ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A7HSL2 | MTQHIVSGGPQVVDSESFSALTNVSRETLDRLLSYEALLRKWQKSINLVSNGSLPELWRRHMLDSAQLVCLVPESARRWIDLGSGGGFPGLVIAILLRERPGFQMHLVESDQRKCVFMREVARVTGAPATVHTVRIEAFAQGAEAGDVVSARALAPLDRLFGWAAPLFGPETIGLFLKGQGLQDELTLARESWIFDAEFSPSQSDPEGSVLKVRGLHGPDGQPHRR | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24833
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 2.1.1.... |
Q31RM0 | MTSGFALDVRNWTETLGWQPSPQQQQQFEALYHGIIAGNQRLNLTRITDPAEFTEKHLWDSLYGLRPLLTDDWSGEIIDIGTGGGFPGLPAAIALTKSRVMLLDSTRKKIQFLQTLAQELGLSNVTVAVGRAEEWGRDRRQRARYDWATIRAVGPATVCAEYCLPLLKIGGKAVLYRGQWTEEEAIALDRAVTILGGEVVDVSATFLPESGAERHCITLQKTAQTPAAYPRMVGLPSQKPLG | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 26661
Sequence Length: 242
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q2JMA3 | MKKADAPSSEPPELKALWESWLADLGWQPSEQQQQQLQQLYPLVMAGNRTQNLTRITDPIDFWEKHLWDSLRGLRLLGSWEAIQAQPWRGIDIGTGAGFPGIPAQIALPQTRFTLLDSTQRKIAFVQDILQRLSLTQARAVAQRAEIWGQDPQERGSYDIALARALASAEICAEYCLPLLKVGGRAILYRGHWTEAEAQTLEQALELLGGKLIHVEAFTTPRSRGVRHCLLLEKVAPTPPPYPRSPGTPKRQPLGQSNRP | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 29090
Sequence Length: 260
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A5GNG2 | MPESTPFAAPGPELWSRLGWTPDAGQREQLITLQELLRDWNTRVNLTRLVEGEDFWVTQVLDSLWPLKPELDTADTPRRCIDVGTGGGFPGLAVAIALPGAELTLVDSVSRKTAAVAAMARSLGMADRVSVRTERVERTGQDPRCRGQFDLALARAVASAPVVAEYLVPLLHTNGQALLYRGRWQQEDQRDLDPALALLKAKTVAIERCELPSARGPRTVIRVMPEQPTPHLYPRAVGIPSKQPLGIQADDNRS | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 27881
Sequence Length: 254
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q3AHY7 | MAATAPEPAFWDALGWQPSQAQRDQLEELQGLLQSWNERVNLTRLVNGDDFWIGQVFDSLWPLAGELQSANEPQHWIDVGTGGGFPGLAIAIALPQAQVTLLDSVGRKTAAVEAMASSLGLADRVGVRTERIETTGRDRHFRGSFDRAVARAVAAAPVVAEYLVPLLKTDGEALLYRGQWADSDAVPFNRALRLLAARLVEVQHRQLPSDRGTRHLLRVKPNGPCPRSYPRAVGTPSRDPLGS | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 26514
Sequence Length: 243
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q0ATU7 | MEYNVKTFKEMLIEENSRHNLVSRKSLPVELEKHIEDSRSLLNFMDLKGSRVVDIGSGAGFPGLVLAIYCPEGEFLLLESDLKKTEFLQAVINRCGLKNCQVLRKRIEEVGRSELRNSFDFCSCRALAMMNIVLEYGLPLLRLGGKLLLWKGKNYSREIEQAANALDILGGKVVDIFTYSLMAERDRAIVVVEKERDTPAKYPRRVGIPAKRPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 24304
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q55787 | MSLNLDKDNRDLSSNQGHLGEFRRGLENWPPGLVWQPDGEQIEAMVKLYQGVLVGNARLNLTRITAPLDFLEKHLWDSLAGVLLSDHSRNCPQARVIDIGTGGGFPGLPVALVWPQWSVALLDSTHKKINYLEELGHRLGLANLAYLVARAEAVGNQPQHRSQYDLALIRAVGEGVVCAEYALPLVKVGGTVVLYRGQWSAAEAEQLERACALLGGKVSATVAAVTPWSGAQRHFIYLTKEKPTPSDFPRAIGVPRSHPLGVEN | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 28790
Sequence Length: 264
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A6LMN3 | MKKESLIKNYIKEIVNAPFNLTAIKNEEEAFHLLALDSLLPLEKMNLIGNFLDVGTGGGVPGVFIGIMFKKLKGTLIDASRKKINYVKNVCIKLGIDNLEFVHGRIEEQIDFIEKFDNVFSKAVAELRIILELTVPYAKVGGRILLYKGKEYLKELNDAKNAIDVLNVDLEDVVEYEILDRKRVLLIFEKKDKVNGFPRRYNRILKNPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 23894
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q9WZG6 | MLEFSSEVSLLDSVKNILLEYGLRFQEPQIEKVDKYIEELLGVPYNLTAHRDLDSAVHKNVVEILLPLKEELKGTLLDVGSGNGVPGLILAIFFSKLKVVLLDSREKSVNFLRGVIEKLDLENVSVVKERAENFSKERREEFDYVTARAVARLNVLVEICTPALKTGGKLLFYKGPSYIEELKEAQRAMKELKVELEKVREYSLKTGERRALLILRKYESSPEKYPRRVGVPFKRPLL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 27235
Sequence Length: 238
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
B0K8H7 | MKNKSVEMLIEGAKEWGIFLEMFHVEHFQKYYALLLEWNQKMNLTAITEESEVVIKHFLDSLSVVKSGKIKEEEKIIDVGTGAGFPCIPLKIVFPKLKATLLDSSKKRITFLEEVINKLGINEIELIHGRAEDIGKDIKYREQFDLSMARAVAPLNILLEYTLPFVKVDGYFIALKGREIEEEIENSQRALKELKGEIEEVKEIKLPYSDIVHHLVIIKKIDNCPTKYPRRANAIQRSPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 27636
Sequence Length: 240
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
B9MQ93 | MFEHIPVLLEESVSFLITNPDGIYVDATFGLGGHSKRILEKISNKGFLIAIDRDLEAIELGKRKLEAYKNVKIVHSSFSKVDELLECLGIEKIDGILFDFGVSSLQLDKQERGFSYNKEAFLDMRMDTTSKLTAYDVVNFYSQEDLEKIIREYGEERFARRIAKAIVERRSKKPIETTTELSSLISSLVPRPKDGSHPAQRTFQAIRIEVNGELDEIKIALEKSLRFLRSGGRICAISFHSLEDRIVKEFFKFHSLECVCPKDIPVCRCGKKKELNIITKKPITPSKEEIESNKRSHSAKLRVAEKV | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35027
Sequence Length: 307
Subcellular Location: Cyt... |
O25411 | MQEIESLHQSVLLQEVLQAFMPLEEGVLIDCTLGLGGHSKALLSQKPHLKLIGIDKDKFAQEIAKERLKAFEGRYNLLSGGFAKRFKEALETHNKEIKGVLVDLGVSSLQLDDDNRGFNFHSHTLDMRMDLESELNAQKVINSYPIVALEKIFRDYGEIKEYKKIAHKIAERRAKKPFKNAKDLSEFLSSFSKNKKIHPATLVFQAVRIEVNSELEELKEFLQCARNLKGAILCVISFHSLEDALVKNAFKDYAKNCICDPSSFKCACSNNHALGEILTKKPITPSPEEIKNNRRSRSAKMRVFQFKP | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34977
Sequence Length: 308
Subcellular Location: Cyt... |
A9B518 | MVSMHIPVLYDAALAALNLRPDGRYIDGTLGWAGHSSGILEGSGPTGRLLAIDQDPMALAAARERLAPYGERATIVHGNYRQMASLAAQHGWQQVDGILLDIGVSSPQLDLPERGFSFQYDAPLDMRMNPTRGESAADLIAQLDETSLANLIYEYGEERLSRRIARRIVEQRSKSPITSTAQLASLVKSAVGGQAGKTHPATRTFQALRIAVNDELGALREGLAAATNLLAPGGRLAVITFHSLEDRIVKEWMRDQASECLIPAKLEILACPHNCAANTGPRSCIYPVGRDCDYVPTLEVLSRKPIEATPEELKANPRAR... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36593
