ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P83858 | MQALNITAEQFSRLLSAHNLTREQFIHRYGLRPLVYTPELPARAKVAFALAGALIFALALFGNSLVIYVVTRSKAMRTVTNIFICSLALSDLLIAFFCIPVTMLQNISDKWLGGAFICKMVPFVQSTAVVTEILTMTCIAVERHQGLVHPFKMKWQYTTRRAFTILGVVWLAAIIVGSPMWHVQRLEIKYDFLYEKEHICCLEEWASPVHQRIYSTFILVILFLLPLVVMLVLYSKIGYELWIKKRVGDSSALQTIHGKEMSKIARKKKRAVIMMVTVVALFAACWAPFHVVHMMVEYSNFEKEYDDVTIKMVFAVAQTIGFFNSICNPFVYAFMNENFKKNFLSAVCYCIVKESSSPARKPGNSGISMMQKRAKLSRPQRPVEETKGDTFSDASIDVKLCEQPREKRQLKRQLAFFSSELSENSTFGSGHEL | Function: Receptor for the orexigenic neuropeptide QRFP. The activity of this receptor is mediated by G proteins that modulate adenylate cyclase activity and intracellular calcium levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49311
Sequence Length: 433
Subcellular Location: Cell membrane
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Q8FKC5 | MRVTDFSFELPESLIAHYPMPERSSCRLLSLDGPTGALTHGTFTDLLDKLNPGDLLVFNNTRVIPARLFGRKASGGKIEVLVERMLDDKRILAHIRASKAPKPGAELLLGDDESINATMTARHGALFEVEFNDQRSVLDILNSIGHMPLPPYIDRPDEDADRELYQTVYSEKPGAVAAPTAGLHFDEPLLEKLRAKGVEMAFVTLHVGAGTFQPVRVDTIEDHIMHSEYAEVPQDVVDAVLAAKARGNRVIAVGTTSVRSLESAAQAAKNDLIEPLFDDTQIFIYPGFQYKVVDALVTNFHLPESTLIMLVSAFAGYQHTMNAYKAAVEEKYRFFSYGDAMFITYNPQAINERVGE | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Mass (Da): 39396
Sequence Length: 356
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
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B0S1J2 | MNTDDFDYELDEKFIAQTPLDKRDESKLMVMDRFNGNTEIKKFYNIIDYLNPGDVLVCNNTRVIPARLFGHRPEKEEKIEVLLLQQTEDKWECLVKPGKKMKLNQVIEFSDSVSAKVVDITEDGSRILKFEYEGIFEERLDELGNMPLPPYIKEKLNDKERYQTVYSKHNGSAAAPTAGLHFTNELLEKIKDKGIYVVFLTLHVGLGTFRPVKVDDVKDHHMHSEYYTISQETVDIINRQKSKGHNIIAVGTTSVRTLETVTHNNNSKLVAESGWTDIFIYPGFEFNIVDSLITNFHLPKSTLMMLVSAFSKKEYIFDAYEKAKQNDFRFFSFGDAMFINGGRNV | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Mass (Da): 39766
Sequence Length: 345
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
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A6GW82 | MKLSHFQFNLPDELLAEYPAENRDESRLMVVNRAKGTIEHKMFKDVLDYFDEGDVLVLNNTKVFPARLYGNKEKTGARIEVFLLRELNAEQRLWDVLVDPARKIRIGNKLYFGDDDSLVAEVIDNTTSRGRTLRFLYDGSYEEFRNKLTELGETPIPKYISREVTPEDAERYQTIYAKEEGAVAAPTAGLHFSKHLMKRLEIKGIQFAEVTLHVGLGTFNPVEVEDLSKHKMDSEELKITQEACDIVNAAKERKSRICAVGTTSMRAIESSVSSARTLNPYDGWTNKFIFPPHDFSLATCMITNFHTPKSTLMMMISAFCGHDLMKEAYAEAIKEKYKFYSYGDAMLII | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Mass (Da): 39857
Sequence Length: 349
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
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Q6MKZ5 | MKKNKKVVVLLSAGLDSTVNAYEAIKHHHEIVLALTFNYGQRAAKKELEASANIAKHLGIPHKVVELPWFKDFNKSSLLVEDQAVPTGSAVEIDNQQKSEETAKSVWVPNRNGIFLNIAAAYAEALGADAVIPGFNAEEAATFPDNSREFLEQATKSLWYSTSNHVTVGCYTAHLKKPDIVRLGQGLKVPWELIWPCYFSGDKWCGQCESCLRSKRAFASANIDVKHLFKE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 25643
Sequence Length: 231
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
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Q89LP8 | MSDAFSSETALVLFSGGQDSTTCLAWALSRFARVETLGFDYGQRHAVELACRDRLFDGLKGLRADWADKLGESHTLSIPTLAAISDTALTRDVAIAMGADGLPNTFVPGRNLVFLTFAAALAYRRGITHIVGGMCETDYSGYPDCRDETVRAMQAALSLGMARKFELHTPLMWIDKAATWKLAHDLGGEGLVDLIREQSHTCYLGERGAQHEWGYGCGECPACSLRAKGWNEYVAHR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 25911
Sequence Length: 237
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
A4YUN8 | MSEQDATALVLFSGGQDSTTCLAWALDRFARVETIGFSYGQRHGIELDCRARLRDGIAQLRADWADKLGCEHTLDIPTLAAISETALTRDVAIEMGADGLPNTFVPGRNLVFLTFAAALAYRRGIRHIVGGMCETDYSGYPDCRDETIKALQVALSLGMARPFELHTPLMWLTKAATWQLAHDLGGRGLVDLIRDESHTCYLGERGARHDWGHGCGRCPACELRAHGWRAYVGGGA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 25805
Sequence Length: 236
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
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A6WXM7 | MKTLVVCSGGLDSVSLAYRIASEHQLTALLSFDYGQRHKKELDSAKACAERLGVPHQIIDITNIGASLTGSALTDDIDVPDGHYAEETMKITVVPNRNAIMLAIAFGVAAAQKAEAIALAVHGGDHFIYPDCRPGFIDAFQTMQNHALDGYADIKLLAPYVHASKADIVIDGAKHGAPFAATWSCYKGGEHHCGRCGTCVERREAFHLAGVEDPTLYEDADFWRSAIEKRNA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 25068
Sequence Length: 232
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
Q8K986 | MKKILIIFSGGQDSTTCLIHYTNIYKEIYCITFDYNQLHKSEIDSARFISNYFNVKKHIFVDLKCLKNLSISSLTDEKISILDNHPLNFSLPSTFVPGRNILFLTLSSIYAFNHQINSIVLGVNEIDFSGYPDCRNAFLKKMNDVVQIGMNCKINFQSPLINLSKAEIWALSDYWNSTQFILNNTVTCYQGIQGKGCGQCQSCILRNDGFNKWKSNPSYYMKKLKEKFNFDN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 26720
Sequence Length: 232
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
O27180 | MRAISILSGGMDSAVATALMMDEYEIHAITFDYGQRSARMELEYARRLSEHLGIEHTTLDLQWLGRLGGSVLTAGGDIPSPSNLDDTVECLETARKVWVPGRNLVFTSIGVSFAEAMDAGAVIVGWDLEEAETFPDNSEEFLDAFNRLLEIGTLDGVRVVAPVIGMTKREIVEAGHEVGLPFELTYSCYAGDRVHCGVCESCMRRRRAFELAGIDDPTEYRE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24470
Sequence Length: 222
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
A0B6A6 | MGRAVCLCSGGLDSTVAATIARRSGMDVYLIHVSYGQQAERREIEAIERIADAIGASDLMCSRIDLFRNISALTTQGARIPRGEEVSLDSESTPPTWVYCRNTVLLSMAAAYAEYLGAHSIYVGFNAEEAMSYPDNRPEFVEQFNALLEKAVASFSRPPKVVAPLVDMRKKDIVRLGADIKAPLELTWSCYLNGEIHCGTCESCQHRRRGFVEAGIPDPTEYQH | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24723
Sequence Length: 224
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
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B0JIA6 | MTKKAIILLSGGLDSATTAAIALAAGYQLIALSFRYGQRHERELAAAKKIANFLNIKEHHLIEVNLSLWGGSALTDQSIAIPQEGINPDIIPITYVPGRNTVFISIALSLAEAREAEAIYLGINAVDYSGYPDCRPEYLDAFQTLANLSSKAGLEGKAPQLIAPLVMDSKVDIVRRAVSLGVPIADTWSCYQGEVEPCGLCDSCRIRDQALIEAGYPELATPLLKNSRGK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24755
Sequence Length: 230
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
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Q1CYI2 | MVKRAVVLISGGLDSTTCLAMAKAKGFEPVCLAVAYGQRHAVELEQARKVAAAMGVTDFRVVSIDLRQVGGSALTADIEVPKDRPSDEMSHGIPVTYVPARNALFLSLALGLAEVVGSTDIYIGVNAVDYSGYPDCRPEFIRSFESMANLATKAGVEGAHFTVHAPLSGLTKADIIREGVKLGVDYGLTHSCYDPDAQGRACGRCDSCVLRKKGFEEAGVPDPTRYTESA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24413
Sequence Length: 230
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
Q30RN3 | MNLKNKKAICIMSGGMDSTLGAYMVKEMGYEIVALHFNYAQRTEAKELFCFKKICEALNVSNSYVLDLDFFSKIGASALTDKSIDIPINGLEEGVPITYVPFRNGIFLSIAAALAEKEEAVLIAIGVVQEDSSGYPDCKDSFITSMEQSINLGTKDETKIKIYMPLVHLSKSQIVEHALRLNVPLELTWSCYKDEEAACGVCDSCRLRLNGFRLANAKDPIEYM | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24862
Sequence Length: 224
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
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A6Q9Q9 | MGKKAVCIISGGMDSALSAKIAQEEGYEIIALHFNYGQRTRNKELECFRKITQELNASESYEIDLDFFEQIGASALTDKSIDVPIGGLEEGVPVTYVPFRNGIFLSIAAAIAEKHGAEALFIGVVEEDSSGYPDCRESYIEQMQKAINLGTKDETNIEIKMPLVSLRKSQIVQKAIELGVPLEDTWSCYQAEDAACGVCDSCRLRLRGFEVAGVKDPIAYRK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24442
Sequence Length: 222
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
Q31NK6 | MAKAVVLLSGGLDSATAAAQAIADGYEAIALSFRYGQRHVRELEAARSVAAALGINQHFFVDVNIAQWGGSSLTDAAEPLPGSGVVAGEIPSTYVPGRNTVFIALALSLAEAQQASAIYLGINAVDYSGYPDCRPDYLAAFQQLASLSSKVGVEGQAPQLVAPLIHDHKVDIVRRAVVLGVPIPATWSCYAGGAEACGRCDSCRIRDRALIEAGYPEWATAIGRSLVSLQP | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24138
Sequence Length: 231
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
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Q8K9N6 | MSLKINNFNFLRPISRKKHRKKIKLNCLNLPFKGKDIWTLYELSWLNKNGLPQIAIAKIEIDVNSANIIESKSFKIYINSFNQMKFNNNIDFINILTNDLTKCICGQISIKLFSLDAIKNETITDFHGICIDNQNIKIESYKYTPSFLMINSERKIIKEDLYTHLFKSNCPVTQQPDWASIYIAYTGLSINHASLLRYLISFRSHNEFHEECIERIFNDINNICKPEELSVYARYTRRGGIDINPWRSNTNFSPFLTRLARQ | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 30731
Sequence Length: 262
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
Q4ZV71 | MHPAAEHSPLGKSSEYIATYTPSLLFPIPRAAKWAELGLTAQTLPYQGVDFWNCYELSWLLPSGKPVVAIGEFSIPAESPNIIESKSFKLYLNSLNQTAFATVEQLQTTLEQDLSAAAGKPVGVRIRSLAEIEEEGVAALPGVCIDDLDISVSSYDRPQPELLCCDDSRVVAESVHSHLLKSNCPVTSQPDWGSVVVEYRGAALDHASLLAYIVSFRQHSDFHEQCVERIFLDLQRLLKPEKLTVYARYVRRGGLDINPYRSTETLDVDNRRLARQ | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 30703
Sequence Length: 276
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
Q1MDH2 | MPNTDVSSLSMLGQQTETAQSPEEAVLEKVPSNHAGTDYVVRFTAPEFTSLCPMTGQPDFAHIVIDYIPGEWLVESKSLKLFLHSFRNHGAFHEDCSIYIAKRIVELLDPRWLRIGAYWYPRGGIPIDVFWQTGKPPEGVWLPEQGVATYRGRG | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 17363
Sequence Length: 154
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
Q7UVG9 | MSDTASFRDTLEVFENPAPTRNFTIEHHCPEFTSVCPKTGQPDYGTIVFTYVPDRVCVELKSLKMYLQKFRNEGIFYEQVTNRILDDFVAVVQPRKVTVESKWTPRGGLNSNIIVTYPDEA | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 13897
Sequence Length: 121
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
Q6N5U5 | MSKTPRKSAPSPSLQLGQAVEWPDRPEAAKLDRVPNPQKDTNFLARFTAPEFTSLCPVTGQPDFAHLVIDYVPGPWLLESKSLKLYLASFRNHGAFHEDCTVAIGKRIATEIKPKWLRIGGYWYPRGGIPIDVFWQTGKLPKDVWVPDQGVQPYRGRG | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 17783
Sequence Length: 158
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
E4RUV9 | MRDYSKEIKSWAAELGFDFCGISAADFLEEEAPRLERWLNRNYHGKMAYMANHFDKRLDPRKLVDGAKSVVSLLLNYYPEEPLDASPYKISKYAYGKDYHYVIKDKLKLLFERIQKEIGEVGGRIFVDSAPVMDKIWAKKAGLGWVGKNSNLINRKMGSFFFIAELILDLPLQADGPIRDYCGTCTACIDACPTDAITPYEVDGSKCISYLTIELKDQIPNEFKGKMENWIFGCDICQDVCPWNSFARPHSTEEFYPNENLKTFQDWDEITSEIFSHLFKKSAVERTKLEGLKRNIAFVKEV | Cofactor: Binds 2 [4Fe-4S] clusters per monomer.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 34760
Sequence Length: 302
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.17.99.6
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Q8Y8H0 | MVVKQKADYAALKEELIAYAYEIGIQKIGFTTADPFLFLKERLLEAEALDLFTGFEHPVIEERVYPELIFKEPQSIIAIALAYPSKLKEAPVSKKGARRGVFARASWGIDYHTVLREKLALLETFLIERLPDVRMKSMVDTGELSDVAVAERAGIGWRGKNTLLITPEYGSWVYLGEMITNIPFEPDTPASDLCGSCNQCVKACPTGSLLGEGKMNPKICLSYLTQTKDFLDEKYREVLHNRLYGCDTCQVVCPYNRGHDFHFHEEMEPDPELVRPELKPLLHISNRAFKEQFGDMAGSWRGKKPIQRNAIIILARYKDKTAVPDLIDCLQNDPRPVIRGTAGWALRKIGGRDAEEAVERALQTEQDVQVLQELTAIPN | Cofactor: Binds 2 [4Fe-4S] clusters per monomer.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 42770
Sequence Length: 379
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.17.99.6
|
Q46I55 | MRNSIDLTKKIKEKAFEEGFDAVGIAKVPGSSRIKLRTASLERWLQAGHQATMEWMKSPRRKDIENMLQGVKSILAVGLNYYVDTERESKDISIARYGWGKDYHKIIEEKLKKVAKFLETERPNAKWKICVDTSAFLDKAWAEEAGIGWIGKHSNVINSEIGSWMFLGHLLSTEVLEADKPSKPICGECEKCIEACPTKAIEEPFIVNSYKCLAYHTLENRDQELPENIINKMGNWIAGCDICQDVCPWNQKHIPSTTEPDLQPSEWILHTTKQDLLSWDDAKWKESLKNSALKRIKPWMWRRNIDSISKKT | Cofactor: Binds 2 [4Fe-4S] clusters per monomer.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 35865
Sequence Length: 312
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.17.99.6
|
