ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P91247 | MAVDMIVEPKWVVQNFGNIRILDASWTFKPKADVAEYKAKYYNKFGVGMNELKNPEYLAEHINGAAHFNFDIAYYPSEDERFTLYTPEEFSSYVKRLGVFNGDHLVIYGRGKDGGMAAASRAYWTFRYYGYTTVSVLNGGIEAFKLAQGVVQSDSKAEGIRCKDAIHFPIGEVCAAKGFKKKTDCDQAFAAKGIKVGDTVVISCGIGLSASAICLAAARSGIVAKLYNGGVHELAYKAPQHLNMRVTLLLHAITVLRCTYIHFTFLYAIVIKIERIV | Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 30699
Sequence Length: 277
Domain: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-termin... |
O17730 | MSLKKIIDVKSVNTLLKKGIINKEGVRIIDCSFAVAPRPDWKEFEQEGYGDFKNLMAEPSPSRNLYLAGHIPEAVHVDLDIATYPSRYQRFQQYRADLFEEYAQMVGLNNKEHFIFYGKGAFGGMLFASKVAWIFKSYGHENISLVDGGFDSWKRNGFEVSTELVKLPAGNFKAEDNFKKYVITFQELEAKKDGEDKQFIEKTSEINFLDSRIRGQFDGTQETGLDPHLVNGTRIAGFKNLPSAELLVKGGNLKSEEEIKSWLTQNGYVENQPTITSCNAGIQAALLAYVIDAVKPSQNPPRVYNGSLKEMELRAPKKIS... | Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 36948
Sequence Length: 328
Domain: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-termin... |
P46700 | MPLPTDPSPSLSAYAHPERLVTGDWLYFHLGKPGLAIVESDENVLLYDVGHIPGAVKVDWHTDLNDPKVRDYITGEQFADLMNRKGIARDDTVVIYGDKSNWWAAYALWVFTLFGHPDVRLLNGGRDLWLAERRDTSLAVPNKTSTSYPVVNRNDAPIRAFKDDVLAILGTQPLIDVRSLDEYTGKCTEMPDSPEESVLRAGHIPTARSIPWEMTVDKSGRFRSSEELERLYDFITPNDKTIVYCRIGERSSHTWFVLTHLLGKPGVRNYDGSWTEWGNTVRVPITAGESPGAVPV | Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 33235
Sequence Length: 296
Domain: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-termin... |
Q729U4 | MPRTEPRVELLAHTPEPLSLLYAAFRQCYHAGFVADMWPRLLSGEIEREKQGAFIASILESGHSSPIEHVSFTFAIEGVSRALTHQLVRHRIASFSQQSQRYVDGSHFDYVMPPAIARNAAAKARFEQFMEDVGSAYRDIKALLEQDGRTGSRANEDARFVLPQAAASKIVVTMNCRALVHFFEERCCMRAQWEIRAVADVMLGLCREVLPELFAHAGAKCERLGYCPEGERFTCGRYPLRQSMP | Cofactor: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as... |
Q5HAK2 | MLVLSIRIKVWQTMESEITKRIVVPELEDILYKEHKVLDKGFVRLVDYMGSDESVVQAARISYGRGTKSVSQDAALINYLMRHSHTTPFEMCEIKFHIKLPIFVARQWVRHRTANVNEYSARYSVLDHEFYIPELDHVATQSEDNAQGRGNSLSNEDAQYVTDLLKRDSDMVYETYNKFLIKGVSREISRISLTLNYYTEWYWKIDLHNLLHFLRLRSDVHAQYEIRVYAETMLEIVKKWVPLTYAAFVEYCLESQSFSKSALSVVKKLIAGEDVAREDTGIGKREWRELMDVLADNK | Cofactor: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as... |
Q748A9 | MKIALLQHTPDPEAAVALAARLCYASVGIDELREKLSASDVTAFLDKIMSLGHQSVLEHASFTFGIEGISRAASHQLVRHRIASYSQQSQRYVTFRGDGFPRVVPGSVSATEKRRQVFESAMQACADAYRALVDDGVPAEDARFVLPNAAETKIIVTMNARELIHFFGLRCCERAQWEIRALAVEMLRLVKGVAPTIFRDAGPGCLTGPCPEGGMTCGKAAEVKRLFREMSI | Cofactor: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as... |
Q9HQ52 | MRVRLLEATENPEELICQSARNDYMSDWVGDTPLDTAMASVDGDTTDEKLSNLIAQLLTRGHYGPFEHPSATFAIEGVSRSCMAQLTRHRHASFDVQSMRYVAFDDVDPAAVAEGELVVTPPSATDPDWVGRNQDAGDIDEETMAEREAVFQASVRRAVEDYQELLGLGMPPEDARFVLPIGTEVNVVITLNPRSLMHVADMRAAADAQWEIRELTEQLLDAAAQWCPHTFEYYDAEMKHRKNRLAP | Cofactor: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as... |
O26061 | MEVICKHYTPLDIASQAIRTCWQSFEYSDDGGCKDKELIHRVGNIFRHSSTLEHLYYNFEIKGLSRGALQELSRHRIASLSVKSSRYTLRELKEVESFLPLNETNLERAKEFLVFVDNEKVNAMSVLALENLRILLSEHNIKNDLAKYAMPESYKTHLAYSINARSLQNFLTLRSSNKALKEMQDLAKALFDALPGEHQYLFEDCLKH | Cofactor: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NAD(P)H and FADH(2) ... |
C5CHB8 | MEIKVLEKGFIRLVEVMGDDFSAVQAARVSYGKGLTTPERDKKLIFYLMEHGHHSPFEHIIFKFHIKLPIFVMRQLVRHRIASINERSGRYTEFSDEWYIPERIRTPDKVNRQGSVFVDDDDLNSEGIRLIEETIEKTYQAYKRLLEMGVARELARIVLPTSMYTECYWTINARSMMNFLNLRADSHAQYEMQQYALAVAKIFKSKCPVTYEAFLNFAYTGDLLKTEGCL | Cofactor: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as... |
B2HKZ0 | MAETAPLRVQLIAKTEFLAPPDVPWTTDADGGEALVEFAGRACYQSWSKPNPKTATNAGYLRHIIDVGHFAVLEHASVSFYISGISRSCTHELIRHRHFSYSQLSQRYVPEGDSRVVVPPGLEDDPELREILIAAADASRATYTELLTKLEARFADQPNAVLRRKQARQAARAVLPNATETRIVVSGNYRAWRHFIAMRASEHADVEIRRLAIECLRQLVAVAPAVFADFEVTTLADGSEVATSPLATEV | Cofactor: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as... |
P31563 | MTLKMFLPVNLVSVCMKLNNSVVMVGLYYGFISAFSIGSSYLFLLRPRFLNDDPDAIEKKASETAGFFTGQLLIFISILYGPLHLALGRPHTILLLLAPYFFFHFLSSNSGQYPSQRFAFPLLTKSMRNRSFQLVFLHSLLFQLFSLSVLGRPMLTRLSYIYIFRSNNKMLFVLSSFVGWLIGHILVLKWAGLVFVWLLKFIRSKTMKYITCNVLIPATKYIIEKWRNSFVAGLIREILAMKQVESALVRIKNSRLLDDVRWWIRGSGLISGLKINIRFYARLILRGFENVYVGAKFRQDMEHLFSIILFAFFLLYLDRT... | Function: Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 117043
Sequence Length: 1005
Subcellular Location: Plastid
|
Q6FEP9 | MQVTTEAVSGVARRLNVSVPTSRINEQFEARLKRTAKTAKINGFRPGKVPLSRVRSDFGPGIYQEVVNDIIRDTVFEAIQQEKINAVGMPNIEKVEHKDDALVYEATVEVYPEVEVKAFDTLEVERKAAEINDKDVDAMIENLQKQRQTWAVTKGMAKKDMQVTFDFEGEVDGEKFEGGSAEDFKLVLGSGRMIPGFEDGIIGMKAGEEKVIDVTFPEDYQAANLAGKAAKFKITVKQVEKPKLPEIDAEFLKIFGISEEDGVEKLKADVRKNMEREVRNGLRNQVKQAAFDALVAANEIDVPSAMVAQEIDRQREQMIQ... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49694
Sequence Length: 4... |
A0LSU9 | MKSAVETLSPTRVKFTVEVGFDELQPTVAAAYRKVAEQVRVPGFRPGKVPPPIIDRRIGRGVVLEQALNDAIPQFYGQAVDEAAVAVISQPEIEVTNFADGEGLTFTAEVDVRPTIELPDPESITVTVDPVTVSDADVDAELAALADRFATLKPVDRPARRGDFVTIDMTVRLDGEVLEDGTVTGASYEVGSAQLVEGLDEALEGLTAGQSAEFDAPLAGPYAGRTARAEVTVRAVREKQVPALDDAFAQQASEFDTLEELRAHIRERIGRTRRIQQHVQARERLLQTLLDSLDIPVPERIVDAEVRSRAEQLRRYAEAR... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48930
