDVQKTNKKLRMGGLWGNKFTIKIRDLNLSEKEIKRISDLKLDYVLNYYGIQRFGLIRPITHIVGKFIYERDFESAFYTYCGTPINETGDSLEARQLVDMGEFKKALKLFNRGHDYEKRLIQQYLKYKDFKMAFTALPPQLNSMFVNAYQAYLFNEMINKRFDYGFDELEGDILEDNTPTGTLIGYDTKFSGGIQGEI... | Function: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 45732
Sequence Length: 390
EC: 5.4.99.27
|
A7HGV2 | MTDAPLVTAELPGSGGSLRRSPEDFRVDEVPAYLPSGAGPHLYLRVEKRGRTTRDALRTLARALGVPERDAGYAGLKDKDAVTTQWLSFPAARDPEPQALASEGLRVLEVSRHANKLRPGHVRANRFQLAVRGGDLARAQAAAAALAERGLPNLFGPQRFGTEGRNAEVGRALLLGDPSPEARRAARDRFLRRLSISAYQALLFNRWLAERMADGLFATAVAGDVLKKLDTGGLFTCADPAVDGPRVQRFEVSPAGPMFGHKLRAAEGEALAREERLLAAEGIQLSDFARGGGEAEGTRRAARLRVEVALAPLEDGYLAT... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 37581
Sequence Length: 349
EC: 5.4.99.27
|
O67616 | MDIRIKEKPEEFYVKEIKKLDLKEKGQYAYFLLKKKDMTTLDAVRHISHRFGIPLKNIGFAGLKDKKAVTEQYISVKDLNEEKIRKMDGYRTENLELKFLGFSDKGLELGEIEGNYFEVVVRGVTKYHRRVFPRMKELVENYGCENYFGEQRFGSVKHAEEFIVKYLLRHEYEEAMKEYLTSLGDKRLKRLLRKAWRDWDRFLSLMPKGAKPELEVVKALRRGESFKNAFMVLPKNIRLMFVFAYQSYLWNRYLYTFVVRYLKYCKTPFLKWELAFFNDMSEVIWEEIKDLEIPYLGVEYKPRNKKAEIVMKEVLQDEGI... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 45775
Sequence Length: 385
EC: 5.4.99.27
|
O28596 | MEEKVGIECYITSTPGMGGEIKAEPEDFYVEEIAEFNLSDEGDFLIIRVEKKNWDTLNFARVLSNALGISQKRISFAGTKDKRALTVQYFSIYGVKKEEIERVNLKDAKIEVIGYARRAIQLGDLLGNFFRIRVYGCRDGEIFQETRNELMEKGTPNFFGLQRFGSIRFITHEVGKLILQNNYEEAFWVYVAKPFEGENEEVRKIREILWETRDAKLGLRELPKYLRYERNLLQKLREGKSEEEALLSLPKNLKMMFVHAYQSYIFNRLLSERIRQFGSLKTLEEGDFACYLTFKTRPTFSDCSEVEVNEARVRFLVKER... | Function: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 47716
Sequence Length: 411
EC: 5.4.99.27
|
Q9PMK3 | MNLEEENTIFKPLYSLKHSPINAYFSKNSDDFVVRERPLYEFSGKGEHLILHINKKDLTTNEALKILSEASGVKIRDFGYAGLKDKQGSTFQYLSMPKKFESFLSNFSHPKLKILEIFTHENKLRIGHLKGNSFFIRLKKVLPSDALKLEQALMNLDKQGFANYFGYQRFGKFGDNYKEGLEILRGKKMKNVKMKEFLISAFQSELFNRYLSKRVELSHFANDFSEKELIQIYKISKEEAKELKKQEQFFKLLKGEVLGHYPFGKCFLCEDLSAELGRFKARDISAMGLLIGAKAYETGEGLALNLENEIFKDTLEFKAK... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 43445
Sequence Length: 372
EC: 5.4.99.27
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Q5JDB6 | MDYREFFSQFKHLSEKPGIGGKIKIYPEDFIVIEEPIPSIFEGRKYAIFLLKKRNWETMAAVKEIAKRAGINYREIGFAGTKDRHAVTYQYISVPAEARERVEQVSIRDIELRFVSYGRFIKLGHLLGNRFRIIVRDVSEDAFDRTKEIVRELREKGGFPNYFGYQRFGERRVVNHIIGKLLLQGDFEGAARLFLGAHDGSMEGDEARKNFWETGDVERALEEFPGFLRYERTLLHRYKDTGNWKRAFLSLPLPIMRIFIHAYQSYLFNLYLSRRIEEGLPLNEPLVGDIVVQVKGGIPYRDRTYRVTETNLEFVREKVR... | Function: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 48538
Sequence Length: 416
EC: 5.4.99.27
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Q5SI49 | MDLVFRPERYPFLTQDLPGVGGEIRVEPEDFQVEEVPAYLPKGEGEHLYLLLEKEGRTTREVLEFLRDEVGVPEKEIGVAGLKDKRAKTRQWFSIPRKYEDALCLLENLQGVRLLAADLHTNKLRTGHLKGNRFHILIRRPKGGVAEAEAVLKRLAEKGVPNYYGPQRFGLGGLNPVRGYKLVKEGKGRGSPWLKRFLIGSLQSLLFNDWVALRMALGLYDRVVPGDWAKKHATGGEFLVEDPGEAERALRLEISATGPLFGKKYPEAQGEARAIEDEVLARYGLKREEFRARRGARRPIRVPLAEWKVEEAPEGLWLSF... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 40182
Sequence Length: 356
EC: 5.4.99.27
|
Q978K9 | MNKPENFEEAIEIKRDPEDFSVEEIADIEPDPNGKYTIIKARVRDWDTNRIAAEIARRLHMSRKRVTFAGTKDKRAVKLQYFCINSADVDVASLSGIKDFEVIESFKSSHYLTLGDLIANHFKIRFYGIDPEMFRERYVHIISKGGFPNFFGDQRFGSRRRNTHEIGKLIIKGEYEEAVKKYIYDEKYDKESYRKHFIDTLDYKTALERFPHSLSFERSLIGYYARNGTFKGAFDSLPKNLTIMFVHAYQSYLFNRILDERLKIYGLNAVLPGDIAFPVDAYFNPDKSKPIEVNSYNREKISKLVSSDKIRISLPIFGYK... | Function: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 47352
