ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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|---|---|---|
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 | MLHTTPSGLLIIDKPQGVTSFDAVAAVRGALHIKKVGHAGTLDPMATGTLVIAFGHATRLLNAIVAHDKTYEATIRLGLRTTTDDAEGEVLVDGEARSRWQTLSAQLTEGGQSGEPTALPTASWQDLLTRTIATNFTGDIEQVPNTFSAIKINGQRAYDLAREGKDVELKPRPVTISEFTVLDIRSGFVAGEQAAEPLREDANTGAIPALDVDVRISCSSGTYIRALARDLGKELGVGGYLTRLRRTRVGRFALPDDASGLIAPEAMLDTRTHTVTAHTDQKTFTNREGQTVTRNKCVLDTPEGLAGDERRNWLLDHALTMEQAARGAMPALDITPEEASELRFGRRIERTISEPTAAIVPQTHDVAAIIERANAHQAKPVTVFPLA | 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 | MSSAGKLPSEIERTLVRKSGAWTNPVYGCAPEKRPILEYIEKGVVNIDKPSGPTSHEVAAWVKAILGVNTAGHAGSLDPKVTGLLPTLLGKATKAVPALRLSGKEYVCHLKLHRAMPPKLVRKVCEEFTGPIYQMPPIKSAVKRVIRVRTIYYIEVLEIEGMSVLFRVGCEAGTYIRKLCHDIGLALGCGGHMQALRRTKAGPFTEKTLVTLHELKDAYVFWKEDGDESELRRVIRPMESAVSHLPKIILRDSAVDAVCSGASLAVPGITSLDSSLAEGELAALFTLKGELVALAKAEMNTEEILKASAGIAASPIRVLMEAGTYPKGWTKKEESVRL | 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 | MILLEKTQEKKINDKEELIVKEEVETNWDYGCNPYERKIEDLIKYGVVVVDKPRGPTSHEVSTWVKKILNLDKAGHGGTLDPKVTGVLPVALERATKTIPMWHIPPKEYVCLMHLHRDASEEDILRVFKEFTGRIYQRPPLKAAVKRRLRIRKIHELELLDKDGKDVLFRVKCQSGTYIRKLCEDIGEALGTSAHMQELRRTKSGCFEEKDAVYLQDLLDAYVFWKEDGDEEELRRVIKPMEYGLRHLKKVVVKDSAVDAICHGADVYVRGIAKLSKGIGKGETVLVETLKGEAVAVGKALMNTKEILNADKGVAVDVERVYMDRGTYPRMWKRKK | 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 | MELIVKEESKTDYNYGSDPYNRDIKTLLNTGLVVIDKPSGPTSHEVAAWVRNMLNLVKAGHGGTLDPKVTGALPVALGNTTKCVPIWHIPPKEYVCLMHLHDDAELVDIENIFKEFTGRIHQRPPLKAAVKRSLRIRKIYEIEILEIDGRDILFRTKCQSGTYLRKLVDDMGEALGTSAHMQELRRTISGPFYENEAVYLQDLLDAYIFWKEDGNEEELRKIVKPLEYGLQHLKKIIIKDSAVDAVCHGATLYSSGISKIEKGLGTDEVVLIETLKGEAVAVGKPLMNTKDMLKTEEGEVVEITRVIMEPGIYPRIWKKRNKNDKSKPELKKK | 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 | MSNLNGFIVVDKPKGPTSHQIDSWIRDITGEPRVGHIGTLDPGVSGVLVMALGKATKLIDIVHRESKEYVSVLRTYDKYDHDSIKSVFKEFTGKIYQIPPVRSAVSRELRIREIYNLELLEMDEKFVLFKVCCESGTYIRTLCTDIGYVLGSGGQMAELRRTRTGPFDESMCHTLQEVSDAFKLKSMGNEKLFKNIFIPMDFIFIKYPKVIVKETALKNIAHGSDIYPAGIHAITGSPKKGDVVAVYTEKNELVATGTMMVNADEIYDLKVIDIDNVLIETGDNDGKDSLVRKDNRWKDIPVQKPERKLHGNLQGSQEWKDTGNRGNPKRGGTGSKGFSSGFRKRKAKR | 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 | MPLNMNKYLTDAYTGGIIKKYPEDFIVEEITPEGIILEVGKSIEFKDEENWKGNYIHFTLEKRNWTTLDAIREIANRVGKQRKHFGFAGNKDKYAVTTQRVGCFNVKLEDLMKVKIKGIILRDFQKTNRKIRLGDLWGNRFTIRVREPELKGKELEEALNKLCKLKYFLNYYGVQRFGTTRPITHIVGRFIIERDWEGAFHAYCGTPLPYDDKKSKLARELVDEENFKEAYKKFPKAFFYERRMIKAYIETGSYQKAFMILPPYLRCMFINAYQSYLFNEIINRRFEYGFEPMEGDILIDNVPSGALFGYKTRFASGIQGEIEREIYERENLSPEDFKIGEFGSFIGDRRAMIGKIYNMKYWIEDDSYVLQFCLKKGNYATSVLREFIEKKD | 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 | MKNISTKESFFKFKFNNRSLYCWGAFMKLRMKPEDFIVEEIIDFNKIAGDRCYLYKLTKRNIESLKAFSYIAKKFKIPLKDIGYCGLKDRHALTTQYISIPKKYGKLSLDEPNLKLELIGESKFLLLGDLEGNRFTITVRGLKKEDIPKIKENLKYLEFGAPNYFDSQRFGSVFDKKFIAKEVIKGNYEEAVKILLTKYKKSEKKLIKDLKRFIDKNWGDWDKIWEYIKENNIKSRLYVNMVKELKKSNDYKKALSYVDDRLKKIFVAAYQSYLWNECVKELLRKYVPEEDRVYYEYECGTLMFYKKMDEEVFNILKDKKFPTIAPDIEYSGEEKEIIEEILKREGLTMEELNNIGELGKFIYSERKILSIPKNLKIGEFEEDELNKGKYKITLSYELEKGSYATIIIKRAFLGVKTKKRKR | 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 | MPININKFILDMERFDGTLKKYPEDFIVEEITPEGTVLEVGKEIGFEDVEKWHGSFIHFTVEKTNWNTMDALKQIVRATKTKRKNFGFAGTKDKFAVTTQRFGCFGLKKEQLENINIKDIVIRDVQKTNKKLRMGGLWGNKFTIKIRDLNLSEKEIKRISDLKLDYVLNYYGIQRFGLIRPITHIVGKFIYERDFESAFYTYCGTPINETGDSLEARQLVDMGEFKKALKLFNRGHDYEKRLIQQYLKYKDFKMAFTALPPQLNSMFVNAYQAYLFNEMINKRFDYGFDELEGDILEDNTPTGTLIGYDTKFSGGIQGEIEKEIVERENLDLKKFKIEDFGNFYGTRRKMVTPIYDFKSRFENEIFELSFKLERGNYATIVTREFTGNLS | 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 | MTDAPLVTAELPGSGGSLRRSPEDFRVDEVPAYLPSGAGPHLYLRVEKRGRTTRDALRTLARALGVPERDAGYAGLKDKDAVTTQWLSFPAARDPEPQALASEGLRVLEVSRHANKLRPGHVRANRFQLAVRGGDLARAQAAAAALAERGLPNLFGPQRFGTEGRNAEVGRALLLGDPSPEARRAARDRFLRRLSISAYQALLFNRWLAERMADGLFATAVAGDVLKKLDTGGLFTCADPAVDGPRVQRFEVSPAGPMFGHKLRAAEGEALAREERLLAAEGIQLSDFARGGGEAEGTRRAARLRVEVALAPLEDGYLATFELPKGSYATVVMRELMKAGAELPEADED | 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 | MDIRIKEKPEEFYVKEIKKLDLKEKGQYAYFLLKKKDMTTLDAVRHISHRFGIPLKNIGFAGLKDKKAVTEQYISVKDLNEEKIRKMDGYRTENLELKFLGFSDKGLELGEIEGNYFEVVVRGVTKYHRRVFPRMKELVENYGCENYFGEQRFGSVKHAEEFIVKYLLRHEYEEAMKEYLTSLGDKRLKRLLRKAWRDWDRFLSLMPKGAKPELEVVKALRRGESFKNAFMVLPKNIRLMFVFAYQSYLWNRYLYTFVVRYLKYCKTPFLKWELAFFNDMSEVIWEEIKDLEIPYLGVEYKPRNKKAEIVMKEVLQDEGITPKMLMAERIGIKLFSDGVRKAFFKPQGLKVIEERKNSLKLSFTLPPGSYATILLRKLFCSDVKS | 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 | MEEKVGIECYITSTPGMGGEIKAEPEDFYVEEIAEFNLSDEGDFLIIRVEKKNWDTLNFARVLSNALGISQKRISFAGTKDKRALTVQYFSIYGVKKEEIERVNLKDAKIEVIGYARRAIQLGDLLGNFFRIRVYGCRDGEIFQETRNELMEKGTPNFFGLQRFGSIRFITHEVGKLILQNNYEEAFWVYVAKPFEGENEEVRKIREILWETRDAKLGLRELPKYLRYERNLLQKLREGKSEEEALLSLPKNLKMMFVHAYQSYIFNRLLSERIRQFGSLKTLEEGDFACYLTFKTRPTFSDCSEVEVNEARVRFLVKERVASLALPLVGYDTKLKGWSRIALDFLSEDNLDLSSFKTKHKEFSSSGSYRPADTLIEHTGLSFTDSTFSFYLPRGCYATVFLREFLKTELS | 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 | MNLEEENTIFKPLYSLKHSPINAYFSKNSDDFVVRERPLYEFSGKGEHLILHINKKDLTTNEALKILSEASGVKIRDFGYAGLKDKQGSTFQYLSMPKKFESFLSNFSHPKLKILEIFTHENKLRIGHLKGNSFFIRLKKVLPSDALKLEQALMNLDKQGFANYFGYQRFGKFGDNYKEGLEILRGKKMKNVKMKEFLISAFQSELFNRYLSKRVELSHFANDFSEKELIQIYKISKEEAKELKKQEQFFKLLKGEVLGHYPFGKCFLCEDLSAELGRFKARDISAMGLLIGAKAYETGEGLALNLENEIFKDTLEFKAKMQGSRRFMWGYLEELKWRYDEEKAHFCIEFFLQKGSYATVVLEEILHKNLFE | 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
|
Q5JDB6 | MDYREFFSQFKHLSEKPGIGGKIKIYPEDFIVIEEPIPSIFEGRKYAIFLLKKRNWETMAAVKEIAKRAGINYREIGFAGTKDRHAVTYQYISVPAEARERVEQVSIRDIELRFVSYGRFIKLGHLLGNRFRIIVRDVSEDAFDRTKEIVRELREKGGFPNYFGYQRFGERRVVNHIIGKLLLQGDFEGAARLFLGAHDGSMEGDEARKNFWETGDVERALEEFPGFLRYERTLLHRYKDTGNWKRAFLSLPLPIMRIFIHAYQSYLFNLYLSRRIEEGLPLNEPLVGDIVVQVKGGIPYRDRTYRVTETNLEFVREKVRKNQAMVSGPLFGFAMRRAKGLPGELEKEILEEEGLSLETFRRLPKPMAEPGGRRELLLRPMGMAYGYIQEEGMCFRFFLPKGTYATSVLREIMKDH | 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
|
Q5SI49 | MDLVFRPERYPFLTQDLPGVGGEIRVEPEDFQVEEVPAYLPKGEGEHLYLLLEKEGRTTREVLEFLRDEVGVPEKEIGVAGLKDKRAKTRQWFSIPRKYEDALCLLENLQGVRLLAADLHTNKLRTGHLKGNRFHILIRRPKGGVAEAEAVLKRLAEKGVPNYYGPQRFGLGGLNPVRGYKLVKEGKGRGSPWLKRFLIGSLQSLLFNDWVALRMALGLYDRVVPGDWAKKHATGGEFLVEDPGEAERALRLEISATGPLFGKKYPEAQGEARAIEDEVLARYGLKREEFRARRGARRPIRVPLAEWKVEEAPEGLWLSFFLPKGSYATSLLREVMKVEALDHLEAEPAPEDAEGL | 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 | MNKPENFEEAIEIKRDPEDFSVEEIADIEPDPNGKYTIIKARVRDWDTNRIAAEIARRLHMSRKRVTFAGTKDKRAVKLQYFCINSADVDVASLSGIKDFEVIESFKSSHYLTLGDLIANHFKIRFYGIDPEMFRERYVHIISKGGFPNFFGDQRFGSRRRNTHEIGKLIIKGEYEEAVKKYIYDEKYDKESYRKHFIDTLDYKTALERFPHSLSFERSLIGYYARNGTFKGAFDSLPKNLTIMFVHAYQSYLFNRILDERLKIYGLNAVLPGDIAFPVDAYFNPDKSKPIEVNSYNREKISKLVSSDKIRISLPIFGYKTWIDNSDFGDVEYGILKEEGISQDDFKNKDFAYLSSSGDRRIISAKPINFSLENNVVEFTLGKGIYATVFLSSIGRLKENVYSDSEAEL | 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
|
Q7MHQ6 | MTDTLASLAYLAGKPTAQAKIKAKPEHFQVREDLGFEFTGSGEHLMVRIRKTGENTSFVANELAKACGVKSKDVSWAGLKDRHAVTEQWLSVHLPKAETPDFSAFLAQYPSIEILATARHNKKLRPGDLVGNDFVVTLSEVSDVDDVLKRLETVAKLGVPNYFGNQRFGNNGNNLQEAKRWGRDNVRSRNQNQRSLYLSAARSWIFNLIVSARLEQSLFDKVLLGDILFKGDEQLLVSAENHADLQSQYDAGDLVISGALAGDNALPTQDDALALEQVFLDAEPDLMALIRGNRMRHDRRAIALKPANLSWQVDGNNIILTFSLDAGSFATSIIRELVQEIAFEREF | 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 | MERLYYLNHAPIDFHFAQTPRDFVVEEIPLYPFSGAGEHLVLKIRKRNLSTFELVDILSSHLGIKSREIGYAGLKDKSALTLQHLSIPAKFGDKLEAFDHPEVKILEQVRHENKIRIGHLKGNRFFIRLKKLSPLNSLKIQGVLEEIKRWGIPNYFGYQRFGNDGNNHEIGRKIAHGEQRVTSPKRRTFLLSAYQSKLFNEWLKERIKLSKILAEFTPSEASRLAPMIPVEQLKALQKQPHPFKILPGEILHHYPHGKIFVAEDMEEESRRFVEKDIVPAGLLSGTKAKSSEGIAHLYEAPFIDEKIQEQGSRRLAWIFPEDLEYRYIEEEAHGELNFYLPKGSYATVLIEELAHREIKID | 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
|