Q9HUL4 | MTPQPLADNLSPPDPARLAQSIKDWGRELGFQQVGISDVELGEHEAHLQRWLEAGYHGEMDYMAAHGSKRSRPAELVPGTLRVISLRMDYLPGDTRMAQVLATPEKAYVSRYALGRDYHKLIRKRLQQLAERIQAEVGPFGFRAFVDSAPVLEKAIAEQAGLGWIGKNTLVLNRKAGSYFFLGELFVDMPLPVDPAMDSEHCGRCSACLDICPTAAFVGPYRLDARRCISYLTIEYKGAIPLELRPLIGNRVFGCDDCQIVCPWNRFARPTGQGDFQPRHSLDNAELAELFLWSEEEFLGRTEGSPLRRAGYERWLRNLAVGLGNAPSTIPVLEALKARRGFPSELVREHVEWALRRHGET | Cofactor: Binds 2 [4Fe-4S] clusters per monomer.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 40509
Sequence Length: 361
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.17.99.6
|
F7ZDR3 | MSGLKEKLVARALEEGFIACRICRPDAVPDVAARLKAFVDAGYHGQMTWMADRMHWRGDPTQLWPQARSVIMLAESYGPEHDPMAVLQQPERGAISVYAQGRDYHDVVKKRLKRLARWLMAEAADADPQVKVFVDTAPVPEKALGQAAGLGWQGKHTNLLSREWGNWAFLGAVFTTLDIAPDAAEVDHCGSCRACLDVCPTDAFPAPYKLDARRCISYLTIEHKGPVPTDLRPLLGNRIYGCDDCLAVCPWNKFATAARDMRLSARPELTAPRLADLAALDDAAFRALFSGSAVKRIGRNRFVRNVLYAIGNSGEASLRQIASELTDDPDDAVADAARWAVAQLGG | Cofactor: Binds 2 [4Fe-4S] clusters per monomer.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 37912
Sequence Length: 346
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.17.99.6
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Q8EAN7 | MSMTVTTSSNVSDAAMLSRLALQIKSWGKALGFAQIGICDTDLTAEEAKLQTWLDKGFHGEMAYMETHGMMRARPHELHSGTVRVISARMDYLPPEAGFATNLASPNMGYISRYAGGRDYHKLIRARLKKLGDQINSELVALGFDAADFRPFVDSAPVLERPLAEKAGIGWTGKHSLILNHDAGSWFFLGELLINLPLPVDIPVQEGCHSCVACITSCPTGAIVEPYTVDARRCISYLTIELQGAIPEEFRPLMGNRIYGCDDCQLVCPVNRAAPLTQESDFHIRPKLKQPELLTLFTWSETEFLKQTEGSAIRRIGHQRWLRNIAVALGNAPSSADIISALEQRKAQADVDEMVKEHIDWALAQQRAGDLQTNNRKTERLVRVIQKGLPRDA | Cofactor: Binds 2 [4Fe-4S] clusters per monomer.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 43580
Sequence Length: 393
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.17.99.6
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P73526 | MGIAPVSETENDEAAQRLQSWIALGYNADMAWMANPKRQNIRELLPSARSVIAVGLNYYTPHQRSGDPAHGKISRYAWGRDYHRVLTKKLKALNLWLEQQVPDLQSRYYVDTGPIQEKAWAERAGLGWVGKNGNLISRDYGSWLFLGEIVTNITLQGDRPHSQHCGTCTRCLEACPTQAIVEPFVVDSNKCIAYHTIENRAEILPTAIADNLQGWVAGCDICQDVCPWNQRFAQPTDVADFDPYEGNLNPELETLANITEADWQQQFTASALRRIKPAMLRRNAQANLQ | Cofactor: Binds 2 [4Fe-4S] clusters per monomer.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 32552
Sequence Length: 289
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.17.99.6
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Q8DLA9 | MVTAAAIKEFAHQLGFHRVGIVDLRTYTDDHPSGVAALQRWLAQGFQGEMAWMANPRRQKIQAVLPGAKSVISVALNYYQPDPQPPPKVKIARYAWGRDYHRVLGKRLQVLGQWLQSQVPEMDYRWYVDTGPVQDKVWAEQAGIGWIGKHSNVISRQYGSWILLGELITTLELTGDRPHTNHCGTCTRCLAACPTGAIVEPYVVDANRCIAYHTIESRAPELPAAIAAHLEGWVAGCDICQEVCPWNQRFAQPTDVEDFAARSPLLQTSLEELATLSDAAWDELTRGSALRRIKSAQWRRNAQAVLSSNPYD | Cofactor: Binds 2 [4Fe-4S] clusters per monomer.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 34870
Sequence Length: 312
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.17.99.6
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Q9KV16 | MDYQQLANQIKQWAIELGFEKVGICDVDLSEHEPALQAWLDAGYHGEMDWMARHGMMRARPAELLPGTLRVISARINYLPPQAQFASNLSDPNQAYISRYALGRDYHKLVRNQLKKLGEKIEQEVGKLGYRPFVDSAPILERPLAQKAGLGWTGKHSLILDKENGSWFFLGELLVDIPLPVDEPSENQCGKCTACITSCPTNAIVAEGVVDARRCVSYLTIEYSGVIPLEFRRAMGNRIYGCDDCQLVCPWNRFAPLTQQSDFHRRQSLNNADLVVLFEWDEATFLKNMEGSAIRRIGHQQWRRNLIIAMGNAPYSPRIIDTLQRHLGQSELLDEHIHWALEEQTQKTATPRQHARLIRIIEKGLPRDA | Cofactor: Binds 2 [4Fe-4S] clusters per monomer.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 42010
Sequence Length: 369
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.17.99.6
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Q6FAK7 | MSKPRIKLKLPDNADKLLLHSCCAPCSGEVMETLLYSGIDYSIFFYNPNIHPVKEYLIRKEENIRFAEKHNIPFIDCDYDTDNWFERAKGMENEPEKGIRCTMCFDMRFERAALYAYENGFKVFSSSLGISRWKNMEQINDCGIRAASHYPDIHYWDYNWRKNGGATRMLEISKREEFYQQEYCGCVYSLRDTNRWRMSQGRDRIQLGVKFYSASDPD | Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 25827
Sequence Length: 218
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
EC: 1.17.99.6
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Q3Z8V0 | MAPKLLLHGCCAHCTAYSFKYWQEQGFAVSVYWYNPNIHPFMEHQSRLEAMRKLSAEMGFELITEPSYHMAEYFKNVSANVDGRCRICFDMRLGQTAAYAAGHGYEYFSSSLFISPHQKHQDAVCSAEALAKETGVRFAYADLRKRYSDSRHITKPLDLYRQQYCGCVYSEYERFGKPNSPA | Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 20991
Sequence Length: 182
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
EC: 1.17.99.6
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Q9XWR6 | MTTMGEDEAPALPKKSPLPEKIDEADVDDDPDDKVIKIVVVGDGASGKTSICQRFAKESFDKSYHQTLGLDFFSRRITLPHEMQVLVQVWDIGGQSIAGEMIDKYLTGANIVFLVYDVTNSKSFENAVDWLSVVKKNTKSSETPVKLVLMGNKTDLEERRVVSVEAHKNFATSNDMMPTYVSAKTGDTVFLTFRQAVAEVLNVGLSRAEVEADIEIVQGSVIEQPKQSDASYARRSDQSRSTSVCSIT | Function: GTPase. Intraflagellar transport (IFT) cargo that undergoes bidirectional IFT along the ciliary axoneme when in active GTP-bound state in amphid and phasmid ciliated sensory neurons. Targeting and function as IFT cargo may depend on the BBSome, an IFT cargo adapter. Does not undergo IFT when in inactive GDP-bound state. May in turn play a role in cilium structure and/or function in ciliated sensory neurons.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27319
Sequence Length: 248
Subcellular Location: Cell projection
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Q90965 | MAYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRDTFNHLTTWLEDARQHSNSNMVIMLIGNKSDLESRREVKKEEGEAFAREHGLIFMETSAKTASNVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGPQHAATNATLAGNQGGQQAGGGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 23522
Sequence Length: 212
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
EC: 3.6.5.2
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P36409 | MYSFLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDNKAIKLQIWDTAGQESFRSITRSYYRGSAGALLVYDITRRDTFNHLTCWLKDARSYANSNMTIILIGNKSDMESKRAVSYEEGRQFADENGLIFLETSAKTASNVEEAFVNTASKIYEKIQKGDFDINNESFGIKLGAPTSKQDGTDQKPAGGGCCK | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 23093
Sequence Length: 207
Subcellular Location: Cell membrane
EC: 3.6.5.2
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P61019 | MAYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRDTFNHLTTWLEDARQHSNSNMVIMLIGNKSDLESRREVKKEEGEAFAREHGLIFMETSAKTASNVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGPQHAATNATHAGNQGGQQAGGGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. Required for protein transport from the endoplasmic reticulum to the Golgi complex. Regulates the compacted morphology of the Golgi.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 23546
Sequence Length: 212
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
EC: 3.6.5.2
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P49103 | MSYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDNKPIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRETFNHLASWLEDARQHANANMTIMLVGNKCDLSHRRAVSYEEGEQFAKEHGLIFMEASAKTAQNVEEAFVKTAGAIYKKIQDGVFDVSNESYGIKVGYVVPGQSGGAGSSSQGGGCCS | Function: Protein transport. Probably involved in vesicular traffic.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22988
Sequence Length: 209
Subcellular Location: Endoplasmic reticulum membrane
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P86207 | SCLLLQFTDKRFQPVHDLTIGVEFGARGAAGALLVYDITRRTASNVEEAFINTAKEIYEK | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. Required for protein transport from the endoplasmic reticulum to the Golgi complex. Regulates the compacted morphology of the Golgi.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 6689
Sequence Length: 60
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
EC: 3.6.5.2
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P53994 | MAYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRDTFNHLTTWLEDARQHSNSNMVIMLIGNKSDLESRREVKKEEGEAFAREHGLIFMETSAKTASNVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGPQHAATNASHGSNQGGQQAGGGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. Required for protein transport from the endoplasmic reticulum to the Golgi complex. Regulates the compacted morphology of the Golgi.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 23548
Sequence Length: 212
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
EC: 3.6.5.2
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Q01971 | MAYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRDTFNHLTTWLEDARQHSNSNMVIMLIGNKSDLESRREVKKEEGEAFAREHGLIFMETSAKTASNVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGPQHGATNATHAGNQGGQQAGGGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. Required for protein transport from the endoplasmic reticulum to the Golgi complex. Regulates the compacted morphology of the Golgi.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 23532
Sequence Length: 212
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
EC: 3.6.5.2
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Q8WUD1 | MTYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMVNIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRETFNHLTSWLEDARQHSSSNMVIMLIGNKSDLESRRDVKREEGEAFAREHGLIFMETSAKTACNVEEAFINTAKEIYRKIQQGLFDVHNEANGIKIGPQQSISTSVGPSASQRNSRDIGSNSGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. Regulates the compacted morphology of the Golgi (Probable). Promotes cytosolic DNA-induced innate immune responses. Regulates IFN responses against DNA viruses by regulating the CGAS-STING signaling axis (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 24214
Sequence Length: 216
Subcellular Location: Cell membrane
EC: 3.6.5.2
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P49104 | MSYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDNKPIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRETFNHLASWLEDARQHANANMTIMLVGNKCDLSHRRAVSYEEGEQFAKEHGLIFMEASAKTAQNVEEAFVKTAGAIYKKIQDGVFDVSNESYGIKVGYAIPGQSGGAGSSSSQGGGCCS | Function: Protein transport. Probably involved in vesicular traffic.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23061
Sequence Length: 210
Subcellular Location: Endoplasmic reticulum membrane
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Q9USX3 | MDNLDEDDLAFFSKPIKKPPLNYAKQLIASSSDSEEESELDTNKQALEHINAQKNITHNENKSAEPLSRQSTILDADEGNQDVSDTTPNACLNEGRHSPKSAISCVTQPVSPVYNTRAAANLRNNSINSEAALSTTSSLLDDDFARRLEEIDRQVQEFEKSSSDMDVQIHTHKREIEEDDDNTSADVPLLKHSKSDHSTLYHSKSEFSTNEPVISVVLQLAVIGQRIPNSNISLPRDWEAPLFFKVKSNQQFRRVRIAYSERKKVDNVVLVFQNQRLWDYGTPKGAGMLKVDTRLVVHAYCHSDFISLKRIKELEVEKLSSVTEDSTAQTCKLITLLLRSSKSEDLRLSIPVDFTVKDLIKRYCTEVKISFHERIRLEFEGEWLDPNDQVQSTELEDEDQVSVVLD | Function: Required for repair of DNA double strand breaks which occur during replication, or induced by UV or gamma radiation, via recombination between sister chromatids. This has a subsequent role in the maintenance of chromosome structure. May work in conjunction with the Smc5-Smc6 complex.
