ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q186F4 | MYNLIKDVKKLNPLVIHYTNNVTINDCANVTLAVGASPLMSFSYEEVEEMVSVANSVVINIGTMNSNMLDLFLLAGKAANKYNKPVVLDPVGVFASKARAELTSRLLNEVKFSVVKGNVSEIKFIGGFNVRGKGVDSFDEEEDSTEIIRKIAEKLECVVVATGKIDIITNGKGTYKINNGTDKLKGITGTGCMTASLIASFMAVTENILEAATMGVLTMSLSGELANLNNPPIGTFKENLMNAIYQMDIDALSKNSNIEFLN | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 28291
Sequence Length: 262
Pathway: Cofactor biosynthesis; thiamine diphos... |
A0Q299 | MLENICINFKKVKEKTPLVHSITNYVTINDCANMLLAYGASPAMVESFDESYDFAKLASCIYINLGTLTREQEQSILMVCISAKNNNIPVVLDPVACGAVPHKIALIEKLFEIGRIDIIKGNIGEIKSLAGYNAKTRGVDSIDNGNDSIDACISLAKKYKCIVAATGVKDIVTDGKRTALIENGSKMLTLITGAGCMVGALTAATAGVEDDKFIATITSILSMNIAAEHTEKEVIGPGSFKVKLIDNIYLLKENHLRKEGKIKWI | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 28656
Sequence Length: 265
Pathway: Cofactor biosynthesis; thiamine diphos... |
Q0TQV3 | MEVLKRENPLIHMITNYVTVNDLAQVTINYGGLPLMATHHDELKEITKMANGLLVNIGTLEPYQMESSMISMKIAKEKGIPSVLDPVGVQASKLRKDFAKKLILEGEPSLIKGNLAEIKTLIGETSNSIGIDSFDDSLSENTKNKIKEYARERNLIVVVSGVVDFITNGEESASVKNGTYKMSKITGTGCMLGALLTLALSFYDHKDLRFKEVVKAVSTWGICGELAEERLREKEGLMTFKHNLLDELSIINDETIKEREKVIYD | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 29495
Sequence Length: 265
Pathway: Cofactor biosynthesis; thiamine diphos... |
Q8E093 | MYLEQLKEVNPLTICITNNVVKNFTANGLLALGASPAMSECIEDLEDLLKVADALLINIGTLTKESWQLYQEAIKIANKNQVPVVLDPVAAGASRFRLEVSLDLLKNYSISLLTGNGSEIAALIGEKQASKGADGGKVADLESIAVKANQVFDVPVVVTGETDAIAVRGEVRLLQNGSPLMPLVTGTGCLLGAVLAAFIGSSDRSDDLACLTEAMTVYNVAGEIAEKVAKGKGVGSFQVAFLDALSQMKSEMIMDK | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 26959
Sequence Length: 256
Pathway: Cofactor biosynthesis; thiamine diphos... |
Q2LWX9 | MQITPENTWAAVKAIRSRAPLIHNITNYVVMNSTANALLALGASPVMAHAQEEVEEMVGIAQALVVNIGTLSPSWVRAMASAALKAADRGIPIILDPVGAGATAYRTRTAFQLLETVSPTIIRGNASEILAFESVETMETRGVDSTELSQNAVDAGRRLNDSYGSTVCISGETDFIIGDRAILGIRNGHPLMTRVTGLGCTASALCGAFAAVNSSFTLAAAQAMAVMGIAGEMAAEISPGPGSLQLHFLDILYRLTEEDIARRLRIVAGE | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 28368
Sequence Length: 270
Pathway: Cofactor biosynthesis; thiamine diphos... |
Q0AZ87 | MLKYCAEIWDEVRNRRPLVHCITNYVTVNDVANIILAAGASPAMVEYPAEASGFAPLASVLYFNLGTLTGEQEAAMLEGRWAAASRDVPLILDPVACGVIGRKVDLIERIKSLGKIQVLKGNIAEIKSLAGLAGKAQGVDSLDTGEGLEEACLQLAVKDKLIAVATGEVDIVAEENRYARIFNGTPLFQNITGAGCMAGGVIAACVGAAPEEAWLASITGLLAFNLAGERAASQAGNRPGTFRTLLFDELFVLRGEELMKEGRLEW | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 28278
Sequence Length: 266
Pathway: Cofactor biosynthesis; thiamine diphos... |
B0KBA7 | MKKELLKILREKKPLVHHITNIVTVNDCANITLAIGALPVMAHALEEVEEMVSAADALVLNIGTLTNEQVEAMIKAGKAANRLKVPVILDPVGAGATKLRTQSSKKILEEVKISVIKGNSAEISILAGKGGKIRGVESQSGADDISEAAKDLANAYNVVVAVSGVTDIITDGKRIAYVKNGHPMMGTVTGTGCMLTSVVASFCGVCEDYFAATVEAFVAFGIAGERAAQSSNVKGPGSFKVTFFDEIYNLTPEIIEKDKKVEYE | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 27951
Sequence Length: 264
Pathway: Cofactor biosynthesis; thiamine diphos... |
B7VS66 | MLTEQIIQSLRAVREQKPLVVNITNYVVMNNTANALLAIGASPIMAHSKQELAEMMSFSGALVINIGTLDSVWTPRMCFAVEQANANNKVVVLDPVGCGASTLRTETSREIARLADKLIIRGNASEIIALAGEQAQSKGVDALDSSDAALGAAQCLVAEYGANVVISGETDYVVTKDSVVTLNNGHPMMPYVTGMGCTLTALTGAFAAVGDESGLAAAAVLGVVGEISAESSRGPGSLQMNLLDELYQLDEETLIQRLKVQ | Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Mass (Da): 27369
Sequence Length: 261
Pathway: Cofactor biosynthesis; thiamine diphos... |
O34664 | MKTINIVAGGPKNLIPDLTGYTDEHTLWIGVDKGTVTLLDAGIIPVEAFGDFDSITEQERRRIEKAAPALHVYQAEKDQTDLDLALDWALEKQPDIIQIFGITGGRADHFLGNIQLLYKGVKTNIKIRLIDKQNHIQMFPPGEYDIEKDENKRYISFIPFSEDIHELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGILIMIRSTD | Function: Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate.
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine diphosphate
Sequence Mass (Da): 24099
Sequence Length: 214
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
EC: 2.7.6.... |
O26949 | MMIMEIENVRRALEMISSAEDFGILIPEVRSNIVMARSNPCGPEDVVAVPGRITEFQGRAFACRDPEYGASSHMARFIIALNEHLPGRRSALNIKFDESIISICEDMGLVVSSYDRSREPDSVRDTEGGSIPWGVEEALRNSESPPDVIYHRGAWGKEPMIVLTGRDAVEVAELAIKILRKYKSLKGDTR | Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine ... |
Q9KP42 | MLALDKVRYEYEHEWFEFDLNVADGDIVALMGPSGAGKSTLLSLVAGFIEPVSGSIKVNDQSVLGLAPYQRPFSMLFQEHNLFAHLTVRENIGLGLHPGLKLNAEQKQQVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCFVQPNPIWLLDEPFSALDPLLREEMLALVKQLASERQRTVVMVTHHLSDARAIASQIAFLSQGKVKVVSDCQAVTAQHPHPELAQFVAAALNEPK | Function: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + thiamine(out) = ADP + H(+) + phosphate + thiamine(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26238
Sequence Length: 238
S... |
Q8DE95 | MLTLQQVHYYYHQDLFAFDLEVEAGSIVALMGPSGAGKSTLLALLAGFIAPQSGQMALDGRLLNTLSPAQRPFSMLFQEHNLFAHLTVRDNIALGLHPGLKLTSQQQKQVEQAAKQVGIEAYLDRLPEQLSGGQRQRVALARCFVQPNPIWLLDEPFSALDPVLRDEMLSLVKQLAQERAITVLMVTHHLSDARAIASHFAYIDKGTIAAHGPIASLNEKHSHPELVEFFQAAV | Function: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + thiamine(out) = ADP + H(+) + phosphate + thiamine(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25793
Sequence Length: 234
S... |
O31617 | MLQLNGKDVKWKKDTGTIQDLLASYQLENKIVIVERNKEIIGKERYHEVELCDRDVIEIVHFVGGG | Function: Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.
PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) by ThiF, then thiocarboxylated (-COSH) by ThiI.
Sequence Mass (Da): 7626
Sequence Length: 66
Pathway: Cofactor biosynthesis; th... |
O32583 | MQILFNDQAMQCAAGQTVHELLEQLDQRQAGAALAINQQIVPREQWAQHIVQDGDQILLFQVIAGG | Function: Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.
PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) by ThiF, then thiocarboxylated (-COSH) by ThiI.
Sequence Mass (Da): 7311
Sequence Length: 66
Pathway: Cofactor biosynthesis; th... |
Q72KL7 | MVWLNGEPRPLEGKTLKEVLEEMGVELKGVAVLLNEEAFLGLEVPDRPLRDGDVVEVVALMQGG | Function: Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.
PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) by TtuC, then thiocarboxylated (-COSH) by the cysteine desulfurases IscS or SufS.
Sequence Mass (Da): 6986
Sequence Length: 64
... |
O32074 | MNQSKQLVRLIEIAIMTAAAVILDIVSGMFLSMPQGGSVSIMMIPIFLISFRWGVKAGLTTGLLTGLVQIAIGNLFAQHPVQLLLDYIVAFAAIGISGCFASSVRKAAVSKTKGKLIVSVVSAVFIGSLLRYAAHVISGAVFFGSFAPKGTPVWIYSLTYNATYMVPSFIICAIVLCLLFMTAPRLLKSDKA | Function: Probably a thiamine-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracyt... |
A2RI47 | MSNSKFNVRLLTEIAFMAALAFIISLIPNTVYGWIIVEIACIPILLLSLRRGLTAGLVGGLIWGILSMITGHAYILSLSQAFLEYLVAPVSLGIAGLFRQKTAPLKLAPVLLGTFVAVLLKYFFHFIAGIIFWSQYAWKGWGAVAYSLAVNGISGILTAIAAFVILIIFVKKFPKLFIHSNY | Function: Probably a thiamine-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracyt... |
Q037U3 | MQQHKQLVVILETAIIAAFAMALTYIPHTTGVSAIELNYGLIPIAVLAMRRGLVPAAWAGFVWGILDLILRGIGGGSVLNPLQGILEYPIAFTLVGLMGLTFASFQKAVRGSEKVKASGYAFAGIIIGTFAKYFIHFIAGVVFWGAYAPKGTNVWVYSLIVNGGSALFSTVLTIVVVGVLLTVAPQLFVAKDGKSFSTKAA | Function: Thiamine-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic so... |
P42461 | MSISRTVFGIAATAALSAALVACSPPHQQDSPVQRTNEILTTSQNPTSASSTSTSSATTTSSAPVEEDVEIVVSPAALVDGEQVTFEISGLDPEGGYYAAICDSVANPGNPVPSCTGEMADFTSQAWLSNSQPGATVEIAEDGTATVELEATATGTGLDCTTQACVAKVFGDHTEGFRDVAEVPVTFAAA | Function: Is necessary for biosynthesis of the 4-methyl-5-(beta-hydroxyethyl)thiazol component from which thiamine is formed.
Location Topology: Lipid-anchor
Sequence Mass (Da): 19251
Sequence Length: 190
Subcellular Location: Cell membrane
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P04990 | MWKGLIHQYKEFLPVTDQTPALTLHEGNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMCASTGNTSAAAAAYAARANMKCIVIIPNGKIAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVNPYRIEGQKTAAFEVCEQLGEAPDVLAIPVGNAGNITAYWKGFKEYHEKNGTGLPKMRGFEAEGAAAIVRNEVIENPETIATAIRIGNPASWDKAVKAAEESNGKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEIPKGSKVVAVLTGNGLKD... | Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Mass (Da): 37464
Sequence Length: 352
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-t... |
Q89AR5 | MKLYNLKKKQDQVNFSKAVKLGLGKNQGLFFPKELPILTKEQLYKLLKMDFLTRSSKILSMFIGDEIHYSELTKRIKNAFSFTTPKIVSISKNIACFELFHGPTLAFKDFGARFMAQILSFLNHDKNDTITILTATSGDTGAAVAHAFFKMKNVRVIILYPKGKISELQEKLFCTLGENIITIAVNGSFDECQKLVKQAFNDDQLRIETGLNSANSINISRLLAQICYYFEAFALLTKKQQKNLVISVPCGNFGNLTAGLLAKALGLPIKSFIASTNSNDTVPRFLKTGFWKPNNTVSTISNAMDISQPNNWPRVEELFK... | Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Mass (Da): 48632
Sequence Length: 430
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-t... |
P23669 | MDYISTRDASRTPARFSDILLGGLAPDGGLYLPATYPQLDDAQLSKWREVLANEGYAALAAEVISLFVDDIPVEDIKAITARAYTYPKFNSEDIVPVTELEDNIYLGHLSEGPTAAFKDMAMQLLGELFEYELRRRNETINILGATSGDTGSSAEYAMRGREGIRVFMLTPAGRMTPFQQAQMFGLDDPNIFNIALDGVFDDCQDVVKAVSADAEFKKDNRIGAVNSINWARLMAQVVYYVSSWIRTTTSNDQKVSFSVPTGNFGDICAGHIARQMGLPIDRLIVATNENDVLDEFFRTGDYRVRSSADTHETSSPSMDI... | Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Mass (Da): 52931
Sequence Length: 481
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-t... |
P00934 | MKLYNLKDHNEQVSFAQAVTQGLGKNQGLFFPHDLPEFSLTEIDEMLKLDFVTRSAKILSAFIGDEIPQEILEERVRAAFAFPAPVANVESDVGCLELFHGPTLAFKDFGGRFMAQMLTHIAGDKPVTILTATSGDTGAAVAHAFYGLPNVKVVILYPRGKISPLQEKLFCTLGGNIETVAIDGDFDACQALVKQAFDDEELKVALGLNSANSINISRLLAQICYYFEAVAQLPQETRNQLVVSVPSGNFGDLTAGLLAKSLGLPVKRFIAATNVNDTVPRFLHDGQWSPKATQATLSNAMDVSQPNNWPRVEELFRRKI... | Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L-serine and 3-chloroalanine into pyruvate. Is also able to rapidly con... |
Q9K7E3 | MSQWRGLLQEYKEFLPVTEETPLLTLGEGNTPLIPLENLSKEWGVKAYVKYEGANPTGSFKDRGMVMAVAKAKEEGSRTIICASTGNTSAAAAAYGARAGLRCIVVIPEGKIALGKLAQAVMYGAEVLEIKGNFDHALDIVRSISEKEPITLVNSVNPYRIEGQKTSAFEICDALGQAPDVLAIPVGNAGNITAYWKGFKEYHEKKGTGLPQMRGFEAEGAAAIVRNQVIEEPETIATAIRIGNPASWTYAVEAAAESNGKIDEVTDEEILAAYQLLAQKEGVFAEPASCASIAGLRKQIASGEIKKGSTVVCVLTGNGL... | Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Mass (Da): 37665
Sequence Length: 354
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-t... |
O24924 | MPFVPTRSLKEKKIDFIEAILNPNAPKGGLYTLERFETLQWQDCLNLSYNDLVECVFERLGLEIPKNLLASALKRYENFDNPKNPAPIFALNERLFVQELYHGPSLAFKDMALQPLASLFSNLAVGKNEKYLMLVSTSGDTGPATLESLAGMPNVFVVCLYPKDGTSLVQKLQMVTQSASNLKVFGISGDFDDAQNALKNLLKDDDFNEALKACQLKLSVANSVNFGRIAFQIVYHIWGFLELYKKGAINSKEKITLAIPSGNFGNALGAFYAKKMGLNIDKIKVVTNSNDVLREFIETGRYDLTHRSLKQTYSPAMDIL... | Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Mass (Da): 54707
Sequence Length: 486
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-t... |
Q8TQD4 | MYHLKCIECGAEYSRDEVIYTCSKCDGLLDVIYDYSSIKIDMEKLKTECPSVWKYAKLLPVEREPVTIQEGGTPLYKCDRLAEKIGIKKLYVKHEGMNPTGSFKDRGMTVGVTKALELGMNTVACASTGNTSAALAIYGAKAGIPVVVLLPAGKVALGKVAQALMHGAKVLSIRGNFDDALALVRTLCSQEKIYLLNSINPYRLEGQKTIGFEIADQLDFKVPDRIVLPVGNAGNITAIYKGFREFKILGITDSLPKMTGIQAEGSCPIVKAIKSGAPAITPEENPETVATAIRIGNPVNATKALSAIRESGGTAESVTD... | Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. Does not catalyze the conversion of O-acetyl-L-homoserine into threonine.