Sequence Length: 4... |
Q0SMP7 | MILSKDIRLLPGSKVEAVIRVSKNIIQEKYNSLLQDYSSRLKIQGFRIGKVPISIIEKKYSEGLRATVLEEVINNSLKEFFKEEPKRPLSYASPTIKEENLRLNLDKDFEFTFVYETYPEFKVPNIDDIDIKVEVPEVFIDDSDIDNEIKSLQIENSIIIEDEEGVVKKDSIVKVDFVELDDLLNEIVSTKRQDFVFTVGKSETYYDFDRDVIGMRINEERVIEKSYITDYKFEELAGSLKKLKIKIKSIKKRDLPLIDDEFAKDISERYNTLDDLKNFIRSKILSLVEEKKEALKLNKFFSTISEKLEIDIPRSMIEAE... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 52842
Sequence Length: 4... |
Q89KG0 | MQVTETLSEGLKHEFKISVPASDLDAKAGAKLVDLKDKVRINGFRPGKVPVAHLKKVYGRSVMAETIDQTIRDTNTQLFSERGFRLATEPKITMPSEQAEVEELLSGKTDLTYTVAIEVVPSIALADFKTFQVEKPVADVTDADVDEAIKRIADTNRGYAAKADGAKAESGDRVTINFKGTINGEVFEGGTGEGIQVVIGSNTFIPGFEEQLTGIGAGETRTLKVSFPKNYMNDKLAGQPAEFETTATSIEAPQDIAIDDEFAKTLGLESLDKLKEAARERLVAEFAGATRQRVKRALLDRLDEAHRFEAPPSLVDEEFN... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50091
Sequence Length: 4... |
Q2GFT7 | MLNSYVVREVSNDKLKWEYEFAVDKKYFLDQLDSKLSEIAMNVKVPGFRVGKASIDLVRKEYLNEAMTSVVKKTIESTSSDFVKNSKFGEIISSNIDIVSYPSYYSDNDKEEDLVYKLSFEVMPEAPLMDIDNIVLSDIEVDIQECDVNEFIENLKKQRPDFVIVDDPEYVIQGSDKLVIDYQNKIKGKILRGGSAKDFVLVLGKGVALREFEDQLIGMKVGESKTFPLTFPNDYGMVHLAGKTTDMSVTVKSVYVMKGMRDSEAIAKDYGFKDVGHMEDFARKRIKQQFDQMVFTIVKKELFDYMDANYVIDVPECVVT... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50188
Sequence Length: 4... |
Q2NDC7 | MQTKETTNEGLKRAYKLTLTAKEIDAKIDAEVKKVAPQVRMPGFRPGKVPANLVRKMHGEQMHAQVINDSIRDSVDALIKEKELRPAMQPKIDLNEDYEQGKDAVVSVSLEILPKVEAPSIDDLKLERLTVPVSDEQVMETIERIAGQNKSYKDAAKTRKAADGDQLIIDFTGSVDGVEFEGGKAEDAPLVLGSGTFIPGFEEQLKGVKTGDEKTITVTFPKDYQAENLAGKEAQFDVKVKQVKVETDTTIDDEFAANLGLENLDKLKELIRGQLEQETNGLTRTAMKRSLLDQLAAGHDFPVPEGMVDAEFEQIWNQLQ... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 58814
Sequence Length: 5... |
B0S2N7 | MSAVLVSKENNQAVFTCEIPAEDFNNAIEESYKKNRSRFSLKGFRKGKVPRKMLERAYGEGLFYEDAVNLLLPGIYEKAIEELELEPVSQPDIDLDDITENNDVKVKFTVDLKPEFELGDYSKLSAEIEEFKVTDSDVDMKVNHELESNARVQEVEGREAKENDTVSINFKGFVDDKAFDGGEAEDYELVLGSHTFIPGFEEQIVGHNAGDEFDVNVKFPEDYHEDSLKGKDAKFECKINSIKEKVLPELDDEFVKDVSEFDTLDEYKKDIKEHLEKDNEQRQLVEKQNKAVEALIEATEISVPESMIDNEVNRQFQDFA... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50867
Sequence Length: 4... |
Q0RPH4 | MKATKETLSPTRVKLTVEVPFDELKPSLDATYRKLARQVRVSGFRPGKVPPRILDQRLGRGVILDEAVQEALPQLYSEAVQAEEVDVLSRPEVDITEFADGGQLVFTAEVDVRPEVALPEFADLSVTVDAVEVTDEQVEEQLGALRDRFAQLQPVERAVQTGDFVSLDLSAQADGKPIEGAEATGLSYEVGSGNLIEGLDEAIVGAADGESRTFTTELLAGDQAGQQAEVTATVRGVKEKELPALDDDFATTASEFDTLDDLRGDVRSRLEQSRRTEQVGQAREKLLESLLERVDVPVPDSLLAGEIEAREHRLSHELEN... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 53253
Sequence Length: 4... |
B0TZA4 | MQVTVEKKEGIHCSLLIEVPANEVDSIVTKEINKTAKTIKMDGFRPGKVPAGMVEKKYGEQIRMEVISDLIPQKYSKAIQDEKLAVAGIEVELKENKKGEPLKFVANLELFPEFEVTGFEKIEVQKPVVELTDKEVKQMIENLRKQLATFSEVERAVQKDDKVVIDFVGKRDGEVFEGGSANDQELVIGSGQMIPGFEDGIIGMNKDEQRTITVTFPEDYQNKDLAGKEATFDITVKKIQEAQLPEVDDEFVAKFGVKGGVDTFEDEIKENMQRELKFILQRKVKDQVFKGLREIAEFETPKALIKREIDAAKQNLVKQM... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49614
Sequence Length: 4... |
Q4FM95 | MKVTVENKKGLNKDIKVFIDKETMNSYMDEKYEEIKKTVNLKGFRPGKVPKEVLKRQFGQAIFSEVLDKVLKDTSVKALEDNKIKPAGQPKLDLKTYGEDKDLEYVMSITELPKVELKSVENIKFDEYSVKIDTNETDKRIKEIAKSQNNFKEVAADVRAVEENLVIFDYKATIDGKDFTGGEGKNTQLILGKDLFIKGFDKQLIGVKKNDEKSVDVTLPENYPQKEYANKKANFICKITEVKKSEEVKIDDVFAKNLGAKDLADLKVLVSKQINDEYKNSLDKLAKTQILKEIENFKVDEIPENLIEEEVKILSQGMTE... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 54804
Sequence Length: 4... |
A3PFE3 | MAKDALIVKTTPLPQSRISFELEIPSETCKTCVNETISTISRSAKIPGFRLGKIPKQVLIQRIGITQLHASALEKIIDKSWQEALKIKSIEPLSEPELVDGFESLLAKFSPEKSLKVTLQTDVAPELKLKKSKGLSVEISKTKFDPKSIDEALEKSRNQFANIIPVTNRAAKLGDIAVVSFKGKYKDSGKEIDGGTSESMDLELEKNKMIPGFVEGIVKMKIGDTKTLNLKFPEDYSHEDSRGKEAIFEVNLKDLKEKELPELNDDFAKQSGNKESLKELKKDIEKQLKDNFEKTQKDIKIEALLDALTNELVTEIPKSM... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 53584
Sequence Length: 4... |
A2C5C0 | MSAAKLNVKTSSKPNSRIAVEVEVPANRCKNSYDEALSKLSRSISIPGFRKGKVPKTVVIQQLGVKRIQASALESLLQKVWTETLDQEGIEPLCEPELEDGFETILENFNPEKTLILKLETDITPIPTLKKSSGLTAEVENLIFDPKKVDELIEQSRAQLATKVPVTDRAAQKGDIALVSFKGSFSDDGSEIEGGSADSIEIELEQGRMIPGFIEGVIGMNINDEKILKCEFPKDYHQEEAKGRKAEFNVSLEDLKIKELPELNDEFAKQASDKENMSDLRADLEKRLKEDNDRKQAKTRQDSLLDVLVKELEVDIPKSL... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 53022
Sequence Length: 4... |
Q73M39 | MDYEKNVTLKEKSHAELSVKIKKSDVQESYKKLLNKYSKELQIPGFRKGKVPVSVLETKYGDAIKGDLAGDLIEESLKEIFESLDEYERPLPYSYPELNEKPELKVEEDFSFTVHYDVFPKVEIKKTEGFTIEVPEASVSEKDIKKELERLQERNALVTACKEGTSAEKDHIATIDYCELDDEGKTISGTERKDFVFTIGSGLNIYKIDDDIVGMKKGESKEITKTFPEDDSNKDLAGKTKKIKVTLTALKYKDLPALDDDFAQDINEKYKNLDELKADIKKKFEISVEEKIKSLQKNALTEQMVKEHTIDLPESMVRAE... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 52111
Sequence Length: 4... |