PTM: Phosphorylated by cds1.
Sequence Mass (Da): 46077
Sequence Length: 406
Subcellular Location: Nucleus
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Q99638 | MKCLVTGGNVKVLGKAVHSLSRIGDELYLEPLEDGLSLRTVNSSRSAYACFLFAPLFFQQYQAATPGQDLLRCKILMKSFLSVFRSLAMLEKTVEKCCISLNGRSSRLVVQLHCKFGVRKTHNLSFQDCESLQAVFDPASCPHMLRAPARVLGEAVLPFSPALAEVTLGIGRGRRVILRSYHEEEADSTAKAMVTEMCLGEEDFQQLQAQEGVAITFCLKEFRGLLSFAESANLNLSIHFDAPGRPAIFTIKDSLLDGHFVLATLSDTDSHSQDLGSPERHQPVPQLQAHSTPHPDDFANDDIDSYMIAMETTIGNEGSRVLPSISLSPGPQPPKSPGPHSEEEDEAEPSTVPGTPPPKKFRSLFFGSILAPVRSPQGPSPVLAEDSEGEG | Function: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.
PTM: Constitutively phosphorylated on serine and threonine amino acids in absence of DNA damage. Hyperphosphorylated by PRKCD and ABL1 upon DNA damage. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 42547
Sequence Length: 391
Subcellular Location: Nucleus
EC: 3.1.11.2
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Q9Z0F6 | MKCLITGGNVKVLGKAVHSLSRIGDELYLEPLKDGLSLRTVNSSRSAYACFLFAPLFFQQYQAASPGQDLLRCKILMKAFLSVFRSLAIVEKSVEKCCISLSGSHSHLVVQLHCKYGVKKTHNLSFQDCESLQAVFDPASCPHLLRTPARVLAEAVLSFPLALTEVTLGIGRGRRVILRSYQEEEADSTSKAMVTETSIGDEDFQQLHAPEGIAVTFCLKEFRGLLSFAESANLPLTIHFDVPGRPVIFTIEDSLLDAHFVLATLLEQDSCSQGPCSPKPHQPVPQKQAHSTPHLDDFTSDDIDCYMIAMETTGGNEGSGAQPSTSLPPVSLASHDLAPTSEEEAEPSTVPGTPPPKKFRSLFFGSILAPVHSPQGPNPVLAEDSDGEG | Function: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity (By similarity).
PTM: Constitutively phosphorylated on serine and threonine amino acids in absence of DNA damage. Hyperphosphorylated by PRKCD and ABL1 upon DNA damage. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex (By similarity).
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 42059
Sequence Length: 389
Subcellular Location: Nucleus
EC: 3.1.11.2
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O66827 | MGKNKTAYVCQECGYKSVKWLGKCPSCGEWNTLVEEFEPQSFSLVKKEPSLVLPVTDWEKEEHERETTGFESLDNALGGGLVKGQVILIAGEPGIGKSTLLLQISDRVANGKKVLYVSGEESGTQIALRAKRLGINNENLLVYPEVNLEKILQTLEKEKPSLLVLDSVQTIFSERLESSAGSVSQVREVTYRITEFCKEKNVPAFIVGQITKEGSIAGPKVLEHIVDTVLQFEGERFNFYRIVKVIKNRFGSTGEIAVFKMTDKGLEEVPEPSAFFISEKANAPGSVVFPHTEGSKPVLLEVQALVIPALYTTPQRRTQGFDPNRLALILAVLEKEAKIFTRDQDVFVNVAGGMSVKEPAADLAVAMAVVSSKKEKEVPKDFVIFGEVGLSGEIRAVHFGDLRLKEAKRFGFKKALIPKSLEIEIDGMEIYPVSHIQEAIEVLF | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
Sequence Mass (Da): 49048
Sequence Length: 444
Domain: Has a putative N-terminal zinc-finger, a middle region with homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease.
EC: 3.6.4.-
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P37572 | MAKTKSKFICQSCGYESPKWMGKCPGCGAWNTMVEEMIKKAPANRRAAFSHSVQTVQKPSPITSIETSEEPRVKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNPSLHVLSETDMEYISSAIQEMNPSFVVVDSIQTVYQSDITSAPGSVSQVRECTAELMKIAKTKGIPIFIVGHVTKEGSIAGPRLLEHMVDTVLYFEGERHHTFRILRAVKNRFGSTNEMGIFEMREEGLTEVLNPSEIFLEERSAGSAGSSITASMEGTRPILVEIQALISPTSFGNPRRMATGIDHNRVSLLMAVLEKRVGLLLQNQDAYLKVAGGVKLDEPAIDLAIVISIASSFRDTPPNPADCFIGEVGLTGEVRRVSRIEQRVKEAAKLGFKRMIIPAANLDGWTKPKGIEVIGVANVAEALRTSLGG | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
Sequence Mass (Da): 49483
Sequence Length: 458
Domain: Has a putative N-terminal zinc-finger, a middle region with homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease.
EC: 3.6.4.-
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Q9SN68 | MAAAGNKSINAKLVLLGDVGAGKSSLVLRFVKDQFVEFQESTIGAAFFSQTLAVNDATVKFEIWDTAGQERYHSLAPMYYRGAAAAIIVFDVTNQASFERAKKWVQELQAQGNPNMVMALAGNKSDLLDARKVTAEDAQTYAQENGLFFMETSAKTATNVKEIFYEIARRLPRVQPTENPTGMVLPDRAMDRAVSSSCCA | Function: Endosomal protein that may be involved in endocytosis . Involved in the trafficking of proteins from prevacuolar compartments (PVCs) to vacuoles . May activate the MON1-CCZ1 complex which acts as guanine nucleotide exchange factors (GEF) for Rab7 protein family, and serves as a link between Rab5 and Rab7 families in PVCs, and mediates PVC maturation . Involved in vacuolar transport of storage proteins with EREX as effector. Regulates membrane trafficking to protein storage vacuoles (PSVs) .
Location Topology: Lipid-anchor
Sequence Mass (Da): 21873
Sequence Length: 200
Subcellular Location: Early endosome membrane
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Q9SR19 | MFSLKSLISSPFTQSTTHGLFTNPITRPVNPLPRTVSFTVTASMIPKRSSANMIPKNPPARQQLYQPFRPPSSPIPTQFRSLDSAGKIEILAGRMALWFEYAPLISSLYTDGFTPPTIEELTGISSIEQNRLIVGAQVRDSILQSIHEPELISAFDTGGAELLYEIRLLSTTQRVAAATFIIDRNIDSKGAQDLARAIKDYPNRRGDVGWLDFDYNLPGDCLSFLYYRQSRENKNPSDQRTSMLLQALGVAESEKAKNRLNTELYGDKEAEKEKEKKKKEEEVKAIRIPVVRLKFGEVAEATSVVVLPVCKAEEGEKKILEAPMEIIAGGDFKVVEAEKGWKRWVVLPSWNPVAAIGKGGVAVSFRDDRKVLPWDGKEEPLLVVADRVRNVVEADDGYYLVVAENGLKLEKGSDLKAREVKESLGMVVLVVRPPREDDDDWQTSHQNWD | Function: Required for assembly or stability of RuBisCO. Acts at a postchaperonin step to fold and/or assemble the large subunit (rbcL) into RuBisCO. RAF1 brackets an rbcL dimer (rbcL(2)), leading to rbcL(8)-RAF1(4) complex formation. In the next step, RBCS displaces RAF1, thus resulting in holoenzyme formation.
Sequence Mass (Da): 50199
Sequence Length: 449
Domain: Has 3 domains, the N-terminal alpha-helical domain, an extended flexible linker and the C-terminal beta-sheet domain. The N-terminal alpha-helical domain stabilizes RbcL dimers and RbcL dimer-dimer interactions, facilitating RbcL(8) formation . The C-terminal beta-sheet domain probably dimerizes Raf1 (Probable). The 2 C-terminal beta-sheet domains are swapped and pack against each other to form the dimer interface (By similarity).