Q8PLR6 | MSETSLLPRAHGAAVLSAAMRSTPDDFQVDELPAFEPSGEGEHLLLTVRKRGQNTAYIAKKLAHWAGIAEMGVSYAGLKDRHAVTTQRFSVHLPRRIAPDIAALDDTQMQVVESSWHNRKLQRGALHGNRFVLTLRQVQGERDAIEQRLQAIAARGIPNWFGEQRFGRDGGNVAAALAMFGHVQADDGTLLPAPTSRRRLRHDQRSMLLSAARSALFNRVLGARVAQGSWDGALEGEAWMLDGSRSVFGPEPWSEALAERLARFDIHPSGPLWGAGQLRSTDQAAAVEQGALSDPPSIALRQGLEAAGLKQERRALRLRPHGLEYQWLEPQTLQLAFALPPGCYATAVLWELGDVADAGRFNVDVRADA | 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
|
O62768 | MNGSKDLPEPYDYDLIIIGGGSGGLAAAKEAAKYDKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALRDSRNYGWNVEETVKHDWERMTEAVQNHIGSLNWGYRVALREKKVTYENAYGEFVGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMQEHGIKFIRQFVPIKVEQIEAGTPGRLRVIAKSTDSDQTIEGEYNTVLLAIGRDACTRKIGLENVGVKINEKTGKIPVTEEEQTNVPYIYAIGDILEGKLELTPVAIQAGRLLAQRLYGGSTVKCDYENVPTTVFTPLEYGSCGLSEEKAVEKFGEENVEVYHSYFWPLEWTIPSRDNNKCYAKVVCNIKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKDQLDSTIGIHPVCAEVFTTLSVTKRSGGNILQTGCUG | 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 catalysis. Also has reductase activity on hydrogen peroxide (H2O2).
PTM: ISGylated.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 54770
Sequence Length: 499
Subcellular Location: Cytoplasm
EC: 1.8.1.9
|
Q17745 | MKSLTELFGCFKRQPRQQEASSPANPHVSDTLSMGVAASGMPPPKRPAPAESPTLPGETLVDAPGIPLKEALKEAANSKIVIFYNSSDEEKQLVEFETYLNSLKEPADAEKPLEIPEIKKLQVSRASQKVIQYLTLHTSWPLMYIKGNAVGGLKELKALKQDYLKEWLRDHTYDLIVIGGGSGGLAAAKEASRLGKKVACLDFVKPSPQGTSWGLGGTCVNVGCIPKKLMHQASLLGHSIHDAKKYGWKLPEGKVEHQWNHLRDSVQDHIASLNWGYRVQLREKTVTYINSYGEFTGPFEISATNKKKKVEKLTADRFLISTGLRPKYPEIPGVKEYTITSDDLFQLPYSPGKTLCVGASYVSLECAGFLHGFGFDVTVMVRSILLRGFDQDMAERIRKHMIAYGMKFEAGVPTRIEQIDEKTDEKAGKYRVFWPKKNEETGEMQEVSEEYNTILMAIGREAVTDDVGLTTIGVERAKSKKVLGRREQSTTIPWVYAIGDVLEGTPELTPVAIQAGRVLMRRIFDGANELTEYDQIPTTVFTPLEYGCCGLSEEDAMMKYGKDNIIIYHNVFNPLEYTISERMDKDHCYLKMICLRNEEEKVVGFHILTPNAGEVTQGFGIALKLAAKKADFDRLIGIHPTVAENFTTLTLEKKEGDEELQASGCUG | 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 Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 74263
Sequence Length: 667
Subcellular Location: Cytoplasm
EC: 1.8.1.9
|
P91938 | MNLCNSRFSVTFVRQCSTILTSPSAGIIQNRGSLTTKVPHWISSSLSCAHHTFQRTMNLTGQRGSRDSTGATGGNAPAGSGAGAPPPFQHPHCDRAAMYAQPVRKMSTKGGSYDYDLIVIGGGSAGLACAKEAVLNGARVACLDFVKPTPTLGTKWGVGGTCVNVGCIPKKLMHQASLLGEAVHEAAAYGWNVDEKIKPDWHKLVQSVQNHIKSVNWVTRVDLRDKKVEYINGLGSFVDSHTLLAKLKSGERTITAQTFVIAVGGRPRYPDIPGAVEYGITSDDLFSLDREPGKTLVVGAGYIGLECAGFLKGLGYEPTVMVRSIVLRGFDQQMAELVAASMEERGIPFLRKTVPLSVEKQDDGKLLVKYKNVETGEEAEDVYDTVLWAIGRKGLVDDLNLPNAGVTVQKDKIPVDSQEATNVANIYAVGDIIYGKPELTPVAVLAGRLLARRLYGGSTQRMDYKDVATTVFTPLEYACVGLSEEDAVKQFGADEIEVFHGYYKPTEFFIPQKSVRYCYLKAVAERHGDQRVYGLHYIGPVAGEVIQGFAAALKSGLTINTLINTVGIHPTTAEEFTRLAITKRSGLDPTPASCCS | 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. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 64322
Sequence Length: 596
Subcellular Location: Mitochondrion
EC: 1.8.1.9
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B9A1H3 | MAAAEAQYDLLVIGGGSGGLACSKRAASHGKKVAVCDFVKPSPPGTTWGLGGTCVNVGCIPKKLMHQAALLGEGMTDAESFGWEVAAPKHNWETMVGNVQGHIKSLNFGYRSDLMSNGVKYYNAYATFLDPHTVEAVDKKGKVTKITASEIVICTGGRPRYPDIPGAKELGITSDDVFALKSPPGRTLVVGASYVALECAGFIKGVGYDTTVMMRSIPLRGFDQQMAGLCKTYMQEHGVAFIEGAVPTAVEATPSGAKKVSWKLADGSVGSGEYDTVLFAIGRDVCTSAIGIDKAGVKLSSNGKVPTVNEQTNVPHIYAIGDIIDGEALNPPSATTELTPVAIQAGKLLADRLYAGKSALMDYSMVATTVYTPLEYGAVGLPEEEAIKLHGEDNIEVYHSYFKPLEWTLPHRGDNVCYAKLICLKPEGERVIGLHVCGPNAGEMTQGFAVAIKAGATKAHFDDTVGIHPTVAEEFTLLAATKRSGDSAEKSGCUG | 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
|
Q16881 | MGCAEGKAVAAAAPTELQTKGKNGDGRRRSAKDHHPGKTLPENPAGFTSTATADSRALLQAYIDGHSVVIFSRSTCTRCTEVKKLFKSLCVPYFVLELDQTEDGRALEGTLSELAAETDLPVVFVKQRKIGGHGPTLKAYQEGRLQKLLKMNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSGASILQAGCUG | 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 catalysis (Probable). Also has reductase activity on hydrogen peroxide (H2O2) .
