ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
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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-terminal rhodanese domain contains the catalytic cysteine residue.
EC: 2.8.1.1
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O17730 | MSLKKIIDVKSVNTLLKKGIINKEGVRIIDCSFAVAPRPDWKEFEQEGYGDFKNLMAEPSPSRNLYLAGHIPEAVHVDLDIATYPSRYQRFQQYRADLFEEYAQMVGLNNKEHFIFYGKGAFGGMLFASKVAWIFKSYGHENISLVDGGFDSWKRNGFEVSTELVKLPAGNFKAEDNFKKYVITFQELEAKKDGEDKQFIEKTSEINFLDSRIRGQFDGTQETGLDPHLVNGTRIAGFKNLPSAELLVKGGNLKSEEEIKSWLTQNGYVENQPTITSCNAGIQAALLAYVIDAVKPSQNPPRVYNGSLKEMELRAPKKISEGPQHLPH | 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-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).
EC: 2.8.1.1
|
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-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).
EC: 2.8.1.1
|
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 the reductant.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+)
Sequence Mass (Da): 27652
Sequence Length: 245
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.148
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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 the reductant.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+)
Sequence Mass (Da): 34876
Sequence Length: 298
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.148
|
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 the reductant.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+)
Sequence Mass (Da): 25383
Sequence Length: 232
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.148
|
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 the reductant.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+)
Sequence Mass (Da): 27622
Sequence Length: 247
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.148
|
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) as the reductant.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+)
Sequence Mass (Da): 24071
Sequence Length: 208
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.148
|
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 the reductant.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+)
Sequence Mass (Da): 26912
Sequence Length: 230
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.148
|
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 the reductant.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+)
Sequence Mass (Da): 27606
Sequence Length: 250
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.148
|
P31563 | MTLKMFLPVNLVSVCMKLNNSVVMVGLYYGFISAFSIGSSYLFLLRPRFLNDDPDAIEKKASETAGFFTGQLLIFISILYGPLHLALGRPHTILLLLAPYFFFHFLSSNSGQYPSQRFAFPLLTKSMRNRSFQLVFLHSLLFQLFSLSVLGRPMLTRLSYIYIFRSNNKMLFVLSSFVGWLIGHILVLKWAGLVFVWLLKFIRSKTMKYITCNVLIPATKYIIEKWRNSFVAGLIREILAMKQVESALVRIKNSRLLDDVRWWIRGSGLISGLKINIRFYARLILRGFENVYVGAKFRQDMEHLFSIILFAFFLLYLDRTPLLYADPADKKLQLQRKLSNETQAAREEKELEERLTEKFEAQRRAQRAAQRKALQEFKQGVVESYLANQAAKDENQIQAQKDEKQIQAEKKATIRAEQVVQYTFGLIEAQRREMEIEAARAMQEAYKGMLAAEEEDVEEGVQEKQEGFPEEPISPSEEREENPKLLILKEKISILTEKISILTEKNDLFSFEIPIITSLFDPQKPLRPLRYIKTCAGVEKAVKNEMSQYFFYPCRSDGKQRLCFTYPPSLATFWEMIQRKMASRFPRIYTKAKWRALRGSAPGSYRQWISRNKKKKNSLSTEFQNRIQTLDQKKSLLNVLARRKRSSLQNVLETRKRLCNYKTKKEYLPEIADPFLTGALRGKSDPEVYDGVRKTSEIKVVFLKNNITMATLGNKNDDDLREEKNAISLLSRMKNPVNKLHLLFVNERDYPFVKPLVNRINGPAVPKKKKTISKSKQNEIKSKQKKVKSKQKKVKSKQKKVKSKQKKVKSKQNEIKSKQNEIKSKQKKVKRKQNEIKSKLNEVKRKQNEIYPKGVKFNATPKTEINPHGIRFDAATIEKYSFATGYSYRPPSFHDIIFKAFVTEPQRNKKKVIELEEEINKQVPRWSYQLIDELEQLEGAEGETQFSDHEIRILPFKRVSVFTEKEAKKKPLIDEEGNYVRHKKTYAVRFLGHMSDFRRGLIKGS | 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
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Q6FEP9 | MQVTTEAVSGVARRLNVSVPTSRINEQFEARLKRTAKTAKINGFRPGKVPLSRVRSDFGPGIYQEVVNDIIRDTVFEAIQQEKINAVGMPNIEKVEHKDDALVYEATVEVYPEVEVKAFDTLEVERKAAEINDKDVDAMIENLQKQRQTWAVTKGMAKKDMQVTFDFEGEVDGEKFEGGSAEDFKLVLGSGRMIPGFEDGIIGMKAGEEKVIDVTFPEDYQAANLAGKAAKFKITVKQVEKPKLPEIDAEFLKIFGISEEDGVEKLKADVRKNMEREVRNGLRNQVKQAAFDALVAANEIDVPSAMVAQEIDRQREQMIQQFTQQFGGAGAQSFDKSMLPDELFKEQAEKSVKLGVLVSKVLADAKLEVDQARVDTYIDEMASSYEDPTEVVDYFKNDKQQRAQIEAVVLEDQVVDHILAAAKVTETEVSYDDLLKEQQARQAR | 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: 444
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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A0LSU9 | MKSAVETLSPTRVKFTVEVGFDELQPTVAAAYRKVAEQVRVPGFRPGKVPPPIIDRRIGRGVVLEQALNDAIPQFYGQAVDEAAVAVISQPEIEVTNFADGEGLTFTAEVDVRPTIELPDPESITVTVDPVTVSDADVDAELAALADRFATLKPVDRPARRGDFVTIDMTVRLDGEVLEDGTVTGASYEVGSAQLVEGLDEALEGLTAGQSAEFDAPLAGPYAGRTARAEVTVRAVREKQVPALDDAFAQQASEFDTLEELRAHIRERIGRTRRIQQHVQARERLLQTLLDSLDIPVPERIVDAEVRSRAEQLRRYAEARGMDAEGLLAQQGESLHDHEAHVRADVERELRVQFLLDTVVAREQLQLQEAELTDYLIQRATRLGVSPDDYANQLVRTNTVPLAVADALRGKALTYLLQRVRVVDTTGAPVNLEGGSTPAAEAEPAVSEA | 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: 449
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q0SMP7 | MILSKDIRLLPGSKVEAVIRVSKNIIQEKYNSLLQDYSSRLKIQGFRIGKVPISIIEKKYSEGLRATVLEEVINNSLKEFFKEEPKRPLSYASPTIKEENLRLNLDKDFEFTFVYETYPEFKVPNIDDIDIKVEVPEVFIDDSDIDNEIKSLQIENSIIIEDEEGVVKKDSIVKVDFVELDDLLNEIVSTKRQDFVFTVGKSETYYDFDRDVIGMRINEERVIEKSYITDYKFEELAGSLKKLKIKIKSIKKRDLPLIDDEFAKDISERYNTLDDLKNFIRSKILSLVEEKKEALKLNKFFSTISEKLEIDIPRSMIEAEIEIAFKDAKRQNKMSLEEFKSMFYSSGYNGSDSLKDEILSNLKSKLIIQKMVDLDPIKVTENDLKDEMVRQSENSGVSYEEIKKFYEDQNLIFYLKDDIKRKIVEKKILASLKEVKGKQVSFKDFVNYKICE | 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: 452