Subcellular Location: Plastid
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P16552 | MNSASTHKNTDFWIFGLFFFLYFFIMATCFPFLPVWLSDVVGLSKTDTGIVFSCLSLFAISFQPLLGVISDRLGLKKNLIWSISLLLVFFAPFFLYVFAPLLHLNIWAGALTGGVFIGFVFSAGAGAIEAYIERVSRSSGFEYGKARMFGCLGWALCATMAGILFNVDPSLVFWMGSGGALLLLLLLYLARPSTSQTAMVMNALGANSSLISTRMVFSLFRMRQMWMFVLYTIGVACVYDVFDQQFAIFFRSFFDTPQAGIKAFGFATTAGEICNAIIMFCTPWIINRIGAKNTLLVAGGIMTIRITGSAFATTMTEVVILKMLHALEVPFLLVGAFKYITGVFDTRLSATVYLIGFQFSKQLAAILLSTFAGHLYDRMGFQNTYFVLGMIVLTVTVISAFTLSSSPGIVHPSVEKAPVAHSEIN | Function: Responsible for transport of raffinose into the cell . Can also transport lactose and melibiose . Has weak activity with maltose .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46693
Sequence Length: 425
Subcellular Location: Cell inner membrane
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P16553 | MKQRLSLAQSALEKLSARRGNTWYPIFHLAPPAGWMNDPNGLIYFNGRYHAFFQHHPASAYQGPMHWGHATSTDMLHWQHELVALAPGDKYDRDGCFSGSAVDDDGVLSLIYTGHICLEDRGNDSIIREVQCLATSHDGIRFEKQGCVLTPPEGIMHFRDPKVWHEDGSWWMVIGARDASDNGQVLLYRGTSLRDWHLEHVLAHSAAGESYMWECPDFFRCGNFHWLMFSPQGMNPSGYRFRNLFQSGVLAGNWKPGSVFALKGVFEELDYGHDFYAPQSMLAEDGRRIIMAWMNMWDSPVPTRSEAWAGCLTLPREVFERDGRLCQRPVREVESLRRKCQPLSPVRLHGVQLLTENVQAAELLVTWHTVDSHAEHYGIRLGEGLRFYVDNQAGRLILWRYYPEEGLDGYRSVELPDTEYLTLRIFLDRSSVEVFVNDGEATLSSRIYPQADSRQLSLYAAHGDAILTDGTLWMLT | Function: May prevent the potential hasard of excessive sucrose accumulation.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 54327
Sequence Length: 476
EC: 3.2.1.26
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Q90523 | RSTFPTRECPELLCQYSCNSQRFAELLRTEFKHRYEGKITNYLHKTLAHVPEIIERDGSIGAWASEGNESGNKLFRRFRKMNARQSKSYELEGILKHHWLYTSKYL | Cofactor: Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+).
Function: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. In addition to its endonuclease activity, RAG1 also acts as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3. Histone H3 monoubiquitination is required for the joining step of V(D)J recombination (By similarity).
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 12598
Sequence Length: 106
Subcellular Location: Nucleus
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Q01883 | MASNKVVFSVLLLVVLSVLAAAMATMADHHQVYSPGEQCRPGISYPTYSLPQCRTLVRRQCVGRGAASAADEQVWQDCCRQLAAVDDGWCRCGALDHMLSGIYRELGATEAGHPMAEVFPGCRRGDLERAAASLPAFCNVDIPNGPGGVCYWLGYPRTPRTGH | Function: Seed storage protein.
PTM: Five disulfide bonds are present.
Sequence Mass (Da): 17568
Sequence Length: 163
Subcellular Location: Secreted
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P10114 | MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDLESEREVSSSEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSACNIQ | Function: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading.
PTM: Ubiquitinated; undergoes 'Lys-63' monoubiquitination and diubiquitination by NEDD4. Multiple lysine residues are probably modified. Ubiquitination requires TNIK, prevents interaction with effectors and inactivates RAP2A.
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 20615
Sequence Length: 183
Domain: The effector domain mediates the interaction with RUNDC3A.
Subcellular Location: Recycling endosome membrane
EC: 3.6.5.2
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Q80ZJ1 | MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDLESEREVSSNEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSACNIQ | Function: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading.
PTM: Ubiquitinated; undergoes 'Lys-63' monoubiquitination and diubiquitination by NEDD4. Multiple lysine residues are probably modified. Ubiquitination requires TNIK, prevents interaction with effectors and inactivates RAP2A.
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 20642
Sequence Length: 183
Domain: The effector domain mediates the interaction with RUNDC3A.
Subcellular Location: Midbody
EC: 3.6.5.2
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P61225 | MREYKVVVLGSGGVGKSALTVQFVTGSFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYERVPMILVGNKVDLEGEREVSYGEGKALAEEWSCPFMETSAKNKASVDELFAEIVRQMNYAAQPNGDEGCCSACVIL | Function: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells.
PTM: Palmitoylated. Unlike RAP2A and RAP2C, palmitoylation of RAP2B is not required for association with recycling endosome membranes and activation of TNIK.
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 20504
Sequence Length: 183
Domain: The effector domain mediates the interaction with RUNDC3A.
Subcellular Location: Recycling endosome membrane
EC: 3.6.5.2
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Q9Y3L5 | MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIVRVKRYEKVPLILVGNKVDLEPEREVMSSEGRALAQEWGCPFMETSAKSKSMVDELFAEIVRQMNYSSLPEKQDQCCTTCVVQ | Function: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May play a role in SRE-mediated gene transcription.
PTM: Palmitoylated. Palmitoylation is required for association with recycling endosome membranes and activation of TNIK.
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 20745
Sequence Length: 183
Subcellular Location: Cytoplasm
EC: 3.6.5.2
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G4MWB1 | MYIPSARTAIVQDDKGGLKIDRNAPMPQPRPNELLVQVKAVAINPCDHKMYERFPTPGAVDGCDFAGIVVQLGSDVKTFQIGDRVCGAVHGSNPSRPESGTFAEYTVSDGEFTLKLPPNLSFREAMGLGTTGLSTIGMAIYKGLMLPGSPLEPAEKPRTVLVHGASSSVGTMALQLIRLMGHIPIATCSPRNFELVKKYGAEEVFDYNDPECGQQIKQYTGNTLAYIIDPFTDVKSVALCYEAMGRAGGRYACLEMYPEFALERRSIKVFFALGMALLGHSLDLAYGYERDEDPEMRSFGIGWYKVLQELLYQGKLRPHPLRELEGGFEGILKGVQMVKNKEVSGQKLVVSLE | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars . The first step in the pathway is catalyzed by the hybrid PKS-NRPS ACE1, assisted by the enoyl reductase RAP1, that are responsible for fusion of the tyrosine precursor and the polyketide backbone . The polyketide synthase module (PKS) of ACE1 is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the tyrosine precursor . Because ACE1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase RAP1 . Reduction by the hydrolyase ORFZ, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ORF3 then yield the required isoindolone-fused macrocycle (Probable). A number of oxidative steps catalyzed by the tailoring enzymes identified within the cluster, including cytochrome P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the short-chain dehydrogenase/reductase OXR1, are further required to afford the final cytochalasans that confer avirulence and which have still to be identified (Probable). The monooxygenase CYP1 has been shown to be a site-selective C-18 hydroxylase whereas the function of CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is present in some intermediate compounds . Finally, SYN2 and RAP2 are not required for avirulence in Pi33 resistant rice cultivars .
Sequence Mass (Da): 38724
Sequence Length: 353
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q9J589 | MENKESVLLELVPKIKAYIKDDTVKEKSYQDFIEKNKELFICNLYNVNMITDEDIKLLYITIEQNIDIDDKSLVAIFSYIGYNFEKNIHDDNSSIDLGDRMTGDMNYNMYDTFFSTLDFIIRQKHVNILVNDEGNNDFNINYRSFTTSLSYKEDKYEQVVNEIPFNMKELLSYVSKNLDQLRFSKKYLDFAYLCRNIGIKISKRKYNVRYIFNYVIDELTIPIVIKDYLDVKYVYLEETNKAYRNNFDNDNKYFYEWGKVIIPKFKNPRLYSYFFLSNYGLCDLFMELINIKQVTFEPRKNPIEYIYVSELKFWEEGGSVDFVPCEHEIAIIDAKKVSLEYYENINKFIAKYIYYEDGLAYCNLCGINIQELNLDATDVTKISLINVTYNKSIFMSEPYNYFSHSQRFIFNTIMSFDTIMKSQMWNMKYNINRLILNFLIDINSKRHEYEKQFATEIKKGIFFLRLSANLFDIQMSSMELFYSAKILNIHFIVALVIVLNSGADFIMYYMTNKKEETNYSDLNHIISVIVFDFLKKTRTVDSKQFNTIELFTETYMKIATEELIVHYNRIKLEMERLIAIKKDRKTPNYDISIYRQIQRTDEIAFFPSCITSTKLFITYEKVVAENTEIITIKHPVRIKEGTDEDKEIFEDIMKKTTKVLIRVNDTNAYNASFFTTHIKLEVEKKKIIIPLTSLFVYNVLKYYSSNVDFYVFKFGDPFPFHYDLISQEHTNHKITGYNMLRQELLPNSNVFTYFSDSLNRQELEFSFYMFLASYVNVTEWIEENSKKIKELYIINFNN | Function: DNA-directed RNA polymerase-associated factor required for the transcription of viral early genes as well as for transcription termination. Within minutes after virus entry, recruits the core RNA polymerase, the early transcription factor (ETF) and other enzymes needed for transcription initiation, elongation, and termination thereby allowing synthesis of early mRNAs which are extruded through pores in the core particle. Recruits the multifunctional J3 protein, with poly(A) polymerase-stimulatory, cap nucleoside-2'-O-methyltransferase, and transcription elongation activities. Interacts with NPH-I, a DNA-dependent ATPase required for the termination of early transcripts. Acts as a transcription termination factor by binding, together with the capping enzyme/VTF, to the termination motif 5'-UUUUUNU-3' in the nascent mRNA. Involved as well in the packaging of RNA polymerase and other components needed for early transcription in assembling virus particles (By similarity).
Sequence Mass (Da): 95221
Sequence Length: 798
Domain: Interacts with ETF via its N-terminus and with DNA-directed RNA polymerase via its C-terminus.
Subcellular Location: Virion
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P01117 | MTEYKLVVVGASGVGKSALTIQLIQNHFVDEYDPTIQDSYRKQVVIDGETCLLDILDTTGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQLKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQELARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCVIM | Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 21715
Sequence Length: 189
Subcellular Location: Host cell membrane
EC: 3.6.5.2
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O43374 | MAKRSSLYIRIVEGKNLPAKDITGSSDPYCIVKVDNEPIIRTATVWKTLCPFWGEEYQVHLPPTFHAVAFYVMDEDALSRDDVIGKVCLTRDTIASHPKGFSGWAHLTEVDPDEEVQGEIHLRLEVWPGARACRLRCSVLEARDLAPKDRNGTSDPFVRVRYKGRTRETSIVKKSCYPRWNETFEFELQEGAMEALCVEAWDWDLVSRNDFLGKVVIDVQRLRVVQQEEGWFRLQPDQSKSRRHDEGNLGSLQLEVRLRDETVLPSSYYQPLVHLLCHEVKLGMQGPGQLIPLIEETTSTECRQDVATNLLKLFLGQGLAKDFLDLLFQLELSRTSETNTLFRSNSLASKSMESFLKVAGMQYLHGVLGPIINKVFEEKKYVELDPSKVEVKDVGCSGLHRPQTEAEVLEQSAQTLRAHLGALLSALSRSVRACPAVVRATFRQLFRRVRERFPGAQHENVPFIAVTSFLCLRFFSPAIMSPKLFHLRERHADARTSRTLLLLAKAVQNVGNMDTPASRAKEAWMEPLQPTVRQGVAQLKDFITKLVDIEEKDELDLQRTLSLQAPPVKEGPLFIHRTKGKGPLMSSSFKKLYFSLTTEALSFAKTPSSKKSALIKLANIRAAEKVEEKSFGGSHVMQVIYTDDAGRPQTAYLQCKCVNELNQWLSALRKVSINNTGLLGSYHPGVFRGDKWSCCHQKEKTGQGCDKTRSRVTLQEWNDPLDHDLEAQLIYRHLLGVEAMLWERHRELSGGAEAGTVPTSPGKVPEDSLARLLRVLQDLREAHSSSPAGSPPSEPNCLLELQT | Cofactor: Binds 3 Ca(2+) ions per C2 domain.
Function: Ca(2+)-dependent Ras GTPase-activating protein, that switches off the Ras-MAPK pathway following a stimulus that elevates intracellular calcium. Functions as an adaptor for Cdc42 and Rac1 during FcR-mediated phagocytosis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 90458
Sequence Length: 803
Domain: The PH domain does not bind phosphatidylinositol 4,5-bisphosphate or phosphatidylinositol 3,4,5-trisphosphate. This lack of binding activity is due to Leu-592, compared to Arg found in other family members.