Sequence Length: 337
Subcellular Location: Cyt... |
B4U8T1 | MHKSVLLKEVTDFLSNPCPKIHIDATLGLGGHAKALLEVCKDTFLIGIDKDENAIEIAKEKLKGFNAVFYHGSFKDFDIVLKEEGLLYFDSILFDFGVSSLQLDEEEGFSFQREDFLDMRMDKRQQKTAYIVINTYKEKELADIFYKYGEERLSKKIARSIVEKRKKKPIETTKELVDIVSSCYPYKYSKINPATKVFQALRIEVNSELEDIKIALSKLLDFAKEGSKFAFISFHSLEDRLVKEFIKNNADKLKVCSKKPITPSDEELLYNKRARSAKLRCAKLCYNEKKDEAFDS | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34138
Sequence Length: 296
Subcellular Location: Cyt... |
Q5R0L7 | MITTSPQHVSVLLEESIEALATDPQGTYIDATFGRGGHTRALLNQLGDDARVIALDQDPEAIAAAAAFADDPRFQIIHTPFSNLQQVLDDLQLNRQVTGILFDLGVSSPQLDDAERGFSFMRDGPLDMRMNTTSGETAAEWLNRAEKDDISWVLKEYGEERFARRIASAIVMDREKKPFTRTKQLAEMIARVSPVKEKHKHPATRTFQAIRIHINRELEQIEQALEASLSGLKEDGRLVVISFHSLEDRLVKRFIRKHSEGKQLPPGLPVTEAERNKDKALEKVGKAIKPGKAEVQLNPRSRSSVLRIARRVRND | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35385
Sequence Length: 315
Subcellular Location: Cyt... |
Q28NM6 | MTDEIDKAPHIPVLLGAILREVAPVSGVWLDGTFGAGGYARGLLEGGADTVIGVDRDPLAFEMAADWAGSYGDALRLKEGTFSNLDTLADEPLDGVALDLGVSSMQLDLAERGFSFMRDGPLDMRMGQIGVSAEDLVNDAPEKLLADILFQYGEERAARRIAKAIVAERLKCRINSTLQLAGIVEKCLPSKKPGQSHPATRSFQAIRIAVNDEFGQLAQGLMAAERALRPGGKLAVVTFHSSEDRIVKKFMSERSSTGGGGSRYAPEAAAKVPGFTLTPRKAIPPDADEIARNTRARSAKLRIATRTDAPAQPVAPETLG... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34865
Sequence Length: 327
Subcellular Location: Cyt... |
A8Z694 | MDEYHIPVLLDEILSFLVKEKNGIYIDTTFGGGGHSLSLLNKLSNKGRVIAFDKDIDSIKNNNILDARFNLIKTNYRFIKKKIKLFNLNKVSGILADLGISSHQINSPKRGFSIRYNSILDMRMDTYNKINAQHIINNYSYNELYNLLIRFGEVKNAKNISKLILKHRKKKYIKSTFDLIKILNFFYKKKNKFLSKIFQSLRIEVNDEINALKDLLKNSLSILKPGGRIAVISYHSIEDRIVKKFLKTGNFNGIIPYDEYGNNLSPLILLEPRIIFSSKEEKKENNRSRSAILRIAEKKI | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34763
Sequence Length: 300
Subcellular Location: Cyt... |
A6WCY2 | MDVDVQDDVQGRAGEGAEERAHDAARRHASVMLERCTRVLSPALDHPGAVTVDVTLGMGGHAHELLRRHPGLRLVGMDRDPQALELAAHRLHEFADRITLVHSVSDGLGEALDDLGLDTVDAVFFDLGVSSLQLDEAERGFSYARDTALDMRMDPGAPTTAADVLNTYSHSQLTRILRVYGEERFAPRIASAIVRERALEPFTSSARLVDLVRANVPAATRRTGGNPAKRTFQALRIEVNDELGVVERSLPVAFERLAPEGRLAVLTFHSLEDRIVKNALRELSSSSAPPDLPFVPAGSGPRAELLTRGGETADEAELAE... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42448
Sequence Length: 391
Subcellular Location: Cyt... |
A1VSU4 | MVKGTWTHRTVLLNEAITALQVNPDGHYIDATFGRGGHSRLLLSQLSALGRVTAFDKDLDAIAEAQSIDDPRFSIRHQGFMHLDQMPQASVAGVLMDLGVSSPQIDNPERGFSFRNEGPLDMRMDTTRGQSVAEWLQDASIEAMTEVIRDYGEERFAGLVARAIDRRRQEHGPLQTTAELADVVASAVKTREPGKDPATRTFQALRIFINAELEELQQALQASLKVLQPGGRLVVISFHSLEDRIVKQFIAAHSREVYDRRAPFAAPKVMQLKALGRTKASEEEVAGNPRSRSAVMRVAERTGEAA | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33808
Sequence Length: 306
Subcellular Location: Cyt... |
B2RIE4 | MHCPDKESVYHIPVMLGECLEGLRIDPDGCYVDVTFGGGGHSRAIVEKLSSKGRLYGFDQDADACRNVLQDERFTFVPSNFRYLANFMDYYGEDGVDGILADLGVSSHHFDEEERGFSFRSESPLLDMRMNARAGRNAAAILNEYDASSLSALFYHYGELKQARRLAASIVHYRESLSGGLQTVGQLLEAVRGLISPREEKKQLACIFQALRIEVNDELGALQQMLEAALGCLRSGGRLVVMTYHSLEDRMVKNFLRYGTVKAPDEDSLRLYGAPQSPWQQITRKPLTASTKELSDNPRSRSAKLRIAEKI | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34794
Sequence Length: 311
Subcellular Location: Cyt... |
A2BUE8 | MQTDLSNSSLFNHKSVMTDEILYSIDQYPFISDNKLTAIDATLGGGGHSYQLLKKYPDLKIIGLDHDPIARESALNKLEEFKSRIEIIPSNFSNFEPKEKVSFVIADLGVNSNQIDSPERGFSFQKDGPLDMRMNPLIKMNAENLIETLSEKDLADLIFKFGDERLSRKISRKIKKDLKEKGKYSGTKDLAYSIAGCFPPKQRYRKIHPATRTFQALRIAVNNEIEALEKFLKIAPDWLLTGGIISIISFHSIEDRLVKNSFKGDYRLKNLTKKPITPNKKEIENNKRSRSAKLRIAQLK | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34207
Sequence Length: 300
Subcellular Location: Cyt... |
A4VIH0 | MSQISSLRHITVLLDEAVAALNVRADGRYLDGTFGRGGHSRLLLQQLGPNGQLLGFDKDPLAIATGQALAAEDGRFVVVQRSFAELGDEVAQRGWTGAVSGILLDLGVSSPQLDDPIRGFSFLNDGPLDMRMDPSRGVSAAEWIASADEDEIARVFKDYGEERFAKRMARAVVQRRAEAPFERTADLAKVLTDANPAWEKGKSPATRAFQGLRIHINNELGDLERGLDAALDALEVGGRLVVISFHSLEDRIVKQFMRRHAKGEADKLPRDLPIIPKAFEPRLKLIGKPQYASEAEVKANPRSRSAVMRVAEKVR | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34555
Sequence Length: 315
Subcellular Location: Cyt... |
C1DTV7 | MVEHYSVLHREVLEFTKDLKEGYFIDATVGGGGHSYLILKQNPKLKIIGVDKDDYALEVAKERLKDFEGRFSLVKSSFKDIDKIVKDLDVNPVVGILFDFGVSHFQLKLPRGFSFQREEPLDMRMDTSSELTAYYVVNYYPESRLFNIISKYGEEKFAKRIAKNIVEYRKKKKIETTKELADIVYRSYPPNLRHSRIHPATKTFQAIRIEVNNELLEIEEALEKAIHIVSKEGIIITISFHSLEDRIVKNTFKKYKELKFLDILTKKPITPKEDEIRENPASRSAKMRVARRL | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34176
Sequence Length: 293
Subcellular Location: Cyt... |
Q6AL31 | MLHNITLSLVPEIITDNILIKAKEIAQFLNIPLSDRREEYPQALIWDRDGLSLCSISAKDGSHAKLLYIDFMGGKNGYRHANDCTTRQPIAKAVGIKPGFRPTVFDATAGMGGDGFVLACLGCRVTLCERSPIMYTLLQDGIERARQDSVMNKIMANLDLIHNNSKQFLENHGTNYHTIYMDPMYPHKKKSALNKKEMRVIRDLVGDDNDSDNLLETALTVAGNRVVVKRPKGAPYIEERKPHHEITMKNSRFDVYLTSYL | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29450
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 2.1.1.242... |
A5EWT6 | MTDYFALKERPPYFPERVPCHILEHVPQGFYLAKHEQRWALCCTDKKPIHIDFTDTLYRRGGKEYLPKAFKNMNGKRIFDATAGWGRDSWLLACRGFQVTLCERQAYLYTLLAQAIELAKNTPETAATAAQLTLVYQDSCQYLRTTSTQFDAIYLDPMYPPRQKSAKVKKEMAILHILLDDEAGDTAENLLLLQTARARCARVVVKRPHTAPPLGNQVPRYCIDAPNTRFDVYLH | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27000