Sequence Length: 409
EC: 5.4.99.27
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Q7MHQ6 | MTDTLASLAYLAGKPTAQAKIKAKPEHFQVREDLGFEFTGSGEHLMVRIRKTGENTSFVANELAKACGVKSKDVSWAGLKDRHAVTEQWLSVHLPKAETPDFSAFLAQYPSIEILATARHNKKLRPGDLVGNDFVVTLSEVSDVDDVLKRLETVAKLGVPNYFGNQRFGNNGNNLQEAKRWGRDNVRSRNQNQRSLYLSAARSWIFNLIVSARLEQSLFDKVLLGDILFKGDEQLLVSAENHADLQSQYDAGDLVISGALAGDNALPTQDDALALEQVFLDAEPDLMALIRGNRMRHDRRAIALKPANLSWQVDGNNIIL... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 38524
Sequence Length: 347
EC: 5.4.99.27
|
P59893 | MERLYYLNHAPIDFHFAQTPRDFVVEEIPLYPFSGAGEHLVLKIRKRNLSTFELVDILSSHLGIKSREIGYAGLKDKSALTLQHLSIPAKFGDKLEAFDHPEVKILEQVRHENKIRIGHLKGNRFFIRLKKLSPLNSLKIQGVLEEIKRWGIPNYFGYQRFGNDGNNHEIGRKIAHGEQRVTSPKRRTFLLSAYQSKLFNEWLKERIKLSKILAEFTPSEASRLAPMIPVEQLKALQKQPHPFKILPGEILHHYPHGKIFVAEDMEEESRRFVEKDIVPAGLLSGTKAKSSEGIAHLYEAPFIDEKIQEQGSRRLAWIFP... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 41776
Sequence Length: 361
EC: 5.4.99.27
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Q8PLR6 | MSETSLLPRAHGAAVLSAAMRSTPDDFQVDELPAFEPSGEGEHLLLTVRKRGQNTAYIAKKLAHWAGIAEMGVSYAGLKDRHAVTTQRFSVHLPRRIAPDIAALDDTQMQVVESSWHNRKLQRGALHGNRFVLTLRQVQGERDAIEQRLQAIAARGIPNWFGEQRFGRDGGNVAAALAMFGHVQADDGTLLPAPTSRRRLRHDQRSMLLSAARSALFNRVLGARVAQGSWDGALEGEAWMLDGSRSVFGPEPWSEALAERLARFDIHPSGPLWGAGQLRSTDQAAAVEQGALSDPPSIALRQGLEAAGLKQERRALRLRP... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 40357
Sequence Length: 369
EC: 5.4.99.27
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O62768 | MNGSKDLPEPYDYDLIIIGGGSGGLAAAKEAAKYDKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALRDSRNYGWNVEETVKHDWERMTEAVQNHIGSLNWGYRVALREKKVTYENAYGEFVGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMQEHGIKFIRQFVPIKVEQIEAGTPGRLRVIAKSTDSDQTIEGEYNTVLLAIGRDACTRKIGLENVGVKINEKTGKIPVTE... | Cofactor: Binds 1 FAD per subunit.
Function: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catal... |
Q17745 | MKSLTELFGCFKRQPRQQEASSPANPHVSDTLSMGVAASGMPPPKRPAPAESPTLPGETLVDAPGIPLKEALKEAANSKIVIFYNSSDEEKQLVEFETYLNSLKEPADAEKPLEIPEIKKLQVSRASQKVIQYLTLHTSWPLMYIKGNAVGGLKELKALKQDYLKEWLRDHTYDLIVIGGGSGGLAAAKEASRLGKKVACLDFVKPSPQGTSWGLGGTCVNVGCIPKKLMHQASLLGHSIHDAKKYGWKLPEGKVEHQWNHLRDSVQDHIASLNWGYRVQLREKTVTYINSYGEFTGPFEISATNKKKKVEKLTADRFLI... | Cofactor: Binds 1 FAD per subunit.
Function: Together with glutathione reductase gsr-1, required for the reduction of disulfide groups in the cuticle during molting.
PTM: Contains a selenide-sulfide bond between Cys-665 and Sec-666. This bond is speculated to serve as redox-active pair (By similarity).
Catalytic Activi... |
P91938 | MNLCNSRFSVTFVRQCSTILTSPSAGIIQNRGSLTTKVPHWISSSLSCAHHTFQRTMNLTGQRGSRDSTGATGGNAPAGSGAGAPPPFQHPHCDRAAMYAQPVRKMSTKGGSYDYDLIVIGGGSAGLACAKEAVLNGARVACLDFVKPTPTLGTKWGVGGTCVNVGCIPKKLMHQASLLGEAVHEAAAYGWNVDEKIKPDWHKLVQSVQNHIKSVNWVTRVDLRDKKVEYINGLGSFVDSHTLLAKLKSGERTITAQTFVIAVGGRPRYPDIPGAVEYGITSDDLFSLDREPGKTLVVGAGYIGLECAGFLKGLGYEPTV... | Cofactor: Binds 1 FAD per subunit.
Function: Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. L... |
B9A1H3 | MAAAEAQYDLLVIGGGSGGLACSKRAASHGKKVAVCDFVKPSPPGTTWGLGGTCVNVGCIPKKLMHQAALLGEGMTDAESFGWEVAAPKHNWETMVGNVQGHIKSLNFGYRSDLMSNGVKYYNAYATFLDPHTVEAVDKKGKVTKITASEIVICTGGRPRYPDIPGAKELGITSDDVFALKSPPGRTLVVGASYVALECAGFIKGVGYDTTVMMRSIPLRGFDQQMAGLCKTYMQEHGVAFIEGAVPTAVEATPSGAKKVSWKLADGSVGSGEYDTVLFAIGRDVCTSAIGIDKAGVKLSSNGKVPTVNEQTNVPHIYAI... | Cofactor: Binds 1 FAD per subunit.