PTM: The N-terminus is blocked.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 70906
Sequence Length: 649
Domain: The N-terminal glutaredoxin domain does not contain the C-P-Y-C redox-active motif normally found in glutaredoxins and has been found to be inactive in classical glutaredoxin assays.
Subcellular Location: Cytoplasm
EC: 1.8.1.9
|
O89049 | MNDSKDAPKSYDFDLIIIGGGSGGLAAAKEAAKFDKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKLEDTVKHDWEKMTESVQNHIGSLNWGYRVALREKKVVYENAYGKFIGPHKIMATNNKGKEKVYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGTPGRLKVTAKSTNSEETIEDEFNTVLLAVGRDSCTRTIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEGKLELTPVAIQAGRLLAQRLYGGSTVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYHSFFWPLEWTVPSRDNNKCYAKVICNLKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTLSVTKRSGGDILQSGCUG | 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 catalysis . Also has reductase activity on hydrogen peroxide (H2O2) .
PTM: ISGylated.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 54670
Sequence Length: 499
Subcellular Location: Cytoplasm
EC: 1.8.1.9
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Q9N2I8 | MAALRGAAARFRGRAPGGARGAAGRQCYDLLVIGGGSGGLACAKEAAQLGKKVAVLDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAPHYGWGVAQAPHSWATLADAVQNHVKSLNWGHRIQLQDRKVKYFNVKASFVDTHTVCGVSKGGEETLLSAEHIVIATGGRPRYPTHIEGALEYGITSDDLFWLKESPGKTLVVGASYVALECAGLLTGLGLDTTVMIRSVPLRAFDQQMASLVTEHMAGHGTRILRGCAPEKVEKLPGQQLRVTWVDLTSDRKDAGTFDTVLWAIGRVPETASLNLEKAGVHTNPVTGKILVDAQETTSVPHIYAIGDVAEGRPELTPTAIMAGRLLAQRLSGRTSDLMDYSSVPTTVFTPLEYGCVGLSEEAAVARHGEEHVEVYHAFYKPLEFTVPQRDASQCYIKMVCLREPPQLVLGLHFLGPNAGEVIQGFALGIKCGASYQQLMRTVGIHPTCAEEVAKLRISKRSGLDPTVTGCUG | 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(+) + NADPH
Sequence Mass (Da): 54670
Sequence Length: 511
Subcellular Location: Mitochondrion
EC: 1.8.1.9
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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 diphosphate.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
Sequence Mass (Da): 20103
Sequence Length: 187
Subcellular Location: Cytoplasm
EC: 2.7.7.87
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P94682 | MSTVLYRCPELLIGGEWRPGRHEQRLVVRNPATGEPLDELRLASADDLQLALQTTQQAFEHWRQVPAHERCARLERGVARLRENTERIAHLLTLEQGKTLAEARMECAMAADLIKWYAEEARRVYGRVIPARLPNSRMEVFKFPVGPVAAFSPWNFPLVLSARKLGGAIAAGCSIVLKAAEETPASVAAMVDCLNQELPPGVVQLLYGVPAEVSQALIASPVVRKVTFTGSVPVGRHLAELSARHLKRITLELGGHAPVIVCGDADIARTVNLMVQHKFRNAGQACLAPTRFFVDRRIYGDFVDAFGATQALRVGAGMAAETQMGPVASARRQAAVQDLIARSVAAGARPVASAVPEAGYFVAPTLLADVPLDAPVMSEEPFGPVACAVPFDSLDQAIAQANHNPYGLAGYLFTDSAKAILAVSERLEVGSLAVNGMGVSVPEAPFGGVKDSGYGSESGTEGMEAFLDTKFMHYVA | 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
Sequence Mass (Da): 51011
Sequence Length: 476
EC: 1.1.1.257
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Q9Z8Z0 | MLTLGLESSCDETACAIVNEDKQILANIIASQDIHASYGGVVPELASRAHLHIFPQVINKALQQANLLIEDMDLIAVTQTPGLIGSLSVGVHFGKGIAIGAKKSLIGVNHVEAHLYAAYMAAQNVQFPALGLVVSGAHTAAFFIENPTSYKLIGKTRDDAIGETFDKVGRFLGLPYPAGPLIEKLALEGSEDSYPFSPAKVPNYDFSFSGLKTAVLYAIKGNNSSPRSPAPEISLEKQRDIAASFQKAACTTIAQKLPTIIKEFSCRSILIGGGVAINEYFRSAIQTACNLPVYFPPAKLCSDNAAMIAGLGGENFQKNSSIPEIRICARYQWESVSPFSLASP | 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, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 36719
Sequence Length: 344
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q8KGA4 | MNILGIETSCDETSAAVLSDGSVRSNIVSSQRCHTDFGGVVPELASREHERLIVSIVDAAITEANIAKNDLDVIAATAGPGLIGAVMVGLCFAEGLAWALGKPFVPVNHVEAHIFSPFISDEPGHREPKGDFVSLTVSGGHTLLSVVRQDLGYEVIGRTIDDAAGEAFDKTGKMLGLGYPAGPVIDRLAREGDSDFHRFPRALTASSQTSKSYRGNFDFSFSGLKTSVRTWLEAHDSEYVQKHQADLAASIQSAIVEVLVEKSVAAALLHKVNAISVAGGVSANSGLRSAMQAACDRHGIELFIPALAYSTDNAAMIATMAQLMIARGKYRIEDNSYGVAPFARFEAARKGAR | 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, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 37475
Sequence Length: 353
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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A0M1X3 | MSDQKINILAIESSCDDTAAAVLCNGKILSNIVATQKVHEQYGGVVPELASRAHQQNIVPVIHQALAKANIDKKDVSAIAFTRGPGLMGSLLVGTSFAKSLSMGLNIPLIEINHMQAHILAHFIEEDDFEKPTFPFLAMTISGGHTQIVKVTDYFKMEVIGETIDDAVGEAFDKSAKILGLPYPGGPLIDKYAQEGDPKAFKFPKPKVDGLNFSFSGFKTAVLYFVQRETKNDPEFVEKNLKDICASIQYTIIGILIDKLKKAVKETGITQVAIAGGVSANSGIRQALKDAEQKWGWKCFVPKFEYTTDNAAMIGIAGYHKYLKKDFADFSVTAQSRYKF | 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, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 37232
Sequence Length: 340
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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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, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 35313
Sequence Length: 320
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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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, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 35210
Sequence Length: 319
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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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, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 33514
Sequence Length: 302
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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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, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 34186
Sequence Length: 307