Subcellular Location: Cytoplasm
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O42785 | MASKFLREYKLVVVGGGGVGKSCLTIQLIQSHFVDEYDPTIEDSYRKQCVIDEEVALLDVLDTAGQEEYSAMREQYMRTGEGFLLVYSITSRQSFEEITTFQQQILRVKDKDYFPMVVVGNKCDLEGEREVTRQEGEALAKSFGCKFIETSAKSRINVDKAFYDIVREIRRYNREMQGYSTGSGGASGINGPPKPMDVENGEQEAGCCSKCLIM | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 24060
Sequence Length: 214
Subcellular Location: Cell membrane
EC: 3.6.5.2
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O14807 | MATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTAGQEEFSAMREQYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHDLVRVIRQQIPEKSQKKKKKTKWRGDRATGTHKLQCVIL | Function: Serves as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Activates the MAP kinase pathway.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 23846
Sequence Length: 208
Subcellular Location: Cell membrane
EC: 3.6.5.2
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O08989 | MATSAVPSENLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTAGQEEFSAMREQYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVDLMHLRKVTRDQGKEMATKYNIPYIETSAKDPPLNVDKTFHDLVRVIRQQVPEKNQKKKKKTKWRGDRATGTHKLQCVIL | Function: Serves as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Activates the MAP kinase pathway (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 23901
Sequence Length: 208
Subcellular Location: Cell membrane
EC: 3.6.5.2
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Q9XI84 | MSASVAVVSGFLRIPSIQKSQNPSFLFSRPKKSLVRPISASSSELPENVRNFWKWLRDQGVVSGKSVAEPAVVPEGLGLVARRDIGRNEVVLEIPKRLWINPETVTASKIGPLCGGLKPWVSVALFLIREKYEEESSWRVYLDMLPQSTDSTVFWSEEELAELKGTQLLSTTLGVKEYVENEFLKLEQEILLPNKDLFSSRITLDDFIWAFGILKSRAFSRLRGQNLVLIPLADLINHNPAIKTEDYAYEIKGAGLFSRDLLFSLKSPVYVKAGEQVYIQYDLNKSNAELALDYGFVESNPKRNSYTLTIEIPESDPFFGDKLDIAESNKMGETGYFDIVDGQTLPAGMLQYLRLVALGGPDAFLLESIFNNTIWGHLELPVSRTNEELICRVVRDACKSALSGFDTTIEEDEKLLDKGKLEPRLEMALKIRIGEKRVLQQIDQIFKDRELELDILEYYQERRLKDLGLVGEQGDIIFWETK | Function: Protein-lysine methyltransferase methylating chloroplastic fructose 1,6-bisphosphate aldolases. Can also use with low efficiency gamma-tocopherol methyltransferase as substrate, but not a cytosolic aldolase. Able to interact with unmethylated Rubisco, but unlike in pea, the complex is catalytically unproductive.
Catalytic Activity: [fructose-bisphosphate aldolase]-L-lysine + 3 S-adenosyl-L-methionine = [fructose-bisphosphate aldolase]-N(6),N(6),N(6)-trimethyl-L-lysine + 3 H(+) + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 54612
Sequence Length: 482
Subcellular Location: Plastid
EC: 2.1.1.259
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Q43088 | MATIFSGGSVSPFLFHTNKGTSFTPKAPILHLKRSFSAKSVASVGTEPSLSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQVPKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFGILPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILPNKRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGVTTEDHAYEVKGAAGLFSWDYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALDYGFIEPNENRHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNRTLPPGLLPYLRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKAVREACKSALAGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDGIFEQKELELDQLEYYQERRLKDLGLCGENGDILGDLGKFF | Function: Methylates 'Lys-14' of the large subunit of RuBisCO. Can also use with lower efficiency chloroplastic fructose-bisphosphate aldolases and gamma-tocopherol methyltransferase as substrates, but not a cytosolic aldolase.
Catalytic Activity: L-lysyl-[ribulose-1,5-bisphosphate carboxylase] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[ribulose-1,5-bisphosphate carboxylase] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 55110
Sequence Length: 489
Subcellular Location: Plastid
EC: 2.1.1.127
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P31181 | MSPQTETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAV | Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity).
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
Sequence Mass (Da): 6152
Sequence Length: 57
Subcellular Location: Plastid
EC: 4.1.1.39
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Q29RT0 | MVEADRPGKLFIGGLNLETDEKSLEATFGKYGRISEVLLMKDRETNKSRGFAFITFESPADAKAAVRDMNGKSLDGKAIKVAQATKPAFESGRRGPPLSRSRGRSRGLRGARGGGPRRPPSRGGPADDGGYAGDFDLRPSRAPLPMKRGPPPPRRAGPPPKRAAPSGPARSGSGGGMRGRAPAARGRDGYEGPPRRDPPPPRRDPYLGSREGGYSPRDGYSSRDYSSARDARDFAPSPREYTYRDYGHSSARDECPSRGYGDRDGYGGRDRDYADHPSGGSYRDPFESYGDPRSAAPARGPPPSYGGGGGRYEEYRGCSPDAYGGGRDGYAGGRSERYSGGRDRVGRADRGLPQSVERGCPPPRESYSRSGRKVPRGGGRLGSRSERGGGGGRSRY | Function: RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment (By similarity).
PTM: O-glycosylated.
Sequence Mass (Da): 42369
Sequence Length: 396
Domain: The RRM domain is necessary for RNA-binding, but not for splice site selection, indicating that its splicing activity does not require direct binding to RNA.
Subcellular Location: Nucleus
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P38159 | MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGRGGSGGTRGPPSRGGHMDDGGYSMNFNMSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGMGGRAPVSRGRDSYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSRDYPSSRDTRDYAPPPRDYTYRDYGHSSSRDDYPSRGYSDRDGYGRDRDYSDHPSGGSYRDSYESYGNSRSAPPTRGPPPSYGGSSRYDDYSSSRDGYGGSRDSYSSSRSDLYSSGRDRVGRQERGLPPSMERGYPPPRDSYSSSSRGAPRGGGRGGSRSDRGGGRSRY | Function: RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment.
PTM: O-glycosylated.
Sequence Mass (Da): 42332
Sequence Length: 391
Domain: The RRM domain is necessary for RNA-binding, but not for splice site selection, indicating that its splicing activity does not require direct binding to RNA.
Subcellular Location: Nucleus
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Q4R7F0 | MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGRGGSGGTRGPPSRGGHMDDGGYSMNFNMSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGMGGRAPVSRGRDSYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSRDYPSSRDTRDYAPPPRDYTYRDYGHSSSRDDYPSRGYSDRDGYGRDRDYSDHPSGGSYRDSYESYGNSRSAPPTRGPPPSYGGSSRYDDYSSSRDGYGGSRDSYSSSRSDLYSSGRDRVGRQDRGLPPSMERGYPPPRDSYSSSSRGAPRGGGRGGSRSDRGGGRSRY | Function: RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment (By similarity).
PTM: O-glycosylated.
Sequence Mass (Da): 42318
Sequence Length: 391
Domain: The RRM domain is necessary for RNA-binding, but not for splice site selection, indicating that its splicing activity does not require direct binding to RNA.
Subcellular Location: Nucleus
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Q9WV02 | MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGLPPPPRSRGPPRGLRGGRGGSGGTRGPPSRGGHMDDGGYSMNFTMSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGLGGRAPVSRGRDGYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSREYPSSRDTRDYAPPPRDYTYRDYGHSSSRDDYPSRGYSDRDGYGRDRDYSDHPSGGSYRDSYESYGNSRSAPPTRGPPPSYGGSSRYDDYSSSRDGYGGSRDSYSSSRSDLYSSGRDRVGRQERGLPPSMERGYPPPRDSYSSSSRGAPRGGGRGGSRSDRGGGRSRY | Function: RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment.
PTM: O-glycosylated.
Sequence Mass (Da): 42301
Sequence Length: 391
Domain: The RRM domain is necessary for RNA-binding, but not for splice site selection, indicating that its splicing activity does not require direct binding to RNA.
Subcellular Location: Nucleus
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Q9H1K0 | MASLDDPGEVREGFLCPLCLKDLQSFYQLHSHYEEEHSGEDRDVKGQIKSLVQKAKKAKDRLLKREGDDRAESGTQGYESFSYGGVDPYMWEPQELGAVRSHLSDFKKHRAARIDHYVVEVNKLIIRLEKLTAFDRTNTESAKIRAIEKSVVPWVNDQDVPFCPDCGNKFSIRNRRHHCRLCGSIMCKKCMELISLPLANKLTSASKESLSTHTSPSQSPNSVHGSRRGSISSMSSVSSVLDEKDDDRIRCCTHCKDTLLKREQQIDEKEHTPDIVKLYEKLRLCMEKVDQKAPEYIRMAASLNAGETTYSLEHASDLRVEVQKVYELIDALSKKILTLGLNQDPPPHPSNLRLQRMIRYSATLFVQEKLLGLMSLPTKEQFEELKKKRKEEMERKRAVERQAALESQRRLEERQSGLASRAANGEVASLRRGPAPLRKAEGWLPLSGGQGQSEDSDPLLQQIHNITSFIRQAKAAGRMDEVRTLQENLRQLQDEYDQQQTEKAIELSRRQAEEEDLQREQLQMLRERELEREREQFRVASLHTRTRSLDFREIGPFQLEPSREPRTHLAYALDLGSSPVPSSTAPKTPSLSSTQPTRVWSGPPAVGQERLPQSSMPQQHEGPSLNPFDEEDLSSPMEEATTGPPAAGVSLDPSARILKEYNPFEEEDEEEEAVAGNPFIQPDSPAPNPFSEEDEHPQQRLSSPLVPGNPFEEPTCINPFEMDSDSGPEAEEPIEEELLLQQIDNIKAYIFDAKQCGRLDEVEVLTENLRELKHTLAKQKGGTD | Function: Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3) . Plays a role in the recycling of transferrin receptor to the plasma membrane .
Location Topology: Lipid-anchor
Sequence Mass (Da): 88870
Sequence Length: 784
Subcellular Location: Cell membrane
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Q88J90 | MSTPVLELRGIVKTFGATRALDGASLRVAAGSVHGLVGENGAGKSTLIKVLAGIHRPDAGSLLLDGQPHGHFSPRQVERLGIGFIHQERLLPARFTVGEALFFGHERRFGPLLDRRSQQREAARLLDDYFGLRLPANALIGELSSAEQQMVQIVRALLIKPRVLVFDEPSVALVQREVERLLRIVQRLRDDGLAIVYISHYLQEIEALCDRVTVLRNGRDVAEVSPRNTSLEQITRLMVNREVGELYPKVAVPAGALLLDVRGLGRARAYQGIDLQVRRGEIVGLTGLVGSGAKELLRSLFGLAPPDSGEVRLDGQPLSLRSPREAVAQGVALMPEERRRQGVALDLSVQENTTLAALSRFVRLGLLSPARERHTTLELIERLRIKAHGAHAKVRQLSGGNQQKVALAKWFARCSSLYLLDEPSVGIDVGAKVEIYRLIGELVKEGAGVLILSSDLPELIGLCDRIHVMHRGAIAARFAAGEANSDRLLAVATGAQRAQNEERPFYAYAIAI | Function: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55901
Sequence Length: 512
Subcellular Location: Cell inner membrane
EC: 7.5.2.7
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Q7UU57 | MIVSDDVVFEAKQISKLFPGVKALDGVDLTLRAGRLTTLLGENGAGKSTLMKILAGVQPPDEGELLVQGEPVHFTSPRDAQDHGIAMIHQELSLVPDLTVAENIFLGREPLRFETLIDYTELNRQANEWLKRLELDVSPTTPVRRLRVGQQQLVEIARALAGNVRILIMDEPTSAITERETEVLFRCIADLKKQGVAIVYITHRLEELEQIADDIVVMRDGCLIGTAEFGELSHDAMVRMMVGRDVKILSKQSSSNNQPVLRAEGISLSHPTRPGDYLVHEVDMHVCKGEVLGIFGLMGAGRTELLECLFGLHPTASTGQVSMHDRSVRLRNPADAISHGLALVPEDRKQDGLVLSMSVGENASLASLKHAERFGFIDRGREREHTRRFVERFRVKTPSLREKIINLSGGNQQKVILAKWLATGPAVLMLDEPTRGIDIHAKNEIYSLINELTADGLAVIMVSSELPEVMAVSDRILVMCEGRATQSFDRSEATEENILQAALPRRNSIPC | Function: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56466
Sequence Length: 511
Subcellular Location: Cell inner membrane
EC: 7.5.2.7
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Q0S9A4 | MSVPPAVPLLEVRDVTKSFGNVAAVQGVSFPLYGGEAHALVGENGAGKSTIVKMLAGVHGPDTGSLLVGGEEVSLGSPSDAKARGIAVIYQEPTLFPDLTIAENIFIGTQPRARLGMIDRSAMNTAARALFDRLGVPMDPDRLASGLSIADQQLVEIAKALSTDANVIVMDEPTAALSGNEVERLFKVARSLCASGSAVMFISHRFEEIFALCQRVTVMRDGRHISTSELAGLTVDDLVRSMVGRDLGALFPKIDVEPGAVVLEIENLSRAGVFSDISFQVRAGEIVALSGLVGAGRSEVMQSAFGVDPRDSGDVRVRGKSLRKGSPKAAMRAGMALVPEDRRQQGLILDMSIERNATLTRSSALARFGFLFGGRERRSAYEWTKKLQTKYARITDPVGVLSGGNQQKVVLAKWMATAPSVLIVDEPTRGIDVGTKAEVHRIISTLASEGVAVVMISSELPEVLGMADRVLVMREGRIVSELSRSEADEEKIMFAATGSEAAA | Function: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53472
Sequence Length: 503
Subcellular Location: Cell membrane
EC: 7.5.2.7
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Q57HW1 | MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETDSLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMMVGRKLEDQYPHLDNAPGEIRLKVDNLCGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALDYFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEVLMAAAVGKLNRVNQE | Function: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55084
Sequence Length: 501
Subcellular Location: Cell inner membrane
EC: 7.5.2.7
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Q9RDH8 | MKKAGILNRHLAGALAELGHGDGVLVCDAGMPVPDGPRVVDLAFRAGVPSFAEVVDGLLAELVVEGATAATEVREANAECAALLDGLFPALALVPHERLKELSAGARLIVRTGEARPYANVLLRCGVFF | Function: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Catalytic Activity: beta-D-ribopyranose = beta-D-ribofuranose
Sequence Mass (Da): 13398
Sequence Length: 129
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.4.99.62
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Q67RD6 | MKKTTLLNQALSEVVAGMGHGDLLVIGDYGLPCPKGVRRIDLALRPGIPAFLDVVETILAELQVEAAVVARETAERNPAVQEGLTRLLGGVPVTTVSHEELKEISARAVALVRTGECTPYANVILRAGVTF | Function: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Catalytic Activity: beta-D-ribopyranose = beta-D-ribofuranose
Sequence Mass (Da): 13898
Sequence Length: 131
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.4.99.62
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P06400 | MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK | Function: Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle . The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes . Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription . Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase . RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C . Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity).