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q89KG0 | MQVTETLSEGLKHEFKISVPASDLDAKAGAKLVDLKDKVRINGFRPGKVPVAHLKKVYGRSVMAETIDQTIRDTNTQLFSERGFRLATEPKITMPSEQAEVEELLSGKTDLTYTVAIEVVPSIALADFKTFQVEKPVADVTDADVDEAIKRIADTNRGYAAKADGAKAESGDRVTINFKGTINGEVFEGGTGEGIQVVIGSNTFIPGFEEQLTGIGAGETRTLKVSFPKNYMNDKLAGQPAEFETTATSIEAPQDIAIDDEFAKTLGLESLDKLKEAARERLVAEFAGATRQRVKRALLDRLDEAHRFEAPPSLVDEEFNLMWNSVKAEMDSAGKTFADEDTTEDAAKEEYRKIADRRVRLGLVLSEIGEKNKITVTDDEVGRAVIERARQMPGREKEVWDYYRSNAQALAQLRAPIYEDKVVDFILELANVTEKKVSREDLYKDDEAEKTAA | 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: 453
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q2GFT7 | MLNSYVVREVSNDKLKWEYEFAVDKKYFLDQLDSKLSEIAMNVKVPGFRVGKASIDLVRKEYLNEAMTSVVKKTIESTSSDFVKNSKFGEIISSNIDIVSYPSYYSDNDKEEDLVYKLSFEVMPEAPLMDIDNIVLSDIEVDIQECDVNEFIENLKKQRPDFVIVDDPEYVIQGSDKLVIDYQNKIKGKILRGGSAKDFVLVLGKGVALREFEDQLIGMKVGESKTFPLTFPNDYGMVHLAGKTTDMSVTVKSVYVMKGMRDSEAIAKDYGFKDVGHMEDFARKRIKQQFDQMVFTIVKKELFDYMDANYVIDVPECVVTQEIAKINKEIRDSGEDIQIDVEKEAIKRVKLGMLLIKMSRHNNITIKNEDVFSFIQSNYADYGVDIGNVLKMLQSNKNFANYISGKVLEEKVINYIIGLAKKDKKVMTAKDISLMFENI | 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: 439
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q2NDC7 | MQTKETTNEGLKRAYKLTLTAKEIDAKIDAEVKKVAPQVRMPGFRPGKVPANLVRKMHGEQMHAQVINDSIRDSVDALIKEKELRPAMQPKIDLNEDYEQGKDAVVSVSLEILPKVEAPSIDDLKLERLTVPVSDEQVMETIERIAGQNKSYKDAAKTRKAADGDQLIIDFTGSVDGVEFEGGKAEDAPLVLGSGTFIPGFEEQLKGVKTGDEKTITVTFPKDYQAENLAGKEAQFDVKVKQVKVETDTTIDDEFAANLGLENLDKLKELIRGQLEQETNGLTRTAMKRSLLDQLAAGHDFPVPEGMVDAEFEQIWNQLQQEAAQEEDPDKALKEIEAEKDDYRAIAERRVRLGLLLSEIGQANGVEISQQEMSMLTMQAAQQYREEDRERFMQFIQQDPMAAAQLRAPLYEDKVVDFLFDKAEVTDREVTREELEAAIEAEAEEEKKPAAKKKAPAKKAEPKKAAAKKAPAKKAPAKKAAAKDGDEKPAAKKAPAKKAPAKKASTKKPAEKKAPAKKPAAKKAPAKKPAAKK | 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: 533
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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B0S2N7 | MSAVLVSKENNQAVFTCEIPAEDFNNAIEESYKKNRSRFSLKGFRKGKVPRKMLERAYGEGLFYEDAVNLLLPGIYEKAIEELELEPVSQPDIDLDDITENNDVKVKFTVDLKPEFELGDYSKLSAEIEEFKVTDSDVDMKVNHELESNARVQEVEGREAKENDTVSINFKGFVDDKAFDGGEAEDYELVLGSHTFIPGFEEQIVGHNAGDEFDVNVKFPEDYHEDSLKGKDAKFECKINSIKEKVLPELDDEFVKDVSEFDTLDEYKKDIKEHLEKDNEQRQLVEKQNKAVEALIEATEISVPESMIDNEVNRQFQDFARRVQQMGLNTDQYFQITNTSEEDVKNELRANAELKVKGDLVLEKYIEKEAIESTDEELDEQLKEFAKVYGKDDEEKFIEEFKNSPNVEFLKEDIKRKKALEKLVENTKFEIKKAEEKEDK | 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: 440
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q0RPH4 | MKATKETLSPTRVKLTVEVPFDELKPSLDATYRKLARQVRVSGFRPGKVPPRILDQRLGRGVILDEAVQEALPQLYSEAVQAEEVDVLSRPEVDITEFADGGQLVFTAEVDVRPEVALPEFADLSVTVDAVEVTDEQVEEQLGALRDRFAQLQPVERAVQTGDFVSLDLSAQADGKPIEGAEATGLSYEVGSGNLIEGLDEAIVGAADGESRTFTTELLAGDQAGQQAEVTATVRGVKEKELPALDDDFATTASEFDTLDDLRGDVRSRLEQSRRTEQVGQAREKLLESLLERVDVPVPDSLLAGEIEAREHRLSHELENIGTDRATYLETLGQTAEEFDAEVRETAGKAIRSQFILDAVIDAESIGIDQGELMEQVIYRAQRSGLQPDVYAQQLAQGEGLQALMADVLRTKALFLLLENAKVVDGEGNPVELALPARPAPDADEDDDHAGHDHEGHDHADHAGHDHAGDDAAAEPAEAPAATAAVDSGDRDI | 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: 493
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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B0TZA4 | MQVTVEKKEGIHCSLLIEVPANEVDSIVTKEINKTAKTIKMDGFRPGKVPAGMVEKKYGEQIRMEVISDLIPQKYSKAIQDEKLAVAGIEVELKENKKGEPLKFVANLELFPEFEVTGFEKIEVQKPVVELTDKEVKQMIENLRKQLATFSEVERAVQKDDKVVIDFVGKRDGEVFEGGSANDQELVIGSGQMIPGFEDGIIGMNKDEQRTITVTFPEDYQNKDLAGKEATFDITVKKIQEAQLPEVDDEFVAKFGVKGGVDTFEDEIKENMQRELKFILQRKVKDQVFKGLREIAEFETPKALIKREIDAAKQNLVKQMGGGQNFDVNQLPDNLFEANAKQKVETSLILDSIIESQKFQAEDAEVESLLDELVQAYEEPEKTKEQIKKNDREISNLKGLVIENKLTDWVLSQAQVTEKQEDFFEVIKENMQAQQAGF | 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: 438
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q4FM95 | MKVTVENKKGLNKDIKVFIDKETMNSYMDEKYEEIKKTVNLKGFRPGKVPKEVLKRQFGQAIFSEVLDKVLKDTSVKALEDNKIKPAGQPKLDLKTYGEDKDLEYVMSITELPKVELKSVENIKFDEYSVKIDTNETDKRIKEIAKSQNNFKEVAADVRAVEENLVIFDYKATIDGKDFTGGEGKNTQLILGKDLFIKGFDKQLIGVKKNDEKSVDVTLPENYPQKEYANKKANFICKITEVKKSEEVKIDDVFAKNLGAKDLADLKVLVSKQINDEYKNSLDKLAKTQILKEIENFKVDEIPENLIEEEVKILSQGMTEEDSKKSRKNFEEIAKKRIKVGLILNEFGEQNKIKVTEQEVQAEVQKQLRMMPGQEKMVMEFYQKNPSALASLRGTVYEEKIIDLIKTKAKPSKKEISKEEAEKILKEHQKQDHNHEHDHNHDHDHPEEKKASKSTKIEKKPKPSASKKPSTKKVSKK | 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: 477
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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A3PFE3 | MAKDALIVKTTPLPQSRISFELEIPSETCKTCVNETISTISRSAKIPGFRLGKIPKQVLIQRIGITQLHASALEKIIDKSWQEALKIKSIEPLSEPELVDGFESLLAKFSPEKSLKVTLQTDVAPELKLKKSKGLSVEISKTKFDPKSIDEALEKSRNQFANIIPVTNRAAKLGDIAVVSFKGKYKDSGKEIDGGTSESMDLELEKNKMIPGFVEGIVKMKIGDTKTLNLKFPEDYSHEDSRGKEAIFEVNLKDLKEKELPELNDDFAKQSGNKESLKELKKDIEKQLKDNFEKTQKDIKIEALLDALTNELVTEIPKSMIDLEVRNNIEQTAQRFAQQGLDVKSTFTPELVKSLAESTRPQAEKNVQRNLALKALAEKENITIDKSEIDLKMKEYDDVISQSSKQIDIKKLTEVISNDLLKEKLIIWLEENSEVNEKTTKTSKATKTSKTTKATKTATKTTKTTKTTKTQNKKEKK | 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: 477