PTM: The N-terminus is blocked.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 52206
Sequence Length: 495
EC: 1.8.1.9
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Q16881 | MGCAEGKAVAAAAPTELQTKGKNGDGRRRSAKDHHPGKTLPENPAGFTSTATADSRALLQAYIDGHSVVIFSRSTCTRCTEVKKLFKSLCVPYFVLELDQTEDGRALEGTLSELAAETDLPVVFVKQRKIGGHGPTLKAYQEGRLQKLLKMNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGI... | Cofactor: Binds 1 FAD per subunit.
Function: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form . Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for cata... |
O89049 | MNDSKDAPKSYDFDLIIIGGGSGGLAAAKEAAKFDKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKLEDTVKHDWEKMTESVQNHIGSLNWGYRVALREKKVVYENAYGKFIGPHKIMATNNKGKEKVYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGTPGRLKVTAKSTNSEETIEDEFNTVLLAVGRDSCTRTIGLETVGVKINEKTGKIPVTD... | Cofactor: Binds 1 FAD per subunit.
Function: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catal... |
Q9N2I8 | MAALRGAAARFRGRAPGGARGAAGRQCYDLLVIGGGSGGLACAKEAAQLGKKVAVLDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAPHYGWGVAQAPHSWATLADAVQNHVKSLNWGHRIQLQDRKVKYFNVKASFVDTHTVCGVSKGGEETLLSAEHIVIATGGRPRYPTHIEGALEYGITSDDLFWLKESPGKTLVVGASYVALECAGLLTGLGLDTTVMIRSVPLRAFDQQMASLVTEHMAGHGTRILRGCAPEKVEKLPGQQLRVTWVDLTSDRKDAGTFDTVLWAIGRVPETASLNLEKAGVH... | Function: Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis (By similarity). Maintains thioredoxin in a reduced state. May play a role in redox-regulated cell signaling.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + N... |
B2I8S9 | MATTLTLSEAVTALQQGDVIAYPTEAVWGLGCDPRQETAVHTLLNIKQRASGKGLILVTAELNTLQDWLDLDTLSPERLHEVQASWPGPHTWVLPASTRAPHWITGHHNGLAVRISAHPLVSALCRAWNMALISTSANVAGQPPARRREDLDPSLLPHLAGIVDGPTGGLAQPTSIRDARSGHILRL | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosp... |
P94682 | MSTVLYRCPELLIGGEWRPGRHEQRLVVRNPATGEPLDELRLASADDLQLALQTTQQAFEHWRQVPAHERCARLERGVARLRENTERIAHLLTLEQGKTLAEARMECAMAADLIKWYAEEARRVYGRVIPARLPNSRMEVFKFPVGPVAAFSPWNFPLVLSARKLGGAIAAGCSIVLKAAEETPASVAAMVDCLNQELPPGVVQLLYGVPAEVSQALIASPVVRKVTFTGSVPVGRHLAELSARHLKRITLELGGHAPVIVCGDADIARTVNLMVQHKFRNAGQACLAPTRFFVDRRIYGDFVDAFGATQALRVGAGMAA... | Function: Involved in the toluene-4-sulfonate degradation pathway. Does not discriminate between the sulfonate and the carboxyl substituents and can also be involved in the p-toluenecarboxylate degradation pathway.
Catalytic Activity: 4-(hydroxymethyl)benzenesulfonate + NAD(+) = 4-formylbenzenesulfonate + H(+) + NADH
S... |
Q9Z8Z0 | MLTLGLESSCDETACAIVNEDKQILANIIASQDIHASYGGVVPELASRAHLHIFPQVINKALQQANLLIEDMDLIAVTQTPGLIGSLSVGVHFGKGIAIGAKKSLIGVNHVEAHLYAAYMAAQNVQFPALGLVVSGAHTAAFFIENPTSYKLIGKTRDDAIGETFDKVGRFLGLPYPAGPLIEKLALEGSEDSYPFSPAKVPNYDFSFSGLKTAVLYAIKGNNSSPRSPAPEISLEKQRDIAASFQKAACTTIAQKLPTIIKEFSCRSILIGGGVAINEYFRSAIQTACNLPVYFPPAKLCSDNAAMIAGLGGENFQKNS... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
Q8KGA4 | MNILGIETSCDETSAAVLSDGSVRSNIVSSQRCHTDFGGVVPELASREHERLIVSIVDAAITEANIAKNDLDVIAATAGPGLIGAVMVGLCFAEGLAWALGKPFVPVNHVEAHIFSPFISDEPGHREPKGDFVSLTVSGGHTLLSVVRQDLGYEVIGRTIDDAAGEAFDKTGKMLGLGYPAGPVIDRLAREGDSDFHRFPRALTASSQTSKSYRGNFDFSFSGLKTSVRTWLEAHDSEYVQKHQADLAASIQSAIVEVLVEKSVAAALLHKVNAISVAGGVSANSGLRSAMQAACDRHGIELFIPALAYSTDNAAMIATM... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
A0M1X3 | MSDQKINILAIESSCDDTAAAVLCNGKILSNIVATQKVHEQYGGVVPELASRAHQQNIVPVIHQALAKANIDKKDVSAIAFTRGPGLMGSLLVGTSFAKSLSMGLNIPLIEINHMQAHILAHFIEEDDFEKPTFPFLAMTISGGHTQIVKVTDYFKMEVIGETIDDAVGEAFDKSAKILGLPYPGGPLIDKYAQEGDPKAFKFPKPKVDGLNFSFSGFKTAVLYFVQRETKNDPEFVEKNLKDICASIQYTIIGILIDKLKKAVKETGITQVAIAGGVSANSGIRQALKDAEQKWGWKCFVPKFEYTTDNAAMIGIAGYH... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
Q7NB15 | MYYKVILGIESSCDDLSIAIAIDNKIVTTKTKSSSSVHANYGGVVPEIAARYHEEILHQTLNEALTEANLTINKIDLITYTENPGLLNCLHVAKVFANTLGYLLKIPAQGINHLYGHIFSPMIDDGDCLYQKSDLIYPALGIVVSGGHTAIYDVQSPSKITLLDETLDDAIGEVYDKVGRALGLQYPAGAKIDQLYNPEQAETVEFLKTNKLSAFSYSGFKSAVLRYIELNKNQPDFNLVQAVSSFQKFIIDDFIDRIKNVINKADSKYQTILLGGGVSANSYLRSELKELAIKTLVPKPIYSGDNAAMIINYAQYLLNE | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