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Mass (Da): 43285
Sequence L... |
A0R220 | MSAAKAAVHQPWPGLIEAYRDRLPIGDDWTTVTLLEGGTPLIHAKRISELTGCTVHLKVEGLNPTGSFKDRGMTVAVTESLARGQQAVLCASTGNTSASAAAYAARAGITCAVLIPQGKIAMGKLAQAVMHGAKIIQVDGNFDDCLELARKLTADFPTIALVNSVNPYRIEGQKTAAFEIVDALGTAPDVHALPVGNAGNITAYWKGYSEYHRDGVSDRLPRMLGTQAAGAAPLVTGAPVKDPETIATAIRIGSPASWNSAVEAQQQSDGRFLAATDEEILAAYHLVARTEGVFVEPASAASIAGLLKSVEDGWVKRGST... | Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Mass (Da): 37443
Sequence Length: 360
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-t... |
I2C644 | MGYRNGNYAAFYVSEPFSESSLGANATKDFVSYNMLRAWKGKDNNYPFNDSHDKTYNVRDGSDWEKTLKPRLRKRLDQSKNIIFFLSKHTENSKALREEIDYGINVKGLPVIVVYPELSEKSDIIDCTTKVFRSEVVNLWSRVPVFKDSMLKVPTIHIPYKKDQIKKALENKDFMINSKISAGSVYFYPC | Function: TIR-like domain-containing component of the Thoeris antiviral defense system, composed of ThsA and ThsB. Expression of ThsA and ThsB in B.subtilis (strain BEST7003) confers resistance to phages SBSphiC, SBSphiJ and SPO1 . Phage infection activates this protein, generating a signal molecule that in turn activa... |
Q9NS62 | MKPMLKDFSNLLLVVLCDYVLGEAEYLLLREPGHVALSNDTVYVDFQYFDGANGTLRNVSVLLLEANTNQTVTTKYLLTNQSQGTLKFECFYFKEAGDYWFTMTPEATDNSTPFPWWEKSAFLKVEWPVFHVDLNRSAKAAEGTFQVGLFTSQPLCPFPVDKPNIVVDVIFTNSLPEARRNSRQPLEIRTSKRTELAQGQWVEFGCAPLGPEAYVTVVLKLLGRDSVITSTGPIDLAQKFGYKLVMVPELTCESGVEVTVLPPPCTFVQGVVTVFKEAPRYPGKRTIHLAENSLPLGERRTIFNCTLFDMGKNKYCFDFG... | Function: Is a positive regulator of nascent focal adhesion assembly, involved in the modulation of endothelial cell attachment to the extracellular matrix.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 94584
Sequence Length: 852
Subcellular Location: Endosome membrane
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Q2HJE9 | MEEYAREPCPWRIVDDCGGAFTMGVIGGGVFQAIKGFRNAPVGMRHRLRGSVNAVRIRAPQIGGSFAVWGGLFSTIDCGLVRLRGKEDPWNSITSGALTGAVLAARSVPLAMVGSAMMGGILLALIEGVGILLTRYTAQQFRNAPPFLEDPGQLPSKEGTPGPGYPSYQQYH | 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): 18321
Sequence Length: 172
Subcellular Location: Mitochondrion inner membrane
|
O60830 | MEEYAREPCPWRIVDDCGGAFTMGVIGGGVFQAIKGFRNAPVGIRHRLRGSANAVRIRAPQIGGSFAVWGGLFSTIDCGLVRLRGKEDPWNSITSGALTGAVLAARSGPLAMVGSAMMGGILLALIEGVGILLTRYTAQQFRNAPPFLEDPSQLPPKDGTPAPGYPSYQQYH | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
PTM: Forms one disulfide bond.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18273
Sequence Length: 172
Subcellular Location:... |
Q9VGA2 | MEYNRQPCPIRIVEDCGCAFMMGTIGGSLFEFLKGFRNAPTGLQRRLYGGIDLVKMRTPSIAGSFAVWGATFSTVDCALVHYRQREDAWNSILSGAATGGILAARNGIRAMANSALVGCLVLAMIEGAGAAVATINAADKGAGIVIKPQRAQWEAILETIDPKRASSTQDFALAEFERVLDKCRASREPNLLQDIPVKSHERDSKQKPFYSLLDLVKLSQMF | 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): 24159
Sequence Length: 222
Subcellular Location: Mitochondrion inner membrane
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Q8GZ79 | MITGYSTPSAHVLMSSRAFKSSSYRAAAGQTQHYLARSSLPVVKNSWGSPPSPFNELPRVSRGVPLSYLSASSSLLLNGEQGSLSGTLPVLPVRRKTLLTPRASKDVPSSFRFPPMTKKPQWWWRTLACLPYLMPLHETWMYAETAYHLHPFLEDFEFLTYPFLGAIGRLPSWFLMAYFFVAYLGIVRRKEWPHFFRFHVVMGMLLEIALQVIGTVSKWMPLGVYWGKFGMHFWTAVAFAYLFTVLESIRCALAGMYADIPFVCDAAYIQIPYD | 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. Seems to be specific for photosynthesis-related pre-proteins. Partially redundant with TIC20-IV, but not with TIC20-II or TIC20-V.