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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A2C5C0 | MSAAKLNVKTSSKPNSRIAVEVEVPANRCKNSYDEALSKLSRSISIPGFRKGKVPKTVVIQQLGVKRIQASALESLLQKVWTETLDQEGIEPLCEPELEDGFETILENFNPEKTLILKLETDITPIPTLKKSSGLTAEVENLIFDPKKVDELIEQSRAQLATKVPVTDRAAQKGDIALVSFKGSFSDDGSEIEGGSADSIEIELEQGRMIPGFIEGVIGMNINDEKILKCEFPKDYHQEEAKGRKAEFNVSLEDLKIKELPELNDEFAKQASDKENMSDLRADLEKRLKEDNDRKQAKTRQDSLLDVLVKELEVDIPKSLIDQEVRIIVEQTAQNFAQQGIDVKSMFTPELVKSLMESSKGEAEKKLRQKFALKALAKSEKIEVSDKEINSKLEQVEADIKLSNEKNIDAKRLKEAITDDLLQEKLFAWLEENNTVVEKPPEKARDQIKEKSSKKKTTKTNKEKKSSKTPKS | 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: 472
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q73M39 | MDYEKNVTLKEKSHAELSVKIKKSDVQESYKKLLNKYSKELQIPGFRKGKVPVSVLETKYGDAIKGDLAGDLIEESLKEIFESLDEYERPLPYSYPELNEKPELKVEEDFSFTVHYDVFPKVEIKKTEGFTIEVPEASVSEKDIKKELERLQERNALVTACKEGTSAEKDHIATIDYCELDDEGKTISGTERKDFVFTIGSGLNIYKIDDDIVGMKKGESKEITKTFPEDDSNKDLAGKTKKIKVTLTALKYKDLPALDDDFAQDINEKYKNLDELKADIKKKFEISVEEKIKSLQKNALTEQMVKEHTIDLPESMVRAELESRWMMMANQFRTTPEELEKMFGKGPQSKAALLEGWREDSEKTLKERVLIETLLKEKNIEVSDDEIEAEYVRLSERMDIALDELKKYYSNPREKEYLSEGLKEEKLFKALYEKSTIKKGKKLTFDELLKD | 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: 451
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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O83519 | MELQKKFTALAQSQVELEVVVAREDAQRHYQRFVEEYLERARLPGFRKGKVPLAVLERKYGSAIRQDAAAALMEKALEEGFAQASQDSQPLPISRPSLKKKPVFDPDEDFSFAVIYDVFPSVELRNTSGFSLSVPTVSVTEEDVSRELTRIQERNALVTDKGADSCAEVGDIATVDYHEVDDSGAVRPGTERAGVVFTLGVEEGPFALGQDILGMKLGQRCLFAKRAGMLKDEAAQVRVTLKALKQRQLPSLDDELAQDVSDAFRTLDDLTRSVRQNLAEALEAALHEYKRRQLLRILVRENPFSLPESLVVGEMESRWALVMRQFGVSLSGTPQNKLQFFQQWRPEVEEHLKQRVIVELLLKQEQVSVSAEEIETEYVRIASKTGSKEERVREYYAGEEKRRALCEGIRERKLCQKLLGRCVTECGPEQSLTDFLQEQSRA | 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
Sequence Length: 442
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q118P4 | MKVTQEKLPASQISLEIEISPEMSKNAYEQIIKKYIRSANIPGFRKGKVPRNILIQRLGKNYIKAMALDDLINNCLEKAREQESIKAIGQFELKTEFEELVKDFEPGKEMAFSAKVDVEPEAKVEDYKGFLVQAEEAKYDSALVDEFLEERRSRMGTLIPIEGRAAEMGDVAIVDFVGIIPSETEGEEAQEVPGGKAQDFQMDLKEGQFIPGFIEGIVGMKLQETKEISAQFPSEYSEANLAGKPVVFTVTLKELKEKELPELDDDLAQEISEFETIDKLREFLEQKFTKEKEEKTKQNKEKAIIDELVTHLEVEIPETLIKNEVQQMLAQSAMDLSQYGIDVKEFFSSEKLPEMQERTRPEAIERLKRDLVIATVAKRESITVDEEEIKAESQKVVKQLKEKDFDSDRLRQVVTQELLKEKTIKWLEANGTVELVPEGTLHTESQTPQTTEILETEVESEIPQASETIVEVKAEEVATVENSQE | 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: 485
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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B3E1Z5 | MQVKIEEISSVKRRISVEVPAERVNTEIEKSFAGIQKKATLAGFRKGKAPLQMVKKFYRNAMQDEVMRRLYEQTLFPALDEHKLEPVDAPMIDDIALVEEGTPFKYSALIEIMPQILLGEYKGLQVKKERYVADEKAVEGEIERMRENMAQLAPVEEGTVEKGMVLTVDFSFAVPGYPEEETSGKDASVEVGNGRLLPGLEEGLIGMALGETKDITVTMPDDNPNKELAGKPGVFTVTLKEIKKKELPELNDEFAQQFGDFETIADMRTKLTEMREQQELERIKTDLKTRIIDALIEKNPLEVPDSMVRRQTDFMLENLKNRLKGQNMSLEMMGLDEDGYRQRFWGEAAQKVKGGLLVMALVEQENIAVEEADLEARYAQIAAGNEDMLSRIKEFYAAQANARNSMVAEIKEDKAIAFLLENAVVTEVEAAELNAPVAGE | 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: 440
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q3M725 | MKVTQEKLPASQIGLEIEITPEITQKTYEQVIKNLSRTVNIPGFRKGKVPRQVLLQRLGKTHIKAAALEELLQDGIEQAIKQESIAAIGQPRLRSSFDDLINSYEPGQPLTFTAAVDVEPEINLVQYTGLEAKAEEIKYDPARVDEVLEKERQELATLIPVEGRAAQIGDVAVVDFKGVIAKAEGDDENAEPEPIPGGDASDFQVELQEDKFIPGFVTGIVGMNPGDTKEVSAQFPDPYVNQELAGKPAIFTVTLKEIKEKELPELNDDFAQEVSDFDTLEALRASLAERYQKEAEDKTKNNQQEALLGELVKHIEVDLPETLIEKEVDAMLTQTAMRLSQQGLDVKKLFTQDIIPQLRERSRPEAVERLKRSLGLQEVAKRESIAVTPEEIQARVTELVQQYPDEDIDVERLHTIVENELLSEKIIDWLLANSTIELVPEGSLASQESEITAPETEAETIEVTAESTTGE | 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: 471
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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B5ZBF7 | MKLLNKIKNENAIEFQVLIEKSEWEKKHNEAFEKVAKKTASKLKIPGFRPGNVPVEEAKKHVNEIEVFETTTNDLVPQALTFLEQDESFTSDNSETVDTPSIDILDFKDGELTLKIAYDLYPVATIDSYNDLVLTPIVNEAFDHEVNAEIEHALSSKSQRRVKDENELIEKGDEVRFDFKGMIDNVPFQGGSAKDHLLTIGSNQFIPGFEDQMIGLKVGEQKNLEVKFPDDYHATDLAGRSAVFEVLIKEITSVKPQELNDEFAKSFNLPNVNTVQELKDYIHNQIVLAKQERNSERAWLEIAQQLLAKAKVTPIPQSLIDREVSTLKQQVISQLSQYKIDLKQYLEFSKKSESQFQEDLVKQAKETIALALLVDDIAENQKIVVSDDEVKERIAEMAKLYQGEEEAIIERLSQNPDAVKEFLLHKKVVNYLIDLNKNNQPKDTASTLSKQEDKPKVAKAKTSNTKKVASKK | 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: 472
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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A1WR16 | MAVTVETLDKLERKMTLSLPVTLIQSEVDMRLRRMARTVKMDGFRPGKVPMAVVARRYGDAVQYEVLTNKVGEAFTVAANEANLRVAGRPRITETQGTAEGHVTFDAIFEVFPEVRIADLANVEIEKLSTEVTEASIDKTLQGLRKQRRSFAQRAHDAPAQDGDGVTVDFEGKIDGEPFANGKAENFRFVIGEGPMPKEFEDAVRGMKSGESKTFPLAFPTQYHGQEVAGKTADFLVTVKKIESAHLPEVGEALARSLGSADGSIEGLRADIRKTLEREIRSHLRARNRRAVMNALLANADLELPKASVQDEIARLKANAYADLKQRGVKDPERLEIPEDKVRPTAERNVRLRLIFSEMVRAHGLRAKPEQVRAYVEELAASYEKPAEMVRGYYGDRRRMLEIESSVSEDNVTEFVFARAKVVARTISVDELLNPKDPKD | 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: 440
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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A5CXJ7 | MKTSLETLKGLSRSLTIDLPIDIFNQKMDKILQKMALEVNIDGFRKGKVPISIVRKRFGNNANSDVINEIVNETLTDALAQVKLTPVAQPVITKVDSNSNKNFSYTVEFEVFPKIKIADFSELSIEQTKVNITKADEQKTLDGLKDRLTEYKAVQCKSKMGDRLSIDFKGLINGETFDGGEAKDFKIVLGKGSMIKGFEEGLIDVAYSSRVVLDLTFPKDYYMDKLASKDVTFEININEIASPKELKLDETFAKKFGEKNMNALRVSMKEQMRVEVDGRIGHLNKNAIFDKLTTANPFNVPQHSIDNEAQNLFKAMQDRMQHQGLSTQGEMPITAFNDEAQRRVKLGLLVNQISRDYKLSVSMKQIDEKLKEISKTYGENAQQMIDFYNQDPTRKSSIELLVVEKMVQDLILDKAQVTFKQKKFQEITQ | 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: 429
