ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
E3YBA4 | MTVKIAQKKVLPVIGRAAALCGSCYPCSCM | Function: Chalkophore involved in scavenging, uptake and suppression of toxicity of copper. Each apo-methanobactin (apo-mb) complexes 1 Cu(2+) or Cu(1+) ion to form Cu(1+)-mb (Cu-mb) which is then taken up by the cell. Enhances growth rate in the presence of copper and reduces growth lag upon exposition to elevated lev... |
P64908 | MSDALDEGLVQRIDARGTIEWSETCYRYTGAHRDALSGEGARRFGGRWNPPLLFPAIYLADSAQACMVEVERAAQAASTTAEKMLEAAYRLHTIDVTDLAVLDLTTPQAREAVGLENDDIYGDDWSGCQAVGHAAWFLHMQGVLVPAAGGVGLVVTAYEQRTRPGQLQLRQSVDLTPALYQELRAT | Function: Toxic component of a type II toxin-antitoxin (TA) system. Degrades NAD(+) by phosphorolysis. Neutralized by its cognate antitoxin MbcA.
Catalytic Activity: NAD(+) + phosphate = ADP-alpha-D-ribose 1''-phosphate + H(+) + nicotinamide
Sequence Mass (Da): 20281
Sequence Length: 186
EC: 2.4.2.-
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Q9XI36 | MENTDELVSIELPAPASWKKLFYPKRAGTPRKTEIVFVAPTGEEISSRKQLEQYLKAHPGNPVISEFEWTTGETPRRSSRISQKVKATTPTPDKEPLLKKRRSSLTKKDNKEAAEKNEEAAVKENMDVDKDGKTENAEAEKEKEKEGVTEIAEAEKENNEGEKTEAEKVNKEGEKTEAGKEGQTEIAEAEKEKEGEKAEAENKEAEVVRDKKESMEVDTSELEKKAGSGEGAEEPSKVEGLKDTEMKEAQEVVTEADVEKKPAEEKTENKGSVTTEANGEQNVTLGEPNLDADAEADKGKESKEYDEKTTEAEANKENDT... | Function: Probable transcriptional regulator (By similarity). Required for nucleolar dominance that consist in the silencing of rRNA genes inherited from one progenitor in genetic hybrids.
Sequence Mass (Da): 42358
Sequence Length: 384
Domain: The methyl-CpG-binding domain (MBD) functions both in binding to methylated ... |
Q9LW00 | MGGEEEVVSVELPAPSSWKKLFYPNKVGSVKKTEVVFVAPTGEEISNRKQLEQYLKSHPGNPAIAEFDWTTSGTPRRSARISEKTKATPSPDKEPPKKRGRTKSPVSKKDAEGEKSEGGGEENSHVKDTEMNPPEGIAENENVTDKNGSGETERVNDAKENIVAEETPNAAPVQEEGESMKEKALDSVDDKSKETDKEKDTGSIEKNSVDVEKKTVEASDEKKNSEAETRNHEENGLTTEAEGKEKTAEGEATG | Function: Transcriptional regulator that binds DNA independently of its methylation status. Required during plant organogenesis and development.
Sequence Mass (Da): 27642
Sequence Length: 254
Domain: The methyl-CpG-binding domain (MBD) functions both in binding to methylated DNA and in protein interactions.
Subcellular... |
Q73XV3 | MTEVSVETTSAGSESPSIPLPVHIDPADLAAELAVVLSERAGEEYLLYERGGEWVLATGVRAMIELDSDELRVIRDGVTQRQHWSGRPGPVLGEAIDRLLLETDQLFGWIAFEFGVYRYGLQQRLAPGTALARVFWPNGRIVVTREAIQLFGTSTGRRDDVLGVLGDGVPGLRDASAVDVVTDPSNYRDRVASAVAEIAAGRYHKVILSRCLQVPFAVDFPSTYRLARRHNTPVRSFLLRLGGIRAVGYSPELVAAVRHDGVVVTEPLAGTRAFGRGALHDRQARDDLESNSKEIVEHAISVRSSLQEMAEIAEPGTAVV... | Function: Involved in the incorporation of salicylate into the virulence-conferring salicylate-based siderophore mycobactin. Catalyzes the initial conversion of chorismate to yield the intermediate isochorismate (isochorismate synthase activity), and the subsequent elimination of the enolpyruvyl side chain in a lyase r... |
P64820 | MTKPTSAGQADDALVRLARERFDLPDQVRRLARPPVPSLEPPYGLRVAQLTDAEMLAEWMNRPHLAAAWEYDWPASRWRQHLNAQLEGTYSLPLIGSWHGTDGGYLELYWAAKDLISHYYDADPYDLGLHAAIADLSKVNRGFGPLLLPRIVASVFANEPRCRRIMFDPDHRNTATRRLCEWAGCKFLGEHDTTNRRMALYALEAPTTAA | Function: Acyltransferase required for the direct transfer of medium- to long-chain fatty acyl moieties from a carrier protein (MbtL) on to the epsilon-amino group of lysine residue in the mycobactin core.