O83519 | MELQKKFTALAQSQVELEVVVAREDAQRHYQRFVEEYLERARLPGFRKGKVPLAVLERKYGSAIRQDAAAALMEKALEEGFAQASQDSQPLPISRPSLKKKPVFDPDEDFSFAVIYDVFPSVELRNTSGFSLSVPTVSVTEEDVSRELTRIQERNALVTDKGADSCAEVGDIATVDYHEVDDSGAVRPGTERAGVVFTLGVEEGPFALGQDILGMKLGQRCLFAKRAGMLKDEAAQVRVTLKALKQRQLPSLDDELAQDVSDAFRTLDDLTRSVRQNLAEALEAALHEYKRRQLLRILVRENPFSLPESLVVGEMESRWA... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49939
Se... |
Q118P4 | MKVTQEKLPASQISLEIEISPEMSKNAYEQIIKKYIRSANIPGFRKGKVPRNILIQRLGKNYIKAMALDDLINNCLEKAREQESIKAIGQFELKTEFEELVKDFEPGKEMAFSAKVDVEPEAKVEDYKGFLVQAEEAKYDSALVDEFLEERRSRMGTLIPIEGRAAEMGDVAIVDFVGIIPSETEGEEAQEVPGGKAQDFQMDLKEGQFIPGFIEGIVGMKLQETKEISAQFPSEYSEANLAGKPVVFTVTLKELKEKELPELDDDLAQEISEFETIDKLREFLEQKFTKEKEEKTKQNKEKAIIDELVTHLEVEIPETL... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 55142
Sequence Length: 4... |
B3E1Z5 | MQVKIEEISSVKRRISVEVPAERVNTEIEKSFAGIQKKATLAGFRKGKAPLQMVKKFYRNAMQDEVMRRLYEQTLFPALDEHKLEPVDAPMIDDIALVEEGTPFKYSALIEIMPQILLGEYKGLQVKKERYVADEKAVEGEIERMRENMAQLAPVEEGTVEKGMVLTVDFSFAVPGYPEEETSGKDASVEVGNGRLLPGLEEGLIGMALGETKDITVTMPDDNPNKELAGKPGVFTVTLKEIKKKELPELNDEFAQQFGDFETIADMRTKLTEMREQQELERIKTDLKTRIIDALIEKNPLEVPDSMVRRQTDFMLENLK... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49430
Sequence Length: 4... |
Q3M725 | MKVTQEKLPASQIGLEIEITPEITQKTYEQVIKNLSRTVNIPGFRKGKVPRQVLLQRLGKTHIKAAALEELLQDGIEQAIKQESIAAIGQPRLRSSFDDLINSYEPGQPLTFTAAVDVEPEINLVQYTGLEAKAEEIKYDPARVDEVLEKERQELATLIPVEGRAAQIGDVAVVDFKGVIAKAEGDDENAEPEPIPGGDASDFQVELQEDKFIPGFVTGIVGMNPGDTKEVSAQFPDPYVNQELAGKPAIFTVTLKEIKEKELPELNDDFAQEVSDFDTLEALRASLAERYQKEAEDKTKNNQQEALLGELVKHIEVDLP... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 52379
Sequence Length: 4... |
B5ZBF7 | MKLLNKIKNENAIEFQVLIEKSEWEKKHNEAFEKVAKKTASKLKIPGFRPGNVPVEEAKKHVNEIEVFETTTNDLVPQALTFLEQDESFTSDNSETVDTPSIDILDFKDGELTLKIAYDLYPVATIDSYNDLVLTPIVNEAFDHEVNAEIEHALSSKSQRRVKDENELIEKGDEVRFDFKGMIDNVPFQGGSAKDHLLTIGSNQFIPGFEDQMIGLKVGEQKNLEVKFPDDYHATDLAGRSAVFEVLIKEITSVKPQELNDEFAKSFNLPNVNTVQELKDYIHNQIVLAKQERNSERAWLEIAQQLLAKAKVTPIPQSLI... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 53601
Sequence Length: 4... |
A1WR16 | MAVTVETLDKLERKMTLSLPVTLIQSEVDMRLRRMARTVKMDGFRPGKVPMAVVARRYGDAVQYEVLTNKVGEAFTVAANEANLRVAGRPRITETQGTAEGHVTFDAIFEVFPEVRIADLANVEIEKLSTEVTEASIDKTLQGLRKQRRSFAQRAHDAPAQDGDGVTVDFEGKIDGEPFANGKAENFRFVIGEGPMPKEFEDAVRGMKSGESKTFPLAFPTQYHGQEVAGKTADFLVTVKKIESAHLPEVGEALARSLGSADGSIEGLRADIRKTLEREIRSHLRARNRRAVMNALLANADLELPKASVQDEIARLKANA... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49075
Sequence Length: 4... |
A5CXJ7 | MKTSLETLKGLSRSLTIDLPIDIFNQKMDKILQKMALEVNIDGFRKGKVPISIVRKRFGNNANSDVINEIVNETLTDALAQVKLTPVAQPVITKVDSNSNKNFSYTVEFEVFPKIKIADFSELSIEQTKVNITKADEQKTLDGLKDRLTEYKAVQCKSKMGDRLSIDFKGLINGETFDGGEAKDFKIVLGKGSMIKGFEEGLIDVAYSSRVVLDLTFPKDYYMDKLASKDVTFEININEIASPKELKLDETFAKKFGEKNMNALRVSMKEQMRVEVDGRIGHLNKNAIFDKLTTANPFNVPQHSIDNEAQNLFKAMQDRM... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48710
Sequence Length: 4... |
Q87R81 | MQVTVETLEGLERRLNITVPAANIEDAVTAELRNIAKNRRFDGFRKGKVPLKMVAKMYGKAVRQDVLGEVMQRHFIEAIVKEKINPAGAPTFAPVENKEGADLVFTATFEVYPEVELKGLENITVEKPLTEVKEADVEEMIETLRKQQATWVEVEEAAEAGKRVSIDFVGSIDGEEFEGGKAENFPLEMGAGRMIPGFEDGIAGKTAGMEFDIDVTFPEDYHAENLKGKAAKFAIKVNKVEARELPELNDEFVAKFGVAEGGVDALKAEVRKNMERELKQAVKTRIKEQAIEGLVKENEIDVPAALIEQEIHVLRQQAAQ... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48255
Sequence Length: 4... |
A8F7F8 | MPLDEFEFSVLKTIQTHHLIFPGHKVLVALSGGMDSMSLLNILLKLRQKLNCEIFAAHLNHMIRENAIRDEQFVYSYCKKAGVKIFVERFDVPKFCADRKIGIEEGARAARYTFLNRIAHENGIDLIALAHNLNDLVETILYRIVRGTGLSGIVCMKLKDENKIRPLLYFKREQIEAYIKRNNIPYVQDETNFNLKYSRNYIRHRIVPALKLLNSDLENAFSQVHFSGMMLENHVKRLIKKYSERIFRCGKRIIFDSKDMDEFEIIELVKYCAGQMNVDLNYRQIQLVVSKLNENSWSIDLSEDIAIKKGFDFFSIEKKC... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q886M6 | MTTSTPNGHDLPARLLQALAPWRTASTWYVGFSGGLDSTVLLHLLAELAKRANLPALHAIHVHHGLQAIADAWPEHCRQVCQALGVAFESVRVKVEPGASVEQAARQARYAAFTERLGEGDVLLTGQHRDDQAETLLFRLLRGAGVRGLAAMPEQRRLGRGHLARPLLGVSRVELESYARRQGLRWVEDPSNDDQQFSRNFLRSQVLPLLTSIWPHATASLARTAGHLGEAQQLLDELAAQDVANAQATTPFSWLGLPVLNLGPIARLSGARQRNVMRHWLAPLTRLPDSDHWAGWEALRDAAQDARPLWRLADGALHRA... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A5WCA0 | MTTPVCISQAFMDSFHAHHAQLLGKRVWLACSGGRDSLGLALLCRTLFDQGRLPFLPQLIHVNHGMQAANDEWAQQVAQWAQQHDMACQIIGLNLTHKSEQAARDGRYQAMMQLMNQDDVLILGHHQDDQVETLLMRLFNGAGVTGLGAMREWTSKQAHTAQSPPDVNKPRQRIFLWRPWLEISRDQITEYAQRHNLKYIDDPTNVAQSPSKLALQTLNDRAWLRSVLLPHITERYPQASEAMARTAQLMQQASDSIDEQVTQDLAQVALAATEQQSVIALDKLAGLSAPRQAALIHHWLAPYPNQLPPSKRLVDEVLAL... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q8Y074 | MLLVDKVAQRVVACAAFVVSGGVPTVAVALSGGRDSAALLHAVAAWRDAAGVPVRLVALHIHHGLQADADAWEAACARMAAAVGAAFRVRRVRVSTDAGRGIEEAAREARYAALDALCAETGATLLLTAHHLDDQAETVLLQLLRGAGLDGLSAMPMARERRVTLLRPWLDVPRGDIEAYARAHALAWVEDPSNGDARYARNALRPLLAGMAGHFPAYRASLARSAAHLAEAAALIEEVAQTDLARIAPAGTLAVAGLAALSGPRQRAALRAWLAGAGLRAVSSRRLEDLRAQLLGARADGAPCVRLPGAQVRRYRGQAW... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q98F87 | MLDTEPDLSTRLFSHIDFTHGAVAAVSGGSDSTALLLLLKHHFDRTGSSAKLLAVTIDHGLRQGSAAEAQAVAKLCAERGIAHRTLTWTGRKPSTGLPAAARDARYHLLAEAARAEGIGLIVTGHTADDQAETVLMRHARDRELADLAGRGLAGMAPATLYDWREWIVRPLLGTRRSALRDFLRREHVGWAEDPTNIDEAFERPRVRAALAGESAGHMENTLRLAGQAAVERGQLGASAANLIRRIASQPSTGLIRLDPALLIADDQAAIYALRILLATAGGAAFLPDQARSAALFVRLKAGFLCATLSRTVVDFRHAGL... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q92JY3 | MPHAVLDTARNFLRSFITPRRILVAVSGGSDSMGLLVALHSAIAADERRGFSLAACTVDHALRPQSACEAEDVAAFCAALGIAHRICRWEGAKPSTGIQAAARNKRYELLAEAADALGADCIAIGHTRDDQQETVAMRIARGKGDGAGDGQGEGHGGAGMAASMLYGRRIWVLRPFLGLARAEIRSFLQARGVSWIDDPSNANPAFERVRVRARIATSGGMPTPLGNGRQRAASSARAAALIEKRIRVHEALVAEVSARHAGEIDDPDWRRALLTVASVLGGREHMPAFATVQRLSQFLRSGEPGRMTAGRVVFDRRASG... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q7UNE1 | MIGDVLPTTPNESPNWHRLRRAIRSTWPNRHGRSSDVATLVGCSGGADSVALICLLAELWAEESNGLNPANETVTKPVAPLVVAHCNHGLRGEESNADEAFVRQICDQLQLPLVIHHVPPLNNSATSGPVSDERTLRQIRRDFFERAAKQHGCRYVAVAHSADDQAETMLHHFIRGTGPLGLAGIAEASELDTDIVVRRPLLQVRRDTLRDGLREIGQPWREDASNRHTIYTRNWIRHDVLPLIESRYPNAVEAIHRAGTLQHEMNEMVRRLAERWLEAFTDFSGDRWTIHTERLSKSATPEKRMDDTNAACSWMIERPV... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q6NAQ6 | MSGTDHEAVSATEARRLFADWKAAPAIVLAVSGGPDSLALMWLAARWRKALKRGPALAVVTVDHGLRPEAAAEARAVKRLAASLDLPHRTLRWSGDKPSTGIQAAARGARYRLLAKAAKTLGASHVMTAHTRDDQAETVLMRLSRGSGIAGLAAMAREIERDGVVLARPLLDVPKARLIATLAKARIAFATDPSNADPRFTRPRLRELMPQLAAEGCDARSLVRLAVRAARADAALELMTDGAEQFLASLDAGSERPGVNARAFLGLAAEIQIRLLLRTLSRHGHEGPPELGKVEALAEALSQAAARRPQAAAKIRLKQT... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q6BXP3 | MAHRLLVNVIFTGASVFGRAFTEAYKQAAKATASTPQGGAAKSTSVGGIPTDEALKILDLKKTDLSVAKIDEKYAYLFDVNSKDKGNSFYLQSKVYYAMDSLRKELDYLDKLKKTKDGSQGEAGPTST | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. ... |
Q54SV6 | MAARLIAKIVFTSGTVLVRSIQMAYKQALLQAESGMGAAAGSMDVKSKMSPIEARKILGLENVETVSKEDIDKKYNELLTINDPKDGGSEYLQIKISGAKHCLHSALKEGKKI | Function: Regulates ATP-dependent protein translocation into the mitochondrial matrix.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12221
Sequence Length: 113
Domain: The J-like region, although related to the J domain does not have co-chaperone activity.
Subcellular Location: Mitochondrion inner ... |
Q9VF08 | MAKYIAQIIVLGAQAVGRAFTKALRQEIAASQEAARRAGGGKQGDKSAESNLRTGMTLEEAKQILNIDDPKNVDAITKNYEHLFQVNERSKGGSFYIQSKVFRAKERLDHEIKAHEQPRSSNTEAAQDTAEESQSRSRQRR | Function: Regulates ATP-dependent protein translocation into the mitochondrial matrix (By similarity). Essential for larval development.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15731
Sequence Length: 141
Domain: The J-like region, although related to the J domain does not have co-chaperone ac... |
Q5B187 | MAHRIVTQVVVTGARVFGRAFAEAYKQASAASKYQQKTGKSAGGSSSSGITLDEACKILNVKPPQAGETNLEQVMERFKKLFDLNDPQKGGSFYLQSKILRARERIEAEVREAERKAAHEKELKEGWKPKVYKDR | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1/sscA) via its interaction with PAM18/TI... |
Q4I375 | MAHKFVVTAFLTGSRILGRSFVAAYKQAQAASAYQRAQVKAGNTTGGASLSSGMTLDEACKILNVKPPAGGQANVEEVLSRYKRLFDANDPQKGGSFYLQSKIVRAKERFEREIGPLREKMEAEAEIKEGFKPKVYKD | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. ... |
Q9Y3D7 | MAKYLAQIIVMGVQVVGRAFARALRQEFAASRAAADARGRAGHRSAAASNLSGLSLQEAQQILNVSKLSPEEVQKNYEHLFKVNDKSVGGSFYLQSKVVRAKERLDEELKIQAQEDREKGQMPHT | Function: Regulates ATP-dependent protein translocation into the mitochondrial matrix. Inhibits DNAJC19 stimulation of HSPA9/Mortalin ATPase activity.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13825
Sequence Length: 125
Domain: The J-like region, although related to the J domain does not have c... |
Q7S6S4 | MAYRLITQVVVVGSRVLGRAFAEAYKQAAASSQYQRAQQKNGNAATGRASLTSGMTLDEACKILNVNKPADGTAANMEEVMERFKRLFDANDPEKGGSFYLQSKVVRARERLEAEIKPKMEEKQAEEEVKEGWNPKIYKDR | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (hsp70-5) via its interaction with tim14/pam1... |
Q6EIX2 | MAKYLTQIIVMGVQVVGRDFAKALRQEFAASQAAADARGHAGHQSAAASNLSGLSLQEAQQILNISKLSPEEVQNYEHLFKVNDKSVGDSFYLQSKVVRAKERLDEELQIQAQEDREKGQMPKT | Function: Regulates ATP-dependent protein translocation into the mitochondrial matrix. Inhibits DNAJC19 stimulation of HSPA9/Mortalin ATPase activity (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13730
Sequence Length: 124
Domain: The J-like region, although related to the J domain... |
Q9C1W5 | MSLPRAVGRFIIVGSQVMSKAFVQAYKQMIANAAQQSTGQAAASKSSTAVRRGEMTIQEAGSILNIKPESLEEGELEKRFQKMFEINDPKKGGSFYLQSKVFRAHEKLKSELDQKIQEQSPAKPTSSP | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (ssc1) via its interaction with PAM18/TIM14. ... |
Q5XGJ0 | MAKYLAQIMVMGMQVVGRAFTRALRQEFAASRAAAEARGRAGTESAAVSSLSGISLQEAQQILNVSKLTPEEIQKNYEHLFKVNDKEVGGSFYLQSKVVRAKERLDQEMDIQSKTEKPKDETTQT | Function: Regulates ATP-dependent protein translocation into the mitochondrial matrix.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13897
Sequence Length: 125
Domain: The J-like region, although related to the J domain does not have co-chaperone activity.