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q87R81 | MQVTVETLEGLERRLNITVPAANIEDAVTAELRNIAKNRRFDGFRKGKVPLKMVAKMYGKAVRQDVLGEVMQRHFIEAIVKEKINPAGAPTFAPVENKEGADLVFTATFEVYPEVELKGLENITVEKPLTEVKEADVEEMIETLRKQQATWVEVEEAAEAGKRVSIDFVGSIDGEEFEGGKAENFPLEMGAGRMIPGFEDGIAGKTAGMEFDIDVTFPEDYHAENLKGKAAKFAIKVNKVEARELPELNDEFVAKFGVAEGGVDALKAEVRKNMERELKQAVKTRIKEQAIEGLVKENEIDVPAALIEQEIHVLRQQAAQRFGGNPEAAAQLPRELFEEQAKRRVVVGLLLGEVIKSEELKADDEKVKALIEEMATAYEDPSEVIAYYEQNEQMMNNMRNVALEEQAIDAIIAKAQVTEKEVGFNELLNQQPAA | 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: 434
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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A8F7F8 | MPLDEFEFSVLKTIQTHHLIFPGHKVLVALSGGMDSMSLLNILLKLRQKLNCEIFAAHLNHMIRENAIRDEQFVYSYCKKAGVKIFVERFDVPKFCADRKIGIEEGARAARYTFLNRIAHENGIDLIALAHNLNDLVETILYRIVRGTGLSGIVCMKLKDENKIRPLLYFKREQIEAYIKRNNIPYVQDETNFNLKYSRNYIRHRIVPALKLLNSDLENAFSQVHFSGMMLENHVKRLIKKYSERIFRCGKRIIFDSKDMDEFEIIELVKYCAGQMNVDLNYRQIQLVVSKLNENSWSIDLSEDIAIKKGFDFFSIEKKCKFMNILKVGKPGVYKFNDWTFELSSEVKSNEYVFIHDQGGVCIRKRKAGEKIAGVKMKDMMIDSKIPAFLRDEMPVVCTIDRIIWVPYVYVDRCFKERKEDSLVLNLLQNPYSCILELRKDERRKMV | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 52344
Sequence Length: 447
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q886M6 | MTTSTPNGHDLPARLLQALAPWRTASTWYVGFSGGLDSTVLLHLLAELAKRANLPALHAIHVHHGLQAIADAWPEHCRQVCQALGVAFESVRVKVEPGASVEQAARQARYAAFTERLGEGDVLLTGQHRDDQAETLLFRLLRGAGVRGLAAMPEQRRLGRGHLARPLLGVSRVELESYARRQGLRWVEDPSNDDQQFSRNFLRSQVLPLLTSIWPHATASLARTAGHLGEAQQLLDELAAQDVANAQATTPFSWLGLPVLNLGPIARLSGARQRNVMRHWLAPLTRLPDSDHWAGWEALRDAAQDARPLWRLADGALHRAQGCIWWLPAGWEQACSEAVNWADPRAPLDLPENGQVSLEGEAPLGDLSVRYRQGAEVMHLSGRGRRDLKRLLNEQAVPAFLRGRWPLLYRDDELLAVANLPGLDGSPNERWRLRWVAPTGDQSLS | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 49247
Sequence Length: 445
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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A5WCA0 | MTTPVCISQAFMDSFHAHHAQLLGKRVWLACSGGRDSLGLALLCRTLFDQGRLPFLPQLIHVNHGMQAANDEWAQQVAQWAQQHDMACQIIGLNLTHKSEQAARDGRYQAMMQLMNQDDVLILGHHQDDQVETLLMRLFNGAGVTGLGAMREWTSKQAHTAQSPPDVNKPRQRIFLWRPWLEISRDQITEYAQRHNLKYIDDPTNVAQSPSKLALQTLNDRAWLRSVLLPHITERYPQASEAMARTAQLMQQASDSIDEQVTQDLAQVALAATEQQSVIALDKLAGLSAPRQAALIHHWLAPYPNQLPPSKRLVDEVLALSFRQDSNHQTCLYFDAGSEQYQVRRYQNKLYRLQHAYAQWLQMMPHQIHLPLAHNAEELSLNLADTDVLSLKQSGLEFDWQLTGVRGLMAHLARLLNSADAKVTPCQLIFEPLPRTIKLALAGRSGRKSGKKLLQALDQPSFMRGSVVLCRLDMMGSDGILQDSSTAVPLFIICIDRIWVLQSQFTALINQLLATEVLSTQILEC | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 59124
Sequence Length: 525
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q8Y074 | MLLVDKVAQRVVACAAFVVSGGVPTVAVALSGGRDSAALLHAVAAWRDAAGVPVRLVALHIHHGLQADADAWEAACARMAAAVGAAFRVRRVRVSTDAGRGIEEAAREARYAALDALCAETGATLLLTAHHLDDQAETVLLQLLRGAGLDGLSAMPMARERRVTLLRPWLDVPRGDIEAYARAHALAWVEDPSNGDARYARNALRPLLAGMAGHFPAYRASLARSAAHLAEAAALIEEVAQTDLARIAPAGTLAVAGLAALSGPRQRAALRAWLAGAGLRAVSSRRLEDLRAQLLGARADGAPCVRLPGAQVRRYRGQAWIEAAGQPGAGPADCPIAVSRFDPARAEVQRVDVAAWGGALLFSPAQAEGIDARILQAPLSLAARRGGERIVLRPGGPSRALKQAYQEAGIPAWARARLPLLYAGERLVFAAGLGPDRSAVAMGSGWHVAWLPAVGQDGLDAG | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 48155
Sequence Length: 462
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q98F87 | MLDTEPDLSTRLFSHIDFTHGAVAAVSGGSDSTALLLLLKHHFDRTGSSAKLLAVTIDHGLRQGSAAEAQAVAKLCAERGIAHRTLTWTGRKPSTGLPAAARDARYHLLAEAARAEGIGLIVTGHTADDQAETVLMRHARDRELADLAGRGLAGMAPATLYDWREWIVRPLLGTRRSALRDFLRREHVGWAEDPTNIDEAFERPRVRAALAGESAGHMENTLRLAGQAAVERGQLGASAANLIRRIASQPSTGLIRLDPALLIADDQAAIYALRILLATAGGAAFLPDQARSAALFVRLKAGFLCATLSRTVVDFRHAGLFLRREARGLPPAATAVDNTIWDGRRHITLNDMSGALLIAPLGAAAARRLAIDDGETPASLIRAALAAEPTLLQAFENLGLPQGEPRLPVFAARPVVSPFARFLPSFDLAPARAVAELIGASPLPASPLGGHSAD | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 48158
Sequence Length: 454
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q92JY3 | MPHAVLDTARNFLRSFITPRRILVAVSGGSDSMGLLVALHSAIAADERRGFSLAACTVDHALRPQSACEAEDVAAFCAALGIAHRICRWEGAKPSTGIQAAARNKRYELLAEAADALGADCIAIGHTRDDQQETVAMRIARGKGDGAGDGQGEGHGGAGMAASMLYGRRIWVLRPFLGLARAEIRSFLQARGVSWIDDPSNANPAFERVRVRARIATSGGMPTPLGNGRQRAASSARAAALIEKRIRVHEALVAEVSARHAGEIDDPDWRRALLTVASVLGGREHMPAFATVQRLSQFLRSGEPGRMTAGRVVFDRRASGLYLYREARNLPVLAVGPGRQGAWDGRFTVKSRGPAVTVAADASGRLWTKRLIDAGLPAGIAKRGSTVAPEIASTDGAGLAFGEAPAQVEYHIGLYDTFLPGFDRIMADAVAVSFGRDRYPAPPVHDVLIEMET | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 48266
Sequence Length: 453
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q7UNE1 | MIGDVLPTTPNESPNWHRLRRAIRSTWPNRHGRSSDVATLVGCSGGADSVALICLLAELWAEESNGLNPANETVTKPVAPLVVAHCNHGLRGEESNADEAFVRQICDQLQLPLVIHHVPPLNNSATSGPVSDERTLRQIRRDFFERAAKQHGCRYVAVAHSADDQAETMLHHFIRGTGPLGLAGIAEASELDTDIVVRRPLLQVRRDTLRDGLREIGQPWREDASNRHTIYTRNWIRHDVLPLIESRYPNAVEAIHRAGTLQHEMNEMVRRLAERWLEAFTDFSGDRWTIHTERLSKSATPEKRMDDTNAACSWMIERPVIVAASQLAWDRLGWSRGSMTMQHWQRLTGLINDQSCWHTSDIDVSTSQAVDGIDHGGHFPGGICLSVEAKQLVLRSE | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 44519
Sequence Length: 397