Sequence Mass (Da): 23799
Sequence Length: 210
Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
EC: 2.3... |
Q73ZP9 | MSDAPAESAPAQIDPAQTDPAEQPVQILPRERSDIPDAVARIPRPPVPHLDPPFALRVARLGDADMVAEWMNRPHLAAAWEYDWPTPRWRRHLGAQLQGSYSLPLIGSMRGVDLAYLELYWAAKDLISRYYDAEPYDLGLHAAIADVKLVNRGLGPMLLPRIVASVFATEPRCRRVMFDPDHRNTTARRLCEYAGCRFLGEHDTTNRRMALYALDAPTTDR | Function: Acyltransferase required for the direct transfer of medium- to long-chain fatty acyl moieties from a carrier protein (MbtL) on to the epsilon-amino group of lysine residue in the mycobactin core.
Sequence Mass (Da): 24906
Sequence Length: 221
Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
EC: 2.3... |
P63453 | MTSSPSTVSTTLLSILRDDLNIDLTRVTPDARLVDDVGLDSVAFAVGMVAIEERLGVALSEEELLTCDTVGELEAAIAAKYRDE | Function: Acyl carrier protein involved in the formation of acyl-S-ACP intermediates within the mycobactin biosynthesis process. The aliphatic chains carried by ACP are subsequently transferred on to the mycobactin core by MbtK (By similarity).
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of ... |
Q73ZP6 | MPAGSPENHVSAELLGILRDDLNVDVSRVTPDARLVDDVGLDSVAFAVGMVAIEERLGVTLTEEELLSCETVGDLQAAIAAEPRETRDE | Function: Acyl carrier protein involved in the formation of acyl-S-ACP intermediates within the mycobactin biosynthesis process.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP, leading to the activated holo-ACP form.
Sequence Mass (Da): 9475
Sequence Length: 89
Pathway: Siderophore b... |
Q1BBA1 | MQTSNSESVSAALTEILRDDMNVDIRRVTRESRLIDDVGLDSVAFAVGMVAIEDRLGVALTEEDLLSCDTVGDLEAAIQAKVPSSPSGQ | Function: Acyl carrier protein involved in the formation of acyl-S-ACP intermediates within the mycobactin biosynthesis process.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP, leading to the activated holo-ACP form.