Subcellular Location: Mitochondrion inner ... |
Q6C331 | MAHRLIYQVVVTGTQVFAKAFTQAYKQAATAQAASKTSKSAASKFGGLQLDEACKILDVDETALDKVVAELNKKHKLEDIAESESVLAQIDKKFTHLYTVNSEHKSGSFYLQSKVYRAMERIRGELELDPLPKPEIEEPKKKEEEKK | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. ... |
P42949 | MAHRAFIQVIITGTQVFGKAFAEAYRQAASQSVKQGATNASRRGTGKGEYGGITLDESCKILNIEESKGDLNMDKINNRFNYLFEVNDKEKGGSFYLQSKVYRAAERLKWELAQREKNAKAKAGDASTAKPPPNSTNSSGADNSASSNQ | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. ... |
Q54K35 | MEAPCPDKIWQDAGGAFAIGYVLMGVVNIGLGFKRSPPNKRVLYTFALLRKKSPKFGGNFAIWGSLFSGFDCTLSYIRKTEDTVNPIAAGALTGGILAARSGWKHSVQAAAFGGIFIGIIEAFQHMMQKRMQAQQEEMTQQHLEERKRYEEERKQREGERKKLNENGKSKKNKQQQNGENDLD | Function: May be involved in the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20556
Sequence Length: 183
Subcellular Location: Mitochondrion inner membrane
|
P59670 | MDHTRDPCPWVILNDFGGAFAMGAIGGTIWHGIKGFRNSPYGERRIGAITAIKMRAPALGGNFGVWGGLFSTFDCAIKGLRNHKEDPWNSILAGFFTGGALAVRGGYKAARNGAIGCAVLLAVIEGVGIGFQKMLAGATKLEAPAPPPSNEKVLA | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16184
Sequence Length: 155
Subcellular Location: Mitochondrion inner membrane
|
P87130 | MASADHTRDPCPYVILNDFGAAFSMGTIGGAIWHSIKGWRNSPPGEKRISAIAAAKTRAPVLGGNFGVWGGLFSTFDCAVKGVRRKEDPWNAIIAGFFTGGALAVRGGWRATRNGAIGCACILAVFEGLGIALGRMNAEYNRPVAPVIPDAPASGSTSAAPAAV | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16901
Sequence Length: 164
Subcellular Location: Mitochondrion inner membrane
|
P39515 | MSADHSRDPCPIVILNDFGGAFAMGAIGGVVWHGIKGFRNSPLGERGSGAMSAIKARAPVLGGNFGVWGGLFSTFDCAVKAVRKREDPWNAIIAGFFTGGALAVRGGWRHTRNSSITCACLLGVIEGVGLMFQRYAAWQAKPMAPPLPEAPSSQPLQA | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
PTM: The disulfide bond is required for stabilization of the TIM23 complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 165... |
Q08749 | MLLFPGLKPVLNASTVIVNPVRAVFPGLVLSTKRSFYSINRLNAENKINDIANTSKEASSSVQMFKPPEFSQFKDSYQKDYERIAKYTLIPLTMVPFYASFTGGVINPLLDASLSSIFLIYLQYGFTSCIIDYIPKEKYPRWHKLALYCLYGGSMLSLYGIYELETKNNGFVDLVKKLWNENDDHLYIFGRN | Function: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force. Its role in the complex is unclear but it may... |
Q9BSI4 | MATPLVAGPAALRFAAAASWQVVRGRCVEHFPRVLEFLRSLRAVAPGLVRYRHHERLCMGLKAKVVVELILQGRPWAQVLKALNHHFPESGPIVRDPKATKQDLRKILEAQETFYQQVKQLSEAPVDLASKLQELEQEYGEPFLAAMEKLLFEYLCQLEKALPTPQAQQLQDVLSWMQPGVSITSSLAWRQYGVDMGWLLPECSVTDSVNLAEPMEQNPPQQQRLALHNPLPKAKPGTHLPQGPSSRTHPEPLAGRHFNLAPLGRRRVQSQWASTRGGHKERPTVMLFPFRNLGSPTQVISKPESKEEHAIYTADLAMGT... | Function: Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA ... |
Q9QXG9 | MAPPPGVGPASLRFAAAASWLVVRRRRVEHFPKVVEFLQSLRAAAPGLVCYRHHERLCMSLKAKVVVELILQARPWDQVLNALKHHFPAESRTTKEDRKLLEARENFCLLVKHLSEDPPSSLQELEQDYGESFLVAMEKLLFEYLCQLEKALPPVRAQELQDALSWSQPGSFITSSVALHQYGMDMGWTFPESSTSGSGNLIEPMEESPHQQTRPAFHSPLPKAKLGPHQPASLEHPEHLAGHRFNLAPLGKRKSRSHWTSAKACHKERPTVMLLPFRNMGLPAQDLSNPKSREEPGAASAASVGTEPVCTEEAKTPSRP... | Function: Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA ... |
Q9YJQ8 | MANEPQEHEEGKPFFPPLGDSGEEGPPNIPQDPTPGTPPGPINSKNEDYPPPLENPGPNKSEGPPDGSGNSSPPVTMLVKNNGDRTKQDVSESGGNNSAPNSVESKHTSSSSSAGNGNETKCPDEQNTQECITTIYIPWEDAKPKLMGLVKLDSSDSEEERSPFNKYPKNYKKLRVDMGENWPPGIPPPQLPPRPANLGQKQSATSKNGPQIILREATEVESQQATDGQLNHRVEKVEKKLTCVICLLIGILVLLILLFMLGFLFLLMK | Function: Transforms host T-cells, inducing T-cell lymphomia in the host. Activates at least SRC and LCK tyrosines kinases, thereby activating signaling pathway transforming host T-cells. Human T-cells transformed ex vivo display a IL2 indenpendent growth phenotype.
PTM: Phosphorylated by host LCK, SRC and less efficie... |
P25818 | MPIRNIAIGRPDEATRPDALKAALAEFISTLIFVVAGSGSGMAFNKLTENGATTPSGLVAAAVAHAFGLFVAVSVGANISGGHVNPAVTFGAFIGGNITLLRGILYWIAQLLGSVVACLILKFATGGLAVPAFGLSAGVGVLNAFVFEIVMTFGLVYTVYATAIDPKNGSLGTIAPIAIGFIVGANILAGGAFSGASMNPAVAFGPAVVSWTWTNHWVYWAGPLVGGGIAGLIYEVFFINTTHEQLPTTDY | Function: Water channel required to facilitate the transport of water, diffusion of amino acids and/or peptides from the vacuolar compartment to the cytoplasm. Does not promote glycerol permeability. May play a role in the control of cell turgor and cell expansion. Its function is impaired by Hg(2+). May be involved in... |
O64964 | MPINRIALGSHQEVYHPGALKAAFAEFISTLIFVFAGQGSGMAFSKLTGGGPTTPAGLIAAAVAHAFALFVAVSVGANISGGHVNPAVTFGAFVGGNITLFRGLLYWVAQLLGSTVACFLLRFSTGGQATGTFGLTGVSVWEALVLEIVMTFGLVYTVYATAVDPKKGSLGTIAPIAIGFIVGANILVGGAFDGASMNPAVSFGPALVSWEWGYQWVYWVGPLIGGGLAGVIYELLFISHTHEQLPSTDY | Function: Water channel required to facilitate the transport of water across cell membrane. May support the rapid influx of water into vacuoles during cell expansion, permit osmotic equilibration between the cytosol and the vacuolar content and rapid transcellular water flow through living cells. Its function is impair... |
Q41963 | MPTRNIAIGGVQEEVYHPNALRAALAEFISTLIFVFAGSGSGIAFNKITDNGATTPSGLVAAALAHAFGLFVAVSVGANISGGHVNPAVTFGVLLGGNITLLRGILYWIAQLLGSVAACFLLSFATGGEPIPAFGLSAGVGSLNALVFEIVMTFGLVYTVYATAVDPKNGSLGTIAPIAIGFIVGANILAGGAFSGASMNPAVAFGPAVVSWTWTNHWVYWAGPLIGGGLAGIIYDFVFIDENAHEQLPTTDY | Function: Water channel required to facilitate the transport of water across cell membrane. May be involved in the osmoregulation in plants under high osmotic stress such as under a high salt condition. Transports urea in yeast cells in a pH-independent manner. Transports H(2)O(2) in yeast cells.
Location Topology: Mul... |
O82598 | MPINRIAIGTPGEASRPDAIRAAFAEFFSMVIFVFAGQGSGMAYGKLTGDGPATPAGLVAASLSHAFALFVAVSVGANVSGGHVNPAVTFGAFIGGNITLLRAILYWIAQLLGAVVACLLLKVSTGGMETAAFSLSYGVTPWNAVVFEIVMTFGLVYTVYATAVDPKKGDIGIIAPLAIGLIVGANILVGGAFDGASMNPAVSFGPAVVSWIWTNHWVYWVGPFIGAAIAAIVYDTIFIGSNGHEPLPSNDF | Function: Potential aquaporin, which may facilitate the transport of water and small neutral solutes across cell membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25914
Sequence Length: 252
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a po... |
P27654 | MSVSKIAFVLSAIASLAVADTSAAETAELQAIIGDINSHLSDYLGLETGNSGFQIPSDVLSVYQQVMTYTDDAYTTLFSELDFDAITKTIVKLPWYTTRLSSEIAAALASVSPASSEAASSSEAASSSKAASSSEATSSAAPSSSAAPSSSAAPSSSAESSSKAVSSSVAPTTSSVSTSTVETASNAGQRVNAGAASFGAVVAGAAALLL | Function: Seems to have esterase activity. Prefers ester of fatty acids from 4 to 16 carbon atoms.
PTM: Extensively O-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20728
Sequence Length: 210
Subcellular Location: Secreted
EC: 3.1.1.-
|
Q9C0W8 | MMSQQLIDFIDSRTRHPYKSDEVEKFQQEVNELQLPDPNSLPILSEEEKRQAREDAAFRRSSEGLEDAWLDSAIPADPTPIFRDTVELLCVYQSFVKKSASLDTVANFLDFSTDFSTLSTKKDETEIAPDCLHYIAELLFQKKEREVKEKWKNELTEKLKTLFNWPAINPNLKESSKFESFFGFVRSIQSFKDSETGLPLFMQVYITPYVNQFRYHFMSQKQTNVLSKPEWFFEFLLKVFRSNRSFYMLMRDIKFFPGVPPFFTFINLLNNVAKEKLTHIIKYDDYLVHLVHETLQYSVRLEQHFHYTQDPLIIFLFEQN... | Function: Required for protein transport between the Golgi and the endoplasmic reticulum. May contribute to tethering of coatomer-coated retrograde transport vesicles to the ER membrane through interaction with and stabilization of the SNARE complex (By similarity).