P75055 | MEQPLCILGIETTCDDTSIGVITESKVQAHIVLSSAKLHAQTGGVVPEVAARSHEQNLLKALQQSGVVLEQITHIAYAANPGLPGCLHVGATFARSLSFLLDKPLLPINHLYAHIFSALIDQDINQLKLPALGLVVSGGHTAIYLIKSLFDLELIAETSDDAIGEVYDKVGRAMGFPYPAGPQLDSLFQPELVKSHYFFRPSTKWTKFSYSGLKSQCFTKIKQLRERKGFNPQTHDWNEFASNFQATIIDHYINHVKDAIQQHQPQMLLLGGGVSANKYLREQVTQLQLPYLIAPLKYTSDNGAMIGFYANLLINGKNN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
Q98R92 | MIILGIETSHDDTSIAIIEKGKILKMITWSQSDFFAQYGGTIPELSSRQHSQNIIRIIDKLKSEFDFSKIDAIAYTEKPGLIGTLQIGFLVAQALSRVLKIKAYPIDHIEGHFFSASFEKNYLFPALALIVSGGHSQLMLAKDKDNIEVIGSTLDDAIGEVFDKVATKLNLGFPGGPKIEALCKDNDFDLVKLTKPKTQGEFDFSFSGMKSQVINLANQKKHSSKNLACSFQKEAVDYLLEKTKKCLEKYKINSLILGGGVAANFLLREGFKKLHENVYIPSKELATDNAAMIAKVLYEKLK | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
Q4A734 | MIILGIETSHDDSSIAILEDGKVLNMWSISQIDIFKKYGGTIPEIASREHVKNIAILQNFLQEFIDLNKIDHIAYTSEPGLIGCLQVGFLFASALSIALNKPLIKINHLDGHFFSGAIDNKEIKYPALGLIVSGGHSQIIYAKNKFDFQIVGETLDDAIGECYDKVSSRLNLGFPGGPIIDKIHASYKGKYLKLTKPKTSGEFDFSFSGIKTQVLNAFNNKKYESIEQIAASFQEVAINYLIEKFKLAIDKFKPESILLGGGVSANKYLREKFKDLHKNTIFPEIKYATDNGAMIAMCAYLRMKKNS | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
O86793 | MADSRDEPLVLGIETSCDETGVGVVRGTTLLADAVASSVDEHARFGGVVPEVASRAHLEAMVPTIDRALKEAGVSARDLDGIAVTAGPGLAGALLVGVSAAKAYAYALGKPLYGVNHLASHICVDQLEHGALPEPTMALLVSGGHSSLLLSTDITSDVRPLGATIDDAAGEAFDKIARVLNLGFPGGPVIDRYAREGDPNAIAFPRGLTGPRDAAYDFSFSGLKTAVARWIEAKRAAGEEVPVRDVSASFQEAVVDVLTRKAVRACKDEGVDHLMIGGGVAANSRLRALAQERCEAAGIRLRVPRPKLCTDNGAMVAALG... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
P0CR36 | MPTPLALLLSAILIIGTYFAMPFWPFRKSNYDPRGKHCYITGGSSGLGKALAERLVKQGAHVTIVGRDSKKAEGVVEELKAIAAPGQIIQCIAADLTSPIASTNAIHAACKPHADQAPDYVYLCAGFSRPKLFVETTKQELKDGLDGVYWVSAYTAHEACQMMSKQRRTGKIIFVASFLSYVSFAGYSSYSPAKYALRGLSDALRSEMLLHNIDIHIFLPCGISGPGFDAENRTKPAVTKKIEEGDTPITPDVCAAALESGLKKGYYQITDNLVTEPIRLRSNGGVPTNNFLLDTLWLIVSSVGVPIWRMTADSAVRSFR... | Function: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Catalytic Activity: NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36490
Sequence Length: 335
Pathway: Lipid metabolism; sphingolipid metabolism.
... |
Q5BE65 | MHPSLPSIIYDASPTALGISAVFGALFFYTLVKMFGFLARENQFVVEGRTVVITGGSEGMGKAVACQLAQKGANIVIVARTLQKLEEAIEAIKGSAANVNKQRFHYISADLTKPEECERIMTEVTEWNDGMPPDIVWCCAGYCTPGYFVETSVQTLKDQMDTVYWTAANTAHAILRKWLVPINPSHQRPLPRRHLIFTCSTLAFVPIAGYAPYSPAKAAMRALSDTLCQEIEVYNGSRASKERARATPADVKIHTVFPMGILSPGFDNEQQIKPALTKQLESADKPQTPKEVARIAIEAIERGEYLITTMFVGDVMKGAA... | Function: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Catalytic Activity: NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 40461
Sequence Length: 369
Pathway: Lipid metabolism; sphingolipid metabolism.
... |
Q7RZR2 | MNHYLFSESLMEQLKTLSTSWSLPVAAVVAAIGIFATMGLFSSKNHMPVEGRTVLLTGASEGMGRSAAIQLSQKGANVILVSRNVGRLEEALVDVRAAAKNPSTQRFTYISADVSEHDYAAAVLAEAIAWNGGRSPDIVWCVAGMSTPLLWTDDGSMAAARRNMDVNYFGSAEMSRAILREWLAPENSTGPNGEPKHLVFTASMLALFAILGYGPYTPTKWALRGLADTLAMEVNYYPDNPVKVHIVYPGTIVSPGYERENQTKPDITVELEKDEPAESPDTVARRAIAGLEAGKYFVDVSFLGRLMQCGIMGGSPRNNW... | Function: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Catalytic Activity: NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 39647
Sequence Length: 362
Pathway: Lipid metabolism; sphingolipid metabolism.
... |
Q6CE86 | MIFPISEIPDKVTHSILEGVSALQNMSHTAFWSTVLGFLVVARIAVILATPKRRVLDIKGKKVVISGGSQGAGAALAELCYTKGANVVIVSRTVSKLEAQVQKIVTKHEPVFEGQTIRYISADLTKEEEAIRVFSEETMPAPPDVIFSCAGAAETGFILDFKASQLARAFSTNYLSALFFVHAGTTRMAKEPISPKNPRYVAIFSSVLAFYPLLGYGQYCASKAAVRSLIDSLRVEALPFNIRVVGVFPGNFQSEGFEEENKSKPEITRQIEGPSQAISAEECAKIVFAQMEKGGQMITTDLIGWILQSIALSSSPRSFS... | Function: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Catalytic Activity: NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 40734
Sequence Length: 372
Pathway: Lipid metabolism; sphingolipid metabolism.