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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O86793 | MADSRDEPLVLGIETSCDETGVGVVRGTTLLADAVASSVDEHARFGGVVPEVASRAHLEAMVPTIDRALKEAGVSARDLDGIAVTAGPGLAGALLVGVSAAKAYAYALGKPLYGVNHLASHICVDQLEHGALPEPTMALLVSGGHSSLLLSTDITSDVRPLGATIDDAAGEAFDKIARVLNLGFPGGPVIDRYAREGDPNAIAFPRGLTGPRDAAYDFSFSGLKTAVARWIEAKRAAGEEVPVRDVSASFQEAVVDVLTRKAVRACKDEGVDHLMIGGGVAANSRLRALAQERCEAAGIRLRVPRPKLCTDNGAMVAALGAEMVARNRAASDWDLSADSSLPVTEPHVPGQGHPHGHPHGHDHVHEVSKENLYS | 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, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 38986
Sequence Length: 374
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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P0CR36 | MPTPLALLLSAILIIGTYFAMPFWPFRKSNYDPRGKHCYITGGSSGLGKALAERLVKQGAHVTIVGRDSKKAEGVVEELKAIAAPGQIIQCIAADLTSPIASTNAIHAACKPHADQAPDYVYLCAGFSRPKLFVETTKQELKDGLDGVYWVSAYTAHEACQMMSKQRRTGKIIFVASFLSYVSFAGYSSYSPAKYALRGLSDALRSEMLLHNIDIHIFLPCGISGPGFDAENRTKPAVTKKIEEGDTPITPDVCAAALESGLKKGYYQITDNLVTEPIRLRSNGGVPTNNFLLDTLWLIVSSVGVPIWRMTADSAVRSFRAKVEKELEAKGYYVS | 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.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.102
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Q5BE65 | MHPSLPSIIYDASPTALGISAVFGALFFYTLVKMFGFLARENQFVVEGRTVVITGGSEGMGKAVACQLAQKGANIVIVARTLQKLEEAIEAIKGSAANVNKQRFHYISADLTKPEECERIMTEVTEWNDGMPPDIVWCCAGYCTPGYFVETSVQTLKDQMDTVYWTAANTAHAILRKWLVPINPSHQRPLPRRHLIFTCSTLAFVPIAGYAPYSPAKAAMRALSDTLCQEIEVYNGSRASKERARATPADVKIHTVFPMGILSPGFDNEQQIKPALTKQLESADKPQTPKEVARIAIEAIERGEYLITTMFVGDVMKGAALGPSPRNSWFRDTCTGWLSNLLFLGVVPDLRKQAFNWGAKNGVPTSPSA | 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.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.102
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Q7RZR2 | MNHYLFSESLMEQLKTLSTSWSLPVAAVVAAIGIFATMGLFSSKNHMPVEGRTVLLTGASEGMGRSAAIQLSQKGANVILVSRNVGRLEEALVDVRAAAKNPSTQRFTYISADVSEHDYAAAVLAEAIAWNGGRSPDIVWCVAGMSTPLLWTDDGSMAAARRNMDVNYFGSAEMSRAILREWLAPENSTGPNGEPKHLVFTASMLALFAILGYGPYTPTKWALRGLADTLAMEVNYYPDNPVKVHIVYPGTIVSPGYERENQTKPDITVELEKDEPAESPDTVARRAIAGLEAGKYFVDVSFLGRLMQCGIMGGSPRNNWVLDTLMGWLIPIIYFFVLRGMNSTIVKWAREKGHPFTHPKKK | 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.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.102
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Q6CE86 | MIFPISEIPDKVTHSILEGVSALQNMSHTAFWSTVLGFLVVARIAVILATPKRRVLDIKGKKVVISGGSQGAGAALAELCYTKGANVVIVSRTVSKLEAQVQKIVTKHEPVFEGQTIRYISADLTKEEEAIRVFSEETMPAPPDVIFSCAGAAETGFILDFKASQLARAFSTNYLSALFFVHAGTTRMAKEPISPKNPRYVAIFSSVLAFYPLLGYGQYCASKAAVRSLIDSLRVEALPFNIRVVGVFPGNFQSEGFEEENKSKPEITRQIEGPSQAISAEECAKIVFAQMEKGGQMITTDLIGWILQSIALSSSPRSFSLLQIPLAIFMCIFSPVWNAFVNRDVRKYFHANTEYVTRHQRGGVGSENPTPQ | 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.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.102
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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.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.102
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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
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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)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine
Sequence Mass (Da): 18405
Sequence Length: 165
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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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 (Probable).
Catalytic Activity: N(1)-methylpseudouridine(1248) in human 18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3-carboxypropyl]pseudouridine(1248) in human 18S rRNA + S-methyl-5'-thioadenosine
Sequence Mass (Da): 33596
Sequence Length: 312
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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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)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine
Sequence Mass (Da): 20066
Sequence Length: 173
Subcellular Location: Cytoplasm
EC: 2.5.1.-
|
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/18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine
Sequence Mass (Da): 20030
Sequence Length: 172
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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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)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine
Sequence Mass (Da): 19233
Sequence Length: 169
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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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)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine
Sequence Mass (Da): 19894
Sequence Length: 173
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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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)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine
Sequence Mass (Da): 18916
Sequence Length: 169
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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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)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine
Sequence Mass (Da): 19197
Sequence Length: 166
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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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 for processing 35S pre-rRNA at site D.