Location Topology: Peripheral membrane protein
Sequen... |
Q58092 | MVKLSGVYKGMRKGYGETLIELGKKYENLVVLDADLSGSTQTAMFAKEFPERFFNAGVAEQNMIGMAAGLATTGKIVFASSFSMFASGRAWEIIRNLVAYPKLNVKIVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRTIAEYKGPVYVRMPRRDTEIIYENEEEATFEIGKGKILVDGEDLTIIATGEEVPEALRAGEILKENGISAEIVEMATIKPIDEEIIKKSKDFVVTVEDHSIIGGLGGAVAEVIASNGLNKKLLRIGINDVFGRSGKADELLKYYGLDGESIAKRIMEEMKKE | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Sequence Mass (Da): 34580
Sequence Length: 316
EC: 2.2.1.1
|
P51854 | MADAEARAEFPEEARPDRGTLQVLQDMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAKRLSFVDVATGWLGQGLGVACGMAYTGKYFDRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKLIESQIQTSRNLDPQPPIEDSPEVNITDVRMTSPPDYRVGDKIATRKACGLALAKLGYANNRVVVLDGDTRYST... | Cofactor: Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Catalytic Activity: D-... |
Q99MX0 | MSEAEASSGMAHNAGPDEKTLQVLRDMANRLRIRSIKATNSSTTSYLIPCSNAEIMSVLFFYTMRYKQEDPENPDNDRCILSKGLPFVNVATGWPGQGLGAACGMAYTGKYFDQASYRVFCLLGDEESTEGSVWEAFAFASYYNLDNLMAIFDVNRIGHSSSMSVEHCIAIYQKRCEAFGWNTYVVDGRDVKTLCHVFSQAAQVRGKPTAVVAKTFKARGMPNVEDAESWYGRPMPKERADAIVKLIESQIQTNKILVPSPPIEDSPQINIMNICMTSPPVYVADDKVSTQRACGLALAKLGHENDRVIVLGSDTKNCNF... | Cofactor: Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Catalytic Activity: D-... |
Q9H0I9 | MMANDAKPDVKTVQVLRDTANRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEVGDISESDLLNLRKLHSDLERHPTPRLPFVDVATGSLGQGLGTACGMAYTGKYLDKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDVNRLGQSGPAPLEHGADIYQNCCEAFGWNTYLVDGHDVEALCQAFWQASQVKNKPTAIVAKTFKGRGIPNIEDAENWHGKPVPKERADAIVKLIESQIQTNENLIPKSPVEDSPQISITDIKMTSPPAYKVGDKIA... | Cofactor: Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Function: Plays an essential role in total transketolase activity and cell proliferation in cancer cells; after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decrea... |
Q9D4D4 | MALARDAKLESDTLQVLQDVANRLRIHSIRATCACSSGHPTSCCSVAEIMAVLFFHTMRYKQADPEHPDNDRFVLSKGHAAPILYAVWVEVGRICESDLLNLRKIHCDLEGHPTPRLSFVDVATGSLGQGLGAACGMAYTGKYFDKASYRVFCLMGDGESSEGSVWEALAFASHYNLDNLVAIFDVNRLGQSGTAPLEHCTAVYEKRCQAFGWNTYVVDGHDVEALCQAFWKAAQVKNKPTALIAKTFKGRGIPNVEDAENWHGKPMPKDRADGIVKLIENRIQTNRNLTPKPPIEDSPRISMSNTKMTSLPVYKLGDMI... | Cofactor: Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Function: Plays an essential role in total transketolase activity and cell proliferation in cancer cells; after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decrea... |
Q58094 | MDNNLEIKDLEKIAKKVRYNIVKMVGLAKSGHPGGSLSATDIIVALYFKLMNYSPDNPYKKDRDRFVLSKGHAAPALYAVLSELGIIEEEELWKLRRLEGKLQGHPSMDTPGVEICTGSLGQGFSAAVGMALGCRLDKLNNYVYVLLGDGECQEGIVWEAAMAAAHYKLDNLIAFIDRNKLQIDGCTEDVMSLGDIKAKFEAFGWDVFEIDGHNFEEIINTVEKAKSMKNGKPKMIIAYTVKGKGVSFMENNVAFHGKAPNEEQLKQALEELSE | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Sequence Mass (Da): 30336
Sequence Length: 274
EC: 2.2.1.1
|
P21726 | MNAPERIDPAARCANALRFLAADAVELARSGHPGAPMGMAEMAEVVWRRHLRHNPANPAWPDRDRFVLSNGHASMLQYALLHLTGYDLPMSQLRQFRQLHAVTPGHPEVDVTPGVETTTGPLGQGLANAVGMALAEKLLAATFNRPGFDIVDHHTYVFLGDGCLMEGLSHEACSLAGTLGLGKLICLYDDNGISIDGEVAGWFADDTPKRFAAYGWHVIADVDGHDAHALDAALHEAKAERDRPTLICCRTVIGKGAPAKAGGHDVHGAPLGAPEIAAMRTALGWEAEPFTVPADVADAWDARAQGAAREAEWEARFVSY... | Cofactor: Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Catalytic Activity: D-... |
O67642 | MVVQLDQIHFFIFHEVLKIFKTMPQLFKTSKKIDELVINTIRFLSVDMVERAKSGHPGMPLGASHIVYLLYDRIMKYNPKNPNWFNRDRFILSAGHGSAMLYAAFYMFGFDLTLEDLKAFRQLNSKTPGHPEYGLTPGVEVTTGNLGQGFGNAVGMAMAEKFLSHYFNREGYPVIDHYTYVLVSDGDLMEGVSYEAASLAGHFKLNKLIAIWDNNHITIDGDTKLTWTEDVLKRFEALGWEVYHLEDGYNLDLLEETILKAKESDKPTFISVRTHIGYGTPLQDTPEVHGKPMGKEIVEETKKKFGWPLEEFYVPEEALN... | Cofactor: Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Catalytic Activity: D-... |
P45694 | MDTIEKKSVATIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTKFMNVSPANPGWFNRDRFVLSAGHGSALLYSMLHLSGFDLSIEDLKGFRQWGSKTPGHPEFGHTAGVDATTGPLGQGIAMAVGMAIAERHLAETYNRDSFNVVDHYTYSICGDGDLMEGISSEAASLAGHLQLGRLIVLYDSNDISLDGDLDRSFSENVKQRFEAMNWEVLYVEDGNNIEELTAAIEKARQNEKKPTLIEVKTTIGFGSPNRAGTSGVHGAPLGKEESKLTKEAYAWTYEEDFYVPSEVYEHFAVAVKESGEKKEQEWNAQFAKYKE... | Cofactor: Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Catalytic Activity: D-... |
P57195 | MYSRKELANAIRMLSIDAVQNAQSGHPGMPMGMADIAEVLWRSFLKHNPANPNWNDRDRFILSNGHGSMLLYSLLHLTGYNLPIEELKKFRQLNSKTPGHPETGETPGVETTTGPLGQGLANAVGMAIAERTLSSYFNRPGYDIINHYTWVFVGDGCLMEGISHEVCSLAGTLNLGKLIVFYDKNGISIDGKTAHWFTDDTAKRFESYNWHVLDNIDGHDSESIERSIKQAKLITNQPSIIICNTIIGFGSPNKSGTAESHGAPLGEVEISLIREQLKWNYPPFQIPKEIYKKWNFIEEGSKLEKKWNEKFSLYQSKYPD... | Cofactor: Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Catalytic Activity: D-... |
P43221 | MLDTKPSATRRIPLVIATVAVGGLAGFAALYGLGLSRAPTGDPACRAAVATAQKIAPLAHGEVAALTMASAPLKLPDLAFEDADGKPKKLSDFRGKTLLVNLWATWCVPCRKEMPALDELQGKLSGPNFEVVAINIDTRDPEKPKTFLKEANLTRLGYFNDQKAKVFQDLKAIGRALGMPTSVLVDPQGCEIATIAGPAEWASEDALKLIRAATGKAAAAL | Function: Involved in cytochrome aa3 assembly.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 23260
Sequence Length: 221
Subcellular Location: Cell membrane
|
Q9I0I4 | MFLRRLSIQWKITLLAGLCLLGVVALLVGLSVYRMQHSSVLVKSASTQMLDESARLRLEARGELQALRIQRYFMDAFQYGKGFSRQILFLRDQAQKRFLDAYDLREDLTRQVRTALAANPEVLGLYVVFEPNALDGKDELFVDQPALGSNDKGRFSLYWAQATPGQLESESMIESELADTSSGPSGAAYNAWYTCPKESGQPCVLDPYFDKVGERQLLMTSIAFPLELDGKVIGVMGLDINLSNLQALSEQGNRELYDGVGQVGILSPAGLFAGNSRDAGLLGKNLAKADPQHAGELLQLLAAGKSRLFNENDDLKVLQP... | Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. TlpQ is a chemoreceptor that binds and me... |