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q6NAQ6 | MSGTDHEAVSATEARRLFADWKAAPAIVLAVSGGPDSLALMWLAARWRKALKRGPALAVVTVDHGLRPEAAAEARAVKRLAASLDLPHRTLRWSGDKPSTGIQAAARGARYRLLAKAAKTLGASHVMTAHTRDDQAETVLMRLSRGSGIAGLAAMAREIERDGVVLARPLLDVPKARLIATLAKARIAFATDPSNADPRFTRPRLRELMPQLAAEGCDARSLVRLAVRAARADAALELMTDGAEQFLASLDAGSERPGVNARAFLGLAAEIQIRLLLRTLSRHGHEGPPELGKVEALAEALSQAAARRPQAAAKIRLKQTLAGAVISLTGDRLVIVPAPPRRGRVR | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 36825
Sequence Length: 346
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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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. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13868
Sequence Length: 128
Domain: The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function (By similarity).
Subcellular Location: Mitochondrion inner membrane
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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 membrane
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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 activity.
Subcellular Location: Mitochondrion inner membrane
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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/TIM14. May act by positioning PAM18/pamR in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15100
Sequence Length: 135
Domain: The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function (By similarity).
Subcellular Location: Mitochondrion inner membrane
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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. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15147
Sequence Length: 138
Domain: The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function (By similarity).
Subcellular Location: Mitochondrion inner membrane
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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 co-chaperone activity.
Subcellular Location: Mitochondrion inner membrane
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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/pam18. May act by positioning tim14/pam18 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15805
Sequence Length: 141
Domain: The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function (By similarity).
Subcellular Location: Mitochondrion inner membrane
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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 does not have co-chaperone activity.
Subcellular Location: Mitochondrion inner membrane
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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. May act by positioning pam18/tim14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14120
Sequence Length: 128
Domain: The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function (By similarity).
Subcellular Location: Mitochondrion inner membrane
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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 membrane
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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. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16500
Sequence Length: 147
Domain: The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function (By similarity).
Subcellular Location: Mitochondrion inner membrane
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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. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16216
Sequence Length: 149
Domain: The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function.
Subcellular Location: Mitochondrion inner membrane
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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
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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
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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
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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): 16584
Sequence Length: 158
Subcellular Location: Mitochondrion inner membrane
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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 be involved in the assembly and stabilization of the TIM22 complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21972
Sequence Length: 192
Subcellular Location: Mitochondrion inner membrane
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Q9BSI4 | MATPLVAGPAALRFAAAASWQVVRGRCVEHFPRVLEFLRSLRAVAPGLVRYRHHERLCMGLKAKVVVELILQGRPWAQVLKALNHHFPESGPIVRDPKATKQDLRKILEAQETFYQQVKQLSEAPVDLASKLQELEQEYGEPFLAAMEKLLFEYLCQLEKALPTPQAQQLQDVLSWMQPGVSITSSLAWRQYGVDMGWLLPECSVTDSVNLAEPMEQNPPQQQRLALHNPLPKAKPGTHLPQGPSSRTHPEPLAGRHFNLAPLGRRRVQSQWASTRGGHKERPTVMLFPFRNLGSPTQVISKPESKEEHAIYTADLAMGTRAASTGKSKSPCQTLGGRALKENPVDLPATEQKENCLDCYMDPLRLSLLPPRARKPVCPPSLCSSVITIGDLVLDSDEEENGQGEGKESLENYQKTKFDTLIPTLCEYLPPSGHGAIPVSSCDCRDSSRPL | 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 damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Plays a role in shelterin complex assembly. Isoform 1 may have additional role in tethering telomeres to the nuclear matrix.