Sequence Mass (Da): 9466
Sequence Length: 89
Pathway: Siderophore b... |
A0QUA1 | MNVLSAALTEAMTTSSADLVVFEPETRTWHRHPWGQVHLRAQNVAERIGQDGSSAVGIVGEPTVEGVAAILGALLAGSAVSILPGLVRGADPDQWADSTLNRFANIGVTTVFSHGSYLEQLRTRDSSLVIHDDAEVAHAQRSTTLELGAPLGEFAVLQGTAGSTGTPRTAQLRPDAVLANLRGLAERVGLAGSDIGCSWLPLYHDMGLTFLLSAAVGGTETWQAPTTAFASAPFSWVHWLTESRATLTAAPNMAYGLIGKYSRRLTDVDLSAMRFALNGGEPVDIDGTARFGTELSRFGFDPGALSPSYGLAESSCAVTV... | Function: Activates lipidic moieties required for mycobactin biosynthesis . Converts medium- to long-chain aliphatic fatty acids into acyl adenylate, which is further transferred on to the phosphopantetheine arm of the carrier protein MbtL . Shows a strong preference for palmitic acid (C16) and cannot use short-chain f... |
Q7XJE6 | MYPPPPSSIYAPPMLVNCSGCRTPLQLPSGARSIRCALCQAVTHIADPRTAPPPQPSSAPSPPPQIHAPPGQLPHPHGRKRAVICGISYRFSRHELKGCINDAKCMRHLLINKFKFSPDSILMLTEEETDPYRIPTKQNMRMALYWLVQGCTAGDSLVFHYSGHGSRQRNYNGDEVDGYDETLCPLDFETQGMIVDDEINATIVRPLPHGVKLHSIIDACHSGTVLDLPFLCRMNRAGQYVWEDHRPRSGLWKGTAGGEAISISGCDDDQTSADTSALSKITSTGAMTFCFIQAIERSAQGTTYGSLLNSMRTTIRNTGN... | Function: Cysteine protease that cleaves specifically after arginine or lysine residues. Does not cleave caspase-specific substrates. Acts as a positive regulator of cell death. Required for both oxidative stress cell death response and hypersensitive cell death response mediated by immune response.
PTM: Proteolyticall... |
A0A7R7ZDZ6 | MFKHTKMLQHPAKPDRPDPLFAKKMQEILGGQFGEISVAMQYLFQGWNTRGNEKYKDLLMDTATEELGHVEMIATMIARLLEDAPLDQQEKAAEDPVIGSILGGMNPHHAIVSGLGAMPESSTGVPWSGGYIVASGNLLADFRANLNAESQGRLQVARLFEMTDDKGVKDMLSFLLARDTMHQNQWLAAIKELEAQEGPVVPGTFPKALEKQEFSHQLINFSEGEESAKQNWLNEKAPDGEAFEYVKEAKTFGEKPELKPAPPCVHNTLPGRE | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Catalyzes the decomposition of hydrogen peroxide into water and oxygen . No significant activity could be detected with any of the other tested substrates, including glutathione, pyrogallol, NADH, NADPH and o-dianisidine .
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Seque... |
Q97FE0 | MFKHEKQLLNGMQVKVERENPQYAVLMQEQLGGANGELKAAMQYLSQSFRVKDQALKDLFLDIGTEELSHMEIVAETINLLNGHSVNYEVVGVGEVESHVLSGLTPFLVNSSGEPWTANYVSVTGDIVADLLSNIASEQRAKVVYEYLYRQINDKEVRRTIDFLLNREEAHNALFREALNKVKNEGSNKDFGVTEDSKLYFDLSTPGRYVQDPNPTEPSFSNPRR | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Catalyzes the decomposition of hydrogen peroxide into water and oxygen.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 25444
Sequence Length: 225
EC: 1.11.1.6
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O43772 | MADQPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTFDCFRKTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKKLQQKHPEDVLSYPQLFAAGMLSGVFTTGIMTPGERIKCLLQIQASSGESKYTGTLDCAKKLYQEFGIRGIYKGTVLTLMRDVPASGMYFMTYEWLKNIFTPEGKRVSELSAPRILVAGGIAGIFNWAVAIPPDVLKSRFQTAPPGKYPNGFRDVLRELIRDEGVTSLYKGFNAVMIRAFPANAACFLGFEVAMKFLNWATPNL | Function: Mediates the electroneutral exchange of acylcarnitines (O-acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-carnitines) with free carnitine ((R)-carnitine or L-carnitine) across the mitochondrial inner membrane, via a ping-pong... |