A0A0H3PEK7 | MRFDFFVSKRLNISRNKALELIENEEVLLNGKSFKASFDVKNFLENLKKTQDLNPEDILLTDGLKLDLLSEIYVSRAALKLKNFLEENGIEIKHKNCLDIGSSTGGFVQILLENQALKITALDVGNNQLHLSLRTNEKIILHENTDLRTFKSEEKFELITCDVSFISLINLLYYIDNLALKEIILLFKPQFEVGKNIKRDKKGVLKDDKAILKARMDFEKACAKLGWLLKNTQKSSIKGKEGNVEYFYYYIKN | Function: Catalyzes the 2'-O-methylation at nucleotide C1920 in 23S rRNA . Enhances motility . Enhances biofilm formation . Involved in the assembly of 70S ribosomes . Involved in virulence by promoting adherence and invasion to host cells . Involved in pathogenicity by modulating secretion of host-protective chemokine... |
P9WJ62 | MARRARVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTVVTDSERAWVSRGAHKLVGALEAFAIAVAGRRCLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLAWSLRNDPRVVVLERTNARGLTPEAIGGRVDLVVADLSFISLATVLPALVGCASRDADIVPLVKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRAQELGWHSVGVKASPLPGPSGNVEYFLWLRTQTDRALSAKGLEDAVHRAISEGP | Function: Acts as a host evasion factor, that significantly contributes to the pathogenesis of M.tuberculosis by modulating adaptive immune responses by inhibiting host-protective Th1 and Th17 cytokine responses as well as autophagy. Catalyzes the 2'-O-methylation at nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA.... |
Q9NV29 | MTEEPIKEILGAPKAHMAATMEKSPKSEVVITTVPLVSEIQLMAATGGTELSCYRCIIPFAVVVFIAGIVVTAVAYSFNSHGSIISIFGLVVLSSGLFLLASSALCWKVRQRSKKAKRRESQTALVANQRSLFA | Function: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor-dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in the regulation of nociception, acting as a modulator of the interactio... |
Q9CQG9 | MTEESTKENLGAPKSPTPVTMEKNPKREVVVTTGPLVSEVQLMAATGGAELSCYRCIIPFAVVVFITGIVVTAVAYSFNSHGSIISIFGLVLLSSGLFLLASSALCWKVRQRNKKVKRRESQTALVVNQRCLFA | Function: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor-dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10 . Involved in the regulation of nociception, acting as a modulator of the interacti... |
Q8WZ71 | MLPLLAALLAAACPLPPVRGGAADAPGLLGVPSNASVNASSADEPIAPRLLASAAPGPPERPGPEEAAAAAAPCNISVQRQMLSSLLVRWGRPRGFQCDLLLFSTNAHGRAFFAAAFHRVGPPLLIEHLGLAAGGAQQDLRLCVGCGWVRGRRTGRLRPAAAPSAAAATAGAPTALPAYPAAEPPGPLWLQGEPLHFCCLDFSLEELQGEPGWRLNRKPIESTLVACFMTLVIVVWSVAALIWPVPIIAGFLPNGMEQRRTTASTTAATPAAVPAGTTAAAAAAAAAAAAAAVTSGVATK | Function: Receptor for brain injury-derived neurotrophic peptide (BINP), a synthetic 13-mer peptide.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30404
Sequence Length: 300
Subcellular Location: Membrane
|
Q91XV7 | MLPLLAALLAAACPLPPARGGATDAPGLSGTPPNASANASFTGEHSTPRLLASAASAPPERAGPEEAPAAPCNISVQRQMLSSLLVRWGRPRGLQCDLLLFSTNAHGRAFFAAAFHRVGPPLLIEHLGLAAGGAQQDLRLCVGCGWVRGRLRAPAGAPTALPAYPAAEPGPLWLQGEPRHFCCLDFSLEELQGEPGWRLNRKPIESTLVACFMTLVIVVWSVAALIWPVPIIAGFLPNGMEQRRTTAGAPAAAPAAVPAGTTAAAAAAAAAAAAAAAVTSGVAPK | Function: Receptor for brain injury-derived neurotrophic peptide (BINP), a synthetic 13-mer peptide.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29005
Sequence Length: 285
Subcellular Location: Membrane
|
A6QQX9 | METAAGSERRSTPGPAVPPPPRGHAPLATASGPLSSPAREPPQPEEERQLRISESGQFSDGLEDRGLLESSTRLKPHEAQNYRKKALWVSWFSIIVTLALAVAAFTVSVMRYSASAFGFAFDAILDVLSSAIVLWRYSNAAAVHSAHREYIACVILGVIFLLSSVCIVVKAIHDLSTKLLPEVDDFLFSVSILSGILCSILAVLKFMLGKVLTSRALITDGFNSLVGGVMGFSILLSAEVFKHNSAVWYLDGSIGVLIGLTIFAYGVKLLIDMVPRVRQTRHYEMFE | Function: Zinc ion transporter that mediates zinc efflux and plays a crucial role in intracellular zinc homeostasis (By similarity). Binds the divalent cations Zn(2+), Ni(2+), and to a minor extent Cu(2+) (By similarity). Is a functional modulator of P2X purinoceptors, including P2RX1, P2RX3, P2RX4 and P2RX7 (By simila... |
Q8TC26 | MEPAAGIQRRSSQGPTVPPPPRGHAPPAAAPGPAPLSSPVREPPQLEEERQVRISESGQFSDGLEDRGLLESSTRLKPHEAQNYRKKALWVSWFSIIVTLALAVAAFTVSVMRYSASAFGFAFDAILDVLSSAIVLWRYSNAAAVHSAHREYIACVILGVIFLLSSICIVVKAIHDLSTRLLPEVDDFLFSVSILSGILCSILAVLKFMLGKVLTSRALITDGFNSLVGGVMGFSILLSAEVFKHDSAVWYLDGSIGVLIGLTIFAYGVKLLIDMVPRVRQTRHYEMFE | Function: Zinc ion transporter that mediates zinc efflux and plays a crucial role in intracellular zinc homeostasis . Binds the divalent cations Zn(2+), Ni(2+), and to a minor extent Cu(2+) (By similarity). Is a functional modulator of P2X purinoceptors, including P2RX1, P2RX3, P2RX4 and P2RX7 . Plays a role in central... |
A9CMA6 | MERAPGSERRSPPGPGVPRPPPRGHAPSTAAPAPNPAPLSSSMQPDEERQPRISESGQFSDGFEDRGLLESSTRLKPHEAQNYRKKALWVSWLSIIVTLALAVAAFTVSVMRYSASAFGFAFDAILDVLSSAIVLWRYSNAAAVHSAHREYIACVILGVIFLLSSICIVVKAIHDLSTRLLPEVDDFLFSVSILSGILCSVLAVLKFMLGKVLTSRALITDGFNSLVGGVMGFSILLSAEVFKHNAAVWYLDGSIGVLIGLTIFAYGVKLLIDMVPRVRQTRHYEMFE | Function: Zinc ion transporter that mediates zinc efflux and plays a crucial role in intracellular zinc homeostasis (By similarity). Binds the divalent cations Zn(2+), Ni(2+), and to a minor extent Cu(2+) . Is a functional modulator of P2X purinoceptors, including P2RX1, P2RX3, P2RX4 and P2RX7 (By similarity). Plays a ... |
Q1JQE1 | MGSCQAGHYLHFCLAHHPPLVCATLILLLLGLSGLGLGGFLLTHRTDLRSPDIPQDWVSFLRSFGQLTLCPVNGTVTGKGRGSHIVGLLTTLNFGDGPDRNKTQTFQAQVQGSRMGLKGSFARELVLVTARVTTERTPGTCLYFSAIPEILPSSQPPIPCSEEGAGNATLSPRMSEECVGVWSHEGLVLTKLLTSEELTLCGSRLLVLGFFLILFCGLCCLTAACFHPRRESHWSRTRL | Function: Cell death receptor specific for IGFBP3, may mediate caspase-8-dependent apoptosis upon ligand binding.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25877
Sequence Length: 239
Subcellular Location: Cell membrane
|
Q86XT9 | MGNCQAGHNLHLCLAHHPPLVCATLILLLLGLSGLGLGSFLLTHRTGLRSPDIPQDWVSFLRSFGQLTLCPRNGTVTGKWRGSHVVGLLTTLNFGDGPDRNKTRTFQATVLGSQMGLKGSSAGQLVLITARVTTERTAGTCLYFSAVPGILPSSQPPISCSEEGAGNATLSPRMGEECVSVWSHEGLVLTKLLTSEELALCGSRLLVLGSFLLLFCGLLCCVTAMCFHPRRESHWSRTRL | Function: Cell death receptor specific for IGFBP3, may mediate caspase-8-dependent apoptosis upon ligand binding.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25724
Sequence Length: 240
Subcellular Location: Cell membrane