Catalytic Activity: N(1)-methylpseudouridine(1191) in yeast 18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3-carboxypropyl]pseudouridine(1191) in yeast 18S rRNA + S-methyl-5'-thioadenosine
Sequence Mass (Da): 32606
Sequence Length: 288
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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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)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine
Sequence Mass (Da): 19314
Sequence Length: 166
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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Q220I8 | MNAVWTDNDTQAEDLSPQGRVASQLVRLKSDLQAFADATASAPATREPKIERETHKLEKRLCRQVGQAIMDFNMIEEGDRVMVCVSGGKDSYGLLDILLKMQQRAPINFEIVAVNLDQKQPGFPAHILPEYLAKLGIEFHIETQDTYSIVKKVIPEGKTMCSLCSRLRRGILYRVADELKITKIALGHHRDDMLQTFFLNMFFGGKLKGMPPKLVSDDGGHIVIRPLANVAEKDLTRWAAHRQFPIIPCSLCGSQENLQRQLIGQMLRDWEKQYPGRTETMFTALQNVVPSHLMDATRYDFKGLKITGVPDADGDRVFDEETFPMAKLAGVQVLGSSC | 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(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Catalytic Activity: AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase]
Sequence Mass (Da): 37932
Sequence Length: 338
Pathway: tRNA modification.
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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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(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Catalytic Activity: AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase]
Sequence Mass (Da): 32317
Sequence Length: 284
Pathway: tRNA modification.
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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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(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Catalytic Activity: AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase]
Sequence Mass (Da): 33484
Sequence Length: 303
Pathway: tRNA modification.
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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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(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Catalytic Activity: AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase]
Sequence Mass (Da): 29404
Sequence Length: 259
Pathway: tRNA modification.
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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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(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Catalytic Activity: AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase]
Sequence Mass (Da): 32950
Sequence Length: 294
Pathway: tRNA modification.
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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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(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Catalytic Activity: AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase]
Sequence Mass (Da): 31298
Sequence Length: 274
Pathway: tRNA modification.
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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P17789 | MKMASQRFCLRWNNHQSNLLSVFDQLLHAETFTDVTLAVEGQHLKAHKMVLSACSPYFNTLFVSHPEKHPIVILKDVPYSDMKSLLDFMYRGEVSVDQERLTAFLRVAESLRIKGLTEVNDDKPSPAAAAAGAGATGSESTATTPQLQRIQPYLVPQRNRSQAGGLLASAANAGNTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDLNESRDSLPSKRSKNSKDHRVVSHHEDNSTSDGNDSDGEGLDTSYMEPQLMLDEYDEPVEFKYNPLTDNSSPTQDHTDGSHLNEQARQQAFLIAAQRKHQVETAAAAAASGIKLNIIGMAAGGAQVKSMVSIPKLTPIGKVNAASTPLVSPAGSFSTATVKPRVQKRPKLGKQNGDVKPAVFSSQEYLDIYNSNDGFKLKAAGLSGSTPNLSAGLGTPSVKTKLNLSSNVGEGEAEGSVRDYCTKEGEHTYRCKVCSRVYTHISNFCRHYVTSHKRNVKVYPCPFCFKEFTRKDNMTAHVKIIHKIENPSTALATVAAANLAGQPLGVSGASTPPPPDLSGQNSNQSLPATSNALSTSSSSSTSSSSGSLGPLTTSAPPAPAAAAQ | 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, eve, h, odd, run, and en . Inhibits Trl-dependent activation of eve . May bind to the region AGGGC/TGG . Degradation of ttk is directed by binding of sinah or sina, via the adapter molecule phyl which binds to the BTB domain of ttk . A second method of degradation exists that is phyl-independent, this is mediated by recognition of motifs in the C-terminus of ttk .
PTM: Polyubiquitinated by sina. Polyubiquitin linkage is mainly through 'Lys-48', but linkage through 'Lys-63' also occurs. Deubiquitination by Usp47 leads to its stabilization.
Sequence Mass (Da): 68771
Sequence Length: 643
Subcellular Location: Nucleus
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Q8AYG3 | MDEEESTERQMQIAMLCQKLAMMKQLFNEDDTDYINQAISSNSPDTCRTFLSNLEKKGNPQADPSLLSKLMDSYTRVFSSMPLGKYSQNESYAKMLVRFAELKAIQDVNDAQTSFDIARSHCKDFAFVHVAYAQFELLQGNMKKCTMILQKAFEMNAKPRHVLEAAVRNLKTGKRQLLSHEDKENLSVSALDHTQGSRRSDGTCELKPSNTFLHSDQKFSPQEENGPVWRTGSQHRRTAMAERVPMVPLSIPENETSDSDCAQKAEAPFTHSSGFSRQTSGSSVRSAFSLCSSKKGTPDGDSYSLNIKPPVISPDYLREDIEEGHTITALLNRAEKRETARTEETTDINQIISTNSTEGCQAFLKNLEKRADPHSDAAFLSKLLDCYSKVFARFPLAEHCKTESYARMLVRYAELKGIEDPEDAADDFSIARSHCKAFAFVHIAHAQFELSRGNSRKSVSILQKALSSNARPIELLQTAIRNLKSGKTLLLPAEHQESSEAENVEAQNGMKREENPVKAPEDHQKPFSKETSSEWKIPALITKHTSPEDRKAPVEPVSSSSSHHAVRTPAPLRLNPSLSCQTPNYRQPNPNSFVTPVVKQRPVIVSVPATAQKMCPTALPCTPQSGVSYIQPPTQTPSSAFSNESITIKGKQFFIFKMIGRGGSSKVYQVFDHKKHVYAVKYVNLEEADAQAVESYKNEIEHLNHLQQYSDQIIKLYDYEITSSYIYMLMECGHLDLNTWLRNRKTVKPLDRKAYWRNMLEAVHTIHKHGIVHSDLKPANFLIVDGSLKLIDFGIANQIQPDVTSIMKDSQVGTLNYMPPEAIKDTSSNGKPGSKISAKGDVWSLGCILYCMTYGKTPFQNITNQISKIHAIIDPSHEIDFPDIPEKDLLDVLKKCLVRNPRERISIAELLDHPYLQLQPQPAPEPAETSSSDFKRILNELVALQSPNSIARAASNLAMMCNSGRKLDVSECVKSSSQTLWK | 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-[protein]