Sequence Mass (Da): 50023
Sequence Length: 451
Domain: The TBM domain mediates interaction with TERF1.
Subcellular Location: Nucleus
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Q9QXG9 | MAPPPGVGPASLRFAAAASWLVVRRRRVEHFPKVVEFLQSLRAAAPGLVCYRHHERLCMSLKAKVVVELILQARPWDQVLNALKHHFPAESRTTKEDRKLLEARENFCLLVKHLSEDPPSSLQELEQDYGESFLVAMEKLLFEYLCQLEKALPPVRAQELQDALSWSQPGSFITSSVALHQYGMDMGWTFPESSTSGSGNLIEPMEESPHQQTRPAFHSPLPKAKLGPHQPASLEHPEHLAGHRFNLAPLGKRKSRSHWTSAKACHKERPTVMLLPFRNMGLPAQDLSNPKSREEPGAASAASVGTEPVCTEEAKTPSRPLGKRALEETPPDSPAASRRTV | 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 damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Plays a role in shelterin complex assembly (By similarity).
Sequence Mass (Da): 37887
Sequence Length: 341
Domain: The TBM domain mediates interaction with TERF1.
Subcellular Location: Nucleus
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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 efficiently by FYN.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 29197
Sequence Length: 269
Domain: The SH3B/LBD1 (SH3-binding) region binds LCK SH3 domain and CSKH (C-terminal Src-related kinase homology) region binds the kinase domains of LCK. Both motif are required to activate LCK (By similarity).
Subcellular Location: Host cell membrane
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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 a vesicle-based metabolite routing through or between pre-vacuolar compartments and the central vacuole. Transports urea in yeast cells in a pH-independent manner. Transports H(2)O(2) in yeast cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25620
Sequence Length: 251
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Vacuole membrane
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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 impaired by Hg(2+).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25821
Sequence Length: 250
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Vacuole membrane
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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: Multi-pass membrane protein
Sequence Mass (Da): 25849
Sequence Length: 253
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Vacuole membrane
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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 pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Vacuole membrane
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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.-
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Q9C0W8 | MMSQQLIDFIDSRTRHPYKSDEVEKFQQEVNELQLPDPNSLPILSEEEKRQAREDAAFRRSSEGLEDAWLDSAIPADPTPIFRDTVELLCVYQSFVKKSASLDTVANFLDFSTDFSTLSTKKDETEIAPDCLHYIAELLFQKKEREVKEKWKNELTEKLKTLFNWPAINPNLKESSKFESFFGFVRSIQSFKDSETGLPLFMQVYITPYVNQFRYHFMSQKQTNVLSKPEWFFEFLLKVFRSNRSFYMLMRDIKFFPGVPPFFTFINLLNNVAKEKLTHIIKYDDYLVHLVHETLQYSVRLEQHFHYTQDPLIIFLFEQNGTYDKWLGLETQLSLTKLEDIKIASDAWELESDQSDDFSSAVPTKMTVRFRDMIETTFSVLQNLPSLDYQFNFWRSVQLKPMMQYVNWLEAFYESHESSSSIHLPGSLQTDKSKFDIAEVERMCKLYSNFKLLMDWLDDIEDEDVYIRIGHKMGSENYAAFYQVKPRLSTLTNGSFRMILRAVSQTLRPLLDNYSDLDTWVIKEQLPGAALLSTSVSAEIVGFQSRLKEIIALLQKLLIGSSQCEAIYQIGTLVESWMIKIVMTHQFSVRGGVQFAMDAMQIVLEFSDYPLLKFERLMSTVELLSLESGENKLIKKLIIEINQKNYDFIDEFFKTKEITLSYEDALGVLYRRVDAWKD | 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
Sequence Mass (Da): 79407
Sequence Length: 678
Subcellular Location: Endoplasmic reticulum membrane
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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
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P51854 | MADAEARAEFPEEARPDRGTLQVLQDMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAKRLSFVDVATGWLGQGLGVACGMAYTGKYFDRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKLIESQIQTSRNLDPQPPIEDSPEVNITDVRMTSPPDYRVGDKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTRPETMVIYTPQERFEIGQAKVLRHCVSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVPQSGKSEELLDMYGISARHIIVAVKCMLLN | 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-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Sequence Mass (Da): 65333
Sequence Length: 596
Subcellular Location: Cytoplasm
EC: 2.2.1.1
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Q99MX0 | MSEAEASSGMAHNAGPDEKTLQVLRDMANRLRIRSIKATNSSTTSYLIPCSNAEIMSVLFFYTMRYKQEDPENPDNDRCILSKGLPFVNVATGWPGQGLGAACGMAYTGKYFDQASYRVFCLLGDEESTEGSVWEAFAFASYYNLDNLMAIFDVNRIGHSSSMSVEHCIAIYQKRCEAFGWNTYVVDGRDVKTLCHVFSQAAQVRGKPTAVVAKTFKARGMPNVEDAESWYGRPMPKERADAIVKLIESQIQTNKILVPSPPIEDSPQINIMNICMTSPPVYVADDKVSTQRACGLALAKLGHENDRVIVLGSDTKNCNFSDIFKKEHPERFIQCCIAEQNMVNVALGCSTRDRTIVFAYSFAAFFTRAFDQIRLGAISQININLIGCHCGVSTGDDNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLAANTKEMCFIRTSQAETAIIYTTQETFQIGQAKVVRHSDNDKVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIATIISNAKATGGRIITVEDHYPEGGIGGAVCAAVSMEPNIVVHNLAVMDVPRSGRCNEALDFSGISSRHIIVAVKCILMT | 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-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Sequence Mass (Da): 65245
Sequence Length: 595
Subcellular Location: Cytoplasm
EC: 2.2.1.1
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Q9H0I9 | MMANDAKPDVKTVQVLRDTANRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEVGDISESDLLNLRKLHSDLERHPTPRLPFVDVATGSLGQGLGTACGMAYTGKYLDKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDVNRLGQSGPAPLEHGADIYQNCCEAFGWNTYLVDGHDVEALCQAFWQASQVKNKPTAIVAKTFKGRGIPNIEDAENWHGKPVPKERADAIVKLIESQIQTNENLIPKSPVEDSPQISITDIKMTSPPAYKVGDKIATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEIFRKEHPERFIECIIAEQNMVSVALGCATRGRTIAFAGAFAAFFTRAFDQLRMGAISQANINLIGSHCGVSTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAANTKGMCFIRTSQPETAVIYTPQENFEIGQAKVVRHGVNDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKATGGRVITVEDHYREGGIGEAVCAAVSREPDILVHQLAVSGVPQRGKTSELLDMFGISTRHIIAAVTLTLMK | 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 decreases and proliferation was significantly inhibited in cancer cells. Plays a pivotal role in carcinogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Sequence Mass (Da): 67877
Sequence Length: 626
EC: 2.2.1.1
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Q9D4D4 | MALARDAKLESDTLQVLQDVANRLRIHSIRATCACSSGHPTSCCSVAEIMAVLFFHTMRYKQADPEHPDNDRFVLSKGHAAPILYAVWVEVGRICESDLLNLRKIHCDLEGHPTPRLSFVDVATGSLGQGLGAACGMAYTGKYFDKASYRVFCLMGDGESSEGSVWEALAFASHYNLDNLVAIFDVNRLGQSGTAPLEHCTAVYEKRCQAFGWNTYVVDGHDVEALCQAFWKAAQVKNKPTALIAKTFKGRGIPNVEDAENWHGKPMPKDRADGIVKLIENRIQTNRNLTPKPPIEDSPRISMSNTKMTSLPVYKLGDMIATREAYGLALAKLGQSNQRVIVLDGDTKNSTFSEVFKKEHPERFIECFIAEQNMVSVALGCATRGRTIAFVSTFAAFLTRAFDQIRMGAISQTNINFVGSHCGVSVGEDGPSQMALEDLAMFRSIPNCTVFYPSDAVSTEHAVYLAANTKGMCFIRTTRPKTAVIYTAEENFVIGQAKVIRQSAVDKVTVIGAGVTLHEALVAAEELSQQGIFIRVIDLFTIKPLDAVTIIQSAKATGGQIITVEDHYREGGIGEAVCAAISREPDIVVRQLAVTEVPRSGKPSELLDMFGISARHIIAAVKDTVMK | 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 decreases and proliferation was significantly inhibited in cancer cells. Plays a pivotal role in carcinogenesis (By similarity).