Sequence Length: 235
Subcellular Location: Cytoplasm
EC: 2.1.1.242... |
Q2MKA7 | MRLGLCVVALVLSWTHLTISSRGIKGKRQRRISAEGSQACAKGCELCSEVNGCLKCSPKLFILLERNDIRQVGVCLPSCPPGYFDARNPDMNKCIKCKIEHCEACFSHNFCTKCKEGLYLHKGRCYPACPEGSSAANGTMECSSPAQCEMSEWSPWGPCSKKQQLCGFRRGSEERTRRVLHAPVGDHAACSDTKETRRCTVRRVPCPEGQKRRKGGQGRRENANRNLARKESKEAGAGSRRRKGQQQQQQQGTVGPLTSAGPA | Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors . Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to incre... |
Q6UXX9 | MQFRLFSFALIILNCMDYSHCQGNRWRRSKRASYVSNPICKGCLSCSKDNGCSRCQQKLFFFLRREGMRQYGECLHSCPSGYYGHRAPDMNRCARCRIENCDSCFSKDFCTKCKVGFYLHRGRCFDECPDGFAPLEETMECVEGCEVGHWSEWGTCSRNNRTCGFKWGLETRTRQIVKKPVKDTILCPTIAESRRCKMTMRHCPGGKRTPKAKEKRNKKKKRKLIERAQEQHSVFLATDRANQ | Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increa... |
Q5M7L6 | MQFQLFSFVLIILNCVDYSHCQANRWRRSKRASYGTNPICKGCLSCSKDNGCLRCQPKLFFYLRREGMRQYGECLQSCPPGYYGVRGPDMNRCSRCRIENCDSCFSRDFCIKCKSGFYSHKGQCFEECPEGFAPLDDTMVCVDGCEVGPWSEWGTCSRNNRTCGFKWGLETRTRQIVKKPAKDTIPCPTIAESRRCKMAMRHCPGGTRTTKKKDKKNKKKKKKLLERAQEQHSVVLATDRSSQ | Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for lgr4-6 receptors. Upon binding to lgr4-6 (lgr4, lgr5 or lgr6), lgr4-6 associate with phosphorylated lrp6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increa... |
Q5R328 | MQLQLISIVLILHFMEYTNCQHHGSRHRGNKQVSGVSSQGCQGGCQTCSVYNGCLTCKPKLFIHLERDGMRQIGVCLASCPNGFYGTRSPDRNDCIKCGSECDSCFNRNFCLRCRAGSYLHKGKCMESCPDGLVPSDTKKECVAACPALCDLCQNSDTCTRCVPGHFLHAGQCHHVCPDEFEPNDSMECIPTVHCEVSEWSEWGTCSRSGKTCGFKWGEETRTRKVLQNPSPMGSPCPPTSEKRECFVKKKRCKPPKGQRRGEKKKRFNLQEKVTAEARRERKREREKETIDREESENRNKTEQRRRRDQSRDAGTV | Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for lgr4-6 receptors, which acts as a key regulator of angiogenesis. Upon binding to lgr4-6 (lgr4, lgr5 or lgr6), lgr4-6 associate with phosphorylated lrp6 and frizzled receptors that are activated by extracellular Wnt receptors, triggerin... |
Q2TJ95 | MHLRLISCFFIILNFMEYIGSQNASRGRRQRRMHPNVSQGCQGGCATCSDYNGCLSCKPRLFFVLERIGMKQIGVCLSSCPSGYYGTRYPDINKCTKCKVDCDTCFNKNFCTKCKSGFYLHLGKCLDSCPEGLEANNHTMECVSIVHCEASEWSPWSPCMKKGKTCGFKRGTETRVRDILQHPSAKGNLCPPTSETRTCIVQRKKCSKGERGKKGRERKRKKLNKEERKETSSSSDSKGLESSIETPDQQENKERQQQQKRRARDKQQKSVSVSTVH | Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors, which acts as a key regulator of angiogenesis . Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggeri... |
Q2I0M5 | MRAPLCLLLLVAHAVDMLALNRRKKQVGTGLGGNCTGCIICSEENGCSTCQQRLFLFIRREGIRQYGKCLHDCPPGYFGIRGQEVNRCKKCGATCESCFSQDFCIRCKRQFYLYKGKCLPTCPPGTLAHQNTRECQGECELGPWGGWSPCTHNGKTCGSAWGLESRVREAGRAGHEEAATCQVLSESRKCPIQRPCPGERSPGQKKGRKDRRPRKDRKLDRRLDVRPRQPGLQP | Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors . Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to incre... |
P40161 | MSKLFLDELPESLSRKIGTVVRVLPSSLEIFEELYKYALNENSNDRSGRHKKPRIDVSSDLLKTDEISETNTIFKLEGVSVLSPLRKKLDLVFYLSNVDGSPVITLLKGNDRELSIYQLNKNIKMASFLPVPEKPNLIYLFMTYTSCEDNKFSEPVVMTLNKENTLNQFKNLGLLDSNVTDFEKCVEYIRKQAILTGFKISNPFVNSTLVDTDAEKINSFHLQCHRGTKEGTLYFLPDHIIFGFKKPILLFDASDIESITYSSITRLTFNASLVTKDGEKYEFSMIDQTEYAKIDDYVKRKQMKDKSMSEELKAKSKSKG... | Function: Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF ... |
A0A364LXP7 | MSKVDVDLGDLLAKVLPTGVKVTIRHISSAPTPCTALFTPPPGEESESTFCENHFLTVSVNADEHDGPEIIVFGIEVLVYSTAHLTTVFVSKADSTGFLHLLKNAPKVSLIRRISNGFLSFLVQTHQRPGVRLVVSLFARAQNQYLFPGSIENSGKHVLDDRGLIKWWCRVVDPILREYEPESGSHEKGLLDRAMESAKSSATAFLIVPGCDKFETRGFFPGTAKSDDKERPRWLNSYPLHQLCDNTDAPPRCLVPRFPDDPKTRFLLDLDDELPQKLEAAGSKEGAGQWRSVKSLDQFWEMMSFRQECSAGRLVGFLWL... | Function: Histone chaperone-dependent acetylase that modifies 'Lys-56' of histone H3 (H3K56ac) . Histone H3 'Lys-56' acetylation may be required for S-phase-linked DNA damage tolerance (By similarity). Also acetylates 'Lys-9' of histone H3 (H3K9ac) . Autoacetylates (By similarity).
Catalytic Activity: acetyl-CoA + L-ly... |
Q5AAJ8 | MLPPDILQNGEFETIYFQTNPTYIKSPIHIPKSTIGKPDTVKIRHFFALLHQDLVVLGLEVFVYLQIYSDFVEKYVYVSKCDTVGLEKSTIKIGKVIGPVLQYIINYNGYKIKMKNLDEKSKDLSDPSTLVRLQRLRDKLPDIYPNLPYYNDIPPKEECIEYRTLPKTQNLRLCVFTKPAKEYLFPNSAKNPYKNLLNGQSLLRWWISIIDSITKGWNNHKLMIPGADKYATRKFIEKYSDWSEGHIFKKDGLAVQAIPLFPDDPKGRFLELVIVECRYGKMTVSRFYQELAYRQEFLLGDCVSLIGCCKENLEVTYHDD... | Function: Histone chaperone-dependent acetylase that modifies 'Lys-56' of histone H3 (H3K56ac), to promote genomic stability, DNA repair and transcriptional regulation during mitotic S-phase . Plays an important role in the regulation of white-opaque genotoxin induced-switching .
Catalytic Activity: acetyl-CoA + L-lysy... |
D3G9N3 | MDNLYTGISKSIESLPPEITFSYGYIFTNFKKLKWPWLNKRKIDNVYLSNHFFFILQEDAMAYAIEVLIFFSSELSVFYISKADSTGFFNRHGSPSPLKAVISTFLSYLIRRFSRKNIPSRISLFSRSQPQYLFPSSSLNPSKHILDDRELVRWWLKVLDSVNGSQCPKKYVLIPGMDPRETLKYTPQHVDTDLNWICGHPYESMGQSAGEIIPRFPDDPKTRFLDQLDRDGEVVSIDKFWELMAFRQECIHGRIVGFFSLEFPGNDQDGTNNTITEDLDLQNGIQINEKIYRMVYEKLLRSDFETLEKSKGATLDLIND... | Function: Histone chaperone-dependent acetylase that modifies 'Lys-56' of histone H3 (H3K56ac) . Histone H3 'Lys-56' acetylation may be required for S-phase-linked DNA damage tolerance (By similarity). Also acetylates 'Lys-9' of histone H3 (H3K9ac) (By similarity). Autoacetylates .