... |
P38342 | MKFTLEDQVVLITGGSQGLGKEFAKKYYNEAENTKIIIVSRSEARLLDTCNEIRIEAHLRRETTDEGQVQHKLAAPLDLEQRLFYYPCDLSCYESVECLFNALRDLDLLPTQTLCCAGGAVPKLFRGLSGHELNLGMDINYKTTLNVAHQIALAEQTKEHHLIIFSSATALYPFVGYSQYAPAKAAIKSLVAILRQELTNFRISCVYPGNFESEGFTVEQLTKPEITKLIEGPSDAIPCKQACDIIAKSLARGDDDVFTDFVGWMIMGMDLGLTAKKSRFVPLQWIFGVLSNILVVPFYMVGCSWYIRKWFRENDGKKAN | Function: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Catalytic Activity: NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 35973
Sequence Length: 320
Pathway: Lipid metabolism; sphingolipid metabolism.
... |
Q750C9 | MMAADDTMSSKRADNCYKKDRGTMVYTPTDAQQATGKVHEKVYKFFESLYWMYYIHLPYYLMTSFDSFCLHVFFLVVFTLSLFGLLKWVLSLYWATVGYMAYAATGQ | Function: Stimulates the activity of serine palmitoyltransferase (SPT).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12532
Sequence Length: 107
Subcellular Location: Endoplasmic reticulum membrane
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Q6CJH4 | MAAEKIYEPYKKSRGTMIYTPTNQQMSRGGIGEKLADFVKNLYWVYYIHLPFYLMTSLDAFCLHTIFLVVVSLSLFGLLKYIFL | Function: Stimulates the activity of serine palmitoyltransferase (SPT).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9813
Sequence Length: 84
Subcellular Location: Endoplasmic reticulum membrane
|
B0R700 | MELHVRYEGDDDPEKCTARKLARFDLAALHRTGRETPAGVVLNPHAERALSPADDTDMLVALDCSWETAGRAMFEIDGEHRALPFLVAANPVNYGQPFQLNTVEAFAGALAILGRWERAEELLSKFTWGHTFLELNEEPLRRYADCEDSSEVVAVQQAYLDAGED | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Catalytic Activity: an N(1)... |
Q9UJK0 | MGRRRAARGPGAEGGRPRHLPTRSLEAFAEEVGAALQASVEPGAADGEGGPGPAALPCTLAMWELGHCDPRRCTGRKLARLGLVRCLRLGHRFGGLVLSPVGKQYASPADRQLVAQSGVAVIDCSWARLDETPFGKMRGSHLRLLPYLVAANPVNYGRPYRLSCVEAFAATFCIVGFPDLAVILLRKFKWGKGFLDLNRQLLDKYAACGSPEEVLQAEQEFLANAKESPQEEEIDPFDVDSGREFGNPNRPVASTRLPSDTDDSDASEDPGPGAERGGASSSCCEEEQTQGRGAEARAPAEVWKGIKKRQRD | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1248 (Psi1248) in 18S rRNA (Probable). It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA ... |
Q12ZL9 | MKKQIDKDYHLHIFHAKQCDPKKCTGKKMARFELARIFDKVQKIPRGSILLDPMAKQALSPADKHEQNITVLDCSWETVEEVFPHLMRLHLQHRALPYLVATNPVNFGRPFKLTSVEAFAAALYILGNKKQAEKILSKFNWGHVFLDMNKEPLEDYSKAKDSNEIIKIQSEYM | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Catalytic Activity: an N(1)... |
Q58118 | MITMPKLFIYHANQCNPKKCTSLKMAKMNKAILLKNPYKVPKNSLILNPYAEKALSPEDKEIVEKFGITALDCSWKEAELMFKKFKFKNQRSLPFLVACNPINYGKPCMLSTLEAFIAALYITNFKDEAWDLTSCFKWAETFIKVNYELLERYSNAKNSMEVVEIQQDFLRK | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 914 in 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Catalytic Activity: an N(1)-methylpseudouridine in 16S... |
Q8TXM4 | MIVLHARDCDPKACTALRAHRMGLVELTRHPGDVPTGAVVLDPTVEKALSREDRDAALERGLVAVDCSWEHVHRYFGPLRRRCRHRILPYLIAANPVNYGKPCKLSTVEALAAALYILGFRREAEEFISRFKWGPAFLELNRERLEAYRRAETSAEVVRVQEEFLPDGL | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Catalytic Activity: an N(1)... |
Q8PSK5 | MNQTKSRDIPLYIYHAGQCDPKKCTGRKMARFELARLYDRISRLPRSAILLDPMAEKALSPADDPKKGIIVLDCSWEEVERVFPELEKLNLEHRALPYMLAGNPVNFGRPFKLNSAEAFAAALYILGYKEQAEKVMSKFNWGHSFLELNREPLEEYSTAKNSTEIVEIQSHYI | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Catalytic Activity: an N(1)... |
O26654 | MKIVVYHAEECDRKKCTSLKLGRKGKFKIVSSLNQLPRGALVLNPFSEKAVSPEDRDMVLRRGIAALDCSWKKVKKSSVIFQTARNHRSLPFLVAANPTNYGKPCILSTAEAVAATLYIVGLKDIASDIMSYFKWGPHFLDLNRELLEAYSRAENSLEVVEIQKKFIGG | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Catalytic Activity: an N(1)... |
Q9UWV6 | MKVYIIDYHKDDPKRCTGKKLVKLKIAEFTRVGKGVVLDPFAQITLSNKDKDIVRRIGITIVDTSWNNTSQSEFKNIRGEHRRIPILFAGNPIHYGIAYKLSSIEALIATLYIVDEVEEAIKLSNVVKWGHTFIELNKELLEAYKNKTEEDIKKIEREIIEKILEK | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Catalytic Activity: an N(1)... |
Q10409 | MGPRSSNRRSNAKDGFKGSNKASKFPLPLAMWDFGHCNPNACSGKRLERLGCVRNLRIGQKFRGVVITPNGKVPVSPADKEYFDNGGASVVECSWARIEEIPFSRIGGRCERLLPYLVASNPVNYGRPWRLNCAEALAACMYIVGYPNEARLLMDNFKWGHSFFEVNEELLDIYAQCHDAQDIQEKEKKYLEEMEASYQEQRNQTTDDIWSAGNLNHKPTLNTSSTHSNSEESRSPLHEPSEASLAHDEHSIPTDDNEETLTNLQANDVDEDEVWRKIVRMKVHSTDT | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Required f... |