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Sequence Mass (Da): 68447
Sequence Length: 627
EC: 2.2.1.1
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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
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P21726 | MNAPERIDPAARCANALRFLAADAVELARSGHPGAPMGMAEMAEVVWRRHLRHNPANPAWPDRDRFVLSNGHASMLQYALLHLTGYDLPMSQLRQFRQLHAVTPGHPEVDVTPGVETTTGPLGQGLANAVGMALAEKLLAATFNRPGFDIVDHHTYVFLGDGCLMEGLSHEACSLAGTLGLGKLICLYDDNGISIDGEVAGWFADDTPKRFAAYGWHVIADVDGHDAHALDAALHEAKAERDRPTLICCRTVIGKGAPAKAGGHDVHGAPLGAPEIAAMRTALGWEAEPFTVPADVADAWDARAQGAAREAEWEARFVSYCAAHPELAEEFVRRANGRLPEGFDAELMALLDAPSPLQGKIATRKASQLCLEALTPALPELLGGSADLTGSNLTNVKASVWVNHAGHGNYVSYGVREFGMAAVMNGIALHGGLIPYGGTFMTFSDYSRNAIRMAALMRLRVVHVLTHDSIGLGEDGPTHQPVEHAASLRLIPNNQVWRPCDGAETAYAWLAALQRENGPTCLVLSRQALMPFERDAAQRADIARGGYVLRDVPAPRVVLIATGSEVEIAARAALDLADAGIAARVVSMPCVELFYAQDAAYRDSVLPPGLPRISVEAGATWYWRGVVGEQGLALGIDSFGESAPAEALYQHFGLTPAHVAAAARVLLEDA | 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-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Sequence Mass (Da): 71474
Sequence Length: 670
Pathway: Carbohydrate biosynthesis; Calvin cycle.
EC: 2.2.1.1
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O67642 | MVVQLDQIHFFIFHEVLKIFKTMPQLFKTSKKIDELVINTIRFLSVDMVERAKSGHPGMPLGASHIVYLLYDRIMKYNPKNPNWFNRDRFILSAGHGSAMLYAAFYMFGFDLTLEDLKAFRQLNSKTPGHPEYGLTPGVEVTTGNLGQGFGNAVGMAMAEKFLSHYFNREGYPVIDHYTYVLVSDGDLMEGVSYEAASLAGHFKLNKLIAIWDNNHITIDGDTKLTWTEDVLKRFEALGWEVYHLEDGYNLDLLEETILKAKESDKPTFISVRTHIGYGTPLQDTPEVHGKPMGKEIVEETKKKFGWPLEEFYVPEEALNYTRRKVEEGKALEEEWNKLYAEYREKYPDLAQTLEKALNKEWSLDWLEKVEEFKEDMPTRKASGKVLNVMADYIPTMIGGSADLSESVNTVLKKYGDFEADTPTGRNVHYGVREHAMGTILNGMAYHGGILPYGGTFLIFSEYMRPAIRTAALANLQVIFVYSHDSIGLGEDGPTHQPVEQLWSLRSIPNLWVVRPADANEVKYAWEIALKRKNGPTAIILTRQKVKTIDRSKYASPEGVRKGAYVIADTEGKPDVVIIATGSEVQVALGAKEILEQKGIKTRVVNMACCELFEEQPEEYKREVLPPEVTKRVAVEAGRDTGWYKYVGSDGLVISLNEFGKSAPGSVLFEYYGFTPENVANKVIEKWFS | 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-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Sequence Mass (Da): 77982
Sequence Length: 689
EC: 2.2.1.1
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P45694 | MDTIEKKSVATIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTKFMNVSPANPGWFNRDRFVLSAGHGSALLYSMLHLSGFDLSIEDLKGFRQWGSKTPGHPEFGHTAGVDATTGPLGQGIAMAVGMAIAERHLAETYNRDSFNVVDHYTYSICGDGDLMEGISSEAASLAGHLQLGRLIVLYDSNDISLDGDLDRSFSENVKQRFEAMNWEVLYVEDGNNIEELTAAIEKARQNEKKPTLIEVKTTIGFGSPNRAGTSGVHGAPLGKEESKLTKEAYAWTYEEDFYVPSEVYEHFAVAVKESGEKKEQEWNAQFAKYKEVYPELAEQLELAIKGELPKDWDQEVPVYEKGSSLASRASSGEVLNGLAKKIPFFVGGSADLAGSNKTTIKNAGDFTAVDYSGKNFWFGVREFAMGAALNGMALHGGLRVFGGTFFVFSDYLRPAIRLAALMGLPVTYVFTHDSIAVGEDGPTHEPVEQLASLRAMPNLSLIRPADGNETAAAWKLAVQSTDHPTALVLTRQNLPTIDQTSEEALAGVEKGAYVVSKSKNETPDALLIASGSEVGLAIEAQAELAKENIDVSVVSMPSMDRFEKQSDEYKNEVLPADVKKRLAIEMGSSFGWGKYTGLEGDVLGIDRFGASAPGETIINEYGFSVPNVVNRVKALINK | 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-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Sequence Mass (Da): 72344
Sequence Length: 667
EC: 2.2.1.1
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P57195 | MYSRKELANAIRMLSIDAVQNAQSGHPGMPMGMADIAEVLWRSFLKHNPANPNWNDRDRFILSNGHGSMLLYSLLHLTGYNLPIEELKKFRQLNSKTPGHPETGETPGVETTTGPLGQGLANAVGMAIAERTLSSYFNRPGYDIINHYTWVFVGDGCLMEGISHEVCSLAGTLNLGKLIVFYDKNGISIDGKTAHWFTDDTAKRFESYNWHVLDNIDGHDSESIERSIKQAKLITNQPSIIICNTIIGFGSPNKSGTAESHGAPLGEVEISLIREQLKWNYPPFQIPKEIYKKWNFIEEGSKLEKKWNEKFSLYQSKYPDLSTEYLRRINKKLPVEWDRVTNNYISFLQKNRQSIASRKASQNTLEKYAMILPELIGGSADLSPSNLTMWSRCNSIKDNLSGNYIHYGVREFGMTAIANGISHHGGFIPYTATFLMFVEYARNAVRMAALMCTKHIFVYTHDSIGLGEDGPTHQPVEQLSSLRITPNIDVWRPSDQVETAVAWKKAIEKTSGPTALILSRQNLDQFERSSEQLENISYGAYILYDSKKRLDIIFISTGSELNVTLIAAKKLASLGYSVRVVSMPCTSVFDRQDASYKEFVLPTYVAKRVAVEASIEDFWYKYVGINGVIIGMKTFGESAPAEDLFKKFGFTVQNIFNKSLILLKS | 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-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Sequence Mass (Da): 74782
Sequence Length: 665
EC: 2.2.1.1
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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
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Q9I0I4 | MFLRRLSIQWKITLLAGLCLLGVVALLVGLSVYRMQHSSVLVKSASTQMLDESARLRLEARGELQALRIQRYFMDAFQYGKGFSRQILFLRDQAQKRFLDAYDLREDLTRQVRTALAANPEVLGLYVVFEPNALDGKDELFVDQPALGSNDKGRFSLYWAQATPGQLESESMIESELADTSSGPSGAAYNAWYTCPKESGQPCVLDPYFDKVGERQLLMTSIAFPLELDGKVIGVMGLDINLSNLQALSEQGNRELYDGVGQVGILSPAGLFAGNSRDAGLLGKNLAKADPQHAGELLQLLAAGKSRLFNENDDLKVLQPLQPIPGAKPWGVLLEVPKSALLGPALALERQLDDMRREGTWVELGLGLGAAVLGLLVLWLSARGVTRPILGVAHMLRDIASGEGDLTQRLPHTGRDELGELAGWFNRFLDKLQPIIRDVKVSVRDARSTADQSAAISSQTSAGMQQQFREIDQVATASHEMTATAQDVARSAAQAADAARGADQATRDGLALIDRTTQSIDSLAANLTSAMGQVEQLASSSEEIGSVLEVIRAIAEQTNLLALNAAIEAARAGDAGRGFAVVADEVRNLARRTQDSVEQIRGVIEGLQQGTRDVVDAMHGSHRQAQGSVEQVDEAVAALQRIGEAVTVINDMNLQIASAAEEQSSVAEEINRNVAAIRDVTESLSSQAEESAQVSQSLNRLANHQQGLMEQFKA | 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 mediates chemotaxis to histamine, a key biological signaling molecule. It binds histamine with high affinity, which permits responses to very low histamine concentrations . Chemotaxis to histamine may play a role in the virulence of P.aeruginosa by recruiting cells at the infection site and consequently modulating the expression of quorum-sensing-dependent virulence genes (Probable). TlpQ also binds and mediates chemotaxis to polyamines such as putrescine, spermidine, cadaverine, agmatine and ethylenediamine . In addition, binds the quorum-sensing signal autoinducer 2 (AI-2), thus inducing chemotaxis toward AI-2 and biofilm formation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77125
Sequence Length: 714
Subcellular Location: Cell membrane
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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 interleukin 8 (IL-8) . Involved in susceptibility to antibiotic capreomycin .
Catalytic Activity: cytidine(1920) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1920) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29175