Catalytic Activity: acetyl-CoA + L-ly... |
Q9Y7Y5 | MPDLWSESILEGRKLSIYHLKSTLEKCPFLFGQSKKSKDFQFGSHLFLVEEQNVFIFGMECIVYEKNKEFIVFVSKADSTGFGSKGVSCNSLAFCCLVTLIDGLRKQGAENVTLTLFAIAQGQYLFPESVDNGQKHVLNDSGLLRWWVNCLEKLRKYYTDSEAPNDSEKQKNSTLLPKAYLFVPGLENIRSYLPNRHWIESNAITTGKAVEELPRFPDDPKCRYLCELQDEKSDMSVEEFWDTLTYRQECSSGKLVGFFTLQLQFYQTREFIAKDNFGDSGVMIPAKLYRVTYDTLLKHPFGSLSDAQSSTEKFLSNTLS... | Function: Histone chaperone-dependent acetylase that modifies 'Lys-56' of histone H3 (H3K56ac), which occurs predominantly in newly synthesized H3 molecule during G1, S-phase and G2/M of cell cycle . Histone H3 'Lys-56' acetylation is required for S-phase-linked DNA damage tolerance and proper silencing in pericentrome... |
P21771 | MSIVGRNAILNLRISLCPLFMGKRSFVSSPVSNSAKAVKFLKAQRRKQKNEAKQATLKASTDKVDPVLGRADTPFITRIMAELKEPLVLSKGYNIEEVDKFLAAIESAKRERAELSGLNTEVVGIEDIEKLEDRREAILRILSMRNSENKNAIKMAVELARKEFERFPGDTGSSEVQAACMTVRIQNMANHIKEHRKDFANTRNLRILVQQRQAILRYLKRDNPEKYYWTIQKLGLNDAAITDEFNMDRRYMQDYEFFGDKILIRDSKKVANQKRKEIRKQKRATF | Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitoch... |
Q12100 | MVKETPLHSSSSTSLSSLFRPTKLKNLSAKIFNGGGNQSYSKTDDVSRSSSRSSKKNTDSDQEDQIKYNKPNDRRSTIGKSPQGNGALSKESHVVASSTLTGISPTSAKKAPIDYSPSRPLPNNHNPVRTGHTVPHLPHSIHNPINYIHQGSKDAFHHPHPVRSTAHSNISTVSSAKSDTPSSNLSYQAHMHPVEILQKQIEDKHFMDSQASTPGSVELQHNSSSGSDDTSSRKKKSLRLTRFFKKIHNDYHDNHHHHHHHNRGSTPTKPKLNLNTNENIVESNGKALYETDNPVELLEKYGIPGRKLGEGASGSVSVVE... | Function: Probable serine/threonine-protein kinase that may be involved in ribosome biogenesis.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 69615
Sequence Length: 620
EC: 2.7.11.1
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P42159 | MWSSPGRNLESGRFNITPRYTGTLSNGSVSSSDKVALSQLTIFNVTVADEGEYTCSVDGESASFRVDLGDSNSSGSNSGVIAGVLITLLLLIALIIILICVFWVVWRYRRRGKFDLGSCRELSCSSCSCVPLLAALKGVKLPTRHRENLNKNGTRLRLNERNHIADTNTEIYSVVQKPLKKISKSPPPLPPLTLTETELNELMSIDEKEELSPIQEKPTRRNTGLSTYSQSGTIPKLAKLTKLRKFKMKENPIYQSADELELELELQVDNTLYALPSKPNSTRNSASFTDDLASDPIYSVAINPSMFTKRSSTIGNDDDL... | PTM: Phosphorylated.
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 67773
Sequence Length: 605
Subcellular Location: Cell membrane
EC: 2.7.10.1
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Q9LTQ0 | MDHSISPEYNFPAITRCSLSNSLPHRPPSPLPSSADIHRFYNSLSPSAPSVPVSSEMESMEAVEKILNYKFSNKSLLKEAITHTSCTDFPSYERLEFIGDSAIGLAISNYLYLTYPSLEPHDLSLLRAANVSTEKLARVSLNHGLYSFLRRNAPSLDEKVKEFSEAVGKEDDLSVSYGGLVKAPKVLADLFESLAGAVYVDVNFDLQRLWVIFRGLLEPIVTLDDLQKQPQPVSMLFKLCHKHKKRIDIKNWKDGNVSIAVIYLDDELLASGRAENKDIARLIAAKEALRKLSEVFPVEMVIDEDSVEIQLTHAKTKLNE... | Cofactor: Binds Mg(2+) or Mn(2+).
Function: Ribonuclease that cleaves double-stranded RNA (dsRNA). Required for 3'-external transcribed spacer (ETS) cleavage of the pre-rRNA precursors. May promote the production of 21 nucleotide small interfering RNA (siRNA) during post-transcriptional gene silencing (PTGS).
Sequence ... |
Q25520 | ALDDVQDGTLVTIKAGNDENVMAELRNCTAVMKNQVAKFNDLRFVGRSGRGKSFTLTITISTFPSQVATYSKAIKVTVD | Function: Plays a pivotal role in regulating the expression of other pair-rule genes such as eve, ftz, and h. Plays a role in the developmental pathways of sex determination and neurogenesis (By similarity).
Sequence Mass (Da): 8569
Sequence Length: 79
Domain: The runt domain is responsible for the DNA-binding properti... |
G5EFQ5 | MTNVFHHVRNFIEQQPAPAKTLEKSSSPNILYTALPKHWRSNKSFQEPFYVVLLTPVPDNTEVSIWAGNDEKPCEEVRNEKAKVHRQVAKFNDLRFVGRSGRGRKFHLTIVIHSAPMMVATVKNVIKVTVDGPRDARIPKPQGSLKRQAEQQTIFPNDIIRTPGPPMPMTMIPPPWFPLPMTQTFPPSFFPLISPGPHPSISAALWKIHSESMKTPIKQKVEQENVSLNTSTCLSSPSIFITPTSDDRKLKRPSSPRSITKSSETSINLIQETPESVESKRRRNVSITSSNSSSPTIWRPF | Function: Transcription factor (By similarity). Binds to regulatory DNA sequences in order to modulate transcription; negatively autoregulates its own expression, perhaps dependent upon CBF beta homolog bro-1 . Promotes proliferation, and prevents differentiation, of seam cells, a stem cell-like lineage, acting in conc... |
Q01196 | MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRM... | Function: Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-... |
Q03347 | MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDGGPALASKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDARQIQPSPPWSYDQSYQYLGSITSSSVHPATPISPGRASGMTSLSAELSSRLSTAPDLTAFGDPRQFPTLPSISDPRM... | Function: Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-... |
Q9XSB7 | MRVGVPPQIPRPSLNSAPSPFNPQGQSQITDPRQAQSPPPWSYDQSYPSYLSQMTSPSIHSTTPLSSTRGTGLPVITDVPRRISGASELGPFSDPRQFPSISSLTESRFSNPRMHYPATFTYTPPVTSGMS | Function: Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, pol... |
Q08775 | MLHSPHKQPQNHKCGANFLQEDCKKALAFKWLISAGHYQPPRPTESVSALTTVHAGIFKAASSIYNRGHKFYLEKKGGTMASNSLFSAVTPCQQSFFWDPSTSRRFSPPSSSLQPGKMSDVSPVVAAQQQQQQQQQQQQQQQQQQQQQQQQQQQQQEAAAAAAAAAAAAAAAAAAVPRLRPPHDNRTMVEIIADHPAELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGEVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKVTVDGPREPRRHRQKL... | Function: Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, pol... |
Q9Z2J9 | MLHSPHKQPQNHKCGANFLQEDSKEALVFKWLISAGHYQPPRPTESVSALSTVHAVIFKAASSIYNRGHKFYLEKKGGTMASNSLFSAVTPCQQSFFWNKTLPVAFKVVALGEVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKVTVDGPREPRRHRQKLDDSKPSLFSDRLSDLGRI | Function: Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, pol... |