Location... |
O82251 | MASLCLSLHQTLTNPLSAPRCRPLSLSFPGSSTFSIRPSSRRATALTTRASYTPTPATERVISIASYALPFFNSLQYGRFLFAQYPRLGLLFEPIFPILNLYRSVPYASFVAFFGLYLGVVRNTSFSRYVRFNAMQAVTLDVLLAVPVLLTRILDPGQGGGFGMKAMMWGHTGVFVFSFMCFVYGVVSSLLGKTPYIPFVADAAGRQL | Function: May be involved in protein precursor import into chloroplasts. Not redundant with TIC20-I, TIC20-IV or TIC20-V.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22912
Sequence Length: 208
Subcellular Location: Plastid
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Q9ZQZ9 | MQGLAATTTNRGSLTFLAPRNHSPISKKFVNPRVFFPNVDSSAKLRLSASSISRRCPREIAPLSATASVDFAAAATSSNQLFANGLPPLAPGLRRHRRPIEPARVAKDDFFKIKLPKIAERPEWWWRTLACVPYLISLQISDVGFYVQPFLEKHDAIGDMIYFIPGAINRWPTWFFMVYCYLGYMWVVKNKELPHYLRFHMMMGMLLETALQVIWCTSNFFPLIHFKGRFGMYYWMAIGFTYICLLLECIRCALAGVYAQIPFMTDAASIHTLFNLGGFQRPLR | Function: Involved in protein precursor import into chloroplasts. Partially redundant with TIC20-I, but not with TIC20-II or TIC20-V.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32520
Sequence Length: 284
Subcellular Location: Plastid
|
Q9FM67 | MAIISQFFAPLPSLTGTLTLTGRSFLPLNLDTQFPKPRLSRDRAATLVLQSKGDDSVDASDRIISAVCYFYPFFDGIQYGKFIITQYQPFQILIQPLFPAIRAFKSFPFNGFLIFITLYFVVVRNPNFSRYVRFNTMQAIVLDVLLIFPDLLERSFNPRDGFGLDVVMSLDSTVFLFLLVSLIYGFSACLFGLTPRLPLVAEAADRQVL | Function: May be involved in protein precursor import into chloroplasts. Not redundant with TIC20-I, TIC20-II or TIC20-IV.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23652
Sequence Length: 209
Subcellular Location: Plastid
|
Q568N3 | MCTAVRQDLSLKCGGTDVKQPGDSQPGHLRALLGFTLPSVYASDSSTQILPKHIGKPEFPDTGWDRIKDLFYNVEGQYTEELRNVVKSGIASAIVGMIYGGLPGARHARQRFIQCSQAEIYRNRVDAVRAAHNAAIRGFLRFGWRWSWRVAAFVTLFNTVNTGLTVYRDQNALSHFAVSGAVTGGVFRLNLGLRGLLSGTIIGVILGFPAGVLILGLQNLGGETMRDKRRRERRELHELRVTEWNARLKVTDDLIGEMSSLKHQDSEIDLQQVEELLSQPRNGNAAKGPYNQ | Function: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32372
Sequence Length: 292
Subcellular Location: Mi... |
Q9NPL8 | MEVPPPAPRSFLCRALCLFPRVFAAEAVTADSEVLEERQKRLPYVPEPYYPESGWDRLRELFGKDEQQRISKDLANICKTAATAGIIGWVYGGIPAFIHAKQQYIEQSQAEIYHNRFDAVQSAHRAATRGFIRYGWRWGWRTAVFVTIFNTVNTSLNVYRNKDALSHFVIAGAVTGSLFRINVGLRGLVAGGIIGALLGTPVGGLLMAFQKYSGETVQERKQKDRKALHELKLEEWKGRLQVTEHLPEKIESSLQEDEPENDAKKIEALLNLPRNPSVIDKQDKD | Function: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32178
Sequence Length: 285
Subcellular Location: Mitochondrion memb... |
Q5XK94 | MAQSDPPKSPDPPLPTSIRNPQTPESGWDRIRELFQPNEQGHYPEEVGSIVKSAVTGALLGGIYGGLPAARHSKERYIQQSQAQIYQHRVEAVRSAHNAALRGFIRYGWRWGWRVAAFVTIFNSVSTGLTVYRDKLALSHYAAAGAVTGGLFRLNLGLVGLLSGSLIGAALGVPAGALISGLQSISGESIREKKRRERQELYENKVQEWSARLQVTDEVLEEMETSQQDPLEQQVEKIQELLQLPRNPAVSPKEGR | Function: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28246
Sequence Length: 256
Subcellular Location: Mi... |
O73792 | QLLQFAADVATGMHYLSDKQFIHRDLAARNVLVGDNLVAKIADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEQPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLNRMQEARKAYVNMALFENFTYAGIDATAEEA | Function: Transmembrane tyrosine-protein kinase that may modulate TEK/TIE2 activity and contribute to the regulation of angiogenesis.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 21190
Sequence Lengt... |
Q13263 | MAASAAAASAAAASAASGSPGPGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKV... | Function: Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target... |
Q1DAT1 | MKVQVEELSPIEKKLSIEVDNARVAEELSRAYSNLGRQVRLPGFRQGKVPRRILEQRFRDQVEDEVIQRVVQSAYVEAIREHNVEVVATPQVTNSGLKPNTPFTFEARVEVKPKVEAKDYVELPLTKSDTAVTDEQVNEQLERMRQSMARLEPVTDRDTAASGDYVTVDFDATVDGQPFAGSKAEGITVQVQPGELVESKIAALEGVKVGESKDIDYAFPQEYRVEEVRGKTARFHITLKGVQKEIVPELNDDFAKQSGVAQSIDELRTKLREDMEKARKSQVEGEEREALMKALLERNTFDVPRAMVERAMDSMLRGAL... | 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): 48091
Sequence Length: 4... |
B2A157 | MSSTWEKIDKNKIKLSVEVDENRVEDALEQAYKKVVKQVEIPGFRKGKVPRKILENRFGPEVLYEDAIEILVPEAYQEALEEHEIEPVDQPEIDIDQMEKGQPLKFNATVEVKPEVELGTYKGLEVEKEKVEVTEEDVENELKQMQEQHAEYEDVEDGEAENGDRLVIDFEGYVDGEPIEGGQAENHNIELGSNQFIPGFEEQLVGSKPGEEKEVKVTFPEDYQNEELKGKEATFNVKVKEIKKKNLLPIDDEFAKDVSDFDTLEEFKNDIRNRLEEEAERAAEQQVEEQVVTKALENAEVEIPQPMIDQEVDNMLKEFE... | 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): 51227
Sequence Length: 4... |
Q9JZ37 | MMSVTVETLENLERKVVLSLPWSEINAETDKKLKQTQRRAKIDGFRPGKAPLKMIAQMYGASAQNDVINELVQRRFYDVAVAQELKVAGFPRFEGVEEQDDKESFKVAAIFEVFPEVVIGDLSAQEVEKVTASVGDAEVDQTVEILRKQRTRFNHVEREARNGDRVIIDFEGKIDGEPFAGGASKNYAFVLGASQMLPEFEAGVVGMKAGESKDVTVNFPEDYHGKDVAGKTAVFTITLNNVSEATLPEVDADFAKALGIADGDVAKMREEVQKNVSREVERRVNEQTKESVMNALLKAVELKAPVALVNEEAARLANEM... | 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): 48325
Se... |
Q0AJI1 | MQTQEEASNPLERNIELSVSREKVEAEVGQRLKRLAPKIKIQGFRPGKVPMKIVAQQYGHQIEHEVLGELLQQQFSESINRENYRIAGVPNFESRNPGTDNSNYEFRATFEIYPNIELGDLNSITINKPVLQIGDVEIQKTLEVLRKQRTNYESVDRPAQTGDRVNINYQGSLDGKNFAGGQADNYSVILGNGHLLEDFEASILGMSTGQEKTFDMTFPEDYSGKEVAGKKVTFTITLNKVEAPKLPDVDGEFAKSLGIEDGNVEKMQSEIKANLQRETTQRIRVKLKEQVMQSLLDKISVDIPKILVQQEIDRLIEEVQ... | 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): 49761
Sequence Length: 4... |
Q82Y58 | MQTQGEASNPLERNIELSVSREKVEAEVGVRLKRLAPKVKVQGFRPGKVPLKIVAQQYGHQVEHEVLGELLQQQFNDAVNQENYRVAGIPGFESRNSDANGATSYEFRATFEIYPDIELGDLSSITVNKPVLQIGDAEIQKTLDILRKQRATYEPTDRPAQTGDRVTIDYRGVLDGEGFPGGQADDYSVILGNGHLLEDFESSILGMTAGQEKTFDMTFPADYPGKDVAGKKVSFTIRLNKLEAPKLPEVDGEFAKSLGVAEGDIDKMRSEIKANLQREISQRIRTKLKEQVMQSLLDKVLIQVPKVLIRQEADRLAEEM... | 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): 49398
Sequence Length: 4... |