P60355 | MFKHTRKLQYNAKPDRSDPIMARRLQESLGGQWGETTGMMSYLSQGWASTGAEKYKDLLLDTGTEEMAHVEMISTMIGYLLEDAPFGPEDLKRDPSLATTMAGMDPEHSLVHGLNASLNNPNGAAWNAGYVTSSGNLVADMRFNVVRESEARLQVSRLYSMTEDEGVRDMLKFLLARETQHQLQFMKAQEELEEKYGIIVPGDMKEIEHSEFSHVLMNFSDGDGSKAFEGQVAKDGEKFTYQENPEAMGGIPHIKPGDPRLHNHQG | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Catalyzes the decomposition of hydrogen peroxide into water and oxygen.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 29743
Sequence Length: 266
Domain: Each subunit is composed of three distinct structural regions: an N-terminal polypeptide, a central f... |
Q9Z2Z6 | MADEPKPISPFKNLLAGGFGGMCLVFVGHPLDTVKVRLQTQPPSLSGQPPMYSGTLDCFRKTLMREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKKLQQKSPEDELSYPQLFTAGMLSGVFTTGIMTPGERIKCLLQIQASSGENKYSGTLDCAKKLYQEFGIRGFYKGTVLTLMRDVPASGMYFMTYEWLKNLFTPEGKSVSDLSVPRILVAGGFAGIFNWAVAIPPDVLKSRFQTAPPGKYPNGFRDVLRELIREEGVTSLYKGFNAVMIRAFPANAACFLGFEIAMKFLNWIAPNL | Function: Mediates the electroneutral exchange of acylcarnitines (O-acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-carnitines) with free carnitine ((R)-carnitine or L-carnitine) across the mitochondrial inner membrane, via a ping-pong... |
P97521 | MAEEPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTIDCFRKTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKRLQQKSPEDELTYPQLFTAGMLSGVFTTGIMTPGERIKCLLQIQASSGKNKYSGTLDCAKKLYQEFGIRGFYKGTALTLMRDVPASGMYFMTYEWLKNLFTPQGKSVHDLSVPRVLVAGGFRGIFNWVVAIPPDVLKSRFQTAPPGKYPNGFRDVLRELIREEGVTSLYKGFNAVMIRAFPANAACFLGFEIPMKILNWIAPNL | Function: Mediates the electroneutral exchange of acylcarnitines (O-acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-carnitines) with free carnitine ((R)-carnitine or L-carnitine) across the mitochondrial inner membrane, via a ping-pong... |
A0R2W9 | MSELRLMAVHAHPDDESSKGAATTARYAAEGARVMVVTLTGGERGDILNPAMDLPEVHGRIAEVRRDEMAKAAEILGVEHHWLGFVDSGLPEGDPLPPLPDGCFALVPLEEPVKRLVRVIREFRPHVMTTYDENGGYPHPDHIRCHQVSVAAYEAAADHLLYPDAGEPWAVQKLYYNHGFLRQRMQLLQEEFAKNGQEGPFAKWLEHWDPDNDVFANRVTTRVHCAEYFHQRDDALRAHATQIDPKGDFFHAPIEWQQRLWPTEEFELARARVPVTLPEDDLFKGVEP | Cofactor: Binds 1 zinc ion per subunit.
Function: A mycothiol (MSH, N-acetyl-cysteinyl-glucosaminyl-inositol) S-conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylating agents and antibiotics. Activity is s... |
P9WJN0 | MSELRLMAVHAHPDDESSKGAATLARYADEGHRVLVVTLTGGERGEILNPAMDLPDVHGRIAEIRRDEMTKAAEILGVEHTWLGFVDSGLPKGDLPPPLPDDCFARVPLEVSTEALVRVVREFRPHVMTTYDENGGYPHPDHIRCHQVSVAAYEAAGDFCRFPDAGEPWTVSKLYYVHGFLRERMQMLQDEFARHGQRGPFEQWLAYWDPDHDFLTSRVTTRVECSKYFSQRDDALRAHATQIDPNAEFFAAPLAWQERLWPTEEFELARSRIPARPPETELFAGIEP | Cofactor: Binds 1 zinc ion per subunit.