Q13761 | MRIPVDPSTSRRFTPPSPAFPCGGGGGKMGENSGALSAQAAVGPGGRARPEVRSMVDVLADHAGELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGDVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPTQVATYHRAIKVTVDGPREPRRHRQKLEDQTKPFPDRFGDLERLRMRVTPSTPSPRGSLSTTSHFSSQPQTPIQGTSELNPFSDPRQFDRSFPTLPTLTESRFPDPRMHYPGAMSAAFPYSATPSGTSISSLSVAGMPATSRFHHTYLPPPYPGAPQNQS... | Function: Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-... |
Q64131 | MRIPVDPSTSRRFTPPSTAFPCGGGGGGKMGENSGALSAQATAGPGGRTRPEVRSMVDVLADHAGELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGDVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPTQVATYHRAIKVTVDGPREPRRHRQKIEDQTKAFPDRFGDLRMRVTPSTPSPRGSLSTTSHFSSQAQTPIQGSSDLNPFSDPRQFDRSFPTLQSLTESRFPDPRMHYPGAMSAAFPYSATPSGTSLGSLSVAGMPASSRFHHTYLPPPYPGAPQSQSGP... | Function: Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-... |
Q89U81 | MIGKLKGLIDSYGEDFVILDVGGVGYQVHCSTRTLQHLPSPGEAAVLSIETYVREDQIKLFGFRTDQEREWFRLLQTVQGVGAKVALAVLGTLAPSDLANAIALRDKAAVARTPGVGPKVAERIVTELKDKAPAFANVDPAVVHLAGAVDDQRAPRPVADAISALVNLGYGQPQAAAAIASASRSAGEGAETAQLIRLGLKELAK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
C0ZAN3 | MIDFVEGTLSYLDSEYIVIETGGIGYRLFCPNPYQFVRYEGNKTKLFTHHHVREDAILLYGFATRDERDLFRKLLDVSGIGPKGGLAILAAATPEQLVMAVQQENVTYLTKFPGIGKKTAQRIILDLKDKLVGYTPSAILTVAAGDLTAGEQAVSALNEALDALTALGYSDGELQKIRNTLSEKSKEGDGVEKLIKQGLALLMRG | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A5EXH7 | MIGWLQGRVLYKQNDQLLINVCGVGYELTVPQSVMASAQVGEELTVFVHHVQREDGQFLYGFSSFLQRQLFRELIRVSGIGPKLSIVILSGLTPEALIAAVRAQESAPFLRLSGIGKKTAERLLIELHDRVEKNDLFLCDESESSRAPIALSASEEAIQALIALELAPAEAELWVKKAQKTLAEDADSAALIKTAFALRLQGAK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A9BIJ5 | MIRKINATIEDFEDEKVLIKIGVLTLEAYPSLNVIRYFKKGDQYEFFASLEISEWNTSLYIFKDKIERDVFESLKKVSKIGPRIASKILRKTDAEEFIQMINSQDTALLSSLPGIGKKTAERLISELSNSFSAYSTGADTQSYGNNNLKEAIEALETLGFQRYEIMKVIGQLDLEDLKTEEIIKECLTRL | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q6LT49 | MIGRLSGTILEKQPPEVLIDVGGIGYEVQMPMSCFYELPEVGQAAVICTHFIVREDAQLLYGFNKKSERELFREVIKANGVGPKLGLAILSAMTASQFVLSVENEDITTLVKIPGVGKKTAERLVIEMRDRLKGWGEGDLFTPASDAAASNAEIQKYSSARAEDEAVSALIALGYKALQAAKVVSQVVKPEMSSENIIREALRSMV | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
B3R0J1 | MYSYIKGKVVNNGQNFVIVDNNNIGYHIIVSNPYFYEINKEYKFFVHFHIKENLQILYGFNDNKNLLFFKKLLDVPTIGPKSALMLSETDNLEQVFQAIENNDNVYLRKFPGIGIKSAQQIILKLKGDLIFSEKIILNPKKTELEKILLNLGFVKKEIKSVLNQIDDKKELELMLKEVLLKLAKNI | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
B2RJ07 | MIEYLKGAIVGLTPTNLVIECAGVGYDVNVSLTTYSAYQGKKEGLIWITQLIREDAHLLYGFSTKEERTLFGQLTSVSGVGPTTARLILSSYAPQELAALITTGQADALKAVKGIGLKTAQRIIVDLKGKIQLETSSDEILSARTAVGDAALNTIASGEEAISALKMLGFADPAIRKAVKSILSEDSSLAVEDIIKRALRML | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A3PCR4 | MISWINGDLVDLWQTNQKFFVLINCQGLGYEIQILESFFLKLRKNQISTKNITLWVKHIKKEDSDLLFGFTSNEQKNFFIEILSIRGVGSQIGIGILNKFSISEVINAIKTQDKKLICSVPGIGQKMSERLILELKSKFKSEILSEEEKSKGELEIKDPEINKMIEDLQLTLQSLSYKNKEINNILPIIIKEIDLLGKKENNLSFEKLLKLAMRYLDEDSSNIAR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q67Q98 | MIAHLRGELVTAGADWVVIDVAGVGYRCLVPASTRSRLPAQGAAVQLYTYLQVREDALTLYGFLTQAEYDLFELLLRVDGVGPKVALAVLSTTDPAAFRRAVAFEDLDAICRVPGIGRKTAQRLVLELKDKIGAVPAGGGGVPDGLPVAVAPAGDAWAEASEALIALGYSRGEAAAALARVRAEAGEAPSVETLVRLALKQLYRG | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q2LRA9 | MIAQIRGKLILKTVSMVIIDNHGIGYEVMIPLSTYYELPDVGSEVSLFVYTFFKQDSILLVGFCTENEKQLFKLMISVSGIGPRLAVNVLSGINSSELIHAIANNDLNRLLKVPGLGRKMAQRVILELRDKVSGWTSKEQITFINNKKDAIDQSVMEEDAISALINLGYKSQAAKDAIDRVISEGGENKSLDVILKKALKVLAM | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q3A231 | MIALLNGQLIEKTVSQVILDVGGVGYRLLIPLSTYYALPDEGDVRLRVHTHVREDALLLFGFLTETEKDLFGLLLSVSGVGPKVALNILSHLPAADLQQALSQGNAKHLATVPGIGKKTAERLVLELREKVGPVQAVPGNAPLPAETAGDLREDALSALVNLGYKENLSRKALDGIDTAPDAPLEDILKQALKLLMR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0LGY7 | MIGHLEGRLRHKAPDYIVIDVHGVGYIVYVPLSTFYDLPGPGDTVALNIHTHIREDAIQLYGFRTVAEKDMFLRLITVNGVGPRLAVNILSGLTPDDLHRIILQQEGFRLKSIPGVGKKIAERILLELRDKMSVKKGREAEQPAPAAESSYGDAYSALVNLGYRPAEAEKALGKAIKSLGADPPVEKLLKETLRLLA | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q2JWZ2 | MIAFLSGHLVAIEWGERSSLTVEVQGIGYRVKAPARFLKQLPPIGEPVRVFTHLVVRETELVLYGFGSPAERDVFVELIKVSGVGPALGLALLNTFGLPELVQAVVTENVRLLSLTPGVGHKTAQRLALELKTKLAHWRQGLENADRPLAGGPPPAIREEVEMALLALGYSLQEIQAALQALPSQPRPTEEWLRDAITYLSRQP | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A5GTL6 | MIGWLHGTIGDRWQEGNRCWLLLICGPVGYELQVSESLWRGTALESPTTVHTHLQQREDGQQLYGFETKADRNLFRLLISVNGVGPQVALGLISGLGAVSLLQAMAAEDVKVLCQAPGVGKRTAERLSLEWRSRLQERWQQQGGSTPLRLVEPVAESRELRATLEALGYGPEEVSAAVAQAGSQGLDPEQPMEEWLRHCLAWLSRQAG | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q3AVK0 | MIGWLQGRHMECWTQGNRSGVLLVCAGVGYEVQLTSRHQKQLQPDSELTLWIHQVQREDGSSLFGFPSRQERDLFRLLIGVNGVGPQAGLALLHECKPQELVAAISGGDLKRLCQAQGIGKRTAERLAVDLRTPIAAFGGLEPQPSLVEGLASEQIPEAGEDVEATLISLGYDELEIRRAIRAIADGASGVPPSGTDQDGWLRSCLQWLSRESA | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q0AX15 | MIAFLKGAVFERRPDSIIIDVNGVGYEVNIHSRLFPRLPQRGEPILIHTFLQVLENEFKLFGFLDQDELRLFKTLLTVSGIGSKGALAVLSTMEPLVFYRAIASQDEKTLVRIPGVGKKTAQRMIFELQDKVPELKLVEVEKEQRPLLDELMEALEILGYSRSEVLPAIMDLNRNKQLGNIVEENIKLVLKAKAQEMRR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