PTM: Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-567 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. SV40 large T antigen, HPV E7 and adenovirus E1A bind to the underphosphorylated, active form of pRb. Phosphorylation at Thr-821 and Thr-826 promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes. Dephosphorylated at Ser-795 by calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-807 and Ser-811 is required for G0-G1 transition. Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis.
Sequence Mass (Da): 106159
Sequence Length: 928
Domain: The Pocket domain binds to the threonine-phosphorylated domain C, thereby preventing interaction with heterodimeric E2F/DP transcription factor complexes.
Subcellular Location: Nucleus
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P13405 | MPPKAPRRAAAAEPPPPPPPPPREDDPAQDSGPEELPLARLEFEEIEEPEFIALCQKLKVPDHVRERAWLTWEKVSSVDGILEGYIQKKKELWGICIFIAAVDLDEMPFTFTELQKSIETSVYKFFDLLKEIDTSTKVDNAMSRLLKKYNVLCALYSKLERTCELIYLTQPSSALSTEINSMLVLKISWITFLLAKGEVLQMEDDLVISFQLMLCVVDYFIKFSPPALLREPYKTAAIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFINSLGIVSSNGLPEVESLSKRYEEVYLKNKDLDARLFLDHDKTLQTDPIDSFETERTPRKNNPDEEANVVTPHTPVRTVMNTIQQLMVILNSASDQPSENLISYFNNCTVNPKENILKRVKDVGHIFKEKFANAVGQGCVDIGVQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTLQHLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKVEANLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDGEGPDNLEPACPLSLPLQGNHTAADMYLSPLRSPKKRTSTTRVNSAANTETQAASAFHTQKPLKSTSLALFYKKVYRLAYLRLNTLCARLLSDHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAAQETFKRVLIREEEFDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFSSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGGNPPKPLKKLRFDIEGADEADGSKHLPAESKFQQKLAEMTSTRTRMQKQRMNESKDVSNKEEK | Function: Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle . The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes. Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription. Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase. RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation . Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation . Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity) .
PTM: Phosphorylated . Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-561 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. Phosphorylation of threonine residues in domain C promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes. Dephosphorylated at Ser-788 by calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-800 and Ser-804 is required for G0-G1 transition (By similarity). Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis (By similarity).
Sequence Mass (Da): 105367
Sequence Length: 921
Subcellular Location: Nucleus
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Q8TC12 | MVELMFPLLLLLLPFLLYMAAPQIRKMLSSGVCTSTVQLPGKVVVVTGANTGIGKETAKELAQRGARVYLACRDVEKGELVAKEIQTTTGNQQVLVRKLDLSDTKSIRAFAKGFLAEEKHLHVLINNAGVMMCPYSKTADGFEMHIGVNHLGHFLLTHLLLEKLKESAPSRIVNVSSLAHHLGRIHFHNLQGEKFYNAGLAYCHSKLANILFTQELARRLKGSGVTTYSVHPGTVQSELVRHSSFMRWMWWLFSFFIKTPQQGAQTSLHCALTEGLEILSGNHFSDCHVAWVSAQARNETIARRLWDVSCDLLGLPID | Function: Retinol dehydrogenase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinol, and to a lesser extent on 13-cis-retinol . Exhibits a low reductive activity towards unsaturated medium-chain aldehydes such as cis -6-nonenal and no activity toward nonanal or 4-hydroxy-nonenal . Has no dehydrogenase activity towards steroid .
PTM: Not glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Sequence Mass (Da): 35386
Sequence Length: 318
Pathway: Cofactor metabolism; retinol metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.300
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Q9QYF1 | MFGFLLLLSLPFILYLVTPKIRKMLSSGVCTSNVQLPGKVAIVTGANTGIGKETAKDLAQRGARVYLACRDVDKGELAAREIQAVTGNSQVFVRKLDLADTKSIRAFAKDFLAEEKHLHLLINNAGVMMCPYSKTADGFEMHIGVNHLGHFLLTHLLLEKLKESAPSRIVNLSSLGHHLGRIHFHNLQGEKFYSAGLAYCHSKLANILFTKELAKRLKGSGVTTYSVHPGTVHSELTRYSSIMRWLWQLFFVFIKTPQEGAQTSLYCALTEGLESLSGSHFSDCQLAWVSYQGRNEIIARRLWDVSCDLLGLPVDW | Function: Retinol dehydrogenase with a clear preference for NADP . Displays high activity towards 9-cis, 11-cis and all-trans-retinol, and to a lesser extent on 13-cis-retinol (By similarity) . Exhibits also reductive activity towards toxic lipid peroxidation products such as medium-chain aldehydes trans-2-nonenal, nonanal, and cis-6-nonenal . Has no dehydrogenase activity towards steroid . Seems to be required for homeostasis of retinol in liver and testis .
PTM: Not glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Sequence Mass (Da): 35148
Sequence Length: 316
Pathway: Cofactor metabolism; retinol metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.300
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Q96NR8 | MLVTLGLLTSFFSFLYMVAPSIRKFFAGGVCRTNVQLPGKVVVITGANTGIGKETARELASRGARVYIACRDVLKGESAASEIRVDTKNSQVLVRKLDLSDTKSIRAFAEGFLAEEKQLHILINNAGVMMCPYSKTADGFETHLGVNHLGHFLLTYLLLERLKVSAPARVVNVSSVAHHIGKIPFHDLQSEKRYSRGFAYCHSKLANVLFTRELAKRLQGTGVTTYAVHPGVVRSELVRHSSLLCLLWRLFSPFVKTAREGAQTSLHCALAEGLEPLSGKYFSDCKRTWVSPRARNNKTAERLWNVSCELLGIRWE | Function: Retinoids dehydrogenase/reductase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinal. Shows very weak activity towards 13-cis-retinol . Also exhibits activity, albeit with lower affinity than for retinaldehydes, towards lipid peroxidation products (C9 aldehydes) such as 4-hydroxynonenal and trans-2-nonenal . May play an important function in photoreceptor cells to detoxify 4-hydroxynonenal and potentially other toxic aldehyde products resulting from lipid peroxidation . Has no dehydrogenase activity towards steroids .
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Sequence Mass (Da): 35094
Sequence Length: 316
Pathway: Cofactor metabolism; retinol metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.300
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Q8NBN7 | MSRYLLPLSALGTVAGAAVLLKDYVTGGACPSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGSTFSSTTLGPIFWLLVKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPEAEDEEVARRLWAESARLVGLEAPSVREQPLPR | Function: Retinol dehydrogenase with a clear preference for NADP. Oxidizes all-trans-retinol, but seems to reduce all-trans-retinal with much higher efficiency . Has no activity toward steroids .
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35932
Sequence Length: 331
Pathway: Cofactor metabolism; retinol metabolism.
Subcellular Location: Mitochondrion inner membrane
EC: 1.1.1.300
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Q17QW3 | MAVGTAAALLAALGGILWLAARRFVGSSVQRLHQGRDSGLMRGKTVLITGANSGLGRATAAELLRLGARVIMGCRDRERAEEAAGQLRREVCPAGGPDSGPNSGGAGELVVKELDLASLSSVRSFCQEMLQEEPRLDVLINNAGVFQCPYMKTEDGFEMQFGVNHLGHFLLTNLLLGLLKSSAPSRIVVVSSKLYKYGDINFEDLNSEQSYNKSFCYSRSKLANILFTRELARRLEGTSVTVNVLHPGIVRTNLGRHIHIPLLVRPLFNLVSWAFFKTPEEGAQTAVYLASSPEVEGVSGRYFGDCKEEELLPKAMDESVARKLWDISEVMVGILK | Function: Retinol dehydrogenase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinol. Shows a very weak activity towards 13-cis-retinol. Has no activity towards steroid.
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Sequence Mass (Da): 36625
Sequence Length: 336
Pathway: Cofactor metabolism; retinol metabolism.
EC: 1.1.1.300
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Q9HBH5 | MAVATAAAVLAALGGALWLAARRFVGPRVQRLRRGGDPGLMHGKTVLITGANSGLGRATAAELLRLGARVIMGCRDRARAEEAAGQLRRELRQAAECGPEPGVSGVGELIVRELDLASLRSVRAFCQEMLQEEPRLDVLINNAGIFQCPYMKTEDGFEMQFGVNHLGHFLLTNLLLGLLKSSAPSRIVVVSSKLYKYGDINFDDLNSEQSYNKSFCYSRSKLANILFTRELARRLEGTNVTVNVLHPGIVRTNLGRHIHIPLLVKPLFNLVSWAFFKTPVEGAQTSIYLASSPEVEGVSGRYFGDCKEEELLPKAMDESVARKLWDISEVMVGLLK | Function: Retinol dehydrogenase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinol. Shows a very weak activity towards 13-cis-retinol. Has no activity towards steroid.
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Sequence Mass (Da): 36865
Sequence Length: 336
Pathway: Cofactor metabolism; retinol metabolism.
EC: 1.1.1.300
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O75452 | MWLYLAVFVGLYYLLHWYRERQVLSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLWGLVNNAGISLPTAPNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFGGGYCISKYGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKSFLEIWDRSSPEVKEAYGEKFVADYKKSAEQMEQKCTQDLSLVTNCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTFLVDAIMYWVSPSPAKAL | Function: Oxidoreductase with a preference for NAD. Oxidizes all-trans-retinol, 9-cis-retinol, 11-cis-retinol and 13-cis-retinol to the corresponding aldehydes . Has higher activity towards CRBP-bound retinol than with free retinol . Oxidizes also 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction .
PTM: Not N-glycosylated.
Location Topology: Single-pass membrane protein
Catalytic Activity: all-trans-retinol--[retinol-binding protein] + NAD(+) = all-trans-retinal--[retinol-binding protein] + H(+) + NADH
Sequence Mass (Da): 35673
Sequence Length: 317
Domain: The C-terminal region plays a crucial role in controlling the activity of RDH16 and its required for endoplasmic reticulum (ER) retention.
Pathway: Cofactor metabolism; retinol metabolism.