Q3JAJ7 | MQVTVEATGELERRLTITLPGSDFESKVQERLRSMVPRIKMDGFRPGKVPYKVVERRYGSAVRQEVSDEFVRDSFRDAIKQESLRPAGMPQIEPPQLEAGESFAYTVTFEVLPEIESVKLEGIKIKQPRAEVTDKDIEGVLKKLQEQHIEWEPMERPAQEADGVTITYHGSIEGKPFPGGSKENFFVILGKGTTLKEFEEHLIGVNKGQELTFEITFPEHYGNQELAGKKASFAVKVISVTAPRLPEINEDFAEKLGVKEGGVAALRQEIKASMTRNLEQAVRDRVREQIMDGLLVANPTTLPISLVKEETSILLEQAKN... | 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): 50196
Sequence Length: 4... |
A6Q1C0 | MEINAQKLNEANATVEAKIAKQDVEKKEEKIAKELAKTMNIPGFRKGKVPPAVIKKRYGDKLAQDAEAELVREALDQALEELGIEKEAMLGEPRFAKYEKGEEVIEMVLEIGVRPNIDITGYEEVIPEYEEPQVSDEEVEKRIEELADAMAQFKEIEEDRPAKEGDLVVIDFKGTLEDGSEIEGGSAQNFELRLGSGQFIPGFEEQVEGMKKGETKTIEVTFPEDYPNKELAGKKANFEVTLHTIKEKEKINIDDELAKKMLQKEDATLDELKEEVRKQLKSEKLSKLYNEELKPKLVEALVEKFEFDLPKNIVDQEIDV... | 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): 49764
Sequence Length: 4... |
A6Q674 | MKVEVKKIDDANVAVQGNIENKVVEANVDKLAREAGKQMKVDGFRKGKVPPHVVKKLHGDKLQQDAEGDALRSLIDLGVKEAGINTADILGEPIFKKYDKKDEGIEVEVEISLRPTIEAEGYEKAVPAFEKPEATEKEVEEKLEEIAAQQAPFEKIKRKRMVRDGDTVVIDFEGFVDGVAFEGGKAEKFSLKIGSGQFIPGFEEQIIGMKYDEEKTITVAFPEEYQSKELAGKEAEFKVKLHEIQEQVPAELNDALAQKLLQDEKATLDTLKEKLKEQIVNEKTSKIYNEELKPKIIEALVAHFDFALPNNIVEQEIDAK... | 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): 48099
Sequence Length: 4... |
Q67SK1 | MKATWDKLENNWMQFEVEVDASEFSKSVEAAFRKMNRQVTIPGFRRGKAPRAVFERVYGKEALVQEAVDQILPRAYSEALEQGQIEPISQPEIEVVQAEDGKPLIFKGKVQVTPEVTLGRLSGFGIEKQVPEVTDQEVEEQLSALRERLATLVTDESGEVGQGSFAVIDFEGFIDGEPFEGGKGEGYTVEIGSGTFIPGFEEGLVGAKAGETREVTVTFPEDYHAQHLAGKQAVFKVTVHEVKKKELPELNDEFAQQVSPFKTVEELRADIKNRLSEAAAQKAEEDFRNKVVEAVADDASVEVPEVLVHDKVHDMIHDFE... | 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): 47932
Sequence Length: 4... |
Q2LTK6 | MDENTVAVKVEEISPVKKKLLFDVPWEDVKRERDTIYRNFSRTAKIKGFRKGKIPRKILELHYKKHAEEETVSSLVSRLYWDALKEHDIRAISQPEIEQQGIEEEKDFSFSATVEVEPQIDPQGYLDMTLSKEEQTVTEDEVDGRLEDIRKMFGTLEEVTEDREIRKGDFVTIDFEGFIDGQNPEEMKRNDYFLEIGSNTMVPGFEDQLLGEKVGTIKEIKIIFPENYQINSNVAGKDATFKVTIKNLKEKKLPELDENFVKNFDKYESLDDLKEDVRKSLFEDHKRKTEADMSKKIMDKLLEMNDFDAPSSYVERQIFF... | 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): 51905
Sequence Length: 4... |
Q3A3X4 | MNVKVEDISSIKKKLSFEISVEAVDTEFSNEYKKLSKTAKIPGFRKGKVPRSVLERQYAGHVEGQVFERLVNETFFKALVDEKINAVSAPEVVDNGPLKPGQAFTYEAEVEVRPDVEAKDYIGLDLKKENFAVEDQDVEDRLQDMLKSRAKVEVSEREVAQAGDIAVIDFEGFVDGEAFAGGKAEGHELELGSNSFIPGFEDQVVGMECGQDKDIEVAFPEDYGNEELAGKPAVFKVRLNQIKERVLPALDEEFAKEAGLESVEDLKIKIRESIEGQERDRIEKDFRERMTDALIEANEFEVPEGMIDSQIDYMLKNLQN... | 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): 49446
Sequence Length: 4... |
Q935Z3 | MSIKVTQEKLPASRVGLQIEVSGEQSRQVYERTLTRLSREVRFPGFRPGKVPRPVLIQRLGETALKANAIEDLVQQSLESAIAQESIPAIGNYQLSSDFETLVAAFQPGESFSFEASVDVQPTATLAQYTGLTVEVAEVPFDANRVDNVLAEQQKQMATLVPVEGRNAAIGDVAVIDFQGILVESGEEIPGGSGTDFQIEVEEDRFIPGFISGIVGMAIEETRTVDATFPETYAQEEVAGKAAQFTITLKELKTRDLPELDDAFAQEASQYETIEELKTALTERFQAEHESEVKASKRDAILTALADQLDVEIPESLLQR... | 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): 52218
Sequence Length: 4... |
A0LEF2 | MNVSVVDLSENQKKLQVEIPPEKVRQEIEGKYREMSRRIKIKGFRPGKVPRSIIKSYYGKTIEQEVSSQFIQETFPEALKETDLKPLVEADVSETHFNDSGSFSYTAIVDVCPPFELEGYRGLEIRKPSIDVADEQVDSELQRLREQHAELRTLETERPAREGDVAVIDFTPSVDGKVFEKGKSADYMAEIGKKAVHPDFDANLIGRRAGETVSFEVDYPENAPMREIAGKRVLFEVTVKEVKEKVLPELDDDFAQAVNSRFDALDALKQTIREELLKREEYQARSDVQQQILDQLLSKVKIELSAKVIDREVDRMVGNL... | 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): 49942
Sequence Length: 4... |
Q2JQ33 | MQVTQEKRPGSRVGLKIVVEADRVKRSYEKTLRQLEQNIQIPGFRKGKAPRNLVVRQVGRERILASAVDDLINEAIQQAFKEAQLTPISRFELDDEVGQLLAQFNPEADFSFSGYVEVYPEARVGQYKGLTVTATRVDVKPEQIDQLIDRWRDQRATLLPVEDRPAQLGDVVVIDFAARDAEGNPLDEMTTQDFQLELKEDNFIPGFVAGIVGMQLDETKEIAATFPDDYFRKELAGKTVTFIVCLREIKAKELPELDDAFVQEISSFQTVAELREHLQKRLEQDALRQSEENLETAILNAILETTEVDLPETLIEQETT... | 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): 61742
Sequence Length: 5... |
B1XL18 | MKVIQEKLPASQVGLEIEVPADVTQKAYDDTVRKLARTVNLPGFRKGKVPKQILIQRLGPNRIKASVLEDLIDDSLKAAIAQENIEALGNFQLKSSFDDLISAYKPGEASSFKAAVDVPATVTLNSYKGLSFKAEKSEYDPADLDEFLTQKQRELATLVPVEDRAAQMGDVAIADYEGRYVNDAGEEEEDIIPGTQAEDFSLDLEEGKFIPGFVDGFVGMKPEETKKFTVTFPEDYGNEEMAGKQVSFTVTLKELKSRELPELDDEFASEATNEEFETLAAWQESLEAQLKENAEISTKNSVRRYLLEQLAANNSTELPE... | 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): 50829
Sequence Length: 4... |
Q6ACP8 | MRAALAAAAALPVPDAEGDHGPARPHPLAPGALVLIGLSGGADSLALAAAAAFEAPRAGFRSGAIVVDHGLQPGSAEVAAGAACQARALGLGPVLVERVRVEAAGGPEGAARAARHTAFDSAARATAAARILLAHTLDDQAETVLLGLARGSGPSSLQGMLPDTGRLLRPFLGLRRATTRAFCADSGLEPWDDPHNDDPAYTRVRVRSAVLPVLEQELGPGVAEALARTAEQLREDDQALDSLALEGAQELVSQADDGSVALEVRGLAAGPPALRQRIIRLVVSAEFGVSLSRSHTLAVAALIADWHGQGPLSLPGVRVV... | 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)... |
Q8F9P6 | MRDKISESTQKIFHAVWERIAPFHEMIQSRPAVLSYSGGKDSSILLHFYFWLWIEKKIPAPCIYHLDHSIRFNLEQEKKIFEYADSTFPFSKIFKKKNIPALSRRLGKTLEETGRAFRYKDLKKISDQYEGYIVTGHHSSDYLETILLNLIRGGGWNSLRTLGWYEKNRFRPLFAFSQDEIETILQSEFWKIFEDESNNSDEYLRNRIRSYIIPLLLREGANPDRIYKNFHRIEKPVSKIFSKKNSDHKIPSFLKIDIWVLNDLSQRERKFFIDRYLRSLNLYPTTRNFFRDLTDLLQKENSFSLENKETWFWKSTSSDL... | 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)... |
Q8YAC7 | MDDTEKRVHKYIEKHDLIRSDDKLLVAVSGGPDSLALLHFLWNSNLVPKEAISVAHLNHQLRENAAKEQRVVETFCERQGIPFYIEEVDIKSRAQSLQKGLEETARIVRYDFFEKVMAEKNINKLVLAHHADDQIETILMRLVRGSASIGWSGIQPKRELKGGQAIRPFLPITKAEIIDYAQKHELAYEIDESNTSQEYTRNRYRAQLLPFLKQENPAVYSHFERFSEETSEDFQFLEALASDLLKKNLIKNGKQTTLLLSSFKNEANPLQRRAIHLLLRYLYNEDASFITVNHIYQIIQMIQSDNPSSSIDLPNKLIAN... | Cofactor: Binds 2 magnesium ions per subunit. One of the ions does not make direct protein contacts.