P73554 | MIQFLQGQVVTVTKNIQNRWFLILSVNGVGYELQVPHSLAQQWTPPPPEPQQVFTHLLVRQDQIALFGFGRLAERDLFGQLMGVTGIGAQLAIALIETLGLEGLVQAVVTGNVKQLCQTPGVGKKGAERLALELKTKLSQWHKLQMGTGETDSTLPTTALLEDLEMTLLALGYTQTEIQQAIAMVSQVPDVAQSEDPEVWIRQAIGWLSDH | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
B7GR18 | MNETTDYGASNTGANEESLRMVSSQPIGNEPASDEELRPHVLGGFIGQPRLKAQLQLFLDAARKRDVPPDHILLAGPPGLGKTTLAMIVANELEVPIRVTSGPAVQHAGDLASILSSLDTGEVLFIDEIHRLPRAAEELLYIAMEDFRVDVMVGKGPGASSIPLTLPRFTVIGATTREGMLPSPLRARFGFTAHLDFYPHDELQKLIERSANVLGVNLGDGSARELALRSRGTPRIANRLLRRVRDWAIVHDLIEVRSDDVKEALALYQIDSEGLDRLDIAVLDAIVRNFNGGPVGLNNLAAMVGEESETVETVCEPYLV... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
P70828 | MKDENSISFLSSNENYLYDKSENELRPKVFEDFKGQVNVKETLSIFIRASKERDEALDHVFLSGPPGLGKTTLASIIAFEMNASIKITSAPAFDKPKDIIGILTGLDEKSVLFIDEIHRLRPIIEEMLCIAMEDYELDWVIGQGANARTVRMPLPKFTLIGATTKPGKVTSPLYARFGITARFELYSEIELVEIIKRNSLILNIEIEEDAAFLLARSSRGTPRIANRLLRRIRDIAQVTGSLVITSDIVSIGLEMLRIDGEGLDEQDRNILRSLILKFNGGPVGVDTLAISVGETADSLEDFYEPYLIMKGFISRTHRGR... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
C0R250 | MDKESITNAEENSYDKPNNNIRPQGFDDFLGQNNIKSKLKVFINSAKKREVSLDHILFYGPPGLGKTTLAQIIANEMGSNIKATSAPIIERPGDLASILTTLGEKDILFIDEIHRLRTVVEEVLYSAMEDFFVDIKVGEGTSAKSFRVKLPHFTLIGATTRSGLLSTPLYDRFGIVERLEFYTNEDLANIVKRSSEFLNINITDEAAISIASRSRGTPRIVNRLLRRVFDFATVHDVLKIDEKFACDSLEKLGIDKNGFEALDKLYLNTIIKHYNGGPVGVDTLSVSLSEQIETIEDVIEPYLIQCGFIKRTPKGRVATN... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A2BZ00 | MAIISSSLDESNIPRSRKELRLVDSKIIADEKINKNLNIVRPTSFKEFIGQEQIKSSLKIAIDASKYRKEALEHTLLYGQPGLGKTTLALLISYEMNSKCRVASAPSIERPRDIVGLLLGLKEGEILFIDEIHRLNKLTEELLYSAMEDFRLDLTMGANRGARCRTINLPKFTLIGATTKLASISAPLRDRFGLCHKIEFYSNDELKQIIFNFSNLINLQLDSDACCSLAKISRGTPRIALRLLKRVRDYAQVMKKTNKISIEIIEKALDSQKIDNRGLDNVDRKFLSFLKLNNNNPIGLDSIAAGMGEESSMLEFVVEP... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
B5ZBT5 | MKTNNEFRPQYLKDFIGKDQLKSNLKIYLNATKRLKSSFDHTLLHGLAGTGKTTLATIIANEMGVDCHMTQGNLLNKPVDIINLLSLIKENDVIFVDEIHACGLAAFETLYSVLEDFCIDISIGKDFNAKMTRLKVPHFTLIGATTMLGKIPEPLEERFGHVFYLSEYETSEIAAIILKNNQIHFQINLNDQEIDLIANSAKGIPRLANRLLKRVVDFKINGFDNIKNIFEKIQIYDFGLEEQDINYLNVLYQQENEIGLKSIAQILRLDQYTIETKIEPYLIQHHFINKNLRGRKITAKGIEFLKNNQLIK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
B3CMH5 | MKSISCSKEYSEDVRNLNIRPEQLDDFVGQKDLIQNLKVFINAAQTRAEALDHVLLYGPPGLGKTTLAQIVSKELRVSFRATSGPLLSKAGDLAAVLTTLNAKDVLFIDEIHRLNRSIEEVLYTAMEDFCLDILVGEGPSTRTLRIDLPPFTLIGATTRLGLLSAPLRDRFGIPLHLEFYSFEELVDIIKRGARVLCAEIEKDAVQEIACRARGTPRIALRLLRRIRDFVEVKDDKKITCEIAGSALSKLGIDKMGLNKLDMDYLRFLFNTSGPVGIDTISIALSEDVGNIEETVEPYLIKVSFVKRTPRGRVLTDQARE... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q74E88 | MRVLGIDPGSRITGYGIIEKIGNRLVHVDNGAIHTDSHREFALRLHKIYEGLSRVIEEYRPDAMAVEQVFLAHNAQSALKLGQARGAAIVAGVSAGLPVSEYTAMQVKQAVVGYGHARKEQVQQMVKSLLNLPEIAQADASDALAVAVCHANSAVMKSVLRSIR | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q7NG73 | MCGMRILGLDPGVAILGYGVLDFFDSAPPVVCDYGIVQTSAKTAFEARLAAIYEDINSLFSAHKPDLVAIEKLFFYKMGNTISVAQARGVVLLCAAQHGVPYVEFSPPQVKLALTGDGRADKRAIQEAVQRELGLITMPKPDDAADALAIALTGWFHHLPPAAREAVPAYSVG | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
A1WZ63 | MTRILGIDPGSRVTGYGIVDDGRPTRLVTEGTLRLPRQAGLAERLGRIFDGLAELIAEHRPQEVALEQVFVHRNADTALKLGHARGAALTACVQAGLPVAEYAPARIKQAIAGSGRADKTQVGYMVRALLRLRTSPAEDAADALAAALCHAHHRSAPLTAATTGARR | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q92M90 | MQNTIRIIGIDPGLRRTGWGVIETLGNSLRFVASGTVTSDGELDLASRLCQLHDGLAEVVHGYQPHEAAVEQTFVNKDATATLKLGQARGIAMLVPARAGLRVAEYAPNAVKKAVIGVGHGEKQQIHMMLKVLMPKAEFKGNDAADALAIAICHAHNRQAVTSRLAALAG | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
A5V884 | MILIGFDPGLGTTGWGVIAADGNRLSHVANGQIKTEPSMELSRRLYLLHSALAEIIRTYRPEAAAVEEVLGNSNAQSTLKLGQARGVVLLAAALAEVSVGEYHPSIVKKAVVGTGGAEKRQVQAMVKVLLPGAKLSGPDAADALAVAVTHAHHLASARAMRRVVA | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q7US71 | MGTQVVTARPGSASCILGIDPGLNTTGYAVISREGPRLCLREAGVIKSRRSDTLPERLREIHVGLSEVFAVHAVDLMALEQLFSHYDRPRTAILMGHARGVICLAAASAGVPVEHYEPTRVKKVMTGNGRAPKSQIQLAVKMQLNLQSVPEPADVADAMAISLCGHYLANNPIDQALA | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q0S1C8 | MRVLGVDPGLTRCGFGVVDGGGGRTVTPIAVDVVRTPADLELSSRLLRISEAAESWIDLHRPEVVAIERVFSQHNVRTAMGTAQAGGVVALAAARRGIPVCFHTPSEVKAAVTGSGSADKAQVTAMVTRILKLAAAPKPADAADALALAICHCWRAPMIERMARAEAAAAEQKRRYQARLAEVKKAGTR | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q6NAT1 | MTAVSIRRPIRILGIDPGLRRTGWGVVDSDGNRLVYVACGSVEPRDTLPLAERLLAIHDGLAKVLAAHAPAEAAVEQTFVNKDGAATLKLGQARGVAMLVPAMHGLLVAEYAPNLVKKTVVGAGHADKTQIQMMLKILLPKADPKTADAADALAIAITHAHHRGAAQRLKAVGA | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
P17608 | MSENYSFSLRKFKLVFLGEQSVGKTSLITRFMYDQFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSSVAIIVYDITNHNSFVNTEKWIEDVRAERGDDVIIVLVGNKTDLADKRQVTQEEGEKKAKELKIMHMETSAKAGHNVKLLFRKIAQMLPGMENVETQSTQMIDVSIQPNENESSCNC | Function: Has a role in retrograde traffricking of proteins from the endosome to the Golgi. Involved in protein transport to the plasma membrane. Involved in the secretory pathway where it has a role in acid phosphatase secretion. Required also in normal glycosylation trafficking pathways.