Subcellular Location: Microsome membrane
EC: 1.1.1.105
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Q09772 | MKRRATFQCPLIESTIKHQSTNYTKTETATTSHEVSENANEHKGKSNIDINKIAYYNVVWRKITMKKHKTWEGDGFLVREDSNLTLYNSDFTRLGSCHSRVPQIKEGELLRISGKEISIEKEISAESYEAGTHIDDSLRDVHMPEMKRKFKPPLRPNTMYQTISALPKPRHDPTVLGALVMSRPKTWDPRTHVDVVIDPFLSKHLYSHQREGVSFLYDCLLGMEGKCGYSAILADEMGLGKTLQTITVVWTLLKQSYYANRSSTINNAMVVAPVTLLKNWENEFYNWLGHERIHVYIARCAEDFQEFTSNKTYSIIITGYETVCTYLRNYGCGIDIDLLICDEAHRLKSMSSQTWITLNKLKTRKRLLLTGTPLQNDLSEYFSMVNFIIPGSLGTPNSFKAQYERPILRSRSMNASSRDISLGAARLQRLFEFTSNFTLRRKANILAKHLPPRTDIVLFIKPTHQQENVYGHVLDGFKSSVDQKGYYLKILTRLSKICNSTILLRNEKENFLSTELQDKHVFEQENMLLSSSKLQILAALLKSFQRGCQKAVIVSQYKETLELIELFLSILHVRFCKLLGSTPFSERDLIVHNFNTSSFKEFSVLLLSSKAGGCGLNLTGSTRLIIYEPSWNPAQDLQALSRIYRSGQKRPVCIYTFLSSGMLDERIFIRQNTKQGLSSSFIDSDASQKKNFFTGEDIKTLFSYSKTETCLTYELAFDSDEIDSLTKKKDPLTKIDHTIDSPNTKEKDKEISSWKKASEYMDTNLGKKCPENAFQGWTWQFPNDLSIMNGVEDYIPLEPLPINCLMHKKFE | Function: Acts with rhp54 to repair meiotic double strand breaks via homologous recombination. Involved in meiotic DNA recombination.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 92965
Sequence Length: 811
Subcellular Location: Cytoplasm
EC: 3.6.4.12
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P38086 | MAVISVKPRRREKILQEVKNSSVYQTVFDSGTTQMQIPKYENKPFKPPRRVGSNKYTQLKPTATAVTTAPISKAKVTVNLKRSISAGPTLNLAKKPNNLSSNENTRYFTIMYRKPTTKKHKTWSGDGYATLKASSDKLCFYNEAGKFLGSSMLPSDSDSLFETLFKAGSNEVQLDYELKENAEIRSAKEALSQNMGNPSPPTTSTTETVPSTKNDGGKYQMPLSQLFSLNTVKRFKSVTKQTNEHMTTVPKTSQNSKAKKYYPVFDVNKIDNPIVMNKNAAAEVDVIVDPLLGKFLRPHQREGVKFMYDCLMGLARPTIENPDIDCTTKSLVLENDSDISGCLLADDMGLGKTLMSITLIWTLIRQTPFASKVSCSQSGIPLTGLCKKILVVCPVTLIGNWKREFGKWLNLSRIGVLTLSSRNSPDMDKMAVRNFLKVQRTYQVLIIGYEKLLSVSEELEKNKHLIDMLVCDEGHRLKNGASKILNTLKSLDIRRKLLLTGTPIQNDLNEFFTIIDFINPGILGSFASFKRRFIIPITRARDTANRYNEELLEKGEERSKEMIEITKRFILRRTNAILEKYLPPKTDIILFCKPYSQQILAFKDILQGARLDFGQLTFSSSLGLITLLKKVCNSPGLVGSDPYYKSHIKDTQSQDSYSRSLNSGKLKVLMTLLEGIRKGTKEKVVVVSNYTQTLDIIENLMNMAGMSHCRLDGSIPAKQRDSIVTSFNRNPAIFGFLLSAKSGGVGLNLVGASRLILFDNDWNPSVDLQAMSRIHRDGQKKPCFIYRLVTTGCIDEKILQRQLMKNSLSQKFLGDSEMRNKESSNDDLFNKEDLKDLFSVHTDTKSNTHDLICSCDGLGEEIEYPETNQQQNTVELRKRSTTTWTSALDLQKKMNEAATNDDAKKSQYIRQCLVHYKHIDPARQDELFDEVITDSFTELKDSITFAFVKPGEICLREQ | Function: Involved in the recombinational repair of double-strand breaks (DSB) in DNA during mitosis and meiosis. Has DNA dependent ATPase activity. Promotes D-loop (displacement loop) formation with RAD51 recombinase. Modifies the topology of double-stranded DNA during the D-loop reaction to facilitate the invasion of the homologous duplex molecule by the initiating single-stranded DNA substrate. Required for adaptation from G2/M checkpoint arrest induced by a double strand break, by participating in monitoring the extent of single-stranded DNA produced by resection of DNA ends. This role is distinct from its roles in recombination. Promotes colocalization of RAD51 and DMC1 during meiotic recombination. Involved in crossover interference.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 107946
Sequence Length: 958
Subcellular Location: Nucleus
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P21405 | MYRPSCLSYVLLVANMWSFAVCANAFIYGSYDPSHNIPIVALMTLCATGLWLSTSVVSFGIRYVRVRVSPEKTQNRTIYVSSGLPHFDPVYGVVKKCEPMGGGPAIELQVNPSWIHLLPTSPAINKVEVGQESAILGSTYSVVETGGEPKSLVAVKSGDSTLGFGARVYHEGMDVLMVPHHVWYNDKPHTALAKNGRSVDTEDWEVEAACADPRIDFVLVKVPTAVWAKLAVRSTKVLAPVHGTAVQTFGGQDSKQLFSGLGKAKALDNAWEFTHTAPTAKGWSGTPLYTRDGIVGMHTGYVDIGTSNRAINMHFIMSCLVSKMETLPPELGYREISLEDVGLRSFEFLEVEIENRGKVKLGKREFAWVPKGKAWADMLDDDDLPLPPKMVNGNLVWADAQESFDGALPLNLLAGGRTQCLAAQIELGDYKFSCGPTHETGGMPFRNCGSSTCKFREVSRKPVADAVTAATKVFPELSELGWPERGSGAEIGSLLLQAGKFVPTKAPSNLEQAYNNLLSRYPRSKPLACFRQGTWSFDAIFEQVVSKATSAEINQKASPGVPLSRLATTNKDLMAQHMQFVAACVTGRVPLLASFEDIHALSPTEMVEMGLCDPVRLFVKQEPHPSRKLKEGRYRLISSVSIVDQLVERMLFGAQNELEIAEWQSIPSKPGMGLSVIHQADAIFRDLRVKHTVCPAAEADISGFDWSVQDWELWADVEMRIVLGSFPPMMARAARNRFSCFMNSVLQLSNGQLLQQELPGIMKSGSYCTSSTNSRIRCLMAELIGSPWCIAMGDDSVEGFVEGAREKYAGLGHLCKDYKPCATTPTGQLYAVEFCSHVIKRNKAFLTSWPKTLYRFLSTPRETLEDLERELASSPMWHKIQSYVRSIPSPDKTARDKSICNGYPLDQEAISTSYSEYSSKSASAEATREAACCAGAQAYPSWGIHGPYCSGDHGEA | Function: Responsible for cleavage of polyprotein P2A and replicase polyprotein P2AB.
PTM: The polyprotein is proteolytically cleaved into several chains by the viral protease.
Location Topology: Multi-pass membrane protein
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 104849
Sequence Length: 956
Subcellular Location: Host membrane
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P25328 | MKEPVDCRLSTPAGFSGTVPPPGRTKAARPGTIPVRRSRGSASALPGKIYGWSRRQRDRFAMLLSSFDAALAAYSGVVVSRGTRSLPPSLRLFRAMTRKWLSVTARGNGVEFAIASAKEFSAACRAGWISGTVPDHFFMKWLPEPVRRKSGLWAQLSFIGRSLPEGGDRHEIEALANHKAALSSSFEVPADVLTSLRNYSEDWARRHLAADPDPSLLCEPCTGNSATFERTRREGGFAQSITDLVSSSPTDNLPPLESMPFGPTQGQALPVHVLEVSLSRYHNGSDPKGRVSVVRERGHKVRVVSAMETHELVLGHAARRRLFKGLRRERRLRDTLKGDFEATTKAFVGCAGTVISSDMKSASDLIPLSVASAIVDGLEASGRLLPVEIAGLRACTGPQHLVYPDGSEITTRRGILMGLPTTWAILNLMHLWCWDSADRQYRLEGHPFRATVRSDCRVCGDDLIGVGPDSLLRSYDRNLGLVGMILSPGKHFRSNRRGVFLERLLEFQTRKTVYEHAVIYRKVGHRRVPVDRSHIPVVTRVTVLNTIPLKGLVRASVLGRDDPPVWWAAAVAESSLLSDYPRKKIFAAARTLRPGLSRQFRRLGIPPFLPRELGGAGLVGPSDRVDAPAFHRKAISSLVWGSDATAAYSFIRMWQGFEGHPWKTAASQETDTWFADYKVTRPGKMYPDRYGFLDGESLRTKSTMLNSAVYETFLGPDPDATHYPSLRIVASRLAKVRKDLVNRWPSVKPVGKDLGTILEAFEESKLCTLWVTPYDASGYFDDSLLLMDESVYQRRFRQLVIAGLMREGRMGDLLFPNWLPPSTVVSGFP | Function: RNA-directed RNA polymerase that replicates the viral (+) and (-) genome.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 91809
Sequence Length: 829
Subcellular Location: Host cytoplasm
EC: 2.7.7.48
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Q07048 | MHHKVNVKTQREVHFPMDLLQACGASAPRPVARVSRATDLDRRYRCVLSLPEERARSVGCKWSSTRAALRRGLEELGSREFRRRLRLADDCWRAICAAVCTGRKFPSFSVTDRPARARLAKVYRMGRRLLVGVVCRGESVVSDLKQECADLRRVIFEGSTRIPSSSLWGLVGVLGWTSPERAMQLTFIGRALPYGSPDVERRALASHAATLSIPAECHPNYLVAAEQFAKSWADDNLPRKFRIYPIAVQESSCMEYSRAQGGLLQSFRKGFVGYDPAAPSADPDDLELAKERGFSRIRASWYSTFRYRGELKSTNQSLEARVAVVPERGFKARIVTTHSASRVTFGHQFRRYLLQGIRRHPALVDVIGGDHRRAVETMDGDFGLLRPDGRLLSADLTSASDRIPHDLVKAILRGIFSDPDRRPPGTSLADVFDLVLGPYHLHYPDGSEVTVRQGILMGLPTTWPLLCLIHLFWVELSDWAPARPNHSRGFVLGESFRICGDDLIAWWRPERIALYNQIAVDCGAQFSAGKHLESKTWGIFTEKVFTVKPVKMKVRVRSEPSLKGYVFSRSSAFSCRMGGKGITGIRAARLYTIGAMPRWSRRIRDVYPGSLEHRTASQRYGEPVTVYRFGRWSSAIPLRWAVRAPTRTVGNPVQSLPDWFTVGPAASSVAADSNAFGAVSRVLRRMFPGLPRKLASAGIPPYLPRVFGGGGLVKSTGLTTKIGAVASRRWMSRIGHDLYRSRERKSTLGRVWTLSTSPAYAASLHEVEKFMDRPDIILTRKCRNPMLKHARELGLFEEVFESRVGGGILWASLNGKALVESHSPSILQVSRNLRRSLACPSGGFLRPSAPIGKLVQRHTLPRGTVWFLESSATDSARQGGMGLPPPPPPPLGGGGMAGPPPPPFMGLRPESSVPTSVPFTPSMFSERLAALESLFGRPPPS | Function: RNA-directed RNA polymerase that replicates the viral (+) and (-) genome.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 104297
Sequence Length: 941
Subcellular Location: Host cytoplasm
EC: 2.7.7.48
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Q9QAZ8 | MRRFEFELARMSGAAFCVVTGYRLLTSKWLADRVEDYRQRVIADRKQILRDAAVIRTSIQKQMELVRISVRKGHSHQEAATERNSATDTMIGVVEKCGYEPYIISPSPREKEYHGSRQFYSLADFRQDYRRDEITDRHVIVMTDVDYYVDMHELVGLGVPILLYTFQPSTVSGEVKDGYFTITDDHVHYRVAGGKDVRHRIWNYNQDTMFVRSKPRGFWASLKQILRDITGITALCGYLYLKLGIAPFGDQVTLFTVDQFKMGEHRNIVSIVPFATCRSNLLKISEYGAELDYMRYQQRNNNANFNAVTYISQEGPLISLGLEGNFASVQLPLQDFENIRTAYELSKNNNLSDTVRRSARSCKEAAIIHKCLQAGCDLASEVVHKPGELARHYQALGDTYDIDPSEQGKCYAREYAPGPLTQTAVFPSESRSNELATIDGRIAGPQAKAKSREHITPKMHKVARDFVRHLVPTAGLGRPYPLTYVEEHQTKPLQRARNDANRYHDEFTMIVKAFQKKEAYNAPNYPRNISTVPHTQNVKLSSYTYAFKEAVLQHVPWYMPTHTPAEIAEAVQSLAASSTELVETDYSKFDGTFLRFMRENVEFAIYKRWVHLDHLTELSTLLGNELQAPAVTRLGIKYDPDCSRLSGSALTTDGNSIANAFVSYLAGRQAGMDDDEAWTWIGIVYGDDGLRSGNVSDALLSKTASSLGFDLKIVNRAPRGSPVTFLSRVYLDPWSSPASVQSPLRTLLKLHTTCDTQSDIEDVGWAKTQAYLVTDCLTPFIGHWCRAYQRNCTARVVQYADYNDIPFWVKNEDHVGNSWPQSDSVDWNDVVANELGLTTAELLKHLAALDAYTGPVSGLPRLTTSLDLEPKMPVALDGEVQAGPSQQPQTDKDGTSPTGDRSAPRRARTALQDADGRACRSRRSDRSPGKRDANVRDKRQRRSTTPPRSRPSVPGPSSSGRRTDGDRVRGGAARQRQRRRSPV | Function: RNA-dependent RNA polymerase which replicates the viral genome composed of 2 RNA segments, RNA1 and RNA2.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 110630