|
Q9D123 | MGSCQAGHNLHLCLAHHPPLVCATLILLLLGLSGLGLGGFLLTHTTGLRSPDIPQDWVSFLRSFGQLSLCPMNETVTGTWQGPHVVGLLTTLNFGDGPDRNKTQTFQAKIHGSQIGLTGSSAGESVLVTARVASGRTPGTCLYFSGVPKVLPSSQPPISCSEEGVGNATLSPVMGEECVRVWSHERLVLTELLTSEELALCGSRVLGLGFFLVLLCGLLCCTTAVCFHPRPEFHWSRTRL | Function: Cell death receptor specific for IGFBP3, may mediate caspase-8-dependent apoptosis upon ligand binding.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25573
Sequence Length: 240
Subcellular Location: Cell membrane
|
A5PJW2 | MAAPGRRWSVLLFRALQSLSARRALHDTAPPRDVLLFEHERGRFFAVLGLFCAGQGVFWASLAIASLARPPTPVRPTDAKTPDHGGLDLRSTLWRYGLAVGCGAIGSLVLGAGLLFSLRSVRSVMLRAGGKQVTLTTHAPFGWGAHFTVPLNQVSCMAHRGEVPAMLPLKVKGRRFYFLLDKAGHFPNTKLFDNTVGAYRSL | Function: Mitochondrial ribosome-associated protein involved in the first steps of cytochrome c oxidase complex (complex IV) biogenesis. Stimulates the translation of MT-CO1 mRNA and is a constituent of early MT-CO1 assembly intermediates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21992
Sequenc... |
Q6DC58 | MAVQHLLFGVRRSCTFILACRRTAFQSSRAFTSIYTQFKVTDTKNIFRPLVFPVRVASAFTFTSAAVAKDVLLFEHDRTRFFRLLAIFCGGQFLFWAYLGHFAFTSLRDTRKYSEPQKVRTELGGFFSFDMNLGSNAWRYGFTSGCLIIGGGILALALLFSRRSVSRVILHKGGAKVSVYTQSPLGPQRSHHLTVPLSQVACYAHRQESHSFIPLKVKGYKFYFLLDKEGTVNNPKLFDITVGAYRPL | Function: Mitochondrial ribosome-associated protein involved in the first steps of cytochrome c oxidase complex (complex IV) biogenesis. Stimulates the translation of MT-CO1 mRNA and is a constituent of early MT-CO1 assembly intermediates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28081
Sequenc... |
A0PJW6 | MAAPWRRWPTGLLAVLRPLLTCRPLQGTTLQRDVLLFEHDRGRFFTILGLFCAGQGVFWASMAVAAVSRPPVPVQPLDAEVPNRGPFDLRSALWRYGLAVGCGAIGALVLGAGLLFSLRSVRSVVLRAGGQQVTLTTHAPFGLGAHFTVPLKQVSCMAHRGEVPAMLPLKVKGRRFYFLLDKTGHFPNTKLFDNTVGAYRSL | Function: Mitochondrial ribosome-associated protein involved in the first steps of cytochrome c oxidase complex (complex IV) biogenesis . Stimulates the translation of MT-CO1 mRNA and is a constituent of early MT-CO1 assembly intermediates .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22049
Seque... |
Q32KQ5 | MVHILVRKVEATNMFFSSWTLVFLAVGIIIEEWAELKLGPQKPTITHSPWICCTPLWPSDGLEVIRNILIVVLSLSFMHNLLLGFEFTYMIPQTKYTLIMTACLAFLTGILLLGALLLYHHMLRQGESVYYSSYKISWIIFTAYLNVLFLFISGFLSLLQYKQPIDGSGSLIPRSARKSQVMEQHGVSIKVVSLPAGTAMPRSIVRLHSAHMKEDSPERLNIQARRVTWAL | Function: Probably inhibits protein phosphatase 1 (PP1) in sperm via binding to catalytic subunit PPP1CC.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26224
Sequence Length: 231
Subcellular Location: Cytoplasmic vesicle
|
Q6GV28 | MVHVSNRSIQGMNILFSSWAVVLMVMGITLDKWVELISEDERAKMNHSPWMMCCPALWPEDDLKVVRIMMTSSLGLSFLLNLILGMKFTYLIPQNKYIQLFTTILSFFSGISLLWALILYHNKLKQGQSMHFSSYRITWIMYTAYLNVFFLSVCGVLSLLECKLSTSSCTCLNIHKSDNECKESENSIEDISLPECTAMPRSIVRAHTVNSLNKKVQTRHVTWAL | Function: Probably inhibits protein phosphatase 1 (PP1) in sperm via binding to catalytic subunit PPP1CC.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25801
Sequence Length: 225
Subcellular Location: Cytoplasmic vesicle
|
Q9D9S2 | MMHIPNRSIQAANIFFSSGAILLLIVGLIMEDWVELIPKVRKDKTTHSPWLGCCPPFWPEESLEVVRRIMRMTLNISIYLNLIIGLQFSYMISQNKCVHLLVGFLSFFAGCLLFYAIIVYHHKLNKGQYVYFVNYKTKWIAFTVYLTIALFLTCGIFCFIQSTNRCECMKFCIPHTESKSQEMIPSTIEVVSLPPRCAMPRSIVHVHSVTSKDGSLNRPHTQARRVTWAL | Function: Probably inhibits protein phosphatase 1 (PP1) in sperm via binding to catalytic subunit PPP1CC.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26483
Sequence Length: 230
Subcellular Location: Cytoplasmic vesicle
|
Q71BG9 | MAEILLTSVINKSVEIAGNLLIQEGKRLYWLKEDIDWLQREMRHIRSYVDNAKAKEAGGDSRVKNLLKDIQELAGDVEDLLDDFLPKIQQSNKFNYCLKRSSFADEFAMEIEKIKRRVVDIDRIRKTYNIIDTDNNNDDCVLLDRRRLFLHADETEIIGLDDDFNMLQAKLLNQDLHYGVVSIVGMPGLGKTTLAKKLYRLIRDQFECSGLVYVSQQPRASEILLDIAKQIGLTEQKMKENLEDNLRSLLKIKRYVILLDDIWDVEIWDDLKLVLPECDSKVGSRMIITSRNSNVGRYIGGESSLHALQPLESEKSFELF... | Function: Inhibitor of viral mouvements which confers resistance to some tobamoviruses including tomato mosaic virus (ToMV) (e.g. strains L, B7 and ToMV1-2) and tobacco mosaic virus (TMV), but not to resistance-breaking isolates (e.g. LIIA and ToMV2(2)) ToMV and tomato brown rugose fruit virus (ToBRFV) . Elicits a hype... |
Q5E975 | MMPSRTNLATGIPSSKVKYSRLSSTDDGYIDLQFKKSPPKIPYKAIALATVLFLIGAFLIIIGSLLLAGYISKGGADRAVPVLIIGILVFLPGFYHLRIAYYASKGYRGYSYDDIPDFDD | Function: Involved in trafficking and recycling of synaptic vesicles.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13158
Sequence Length: 120
Subcellular Location: Membrane
|
Q9DAV9 | MEYPWDDLTLAFSRTSMFPFFDIAHYLVSVMALKQRPGAVAAAWNNPLASWLSAMLHCFGGGILSCMLLAESPLKFLTNHTNILLASSIWYIVFFCPRDLVSQGYSYQPIQFLAAGMKEVTRTWKIVGGVSDANSYYRNAWIVMIVVGWARGAGGAVVTACEQLLKGDWKPEGDEWLKMSFPCKITLLGSIMFTFQHTRHLAISKHDLMFLYTIFLVTIKVTMMMTKDTAVTLTPFEDTLTRMLFGRRQQQQFSSSEKKTEVKPSSNGSASSASKRGAEPSGGAKRHAKKED | Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32640
Sequence Length: 292
... |
Q9NV64 | MPGGRRGPSRQQLSRSALPSLQTLVGGGCGNGTGLRNRNGSAIGLPVPPITALITPGPVRHCQIPDLPVDGSLLFEFLFFIYLLVALFIQYINIYKTVWWYPYNHPASCTSLNFHLIDYHLAAFITVMLARRLVWALISEATKAGAASMIHYMVLISARLVLLTLCGWVLCWTLVNLFRSHSVLNLLFLGYPFGVYVPLCCFHQDSRAHLLLTDYNYVVQHEAVEESASTVGGLAKSKDFLSLLLESLKEQFNNATPIPTHSCPLSPDLIRNEVECLKADFNHRIKEVLFNSLFSAYYVAFLPLCFVKSTQYYDMRWSCE... | Function: Regulates autophagy by controlling the spatial distribution and levels of the intracellular phosphatidylinositol 4-phosphate (PtdIns(4)P) pools . Modulates (PtdIns(4)P) levels by regulating the ER-to-Golgi trafficking of the phosphatidylinositide phosphatase SACM1L .
Location Topology: Multi-pass membrane pro... |
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