Location Topology: Lipid-anch... |
Q27324 | MAPNLLTIGLLLTLIASGQAHLNIFLNLHEVLRLIGVSAELYYVREGAINDYALNFAVPVPANISDVTFTWQSLVDHPLPYSINIATSDTEVLPRPILNISRIGDVPVEPQTWGIALKCSGTRNAEVTVTINVEVILDRATNNNTNLIFKRKKICLREEQDSAHEEYDDDDLDLLQTARKGHGGDIHYVDRNDEHVVANGHQAPEKQRPVVTESPVGRGNSGGSKRDFDPMLRENLVPPASGLVTLIVGGILALVLVSTLILIAYCAKGPSKRHPSNGVHLIKTSSFQRLPTISSTAHNSIYVCPSTITPTYATLTRPFR... | Function: Probable coreceptor of Wnt proteins. Involved in neuronal pathway recognition and ventral muscle attachment site selection. Non-vital for development. May be part of a signal transduction cascade involved in learning and possibly memory.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L... |
Q9V422 | MESVNKCGKSASTRNCTVKMSRKMWVLSLLALAALQLHSGSEVAAHLNVFLNPVEVMRLLGVSAEVYYVREGHINNYALNFIVPVPANVKDISFTWQSLAGRGLPYSINVVSSDQEVLPRPAINVSHSGEIPTTIQTWSIALKCSGLKAAEVDVTVSLEVVLNRSLNNVTHLVFRRKKICLMNDSAEDLSEDVDDPQLLETVMLPPTGLITLVVGVSVAMGSVCLLLMIAYCVKGAANKRQHHQHGGQPMRTSSFQRLNTHPPCQSSMGSAAYMTPSIIAPIHGSSLPRKVPVSVEQQHPEELHRRISELTVERCRVRLS... | Function: May play an essential role in neuronal pathway recognition and ventral muscle attachment site selection.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 64938
Sequence Length: 584
Subcellular Locatio... |
P33497 | TTTVVNYTAKKSYCRRAVELTLGSLGVSSELQQKLQDVVIDRNALSLGKVLGEGEFGSVMEGRLSQPEGTPQKVAVKTMKLDNFSHREIEEFLSEAACIKDFDHPNVIKLLGVCIELSSQQIPKPMVVLPFMKYGDLHSFLLRSRLEMAPQFVPLQMLLKFMVDIALGMEYLSSRQFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTTKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYEYLFHGQRLKKPENCLDELYDIMSSCWRAEPADRPTFSQLKVHLEKLLESLP... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 49108
Sequence Length: 442
Subcellular Location: Host cell membrane
EC: 2.7.10.1
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G5EGT9 | MILRYLIFFAQLWALCLANVNMFISKEEMNRTFGVKAELNYIEMGNVSSYSTKFHYRVMANIDYLSFTWNAVGIVHYEVYVESDDSSVLPIVRIPLKGTVPESLQDFTVEYRCAGHRSGQFAVSLYFTFKYGNKEPLKVKLRQEKICASRDGRRGLNGGYEGHEVDDTDSIDKAFFVIICIAAAFLLIVAATLICYFKRSKKEDMIPTRLPTSFRNSLKSTKSAQPFLLSTPRDGPPTLSAISSAPCSSSSASGNSIIPSKPRNIDVRRALLQLYQDRDAFQSLPLDMEGTFGEVRYAIWRQVDDVLNGDVDDEEDTFCN... | Function: Has no detectable kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo (By similarity). Receptor which may act as a receptor for Wnt ligand mom-2. Plays a role in controlling P7.p vulva precursor cell lineage orientation during vulva development . Regulates pop-1 asymmetric distri... |
Q01887 | MRAGRGGVPGSGGLRAPPPPLLLLLLAMLPAAAPRSPALAAAPAGPSVSLYLSEDEVRRLLGLDAELYYVRNDLISHYALSFNLLVPSETNFLHFTWHAKSKVEYKLGFQVDNFVAMGMPQVNISAQGEVPRTLSVFRVELSCTGKVDSEVMILMQLNLTVNSSKNFTVLNFKRRKMCYKKLEEVKTSALDKNTSRTIYDPVHAAPTTSTRVFYISVGVCCAVIFLVAIILAVLHLHSMKRIELDDSISASSSSQGLSQPSTQTTQYLRADTPNNATPITSSSGYPTLRIEKNDLRSVTLLEAKAKVKDIAISRERITLK... | Function: May be a coreceptor along with FZD8 of Wnt proteins, such as WNT1, WNT3, WNT3A and WNT5A. Involved in neuron differentiation, axon guidance, corpus callosum establishment and neurite outgrowth. In response to WNT3 stimulation, receptor C-terminal cleavage occurs in its transmembrane region and allows the C-te... |
P41924 | MSHSQRTYDLLIKLLLIGDSGVGKSCLLLRFCEDQFTPSFITTIGIDFKIRTIDIGNQRVKLQVWDTAGQERFRTITTAYYRGAMGILLVYDVTDEKSFNNIENWYQNVQSYANEGVELILVGNKCDLDEKRVVSTEQGQALADKFGIPFLEASSKTNINVEECFYSVATRIRDTVAKTKGNESGSGGINIAEGEENSASKCC | Function: Protein transport. Probably involved in vesicular traffic (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 22608
Sequence Length: 203
Subcellular Location: Cell membrane
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P41925 | MESMDAKIVLLGAQGVGKTCFVTRYVNNKFQAGQASTIGASFSRKRVVVNDTTVRLQIWDTAGQERFRSMAPIYYRSASCGILCYDVTSRASFDAMHLWLLELKQNLSSDIIIHIVGTKVDLVKDEPSLREVPFEQCVEYASEWLQDDSCCHEISAKDDEGVEEVFEVIITKLLDKREADEQQKHNSQRQRQSVVYLHTDEDEQKSSCC | Function: Protein transport. Probably involved in vesicular traffic (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 23768
Sequence Length: 209
Subcellular Location: Cell membrane
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Q9Y6Y8 | MAERKPNGGSGGASTSSSGTNLLFSSSATEFSFNVPFIPVTQASASPASLLLPGEDSTDVGEEDSFLGQTSIHTSAPQTFSYFSQVSSSSDPFGNIGQSPLTTAATSVGQSGFPKPLTALPFTTGSQDVSNAFSPSISKAQPGAPPSSLMGINSYLPSQPSSLPPSYFGNQPQGIPQPGYNPYRHTPGSSRANPYIAPPQLQQCQTPGPPAHPPPSGPPVQMYQMPPGSLPPVPSSVQSPAQQQVPARPGAPSVQVPSPFLLQNQYEPVQPHWFYCKEVEYKQLWMPFSVFDSLNLEEIYNSVQPDPESVVLGTDGGRYD... | Function: Plays a role in the organization of endoplasmic reticulum exit sites. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P) and phosphatidylinositol 5-phosphate (PI(5)P).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 111076
Sequence Len... |
O75746 | MAVKVQTTKRGDPHELRNIFLQYASTEVDGERYMTPEDFVQRYLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAFESVLCAPDSMFIVAFQLFDKSGNGEVTFENVKEIFGQTIIHHHIPFNWDCEFIRLHFGHNRKKHLNYTEFTQFLQELQLEHARQAFALKDKSKSGMISGLDFSDIMVTIRSHMLTPFVEENLVSAAGGSISHQVSFSYFNAFNSLLNNMELVRKIYSTLAGTRKDVEVTKEEFAQSAIRYGQVTPLEIDILYQLADLYNASGRLTLADIERIAPLAEGALPYNLAELQRQQSPGLGRPIW... | Function: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle . Also mediates the uptake of L-cysteinesulfinate by mitochondria in exchange of L-glutamate and proton. Can also exchange... |
Q9UJS0 | MAAAKVALTKRADPAELRTIFLKYASIEKNGEFFMSPNDFVTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALFMVAFQLFDKAGKGEVTFEDVKQVFGQTTIHQHIPFNWDSEFVQLHFGKERKRHLTYAEFTQFLLEIQLEHAKQAFVQRDNARTGRVTAIDFRDIMVTIRPHVLTPFVEECLVAAAGGTTSHQVSFSYFNGFNSLLNNMELIRKIYSTLAGTRKDVEVTKEEFVLAAQKFGQVTPMEVDILFQLADLYEPRGRMTLADIERIAPLEEGTLPFNLAEAQRQKASGDSARP... | Function: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle . Also mediates the uptake of L-cysteinesulfinate by mitochondria in exchange of L-glutamate and proton. Can also exchange... |