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 ami... |
Q8EWQ7 | MKHKYLIAVSGGPDSMALLNKKRHLVEAVCHVNYHDREDSDNDEKIVRDYCKKYNLKLFVFDTHKDDVSKYKDINNLQTWYREIRYDFFEKISQELGIKKILIAHQKNDFLESAYMSLNKNKKNLFLGIRRKSKFRSLILIRPLLNKTKKSLEQYCRSKNIEFVIDYTNFWDRYSRNVVRKMMAEWDKKTFQKFYLKVKWFNLKNMFFIKLLDSKFNNWIKQDFDINYFLKIKNNYKESLIYLFLNHIGIKPNENKIEQIIEFINKNKNGSVKKYRLKENQFIEIKNKKILYSIC | 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)... |
Q6F0E4 | MERFKLNTTLSYLVAVSGGPDSMFMLNELIKMNIKEIVVCHVNYNFREDSWKDQKLVEDFCLKNNLKLEKLIINQDYSKLKENFESWARNIRYDFFVEISKKYNIQNVLIAHNRNDLVETFLLQQDRKGYVKHYGLNKTSTYKEITIVRPMLNILKSEILKSLKEENIAFVIDSTNEDKKYKRNKIRANLSESTFNDFEETIKKLNKKLEIINLEVNWYVNNNMSADELKINKNLQDQDLEFIQRTIYKWLEVIKKDFVIQNRRNKTIFEIAKNIKVSEKVFWEINIGEYSIIKDYENLFIIETKAIQPKTILIKSKEDL... | 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)... |
Q601M6 | MQIKIKSKEKYLIGVSGGSDSMFLLNKYKNQDVIVAHINYNLRPEAIFETLLVSKFCQKYNLELKILSFDSFKIKKNLQSGLRLGRYQFFEKIYKEFNCTKLLVGHHRDDFLETVFLQKKQKKIVTFWGIHKKNNLFNMEILRPFLYWRTKKQIIRICQQKKIPYLDDQSNFTGKYQRNQIRFLLEKKSDFSLFFLFLFYYLINIFKLIILKNQKKILQNWQKTGYNINFFKKIKIKSKIIFLFVNQNFDNVKLTRGKINEIINFICGKSTSGAFLLKKNNYIIKKKWKILPKSSKI | 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)... |
Q9MUR3 | MIFLYSKIHKDIIIHNLLKKNDRILIAASGGQDSISLIKILVELQPQWNWDLGIVNCDHSWNQSSRKGSSQIAQIAQLLNIDFYQIVTCHQLINEEKAREWRYQKIEDIAFSNKYNVIVTAHNASDRIETFFFNLLRGTSITGVQSLLWTRSLSSGINIVRPLLNTTRFELKNFVKEIHLPLWPDTSNQSLFFKRNRIRKQLLPYLRKYFNPKVDKVIAQFAEIIHDESFYMENVTQIIEKQLFFGSKNIQQEFIENLPIAIERRIIKKMIEKKLSENHCNFLNIEQIRFFFQKNRKKYSLLECIHFFSN | 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)... |
Q607F5 | MRLSLDSFRAGLHPGSTYRVAFSGGLDSAVLLDLMCQVRRVSGIGVRAIHVHHGIQPEADAWSRHCAAVADRYGVALDILQIDGRSRPGDSPEAAARTARYHSLEASLDPGDILVTAQHLDDQAETLLLQLLRGAGLAGLAAMPNAVPFGAGILHRPLLRFGRRDILAYAQERGLSWIEDPSNRDERYDRNFIRRRILPQLAGRWPAVAANLTRSAGHCAEAAGLLDRLADTLMAAATAADEPGTLVLEIVQRLQPDEQRLLLRRWIHKRGLRAPPAKLLERIRKEVVETAGDRTPMIAWAEGTVRRYRHRLHLLPPSAD... | 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)... |
B8IP16 | MTEAARPLDREEFARRLDRWLGPGAAGGVVLAVSGGPDSTALMGGAARLPPLVPVMVATVDHGLRPEAAAEAEAVARLAGRLGLPHRILAWTGPKPRTRLQEAARAARYRLLLDLAREQGAAALLTAHTLDDQAETVLMRLCAGSGPAGLGGIEPVRHLGGLALVRPFLDLPKARLVATCAAEGWPFVVDPGNADARFARGRLRRVMPHLAAEGLTAARLARLAERLRRNEAALAAAADAALDALARPGARPGGMMLDARGLAVLPEAVALRVLARAIATVVGGNARPARLERLEDVLFGRLLPAIAAGGRLRCTLGGAL... | 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)... |
A2SIL9 | MSGSRATAATTTPRSAEPPRGLAVAYSGGRDSTALLHATLIAARDSGLTVHALHVHHGLSARADAWLAHCESQCRRWARRGLPVCFRAMRVQLACRSGDSLEAVARAARYAALRTLAVEQGVALVLLAHHQRDQAETLLLQALRGAGVAGLAGMPRSIERDGITWARPWLARPREAIEAYVRRYRLSYIDDDSNDDPRFARNRLRLQVWPALQAAFPQAEGTLADAARWAQQAAACVADLAALDLAACAATNDVLPLTAWRQLAPHRAVHALRRWLQQAGVTAPTAADLERLMAELPAGAPARWPLKGGELRRYRGELRF... | 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)... |
Q7NAI9 | MSTTNKKQYLIGVSGGPDSIYLLDRYQDQIKVACHINYNKRPTALRDQLIVSDYCLKNKIPLEILSVSPSYQYHKNFQDQARKIRYDFFLSTGLKYQVDQCLIAHHKDDFLETAIMQYDKNQELLFYGLHQESSYQSLKIFRPLLNLWKDEILSYLEQDKIVYGVDESNFLSTYQRNKIRTNLSKLSQEQKQARLDFFLELNKKNQVRYQSVKDFFSSWDCNYLDLINSLEYYNLLYLWFSKNNIKYSKQKAENILSFLQKKNNKRFRLKAGVYLIKEGIKLKIVKL | 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)... |
Q9C0N3 | MFGLGRPQPTSAEKIAAVENELKVVAEMHSRMVKICTLKCIDKSYREGDLSKGESVCLDRCAAKFFETHQKISDQLQKETQARGGGGFGM | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membran... |
Q9UTE9 | MSMFGIGKNNQTINPQNIAMAEQEVEMMSDIFNRLVMTCHKKCISPKYYEADLTKGESVCIDRCVSKYFEANQSLSQHMQKRGQENPTP | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membran... |
Q6C6U1 | MSFLGLGGQNPNGPSNPQKLLAAEAELDMVTDMFNRLVESCHEKCIKADYSSGDLNANEGLCLDRCVAKYFDVNTKVGEVSMRGADGNYGLEDTANTVHAEAWKQRILHGPTLNVKYVHRIKVHEIVRLTMVYLAPWHFN | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membran... |
P87108 | MSFLGFGGGQPQLSSQQKIQAAEAELDLVTDMFNKLVNNCYKKCINTSYSEGELNKNESSCLDRCVAKYFETNVQVGENMQKMGQSFNAAGKF | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membran... |
P32830 | MSFFLNSLRGNQEVSQEKLDVAGVQFDAMCSTFNNILSTCLEKCIPHEGFGEPDLTKGEQCCIDRCVAKMHYSNRLIGGFVQTRGFGPENQLRHYSRFVAKEIADDSKK | Function: Essential 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. In the TIM22 complex, it acts as a ... |
Q9XH48 | MDSYSSPPMGGSGSSVSPEVMMESVKTQLAQAYAEELIETLRTKCFDKCVTKPGSSLGGSESSCISRCVERYMEATAIISRSLFTQR | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
Q75F72 | MALSSIFGGGSPSQQSNLPTSSASSSVKDQLKGQIAQELAVANATELVNKVTENCFEKCLMAPYTSKQDTCVDQCLAKYMRSWNAISQAYVARIQQASANGDI | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
Q4X0V2 | MAIWGSSSSNTASSGEADIKTHLMNQVRQEAAVTNARNLIGKVNEHCFEACIPNPGTSLSSAEHTCLSQCMEKYISFWNAVSRGYIARLANERKAYGGGALDASFVQSGESSL | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
Q9Y193 | MEQILDVESLKKLTPEQQKTLISGVKQQAAILTAQNMITDXSERCLTKCITXPGSALSXTERQCLQRCMDRFMETYXLASQXLQNRVXEEIAAXTRMT | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