Sequence Length: 983
EC: 2.7.7.48
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P17460 | MPLLHTLNTALAVGLLGARYYPEVQTFLGLPDYVGHMKNVVRSVFQGSGLVVVSSDTVGVRGTYSNRGQIGSSLGCILAVPDSGADIEIDLDRLVGTEEEATSCLVEAVGSTADVPRRRVRQKGRFAMHAVNAAKLHFCGVPKPTEANRLAVSKWLVQYCKERHVVDSHIRTIVNTALPRVFTPDAEDIQVVLDLHSVRAHDHRNALAEAGKVRKWWVNLAMHPMTGRSWSRAWRRLCRLPDDQAISFVRXGCLRELVGRETQISRGENPAMRVFPLANPPKVRRIFHICGMGNGLDFGVHNNSLNNLRRGLMERVFYVEDAQKQLKPAPQPIPGIFGKLSGIRRRLVRLAGNHTPVPREKYPSFYKGRRATIYQKALDSLHDRPVSRKDAELKTFVKAEKINFTAKKDPAPRVIQPRDPRYNIEVGKYLKPYEHHLYRAIDAMWGGPTVLKGYDVGELGNIMSNTWDKFRKTCAIGFDMKRFDQHVSVDALRWEHSVYNAGFNCPELAQLLTWQLTNKGVGRASDGFIKYQVDGCRMSGDVNTALGNCLLACSITKYLMKGIKCKLINNGDDCVLFFEADEVDRVRERLHHWIDFGFQCIAEEPQYELEKVEFCQMSPIFDGEGWVMVRNPRVSLSKDSYSTTQWANEKDAARWLAAIGECGLAIAGGVPVLQSYYSCLKRNFGPLAGDYKKKMQDVSFDSGFYRLSKNGMRGSKDVSQDARFSFYRGFGYTPDEQEALEEYYDNLQLLCEWDPTGYKEELSDRWILNEFPTTL | Function: RNA-dependent RNA polymerase that plays an essential role in the virus replication.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 87648
Sequence Length: 775
EC: 2.7.7.48
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P24230 | MKGRLLDAVPLSSLTGVGAALSNKLAKINLHTVQDLLLHLPLRYEDRTHLYPIGELLPGVYATVEGEVLNCNISFGGRRMMTCQISDGSGILTMRFFNFSAAMKNSLAAGRRVLAYGEAKRGKYGAEMIHPEYRVQGDLSTPELQETLTPVYPTTEGVKQATLRKLTDQALDLLDTCAIEELLPPELSQGMMTLPEALRTLHRPPPTLQLSDLETGQHPAQRRLILEELLAHNLSMLALRAGAQRFHAQPLSANDTLKNKLLAALPFKPTGAQARVVAEIERDMALDVPMMRLVQGDVGSGKTLVAALAALRAIAHGKQVALMAPTELLAEQHANNFRNWFAPLGIEVGWLAGKQKGKARLAQQEAIASGQVQMIVGTHAIFQEQVQFNGLALVIIDEQHRFGVHQRLALWEKGQQQGFHPHQLIMTATPIPRTLAMTAYADLDTSVIDELPPGRTPVTTVAIPDTRRTDIIDRVHHACITEGRQAYWVCTLIEESELLEAQAAEATWEELKLALPELNVGLVHGRMKPAEKQAVMASFKQGELHLLVATTVIEVGVDVPNASLMIIENPERLGLAQLHQLRGRVGRGAVASHCVLLYKTPLSKTAQIRLQVLRDSNDGFVIAQKDLEIRGPGELLGTRQTGNAEFKVADLLRDQAMIPEVQRLARHIHERYPQQAKALIERWMPETERYSNA | Function: Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA). Has a role in constitutive stable DNA replication (cSDR) and R-loop formation. Is genetically synergistic to RadA and RuvABC .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 76430
Sequence Length: 693
EC: 3.6.4.12
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P43809 | MSLELLDAVPLTSLSGVGAAISNKLAKIGIHNLQDLLFHLPIRYEDRTRITLIANLRPEQYFTIEGIVQTCEVAFGRRPILSVSLSDGTSKIMLRFFNFNAGMRNSFQVGVRVKAFGEVKRGRHMPEIHHPEYQIVRDNAPIVLEETLTPIYSTTEGLKQNSLRKLTDQALALLDKVQIAEILPNEFNPHQYSLKEALRLLHRPPPDISLEMLEQGKHPAQQRLIFEELLAHNLAMQKVRLGTQQFSALPLHYQTDLKQRFLATLPFQPTNAQKRVVSDIEQDLIKDYPMMRLVQGDVGSGKTLVAALAALTAIDNGKQVALMAPTEILAEQHANNFRRWFKPFGIEVGWLAGKVKGKSRQAELEKIKTGAVQMVVGTHALFQEEVEFSDLALVIIDEQHRFGVHQRLMLREKGEKAGFYPHQLIMTATPIPRTLAMTVYADLDTSIIDELPPGRTPITTVVVSEERRAEIVMRVKNACVNEKRQAYWVCTLIDESEVLEAQAAEAIWEDLTKALPMLNIGLVHGRMKPQEKQDVMMRFKNAELDLLVATTVIEVGVDVPNASLMIIENAERLGLSQLHQLRGRVGRGCTASFCVLMYKPPLGKVSQKRLQVLRDSQDGFVISEKDLEIRGPGEVLGTKQTGIAELRVANLMRDRKMIPTVQHYAKSLIQKYPDVAESLIRRWLNNKEIYSNA | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 78086
Sequence Length: 693
EC: 3.6.4.12
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O26051 | MQETDNLLKTLNVKSLLEALLVYTPKGYKDLNLLERFETGLSGVLEVGILEKRNYAKVLKIFAYSKRFYKNLELVFFNYSAFHHSQFKTGESLFIYGKLEQSSFNQAYIINTPKIITKFGKISLIFKKVKNHKKIQENLQKLISLENLKKEGVKENIAHLLLEIFFPTPHFVKDFETNKNFPSQHLNALKYIEMLFYMKNLERKKLQFGAKIACPNNNERLKAFIASLPFKLTRDQQNAIKEIQNDLTSSIACKRLIIGDVGCGKTMVILASMVLTYPNKTLLMAPTSILAKQLYNEALKFLPPYFEVELLLGGSYKKRSNHLFETITHVVIGTQALLFDKRDLNEFALVITDEQHRFGTKQRYQLEKMASSKGNKPHSLQFSATPIPRTLALAKSAFVKTTMIREIPYPKEIETLVLHKRDFKIVMEKISEEIAKNHQVIVVYPLVNESEKIPYLSLSEGASFWQKRFKKVYTTSGQDKNKEEVIEEFRESGSILLATTLIEVGISLPRLSVMVILAPERLGLATLHQLRGRVSRNGLKGYCFLCTIQEENERLEKFADELDGFKIAELDLEYRKSGDLLQGGEQSGNSFEYIDLAKDENIIAEVKRDFLKAASVSRGTFEN | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 71393
Sequence Length: 623
EC: 3.6.4.12
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O69460 | MVSLSDRLDYIVGAKAADSLDEVFGIRTVDDLLRHYPRSYTKGATVRGAQDERPEAGEHITIVDVITEAVTLPMKKDSKKKYLRLTVGSGRNKVIATFFNAGYISKGLTKDTRVMLSGEVGFFRGVMQLTHPAFLILDSPDGRNRGSSSLRRIADASQAVSGEVLMSAFERRFFPIYPASTKLQSWDIYACVRQVLEVLDPVADPLPADLRAKHGLVSEDEALRAIHLAESESDRRRARERLTFDEAVGLQWALVTRRHGELSESGPSAPPRSDGLMAELMRRLPFELTEGQREVRDVLSDGLAATRPLNRLLQGEVGSGKTIVAVLAMLQMIDAGYQCVLLAPTEVLAAQHLLSIRDVLGPLGMGCQLGGAENATQVALLTGSMTMAQKKKVRADIFSGQTGIVIGTHALLQDAIEFHNLGMVVVDEQHRFGVEQRDQLRTKARTGIMPHLLVMTATPIPRTVALTVYGDLEMSTLRELPRGRQPITSNVIFVKDKPGWLDRAWQRILEEVAAGRQAYVVAPRIDETEDPQKGGQNSRPSETADGLYARLRSGELANVRLALMHGRLSADEKDAAMMAFRAGEIDVLVCTNVIEVGVDVPNATIMLVMDADRFGISQLHQLRGRIGRGTHPSLCLLASWVSPGSPAGRRLCAVAETMDGFALADLDLKERREGDVLGRNQSGKAITLRMLSLAEHQVFIEAARDFCTRAYEYPHLGLAPHPGLADLAARFIDTDRIEYLGKS | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 81505
Sequence Length: 743
EC: 3.6.4.12
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O50581 | MAKVNLIESPYSLLQLKGIGPKKIEVLQQLNIHTVEDLVLYLPTRYEDNTVIDLNQAEDQSNVTIEGQVYTAPVVAFFGRNKSKLTVHLMVNNIAVKCIFFNQPYLKKKIELNQTITVKGKWNRVKQEITGNRVFFNSQGTQTQENADVQLEPVYRIKEGIKQKQIRDQIRQALNDVTIHEWLTDELREKYKLETLDFTLNTLHHPKSKEDLLRARRTYAFTELFLFELRMQWLNRLEKSSDEAIEIDYDIDQVKSFIDRLPFELTEAQKSSVNEIFRDLKAPIRMHRLLQGDVGSGKTVVAAICMYALKTAGYQSALMVPTEILAEQHAESLMALFGDSMNVALLTGSVKGKKRKILLEQLENGTIDCLIGTHALIQDDVIFHNVGLVITDEQHRFGVNQRQLLREKGAMTNVLFMTATPIPRTLAISVFGEMDVSSIKQLPKGRKPIITTWAKHEQYDKVLMQMTSELKKGRQAYVICPLIESSEHLEDVQNVVALYESLQQYYGVSRVGLLHGKLSADEKDEVMQKFSNHEINVLVSTTVVEVGVNVPNATFMMIYDADRFGLSTLHQLRGRVGRSDQQSYCVLIASPKTETGIERMTIMTQTTDGFELSERDLEMRGPGDFFGVKQSGLPDFLVANLVEDYRMLEVARDEAAELIQSGVFFENTYQHLRHFVEENLLHRSFD | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 78343
Sequence Length: 686
EC: 3.6.4.12
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P35243 | MGNSKSGALSKEILEELQLNTKFSEEELCSWYQSFLKDCPTGRITQQQFQSIYAKFFPDTDPKAYAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMITPEDVKLLPDDENTPEKRAEKIWKYFGKNDDDKLTEKEFIEGTLANKEILRLIQFEPQKVKEKMKNA | Function: Acts as a calcium sensor and regulates phototransduction of cone and rod photoreceptor cells (By similarity). Modulates light sensitivity of cone photoreceptor in dark and dim conditions (By similarity). In response to high Ca(2+) levels induced by low light levels, prolongs RHO/rhodopsin activation in rod photoreceptor cells by binding to and inhibiting GRK1-mediated phosphorylation of RHO/rhodopsin (By similarity). Plays a role in scotopic vision/enhances vision in dim light by enhancing signal transfer between rod photoreceptors and rod bipolar cells (By similarity). Improves rod photoreceptor sensitivity in dim light and mediates response of rod photoreceptors to facilitate detection of change and motion in bright light (By similarity).
PTM: The N-terminal glycine is linked to one of four different types of acyl groups. The most abundant is myristoleate (14:1), but 14:0, 14:2, and 12:0 acyl residues are also present (By similarity). The Ca(2+) induced exposure of the myristoyl group, known as the calcium-myristoyl switch, promotes RCVRN binding to the photoreceptor cell membranes only when intracellular Ca(2+) concentration is high (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 23130
Sequence Length: 200
Domain: EF-hand 2 and EF-hand 3 domains are the low-affinity and the high-affinity calcium binding sites, respectively. EF-hand 1 and EF-hand 4 domains do not bind calcium due to substitutions that disrupt their respective Ca(2+) binding loops. The cooperative binding of calcium to the EF-hand 2 domain following EF-hand 3 domain calcium binding requires myristoylation (By similarity). Calcium binding to the 2 EF-hand domains induces exposure of the myristoyl group through a protein conformation change, this process known as the calcium-myristoyl switch facilitates binding to photoreceptor cell membranes (By similarity).
Subcellular Location: Photoreceptor inner segment
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