Q9QXX4 | MAAAKVALTKRADPAELKAIFLKYASIEKNGEFFMSPHDFVTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALFMVAFQLFDKAGKGEVTFEDVKQIFGQTTIHQHIPFNWDSEFVQLHFGKERKRHLTYAEFTQFLLEIQLEHAKQAFVQRDNAKTGKVSAIDFRDIMVTIRPHVLTPFVEECLVAAAGGTRSHQVSFSYFNGFNSLLNNMELIRKIYSTLAGNRKDVEVTKEEFALAAQKFGQVTPMEVDILFQLADLYEPRGRMTLADIERIAPLEEGMLPFNLAEAQRQQKASGDAAR... | Function: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle (By similarity). Also mediates the uptake of L-cysteinesulfinate by mitochondria in exchange of L-glutamate and proton. Ca... |
F4JUU5 | MEISGRRMRRFRMRFRRDHLTGGENIENEASCCYCDLKISNFNEPIFRLGRRFSGVLKVWFSIGLGFGVASLILVTVFLLLQFHSNPLFSNRLTSAVFGFSPSTRVSLSGIAYVLVSTVITVSVHELGHALAAASEGIQMEYIAVFIAAIFPGGLVAFDNDVLQSLPSFNALRIYCAGIWHNAVFCALCVFALFLLPVMLSPFYKHGESLTVVDVPSVSPLFGYLSPGDVIVSLDGIQVHKPSEWLELAAILDKENSKTSNGSLYLGGSRRFHHGKGYCVPISLIEEGYKGKMVENQFVCPGDLTAFRTMPCSNAAIREV... | Function: Metalloprotease that catalyzes the second step (site-2 cleavage) in the proteolytic activation of various factors, after site-1 cleavage. Part of a regulated intramembrane proteolysis (RIP) cascade. After ER stress, cleaves BZIP17 and BZIP28 proteins which functions as stress sensors and transducers in ER str... |
Q2TAD4 | MNGFSTEEDSRDGPPAQAAPFFGQTCCLIDGGERCPRPAGNASFSKRVQKSISQKKLKLDIDKSVRHLYICDFHKNYIQSVRNKRKRKTSDDGGDSPEHETDVPEVDLFQLQVNTLRRYKRYYKLQTRPGLNKAQLAETVSRHFRNIPVNEKETLAYFIYMVKSNRSRLDQKSESSKQLDA | Function: Functions as transcription repressor, probably via its interaction with histone deacetylase complexes. Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus. Binds DNA, apparently without sequence-specificity, and bends bound double-stranded DNA. Binds ... |
Q6ZUB0 | MENILCFLNSYTETGLSPDSHCLDIDLNFICLSGLGLFILYLFYMVLTLYSSPTEKNNDTQKHQGRARRKRKSVTFKDRKSLQKEAEEERKLHSFLKSFGPPVSCSPLGQHHDTTLFRRLLCPDPVCRVCNRATADIQRLLSWESLKDAAPSVSPLASSASGAESSFTLASTPSATTPEDLILSSRPKPSPPPPLILSPDLITTLADLFSPSPLRDPLPPQPVSPLDSKFPIDHSPPQQLPFPLLPPHHIERVEPSLQPEASLSLNTIFSFGSTLCQDISQAVNRTDSCARHHGPPTPSALPPEDCTVTQSKSNLTVLKT... | Function: May play a role in spermatogenesis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 102306
Sequence Length: 917
Subcellular Location: Membrane
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Q869W7 | MIFDSLISLIPISMIMVGCCSNVISLELIMKQSQSHAILVTFFQFATVAFISFFVNIRWKQVFSIFWIPIGLRERKIPLKTYFLMVSIFFILSVLNNKALDCDIPIPFHMIFRSSSLLSTIVIGSIFYRKSYSKQQILSLIMVTLGIIFATFSSMPDSKKEISLGHEPNLLRFSIGMLMLIAAMFLSSILGLIQEHTYKLYGKDRHYETIFYSHLFSLPFFLLFKDDILHHIQLNNDSALMALPFGFGSFPTLWVYLIVNVLTQYVCIQGVFILTGKTSTLTCTLVISIRKFLSIIISVIYFNNHFTSLLFTGTILVFLG... | Function: Sugar transporter that specifically mediates the transport of UDP-N-acetylglucosamine (UDP-GlcNAc) from cytosol into Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40145
Sequence Length: 351
Subcellular Location: Golgi apparatus membrane
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Q9W429 | MALNLKALLGMLFVFIGCCSNVVFLELIIQIDPGAGNLITFAQFLFIALEGLVFTSKFFTVRPKIALKDYVILVALFFGANVCNNYAFNFNIPMPLHMIFRSGSLMANMIMGIVLLKKRYNLRQYSSVAMITAGIILCTLVSSGDVKDNTHHSLKVDTSYSDFFWWTVGIGLLTIALLVTAYMGIYQEVIYKKYGKHPSEALFFTHMLPLPGFLIMAGNIVQHFGIAWSSEPVAVPLLGAIGLEWKFPLMLFYLLCNVVTQYVCISAVYVLTTECASLTVTLVVTLRKFVSLLFSIIYFRNPFTLNHWVGTILVFFGTIL... | Function: Sugar transporter that specifically mediates the transport of UDP-N-acetylglucosamine (UDP-GlcNAc), GDP-fucose and UDP-xylose. Functions redundantly with nac in the O-fucosylation of Notch, positively regulating Notch signaling. Involved in the biosynthesis of heparan sulfate-glycosaminoglycan (HS-GAG) and in... |
Q969S0 | MRPALAVGLVFAGCCSNVIFLELLARKHPGCGNIVTFAQFLFIAVEGFLFEADLGRKPPAIPIRYYAIMVTMFFTVSVVNNYALNLNIAMPLHMIFRSGSLIANMILGIIILKKRYSIFKYTSIALVSVGIFICTFMSAKQVTSQSSLSENDGFQAFVWWLLGIGALTFALLMSARMGIFQETLYKRFGKHSKEALFYNHALPLPGFVFLASDIYDHAVLFNKSELYEIPVIGVTLPIMWFYLLMNIITQYVCIRGVFILTTECASLTVTLVVTLRKFVSLIFSILYFQNPFTLWHWLGTLFVFIGTLMYTEVWNNLGTT... | Function: Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for another nucleotide sugar. May couple UDP-alpha-D-glucuronate (UDP-GlcA) or UDP-alpha-D-xylose (UDP-Xyl) efflux to UDP-alpha-D-glucuronate (UDP-GlcA) influx into the ER lumen, which in turn stimulates gl... |
Q9NQQ7 | MGRWALDVAFLWKAVLTLGLVLLYYCFSIGITFYNKWLTKSFHFPLFMTMLHLAVIFLFSALSRALVQCSSHRARVVLSWADYLRRVAPTALATALDVGLSNWSFLYVTVSLYTMTKSSAVLFILIFSLIFKLEELRAALVLVVLLIAGGLFMFTYKSTQFNVEGFALVLGASFIGGIRWTLTQMLLQKAELGLQNPIDTMFHLQPLMFLGLFPLFAVFEGLHLSTSEKIFRFQDTGLLLRVLGSLFLGGILAFGLGFSEFLLVSRTSSLTLSIAGIFKEVCTLLLAAHLLGDQISLLNWLGFALCLSGISLHVALKALH... | Function: May play an important role in the cellular response to tissue hypoxia. May be either a GDP-fucose transporter that competes with SLC35C1 for GDP-fucose, or a factor that otherwise enhances the fucosylation of Notch and is required for optimal Notch signaling in mammalian cells.
Location Topology: Multi-pass m... |
Q9NTN3 | MAEVHRRQHARVKGEAPAKSSTLRDEEELGMASAETLTVFLKLLAAGFYGVSSFLIVVVNKSVLTNYRFPSSLCVGLGQMVATVAVLWVGKALRVVKFPDLDRNVPRKTFPLPLLYFGNQITGLFSTKKLNLPMFTVLRRFSILFTMFAEGVLLKKTFSWGIKMTVFAMIIGAFVAASSDLAFDLEGYAFILINDVLTAANGAYVKQKLDSKELGKYGLLYYNALFMILPTLAIAYFTGDAQKAVEFEGWADTLFLLQFTLSCVMGFILMYATVLCTQYNSALTTTIVGCIKNILITYIGMVFGGDYIFTWTNFIGLNIS... | Function: Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for either their cognate nucleoside monophosphate or another nucleotide sugar . Transports various UDP-sugars including UDP-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc), UDP-N-acetyl-alpha-D-galactosamine (UDP... |
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