O45319 | MDQLLDVETLKKLSPEQQEQVISGVKQQAALANAQNLVTDISEKCTNKCITAPGSSLASGEKQCLQRCMDRFMESWNLVSQTLQKRLQEEMASSGGMGGGFGQGPSFS | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
Q5AF54 | MAFWNSSSSSSSSGQTDSSSTSSPASLRSQQIKQDLQNQISQELAAANATELVRTITENCFDKCILIPKDTLSPTELQCISQCREKYMRSWNVISKAYIGRIQQEQHH | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
P0CS01 | MSSFFGSGAGSPSNDMTARKEQMKQSIQQELAIANAQQLINKINENCFAKCVTKPSTSLSSSQESCLSQCMTLYMAAFDQVSRSYVARISKERGVAPGL | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
Q9XGX8 | MDKNMLGDLDNLPEEDKLKMASMIEQLQIRDSLRMYNNLVERCFTDCVDSFRRKTLDKQEETCVKRCAEKFLKHSMRVGLRFAELNQGAATTD | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer ... |
Q9WV98 | MAAQIPESDQIKQFKEFLGTYNKLTETCFLDCVKDFTTREVKPEEVTCSEHCLQKYLKMTQRISVRFQEYHIQQNEALAAKAGLLGQPR | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer ... |
Q8J1Z1 | MDGLTAAESRELDQRLQKRQVKEFMSVFGNLVDNCFTACVDDFTSKALSGRESGCISRCVLKSMSTQTRLGERFGELNAAMTAEMQRR | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membran... |
Q9P7K0 | MDRLNVKEQEHLTQVLEAKQLKEYLNMYSTLTQNCFSDCVQDFTSSKLSNKESECIAKCADKFLKHSERVGQRFAEFNAKYMGQ | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membran... |
O74700 | MDALNSKEQQEFQKVVEQKQMKDFMRLYSNLVERCFTDCVNDFTTSKLTNKEQTCIMKCSEKFLKHSERVGQRFQEQNAALGQGLGR | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membran... |
Q8R183 | MNQIQVFISGLILLLPGAVESHTAVQGLAGHPVTLPCIYSTHLGGIVPMCWGLGECRHSYCIRSLIWTNGYTVTHQRNSLYQLKGNISEGNVSLTIENTVVGDGGPYCCVVEIPGAFHFVDYMLEVKPEISTSPPTRPTATGRPTTISTRSTHVPTSTRVSTSTSPTPAHTETYKPEATTFYPDQTTAEVTETLPDTPADWHNTVTSSDDPWDDNTEVIPPQKPQKNLNKGFYVGISIAALLILMLLSTMVITRYVVMKRKSESLSFVAFPISKIGASPKKVVERTRCEDQVYIIEDTPYPEEES | Function: Cell surface glycoprotein that participates in iron homeostasis in the liver, the kidney, the retina and oligodendrocytes by acting as a receptor of H-ferritin . Mechanistically, mediates iron-containing ferritin uptake via an endocytic pathway, trafficking to endosomes and subsequently to lysosomes . Plays a... |
Q96H15 | MSKEPLILWLMIEFWWLYLTPVTSETVVTEVLGHRVTLPCLYSSWSHNSNSMCWGKDQCPYSGCKEALIRTDGMRVTSRKSAKYRLQGTIPRGDVSLTILNPSESDSGVYCCRIEVPGWFNDVKINVRLNLQRASTTTHRTATTTTRRTTTTSPTTTRQMTTTPAALPTTVVTTPDLTTGTPLQMTTIAVFTTANTCLSLTPSTLPEEATGLLTPEPSKEGPILTAESETVLPSDSWSSVESTSADTVLLTSKESKVWDLPSTSHVSMWKTSDSVSSPQPGASDTAVPEQNKTTKTGQMDGIPMSMKNEMPISQLLMIIA... | Function: Phosphatidylserine receptor that plays different role in immune response including phagocytosis of apoptotic cells and T-cell regulation. Controls T-cell activation in a bimodal fashion, decreasing the activation of naive T-cells by inducing cell cycle arrest, while increasing proliferation of activated T-cel... |
Q6U7R4 | MSKGLLLLWLVTELWWLYLTPAASEDTIIGFLGQPVTLPCHYLSWSQSRNSMCWGKGSCPNSKCNAELLRTDGTRIISRKSTKYTLLGKVQFGEVSLTISNTNRGDSGVYCCRIEVPGWFNDVKKNVRLELRRATTTKKPTTTTRPTTTPYVTTTTPELLPTTVMTTSVLPTTTPPQTLATTAFSTAVTTCPSTTPGSFSQETTKGSAFTTESETLPASNHSQRSMMTISTDIAVLRPTGSNPGILPSTSQLTTQKTTLTTSESLQKTTKSHQINSRQTILIIACCVGFVLMVLLFLAFLLRGKVTGANCLQRHKRPDNT... | Function: Phosphatidylserine receptor that plays different role in immune response including phagocytosis of apoptotic cells and T-cell regulation . Controls T-cell activation in a bimodal fashion, decreasing the activation of naive T-cells by inducing cell cycle arrest, while increasing proliferation of activated T-ce... |
P81546 | MAPFAPLASCILLLLWVTAPSRACTCAPPHPQTALCNSQIVIRAKFVGTAEVNQTDLNRRYEIKMTKMFKGFSALGNASDIRFVDTPALESVCGYLHRSQNRSEEFLVAGNLRDGHLQINTCSFVAPWSSLSTAQRRGFTKTYAAGCEGCTVFTCSSIPCKLQSDTHCLWTDHFLTGSDKGFQSRHLACLPREPGICTWQSLRPRMA | Function: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP1... |
P01033 | MAPFEPLASGILLLLWLIAPSRACTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRFVYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTYTVGCEECTVFPCLSIPCKLQSGTHCLWTDQLLQGSEKGFQSRHLACLPREPGLCTWQSLRSQIA | Function: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP1... |
P12032 | MMAPFASLASGILLLLSLIASSKACSCAPPHPQTAFCNSDLVIRAKFMGSPEINETTLYQRYKIKMTKMLKGFKAVGNAADIRYAYTPVMESLCGYAHKSQNRSEEFLITGRLRNGNLHISACSFLVPWRTLSPAQQRAFSKTYSAGCGVCTVFPCLSIPCKLESDTHCLWTDQVLVGSEDYQSRHFACLPRNPGLCTWRSLGAR | Function: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP1... |
P97273 | RRNRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQQLQQDSGGGGGGGGAGCPQQQQAQQQSPRRVAVPVLVKDGKPCPA | Function: Transcription factor that binds and activates the promoter of thyroid specific genes such as thyroglobulin, thyroperoxidase, and thyrotropin receptor. Crucial in the maintenance of the thyroid differentiation phenotype. May play a role in lung development and surfactant homeostasis (By similarity).