C4KHW1 | MKVYVIDYHKDDPKKCTGRKLVKLKLAELTRVGRGIILNPFSERTLSINDKDILIKSGITIIDTSWNNTSQNEFKNVRGEHRRLPILFAGNPIHYGIAYKLSSLEALMATLYILDEVKEAIKFSNVVKWGHTFIELNKELLEAYRNKDEEEIKKIEKEIIEKILRK | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Catalytic Activity: an N(1)... |
Q220I8 | MNAVWTDNDTQAEDLSPQGRVASQLVRLKSDLQAFADATASAPATREPKIERETHKLEKRLCRQVGQAIMDFNMIEEGDRVMVCVSGGKDSYGLLDILLKMQQRAPINFEIVAVNLDQKQPGFPAHILPEYLAKLGIEFHIETQDTYSIVKKVIPEGKTMCSLCSRLRRGILYRVADELKITKIALGHHRDDMLQTFFLNMFFGGKLKGMPPKLVSDDGGHIVIRPLANVAEKDLTRWAAHRQFPIIPCSLCGSQENLQRQLIGQMLRDWEKQYPGRTETMFTALQNVVPSHLMDATRYDFKGLKITGVPDADGDRVFDE... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Function: Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(... |
Q0VQ34 | MSDNADTKKRTRLNKLQKKLRRETGRAIADFNMISEGDKVMVCLSGGKDSYTMLEILRNLQHSAPVNFELVAVNMDQKQPGFPEHILPEYLEKEGVAYHILEKDTYSIVKEKVPEGKTTCGLCSRLRRGSLYGFAEEIGANKIALGHHRDDIVETLFLNMFYGGKMKAMPPKLRSDDSRNVVIRPLAYCREKDIIEFSALKEYPIIPCNLCGSQKNLQRQVIKEMLQQWDKQQPGRIENIFAAVQNIAPSQLADTRLFDFENLEQGQQQGGDQAHRLDVVNLFG | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Function: Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(... |
A7H8W2 | MRAPRRRCYRVRPMHDVSKLEKRLLRAAANAIRDFELIGDGDRIMVAVSGGKDSYTLLHVLMRLRERAPIDFDLVAVNLDQGQPGYPAEIVERHFQAVGVPHRMLYADTYSIVRRLVPEGKTTCPVCSRLRRGVLYNAAAEMGCTKIALGHHRDDLVETLLLSALYSGALKSMPPKLRSDDGRNVVVRPLCYAAEEDIAAFATAMRFPIVPCDLCGSQPNLRRKRVKALLAELSDEHPAVKGNLLNALGHVVPSHLLDRDLHRLVASTGRDPWLDGDEDEDGGCLQGEVADALVKLAGAREDA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Function: Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(... |
Q6MLE7 | MKSAVNFELPLAVKIRKQIVQALNDFNMIEDGDKVMVCVSGGKDSSVLLALLTEIQRRSERKFQIEAAILDQKQPGFDVSKFKVWVESLGVPFHIVEKDTYSIVKEKVQGGTFCSLCSRLRRAILYDFAHANGFTKLALGHHRDDVVHTALLNMFYVGTTAAMPPKLKSDDERNILVRPLCYVSERDIEELAAEWAFPVIPCNLCGSQDGLKRQRIKKLVRDLEKEIPNIYASIQTSMTNIKPSQLMDQDLWDFKNLKT | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Function: Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(... |
Q92PH1 | MELAQSSPDETDSVIVDDAAFEGAAHPLFSRMPSSVSFNKLRKRLLRQVRQALDDFGMLKGSRRWLVGVSGGKDSYSLLALLMDLQWRGLLPVELVACNLDQGQPNFPKHVLPDYLRSIGVKHRIEYRDTYSIVKEKVPAGATYCSLCSRLRRGNLYRIGREEGCDALVLGHHREDILETFFMNFFHGGRLASMPAKLLNDEGDLTVLRPLAYAAEDDLAKFAAAMEFPIIPCDLCGSQDGLERNAMKAMLADIERRMPGRKDTMLRALGHVNASHLLDPKLFDFQSLSPEPKE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Function: Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(... |
Q16A99 | MLDHSDEIHPLFHGAPKTTEFRKLRKRLVRQTRDAIERYGMIEKDARWLVCLSGGKDSYTLLAVLYELKWRGLLPVELLACNLDQGQPGFPATVLPEFLKKMEVPHRVEYQDTYSIVMDKVPQGRTLCALCSRLRRGHLYRIAREEGCSAVVLGHHRDDILETFFMNLFHGGRLATMPPKLVNEEGDLFVYRPLAHVSEADCDRFSTAMGYPIIPCDLCGSQDGLQRQQVKAILEGWEKNSPGRRQVMFKALMNTRPSHLLDTALFDFAGLARK | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Function: Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(... |
P17789 | MKMASQRFCLRWNNHQSNLLSVFDQLLHAETFTDVTLAVEGQHLKAHKMVLSACSPYFNTLFVSHPEKHPIVILKDVPYSDMKSLLDFMYRGEVSVDQERLTAFLRVAESLRIKGLTEVNDDKPSPAAAAAGAGATGSESTATTPQLQRIQPYLVPQRNRSQAGGLLASAANAGNTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDLNESRDSLPSKRSKNSKDHRVVSHHEDNSTSDGNDSDGEGLDTSYMEPQLMLDEYDEPVEFKY... | Function: Binds to a number of sites in the transcriptional regulatory region of ftz . Isoform beta is required to repress inappropriate segmentation gene transcription and repress genes incompatible with development of photoreceptor cell fates . Probable repressor of the transcription of the segmentation genes ftz, ev... |
Q8AYG3 | MDEEESTERQMQIAMLCQKLAMMKQLFNEDDTDYINQAISSNSPDTCRTFLSNLEKKGNPQADPSLLSKLMDSYTRVFSSMPLGKYSQNESYAKMLVRFAELKAIQDVNDAQTSFDIARSHCKDFAFVHVAYAQFELLQGNMKKCTMILQKAFEMNAKPRHVLEAAVRNLKTGKRQLLSHEDKENLSVSALDHTQGSRRSDGTCELKPSNTFLHSDQKFSPQEENGPVWRTGSQHRRTAMAERVPMVPLSIPENETSDSDCAQKAEAPFTHSSGFSRQTSGSSVRSAFSLCSSKKGTPDGDSYSLNIKPPVISPDYLRED... | Function: Phosphorylates proteins on serine, threonine, and tyrosine (By similarity). Involved in mitotic cell cycle checkpoint control. Required for fin and heart regeneration. Required to prevent chromosome segregation errors during meiosis.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl... |