Sequence Length: 253
EC: 2.1.1.226
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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. Is likely involved in ribosomal biogenesis. Also exhibits hemolytic activity in vitro, by binding with and oligomerizing into host cell membranes.
Catalytic Activity: cytidine(1409) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1409) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28074
Sequence Length: 268
Subcellular Location: Cytoplasm
EC: 2.1.1.226
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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 interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons. Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14386
Sequence Length: 134
Subcellular Location: Cell membrane
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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 interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons . Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14504
Sequence Length: 134
Subcellular Location: Cell membrane
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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
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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
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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 similarity). Plays a role in central nervous system development and is required for myelination, and survival and proliferation of oligodendrocytes (By similarity).
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31195
Sequence Length: 287
Subcellular Location: Cytoplasmic vesicle
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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 nervous system development and is required for myelination, and survival and proliferation of oligodendrocytes .
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31469
Sequence Length: 289
Subcellular Location: Cytoplasmic vesicle
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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 role in central nervous system development and is required for myelination, and survival and proliferation of oligodendrocytes (By similarity).
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31344
Sequence Length: 288
Subcellular Location: Cytoplasmic vesicle
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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
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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
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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
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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
Sequence Length: 202
Subcellular Location: Mitochondrion inner membrane
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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
Sequence Length: 248
Subcellular Location: Mitochondrion inner membrane
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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
Sequence Length: 202
Subcellular Location: Mitochondrion inner membrane
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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
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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
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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
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Q71BG9 | MAEILLTSVINKSVEIAGNLLIQEGKRLYWLKEDIDWLQREMRHIRSYVDNAKAKEAGGDSRVKNLLKDIQELAGDVEDLLDDFLPKIQQSNKFNYCLKRSSFADEFAMEIEKIKRRVVDIDRIRKTYNIIDTDNNNDDCVLLDRRRLFLHADETEIIGLDDDFNMLQAKLLNQDLHYGVVSIVGMPGLGKTTLAKKLYRLIRDQFECSGLVYVSQQPRASEILLDIAKQIGLTEQKMKENLEDNLRSLLKIKRYVILLDDIWDVEIWDDLKLVLPECDSKVGSRMIITSRNSNVGRYIGGESSLHALQPLESEKSFELFTKKIFNFDDNNSWANASPDLVNIGRNIVGRCGGIPLAIVVTAGMLRARERTEHAWNRVLESMGHKVQDGCAKVLALSYNDLPIASRPCFLYFGLYPEDHEIRAFDLINMWIAEKFIVVNSGNRREAEDLAEDVLNDLVSRNLIQLAKRTYNGRISSCRIHDLLHSLCVDLAKESNFFHTAHDAFGDPGNVARLRRITFYSDNVMIEFFRSNPKLEKLRVLFCFAKDPSIFSHMAYFDFKLLHTLVVVMSQSFQAYVTIPSKFGNMTCLRYLRLEGNICGKLPNSIVKLTRLETIDIDRRSLIQPPSGVWESKHLRHLCYRDYGQACNSCFSISSFYPNIYSLHPNNLQTLMWIPDKFFEPRLLHRLINLRKLGILGVSNSTVKMLSIFSPVLKALEVLKLSFSSDPSEQIKLSSYPHIAKLHLNVNRTMALNSQSFPPNLIKLTLAYFSVDRYILAVLKTFPKLRKLKMFICKYNEEKMDLSGEANGYSFPQLEVLHIHSPNGLSEVTCTDDVSMPKLKKLLLTGFHCRISLSERLKKLSK | 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 hypersensitive reaction in response to avirulent (Avr) movement proteins from resistance inducing tobamoviruses (e.g. ToMV and TMV) strains, thus leading to programmed cell death; this local extreme resistance requires rbcS .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 98786
Sequence Length: 861
Subcellular Location: Cell membrane
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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
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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
Subcellular Location: Endoplasmic reticulum membrane
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Q9NV64 | MPGGRRGPSRQQLSRSALPSLQTLVGGGCGNGTGLRNRNGSAIGLPVPPITALITPGPVRHCQIPDLPVDGSLLFEFLFFIYLLVALFIQYINIYKTVWWYPYNHPASCTSLNFHLIDYHLAAFITVMLARRLVWALISEATKAGAASMIHYMVLISARLVLLTLCGWVLCWTLVNLFRSHSVLNLLFLGYPFGVYVPLCCFHQDSRAHLLLTDYNYVVQHEAVEESASTVGGLAKSKDFLSLLLESLKEQFNNATPIPTHSCPLSPDLIRNEVECLKADFNHRIKEVLFNSLFSAYYVAFLPLCFVKSTQYYDMRWSCEHLIMVWINAFVMLTTQLLPSKYCDLLHKSAAHLGKWQKLEHGSYSNAPQHIWSENTIWPQGVLVRHSRCLYRAMGPYNVAVPSDVSHARFYFLFHRPLRLLNLLILIEGSVVFYQLYSLLRSEKWNHTLSMALILFCNYYVLFKLLRDRIVLGRAYSYPLNSYELKAN | 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 protein
Sequence Mass (Da): 55667
Sequence Length: 488
Subcellular Location: Endoplasmic reticulum membrane
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