PTM: Phosp... |
Q9DCD5 | MSSAAPAKKPYRKAPPEHRELRLEIPVSRLEQEESLTDAERMKLLQQENEELRKRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHALASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDARNTINKLEELNERYRLDCNLAVQLLKCNKSHFRNHKLADLPCELQDMVRKHLRSGQEVASPSPSPSSSLSPGAVVPTSVIARVLEKPESLLLNSAQSGSAGRPLAEDVFVHVDMSGGDPASPPAPGSPNGECCSVSTAGGSPEEELPLPAFDKLSPYPTPSPPHPL... | Function: Plays a role in regulating the structure of the Golgi apparatus.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60520
Sequence Length: 549
Subcellular Location: Golgi apparatus
|
Q7L0Y3 | MAAFLKMSVSVNFFRPFTRFLVPFTLHRKRNNLTILQRYMSSKIPAVTYPKNESTPPSEELELDKWKTTMKSSVQEECVSTISSSKDEDPLAATREFIEMWRLLGREVPEHITEEELKTLMECVSNTAKKKYLKYLYTKEKVKKARQIKKEMKAAAREEAKNIKLLETTEEDKQKNFLFLRLWDRNMDIAMGWKGAQAMQFGQPLVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALHRELVKRYQEKWDKLLLTSTEKSHVDLFPKDSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPG... | Function: Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation . Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends . Together with HSD17B10/MRPP2, forms a subcomplex of the mitochon... |
A4IHS0 | MAFVNTLLRTIRCSAVHTLVQEGRSLSLLKASHQLTQSRKIMLSNHVRKEEAKSEPNETLDLEEWKSILKSDIGNAEMVKTETQEDSSLNEMQELVEMWRLAGRAVPQSITTEQLQVLMELPTKTARKKYLKYLSVREVMKTNRKEKKKELKESKSKIESLDQLETKEDTPEKKNTFLLHVWDKSIDTMQRWKCVQAMKFGQPLVFDMVYEKNMSRYELENTVCQLMESEGWNRRSTDPFHIYFCSLQPYSMYHKELVKRYIGAWDNVFVTATDKSHVEMFPKEQLVYLTADSPNELKHFDHTKIYIIGSLVDRCQQTGL... | Function: Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation. Component of mitochondrial ribonuclease P, which cleaves tRNA molecules in their 5'-ends. Together with hsd17b10/mrpp2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays func... |
Q12893 | MQRALPGARQHLGAILASASVVVKALCAAVLFLYLLSFAVDTGCLAVTPGYLFPPNFWIWTLATHGLMEQHVWDVAISLTTVVVAGRLLEPLWGALELLIFFSVVNVSVGLLGAFAYLLTYMASFNLVYLFTVRIHGALGFLGGVLVALKQTMGDCVVLRVPQVRVSVMPMLLLALLLLLRLATLLQSPALASYGFGLLSSWVYLRFYQRHSRGRGDMADHFAFATFFPEILQPVVGLLANLVHSLLVKVKICQKTVKRYDVGAPSSITISLPGTDPQDAERRRQLALKALNERLKRVEDQSIWPSMDDDEEESGAKVDS... | Function: May play a role in retrograde transport of proteins from the Golgi to the endoplasmic reticulum. May indirectly play a role in protein glycosylation in the Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38197
Sequence Length: 351
Subcellular Location: Golgi apparatus
|
Q9WUH1 | MQRALPGARQHLGAILASASVVVKALCAVVLFLYLLSFAVDTGCLAVTPGYLFPPNFWIWTLATHGLMEQHVWDVAISLATVVVAGRLLEPLWGALELLIFFSVVNVSVGLLGALAYLLTYMASFNLVYLFTIRIHGALGFLGGVLVALKQTMGDCVVLRVPQVRVSVVPMLLLALLLLLRLATLLQSPALASYGFGLLSSWVYLRFYQRHSRGRGDMADHFAFATFFPEILQPVVGLLANLVHGLLVKVKICQKTVKRYDVGAPSSITISLPGTDPQDAERRRQLALKALNERLKRVEDQSAWPSMDDDEEEAGAKTDS... | Function: May play a role in retrograde transport of proteins from the Golgi to the endoplasmic reticulum. May indirectly play a role in protein glycosylation in the Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38099
Sequence Length: 350
Subcellular Location: Golgi apparatus
|
Q12239 | MQYSSRFLELNIPDSFLNINKIPDATKFITVTYICLTATLFCIRRSLYNKLVLEDPNLDYNLITSPLLQMVPSQIWRYPTSLVLSNFIDTKAWKVVVNLLNLIIGGSFIERNWNSSKEMFKFIIVLGSLTNVLIIMLTLLVSFFSNKVRLDIPLDGNYTILIGFPIIYRQLLPETTIIHLKTPQFLAKNFRFKLLPIFVMFTMTVTQIIWFHHFAQLFSIWVTFFASWSYLRFFQKLAPLNCPSLPTTNSQGGQEILVGDASDTFQLIYFFPDLIKPILRPIFNFIYNVVVVKFKVIKPFHDIDIDIGNTIAESRGAKKI... | Function: May play a role in retrograde transport of proteins from the Golgi to the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39742
Sequence Length: 342
Subcellular Location: Golgi apparatus membrane
|
Q7ZVW1 | MSSQSLHDCLRGRCLGVLRRMEIIGRFRYYFQHPWSRLLVSYLVTFFNFLIFAEDPVSHSQKEAHMSVVGNCFSFIISKYPAGFWSVLKVLLWVLAIICGLIAGKFIFHRRLFGRVLRLKMFREDHGSWMTMFFSTILSLFIFSHIYNLLLLMSVRMRPYMVTEYMGIRNESFMKMAAVGTWMGDFVTAWMVTDMMLQDTHYPDWGRTARHLWRQGHNRIVLFWTVLICLTSVVVLVISTDWIRWDNLNRGFLPSDEVSRAFLASFILVFDLLIVMQDWEFPHFMGDLDMNLPGLSTTQLKIRLPVCKRIFKEEYHIHIT... | Function: May be involved in endoplasmic reticulum (ER) stress-induced cell death pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47573
Sequence Length: 401
Subcellular Location: Cell membrane
|
Q9H0C3 | MGKDFRYYFQHPWSRMIVAYLVIFFNFLIFAEDPVSHSQTEANVIVVGNCFSFVTNKYPRGVGWRILKVLLWLLAILTGLIAGKFLFHQRLFGQLLRLKMFREDHGSWMTMFFSTILFLFIFSHIYNTILLMDGNMGAYIITDYMGIRNESFMKLAAVGTWMGDFVTAWMVTDMMLQDKPYPDWGKSARAFWKKGNVRITLFWTVLFTLTSVVVLVITTDWISWDKLNRGFLPSDEVSRAFLASFILVFDLLIVMQDWEFPHFMGDVDVNLPGLHTPHMQFKIPFFQKIFKEEYRIHITGKWFNYGIIFLVLILDLNMWK... | Function: Involved in endoplasmic reticulum (ER) stress-induced cell death pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60185
Sequence Length: 514
Subcellular Location: Cell membrane
|
Q4V9L6 | MVSAAAPSLLILLLLLLGSVPATDARSVPLKATFLEDVAGSGEAEGSSASSPSLPPPWTPALSPTSMGPQPITLGGPSPPTNFLDGIVDFFRQYVMLIAVVGSLAFLLMFIVCAAVITRQKQKASAYYPSSFPKKKYVDQSDRAGGPRAFSEVPDRAPDSRPEEALDSSRQLQADILAATQNLKSPTRAALGGGDGARMVEGRGAEEEEKGSQEGDQEVQGHGVPVETPEAQEEPCSGVLEGAVVAGEGQGELEGSLLLAQEAQGPVGPPESPCACSSVHPSV | Function: Plays an important role in bone formation and normal bone mineralization. Promotes the differentiation of myoblasts into osteoblasts . May induce the commitment and differentiation of myoblasts into osteoblasts through an enhancement of BMP2 production and interaction with the BMP-RUNX2 pathway. Up-regulates ... |
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