P33981 | MESEDLSGRELTIDSIMNKVRDIKNKFKNEDLTDELSLNKISADTTDNSGTVNQIMMMANNPEDWLSLLLKLEKNSVPLSDALLNKLIGRYSQAIEALPPDKYGQNESFARIQVRFAELKAIQEPDDARDYFQMARANCKKFAFVHISFAQFELSQGNVKKSKQLLQKAVERGAVPLEMLEIALRNLNLQKKQLLSEEEKKNLSASTVLTAQESFSGSLGHLQNRNNSCDSRGQTTKARFLYGENMPPQDAEIGYRNSLRQTNKTKQSCPFGRVPVNLLNSPDCDVKTDDSVVPCFMKRQTSRSECRDLVVPGSKPSGND... | Function: Phosphorylates proteins on serine, threonine, and tyrosine . Probably associated with cell proliferation . Phosphorylates MAD1L1 to promote mitotic checkpoint signaling . Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic ch... |
Q4R7H0 | MGSSQEEGLPCQPSQPDHDTGGHGGPDLEGAGRVSTTPGPPGLLTSHPPADSDDTDATGPPAALLEGLLLGDGKPSPHSTRPGPFFYIGGNNGAAIISSYCKSKGWRRIQDSRREDYVLKWCEVKSRDSYGSFREGEQLLYQLPNNKLLTTKIGLLSTLRGRAWAMSKASKAPGGTQARLGKDATAPTLEDLPWTSPGHLRPQRVLRMEEFFPETYRLDLKHEREAFFTLFDETQIWICKPTASNQGKGIFLLRNQEEVAALQAKTRRAEDDPIHHKSPFRGPQARVVQRYIQNPLLLDGRKFDVRSYLLIACTTPYMIF... | Function: Polyglycylase which modifies both tubulin and non-tubulin proteins, generating polyglycine side chains of variable lengths on the gamma-carboxyl groups of specific glutamate residues of target proteins. Involved in the elongation step rather than the initiation step of the polyglycylation reaction. Polyglycyl... |
A4Q9F3 | MALHPQAGRPHRDGSEAQAEAAAQDLGRLPSPSKVGAAVCRIQGLGHRAARRPRRGIGTTSASRVPRPGALMPATRNRPRFIHCRGQPPRTRVSSKRSKRSRIHPCHTEVPGWTHEKQMGSSVKERLRPELSQLDQDADDLEEEEAARLPVTSPDGLLMEGDKQPSPGQGPFFYIGGTNGASIISNYCESKGWQRTQDSHCEDYKLKWCEIKCRDNYCSFREGQQLLFQLPNNKLLTTKIGLLSALREHARTLSKARMLPSTQTKVLKMEEFFPETYRLDIRDERQAFFALFDETQMWICKPTASNQGKGIFLIRSQEEA... | Function: Polyglycylase which modifies both tubulin and non-tubulin proteins, generating polyglycine side chains of variable lengths on the gamma-carboxyl groups of specific glutamate residues of target proteins . Involved in the elongation step rather than the initiation step of the polyglycylation reaction . Polyglyc... |
H2KZM9 | MGCKISTEFCSDNPVGSISTSKVHPTDLSTPSYAIKPVEFYEEPLKDDQLFYKVALAKKEYREKEKDKKEQLSSNRRVSLQVEPNKLPIPLTRSSSLSSIMENRPPSGISNSSFIRSRNTASRRFTIDTSRAKSNQYVVSLCSKKIGIIEYPDGRSDKQPCDVYWHNVVLSDMNKIVTSPQSRVNKFPGMTELAKKISLTHSISSMQKLFPDEYAFYPNSWFLPAHLADFHAFYRKAQALGKTEMWFIVKPDEGAQGTGIYLINSPNQIRNVDQRQLVQEYVADPLLMNDKLKFDFRVYGVIKSINPLSIYVAREGMARF... | Function: Polyglutamylase which preferentially modifies tubulin . Involved in the side-chain initiation step of the polyglutamylation reaction . By controlling tubulin glutamylation, regulates ciliary specialization and motor-based transport. Promotes the formation of A and B tubule singlets by splaying microtubule dou... |
A4Q9F4 | MRRSSPEKKPEAEWEADAAAAAAATAAATESLPAETEKQQGVDAGAAGDPERLELEEQPKDVGRIPTPTRRHAPEEGEARVVRRLPPALPLAQPRPAARALSQLVKARGRSRSRVYRRSAGSMRPVTVDSSKARTSLDALKISLRQLRWKEFPFGRRLPCDIYWHGVSFRDSDILSGQVNKFPGMTEMVRKVTLSRALRIMQNLFPEEYNFYPRSWILPEEFQLFVSQVQTVKEGDPSWKPTFIVKPDSGCQGDGIYLIKDPCDGRLTGTLHNRPAVVQEYIRKPLLIDKLKFDIRLYVLLKSLDPLEIYIAKDGLSRFC... | Function: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin . Preferentially mediates ATP-dependent polyglutamate long side-chain elongation over the initiation step of the pol... |
A6NNM8 | MEPSTCRTMESEEDYVEEKESEKCVKEGVTNPSNSSQQALLKADYKALKNGVPSPIMATKIPKKVIAPVDTGDLEAGRRKRRRKRRSLAINLTNCKYESVRRAAQMCGLKEVGEDEEWTLYWTDCAVSLERVMDMKRFQKINHFPGMTEICRKDLLARNLNRMYKLYPSEYNIFPRTWCLPADYGDFQSYGRQRKARTYICKPDSGCQGRGIFITRNPREIKPGEHMICQQYISKPLLIDGFKFDMRVYVLITSCDPLRIFTYEEGLARFATTPYMEPSHNNLDNVCMHLTNYAINKHNENFVRDGAVGSKRKLSTLNIW... | Function: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates ATP-dependent polyglutamate side-chain elongation of the polyglutamylation reaction but not the initiation... |
Q8K9B6 | MEKKNIILNLIGLRCPEPIMVIRKTLRKMKKNEKILVLADDPSTKRDIPYFCYFMEHQLLDRFIHVKPYRYLLKKG | Function: Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity... |
Q89AB9 | MTVDNNVLDLRKLRCPEPIMLLRKKIREIKNGTTLLILSDDPSTIREIPQYCKFMHHKLLKINTKDTIYKFWIQKTHKM | Function: Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity... |
A7ZT06 | MTDLFSSPDHTLDALGLRCPEPVMMVRKTVRNMQPGETLLIIADDPATTRDIPGFCTFMEHELVAKETDGLPYRYLIRKGG | Function: Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity... |
Q7N9B7 | MSSLSYCLLVTGPAYGTQQASSAYQFAQALITMGHKLNTVFFYREGVYNGNQLTSPASDEFDLVSAWQMMATEHRFSMHICIAAALRRGVIDAQQASELNLPVANLAEGFELSGLGTLAEAMLICDRVVQF | Function: Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE.