Sequence Mass (Da): 110012
Sequence Length: 982
EC: 2.7.12.1
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P33981 | MESEDLSGRELTIDSIMNKVRDIKNKFKNEDLTDELSLNKISADTTDNSGTVNQIMMMANNPEDWLSLLLKLEKNSVPLSDALLNKLIGRYSQAIEALPPDKYGQNESFARIQVRFAELKAIQEPDDARDYFQMARANCKKFAFVHISFAQFELSQGNVKKSKQLLQKAVERGAVPLEMLEIALRNLNLQKKQLLSEEEKKNLSASTVLTAQESFSGSLGHLQNRNNSCDSRGQTTKARFLYGENMPPQDAEIGYRNSLRQTNKTKQSCPFGRVPVNLLNSPDCDVKTDDSVVPCFMKRQTSRSECRDLVVPGSKPSGNDSCELRNLKSVQNSHFKEPLVSDEKSSELIITDSITLKNKTESSLLAKLEETKEYQEPEVPESNQKQWQSKRKSECINQNPAASSNHWQIPELARKVNTEQKHTTFEQPVFSVSKQSPPISTSKWFDPKSICKTPSSNTLDDYMSCFRTPVVKNDFPPACQLSTPYGQPACFQQQQHQILATPLQNLQVLASSSANECISVKGRIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENGKSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAKGTTEEMKYVLGQLVGLNSPNSILKAAKTLYEHYSGGESHNSSSSKTFEKKRGKK | 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 checkpoint .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 97072
Sequence Length: 857
EC: 2.7.12.1
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Q4R7H0 | MGSSQEEGLPCQPSQPDHDTGGHGGPDLEGAGRVSTTPGPPGLLTSHPPADSDDTDATGPPAALLEGLLLGDGKPSPHSTRPGPFFYIGGNNGAAIISSYCKSKGWRRIQDSRREDYVLKWCEVKSRDSYGSFREGEQLLYQLPNNKLLTTKIGLLSTLRGRAWAMSKASKAPGGTQARLGKDATAPTLEDLPWTSPGHLRPQRVLRMEEFFPETYRLDLKHEREAFFTLFDETQIWICKPTASNQGKGIFLLRNQEEVAALQAKTRRAEDDPIHHKSPFRGPQARVVQRYIQNPLLLDGRKFDVRSYLLIACTTPYMIFFSHGYARLTLSLYDPHSSDLSGHLTNQFMQKKSPLYVLLKEDTVWSMERLNRYINTTFWKARGLPKDWVFTTLTKRMQQIMAHCFLAAKSKLECKLGYFDLIGCDFLIDDNFKVWLLEMNSNPALHTNCEVLKEVIPGVVIETLDLALETFQKSLRGQKMLPLLSQRRFVLLHNGEADVWPRLGGSCSLRRRLPPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGTGDRHPEQEPSPGTAKEEREEPENARPWGGHPRPTPHAPATLPAFRDL | 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. Polyglycylates alpha-tubulin and beta-tubulin. Polyglycylates non-tubulin proteins such as nucleosome assembly protein NAP1.
Catalytic Activity: (glycyl)(n)-glycyl-L-glutamyl-[protein] + ATP + glycine = (glycyl)(n+1)-glycyl-L-glutamyl-[protein] + ADP + H(+) + phosphate
Sequence Mass (Da): 68941
Sequence Length: 618
Domain: Gln-246 is the main determinant for regioselectivity, which segregates between initiases and elongases in all tubulin--tyrosine ligase family. A glutamine residue at this position is found in elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-chain elongation, whereas an arginine residue is found in initiases TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
Subcellular Location: Cytoplasm
EC: 6.3.2.-
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A4Q9F3 | MALHPQAGRPHRDGSEAQAEAAAQDLGRLPSPSKVGAAVCRIQGLGHRAARRPRRGIGTTSASRVPRPGALMPATRNRPRFIHCRGQPPRTRVSSKRSKRSRIHPCHTEVPGWTHEKQMGSSVKERLRPELSQLDQDADDLEEEEAARLPVTSPDGLLMEGDKQPSPGQGPFFYIGGTNGASIISNYCESKGWQRTQDSHCEDYKLKWCEIKCRDNYCSFREGQQLLFQLPNNKLLTTKIGLLSALREHARTLSKARMLPSTQTKVLKMEEFFPETYRLDIRDERQAFFALFDETQMWICKPTASNQGKGIFLIRSQEEAAALQAKTQSIEDDPIYRKMPFRAPQARVVQRYVQNPLLLDGKKFDVRSYMLIACAMPYMVFFGHGYARLTLSLYNPHSSDLSGHLTNQFMQKKSPLYTLLKESTVWTMEHLNRYINDKFRKTKGLPRDWVFTTFTKRMQQIMSHCFLAVKSKLECKLGYFDLIGCDFLIDENFKVWLLEMNANPALHTNCEVLKAVIPGVVIETLDLALETCQKSLHSQKMLPLLSQRRFVLLYNGETTDLWPRLASSRPLNRLPNPNPNPNPNANPHPHPHPNPHPHPNPHPNANPHPPRPTCEAASSALSSARAAISERPGARKSMPSRGAPVCTPRKSRLSDSSGSSIAESEPSLCSGSLEGSRDTAREPSLGPPEEEREEEQRSTSHRGS | 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 . Polyglycylates alpha-tubulin and beta-tubulin . Polyglycylates non-tubulin proteins such as nucleosome assembly protein NAP1 .
Catalytic Activity: (glycyl)(n)-glycyl-L-glutamyl-[protein] + ATP + glycine = (glycyl)(n+1)-glycyl-L-glutamyl-[protein] + ADP + H(+) + phosphate
Sequence Mass (Da): 79250
Sequence Length: 704
Domain: Gln-307 is the main determinant for regioselectivity, which segregates between initiases and elongases in all tubulin--tyrosine ligase family. A glutamine residue at this position is found in elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-chain elongation, whereas an arginine residue is found in initiases TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
Subcellular Location: Cytoplasm
EC: 6.3.2.-
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H2KZM9 | MGCKISTEFCSDNPVGSISTSKVHPTDLSTPSYAIKPVEFYEEPLKDDQLFYKVALAKKEYREKEKDKKEQLSSNRRVSLQVEPNKLPIPLTRSSSLSSIMENRPPSGISNSSFIRSRNTASRRFTIDTSRAKSNQYVVSLCSKKIGIIEYPDGRSDKQPCDVYWHNVVLSDMNKIVTSPQSRVNKFPGMTELAKKISLTHSISSMQKLFPDEYAFYPNSWFLPAHLADFHAFYRKAQALGKTEMWFIVKPDEGAQGTGIYLINSPNQIRNVDQRQLVQEYVADPLLMNDKLKFDFRVYGVIKSINPLSIYVAREGMARFCTEKYEKPDSSNFKNLYAHLTNYSLNKANEAYVHSNTLQDQTRGSKRLLSTVFHQLESRGVKTKRLWHDIKLILVKTTLAMLPEIMLHYEHHFYDSTGPQCFQIMGFDVMIREDGTPILLEVNAAPSLTADHIVPHPGRTLLEGGQRVRSIVDEVIKIPLVRDTLLLVLGLMEEEYQNNSLKGETKSLDDMQTIKQRRKPHLSEIFPTRYGAHSGHLLFLDKAMYIYMQFVQLRSNVNITNAGLKQFVRKCNLIDIIPVVHVDAKVSEINYYFTGEKRTNGNGLPFHAFLMFLFFIAEKKFVLENDLLSKVQRLLSFCDMSLRRYGVRSARLRRAEVDSTIGNVEIYMLPSRMARNRSGTNGRKQNFTDDNNNPNSFAHLPKINERL | 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 doublets in cilia . Together with ttll-4 and 5, required for male mating .
Catalytic Activity: ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate
Sequence Mass (Da): 81077
Sequence Length: 707
Subcellular Location: Cell projection
EC: 6.-.-.-
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A4Q9F4 | MRRSSPEKKPEAEWEADAAAAAAATAAATESLPAETEKQQGVDAGAAGDPERLELEEQPKDVGRIPTPTRRHAPEEGEARVVRRLPPALPLAQPRPAARALSQLVKARGRSRSRVYRRSAGSMRPVTVDSSKARTSLDALKISLRQLRWKEFPFGRRLPCDIYWHGVSFRDSDILSGQVNKFPGMTEMVRKVTLSRALRIMQNLFPEEYNFYPRSWILPEEFQLFVSQVQTVKEGDPSWKPTFIVKPDSGCQGDGIYLIKDPCDGRLTGTLHNRPAVVQEYIRKPLLIDKLKFDIRLYVLLKSLDPLEIYIAKDGLSRFCTEPYQEPNPQNLHHVFMHLTNYSLNIHSGKFVHSDSASTGSKRTFSSILCRLSSKGVDIKKVWSDIISLVIKTVIALTPELKVFYQSDIPTGRPGPTCFQILGFDILLMKNLKPMLLEVNANPSMRIEHEYELSPGVFENIPSLVDEEVKVAVIRDTLRLMDPLKKKKEIHFPDIYMDRKHRIPPVSDRMSSWKHKGSSLSIVRSQQMEKSFTSKEDLNCDPTGGDSEPNPEAHLPSICLKQVFPKYAKQFNYLRLVDRMANLFIRFLGIKGTMKLGPTGFRTFIRNCKLSSSSLSMAAVDILYIDITRRWNSVTVDQRDSGMCLQAFVEAFFFLAQRKFKLQPLHEQVASLIDLCEYHLSVLDEKRLLCHRGRPLQRNPPQMNRPEHSATGSSAPRVIGASKLSQS | 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 polyglutamylation reaction . Preferentially modifies the alpha-tubulin tail over a beta-tail . Required for CCSAP localization to both spindle and cilia microtubules (By similarity). Promotes tubulin polyglutamylation which stimulates spastin/SPAST-mediated microtubule severing, thereby regulating microtubule functions .
Catalytic Activity: ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate
Sequence Mass (Da): 82361
Sequence Length: 727
Domain: The flexible c-MTBD (cationic microtubule binding domain) region mediates binding to microtubules. It is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding.
Subcellular Location: Cytoplasm
EC: 6.3.2.-
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A6NNM8 | MEPSTCRTMESEEDYVEEKESEKCVKEGVTNPSNSSQQALLKADYKALKNGVPSPIMATKIPKKVIAPVDTGDLEAGRRKRRRKRRSLAINLTNCKYESVRRAAQMCGLKEVGEDEEWTLYWTDCAVSLERVMDMKRFQKINHFPGMTEICRKDLLARNLNRMYKLYPSEYNIFPRTWCLPADYGDFQSYGRQRKARTYICKPDSGCQGRGIFITRNPREIKPGEHMICQQYISKPLLIDGFKFDMRVYVLITSCDPLRIFTYEEGLARFATTPYMEPSHNNLDNVCMHLTNYAINKHNENFVRDGAVGSKRKLSTLNIWLQEHSYNPGELWGDIEDIIIKTIISAHSVLRHNYRTCFPQYLNGGTCACFEILGFDILLDHKLKPWLLEVNHSPSFTTDSCLDQEVKDALLCDAMTLVNLRGCDKRKVMEEDKRRVKERLFQCYRQPRESRKEKTESSHVAMLDQERYEDSHLGKYRRIYPGPDTEKYARFFKHNGSLFQETAASKAREECARQQLEEIRLKQEQQETSGTKRQKARDQNQGESAGEKSRPRAGLQSLSTHLAYRNRNWEKELLPGQLDTMRPQEIVEEEELERMKALLQRETLIRSLGIVEQLTRLQHPGPQGQKKLHESRDRLGSQELKSMSLVLLVLLRGAATEQGAPHFLHPVLPHESIPRILGALPSMNAAIPHVPRYHLQPKNFNWTGEPAAINSCSLSMKKAGRCYFSSARIRLTSQGQASRRLEAINRVLAGSVPPTLTPKQGYFLQPERVASDSWTECTLPSMVNSEHRAAKVPLCPASAPMLQRSRALLNINQFR | 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 step. Preferentially modifies the alpha-tubulin tail over a beta-tail.
Catalytic Activity: (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate
Sequence Mass (Da): 93645
Sequence Length: 815
Domain: The flexible c-MTBD (cationic microtubule binding domain) region mediates binding to microtubules. It is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding.
EC: 6.3.2.-
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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. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthesis of molybdopterin.
Sequence Mass (Da): 9206
Sequence Length: 76
Pathway: tRNA modification.
Subcellular Location: Cytoplasm
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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. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthesis of molybdopterin.
Sequence Mass (Da): 9509
Sequence Length: 79
Pathway: tRNA modification.
Subcellular Location: Cytoplasm
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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. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthesis of molybdopterin.
Sequence Mass (Da): 9095
Sequence Length: 81
Pathway: tRNA modification.
Subcellular Location: Cytoplasm
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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.-
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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.-
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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 bonds.
Sequence Mass (Da): 8680
Sequence Length: 74
Subcellular Location: Secreted
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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 sequences of this peptide have also been found in the venom. It is possible they have been cleaved in the venom.
Sequence Mass (Da): 7320
Sequence Length: 68
Subcellular Location: Secreted
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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
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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
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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
Sequence Length: 46
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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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.
Subcellular Location: Secreted
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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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