Sequence Mass (Da): 14290
Sequence Length: 131
Subcellular Location: Cytoplasm
EC: 2.8.1.-
|
Q9I0N3 | MKFAIALFDPPHSPAARRALRFSEAALAGGHEIVRLFFYQDGVHSASANVVSGQDEFDLPAAWRELVERNGLDAVVCIAAALRRGVLNAEEAERYGRPGANLGAPWELSGLGQLHEAAQSADRLVCFGGDR | Function: Could be part of a sulfur-relay system.
Sequence Mass (Da): 14086
Sequence Length: 131
Subcellular Location: Cytoplasm
EC: 2.8.1.-
|
P60979 | AECLMIGDTSCVPRLGRRCCYGAWCYCDQQLSCRRVGRKRECGWVEVNCKCGWSWSQRIDDWRADYSCKCPEDQ | Function: Potently blocks vertebrate calcium channels Cav1 and Cav2. Is the most active on Cav2.2/CACNA1B (from HEK) (IC(50)=2.3 nM), followed by Cav2.1/CACNA1A (IC(50)=4.3 nM), Cav2.2/CACNA1B (from oocyte) (IC(50)=14.4 nM), Cav1.2/CACNA1C (IC(50)=26.8 nM), and Cav2.3/CACNA1E (IC(50)=96.4 nM).
PTM: Contains 6 disulfide... |
A0A348G5W0 | MKPSSLTLAFLVVFMMAIMYNSVQAEALADADAEAFAEAGVKELFGKAWGLVKKHLPKACGLLGYVKQ | Function: This homodimer composed of two cationic amphipathic alpha-helical peptides has antimicrobial activities against E.coli (MIC=3.1 uM), S.aureus (MIC=3.1 uM), and S.cerevisiae (MIC=3.1 uM).It also shows histamine-releasing activity (66.4% at 10 uM) and a weak hemolytic activity (10.5% at 50 uM).
PTM: Truncated s... |
W4VSI6 | MKTIFALVFCCAIAVVVLGFGENEGSTIDHDQNNCKGPGSRCSNKNECCKPKDMETYTYYCGSRWDSSSGDFVRKCVICNRESSMC | Function: Probable neurotoxin with ion channel impairing activity.
Sequence Mass (Da): 9541
Sequence Length: 86
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
A0A452CSQ9 | SNRWNLGYGIPHKQVKLPNGQLCKEPGDSCSKRDECCKADDQKTYSSGCAQTWSAMEGGFVRECYICAVESSMC | Function: Probable neurotoxin with ion channel impairing activity.
Sequence Mass (Da): 8187
Sequence Length: 74
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
P83559 | GGCIKWNHSCQTTTLKCCGKCVVCYCHTPWGTNCRCDRTRLFCTED | Function: Competes for binding at site 3 of the insect voltage-gated sodium channel (Nav) . Insecticidal neurotoxin . Causes temporary paralysis to lepidopteran larvae (10.3 nmol/g) or to crickets (doses from 0.93 to 119 ug/g) . Is not toxic to mice when injected intracranially (high doses) .
Sequence Mass (Da): 5233
S... |
P34079 | ADCSATGDTCDHTKKCCDDCYTCRCGTPWGANCRCDYYKARCDT | Function: Toxin that inhibits presynaptic voltage-gated calcium channel (Cav) in Drosophila nerve terminals, most likely through specific block of the Cav2 channel (known as Dmca1A).
PTM: Contains 5 disulfide bonds.
Sequence Mass (Da): 4881
Sequence Length: 44
Domain: The presence of a 'disulfide through disulfide knot... |
P36984 | EEQVNVPFLPDERAVKCIGWQETCNGQLPCCDGCVMCECNIMGQNCRCNHPKMTSECGSRR | Function: Potent toxin that may paralyze and/or kill insect pests such as H.virescens (lepidoptera), S.exigua (beet armyworm) and M.sexta (tobacco hornworm).
Sequence Mass (Da): 6853
Sequence Length: 61
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellu... |
P36987 | ALKCQGWVDYCNGNVECCNECVMY | Function: Potent toxin that may paralyze and/or kill insect pests such as H.virescens (lepidoptera), S.exigua (beet armyworm) and M.sexta (tobacco hornworm).
PTM: Contains 5 disulfide bonds.
Sequence Mass (Da): 2745
Sequence Length: 24
Subcellular Location: Secreted
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