Function: A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-inositol) S-conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate (AcCys S-conjugate, a mercapturic acid) and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylatin... |
P05528 | MVTLKMAIIFLMEQIRTPFSLIWTIMSPTVLFFFLHFNEIELHYGDTAWLGKQISWFVGYISFSVVLFNYCLYLVGRRESGFIATFVHNMDGRLLFIRSQLIASLIMSILYVFFFILVVLTGFQASPDYQIVMIILKSIYINAFMMVSLTFMASFRVTFQTASTIYSVLITVCMVSGIVSLKYNEGIVYWINQVNPIAIYSTILQSDQELSLMTIFFYSIMLIISIISALTFKTEPVWSSQ | Function: Together with two further proteins McbF and McbG this protein causes immunity to the peptide antibiotic microcin B17 (MccB17), which inhibits DNA replication in enterobacteriaceae. Immunity is determined by two different mechanisms. McbE is involved in the production of extracellular MccB17 and, in a complex ... |
P10911 | MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVMLSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIENFALTVKEMAQMLQSFGTELAETELPDDIPSIEEILAIRAERYHLLKNDITAVTKEGKILLTNLEVPDTEGAVSSRLECHRQISGDWQTINKLLTQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQQLVTEVEFLLNQQAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRCNELRYLSDILVNEIKAKRIQ... | Function: Guanine nucleotide exchange factor (GEF) that modulates the Rho family of GTPases. Promotes the conversion of some member of the Rho family GTPase from the GDP-bound to the GTP-bound form. Isoform 1 exhibits no activity toward RHOA, RAC1 or CDC42. Isoform 2 exhibits decreased GEF activity toward CDC42. Isofor... |
Q54EV4 | MVINNQNNNNQNNNQNNNNKNDNLNNSTTTTTTTATTTKSSTLFHSNDFFSGLIAGIVSRTLTAPLERIKILNQVEVILKDGTKYNRIIPAFKVIIKEEGIAGLFRGNFVNIIKAGPQSAIRFYSYGAFKRMASEPDGSISVINRMWAGASSGVVSVALTHPLDVIKTHITVIAPTAATIKNVTKGIYRDLGIIGFFRGLSAGILNIAPFAALNFTFYETIKEKTQQYILKSPPLYAPSIYGAISGGLTMTILYPLDVVKRRIMLQHFDRNQLPIYKNFIDAIIKITKTEGISALYKGIRPAYLKVIPTVSINFLIYEGA... | Function: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36132
Sequence Length: 327
Subcellular Location: Mitochondr... |
Q54MZ4 | MSNNNNNNNNNNNNNNNNNNNNNNNNNNDKNNNNNIDSSIKEKKLKEWFDKFDVDKDGSLDSNELKKGFKLHANIDMKDEQITKMMERADSNKNHRIEWDEFLKVASDSSSPEIEDIAEHWLQYSTKPIVHAPADVPSWKLLLSGGVAGAVSRTCTSPLERLKILNQVGHMNLEQNAPKYKGRGIIQSLKTMYTTEGFIGFFKGNGTNVIRIAPYSAIQFLSYEKYKNFLLNNNDQTHLTTYENLFVGGAAGVTSLLCTYPLDLIRSRLTVQVFGNKYNGIADTCKMIIREEGVAGLYKGLFASALGVAPYVAINFTTYE... | Function: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48684
Sequence Length: 434
Subcellular Location: Mitochondr... |
B0G159 | MVLNENDKEFVKKLFDSLDKDNNGKLTREEIKEGFFKLRIPSSEKDIESFLTNVDKDKDGSVSFKEFEDFTIENIKKLKIVFEELDTNKSGTLDIHEIEESIKKLNIPLYSEQELIRLFHRIDKNRDNQIDFNEWRELLVLLPNSNLQLIISFWKDSQILDAGFDNGGFIPPMVEKKEKASSLRNTITYMLAGSVAGFASRTSTAPLERVKIMCQLNHGKPISLISAFKACYKDGGIKGFFRGNLANIIKVSPESAVKFGTYEYVKKLFAENDCELTSAQRFISGSVAGVVSHTTLFPLEVVRLRLSAEIAGTYNGIFDC... | Function: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53100
Sequence Length: 472
Subcellular Location: Mitochondr... |
Q8NI22 | MTMRSLLRTPFLCGLLWAFCAPGARAEEPAASFSQPGSMGLDKNTVHDQEHIMEHLEGVINKPEAEMSPQELQLHYFKMHDYDGNNLLDGLELSTAITHVHKEEGSEQAPLMSEDELINIIDGVLRDDDKNNDGYIDYAEFAKSLQ | Function: The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.
Sequence Mass (Da): 16390
Sequence Length: 146
Domain: Essentially unstructured in the absence of calcium ions. Requires calcium ions for folding.
S... |
Q55E85 | MDSTKTNNKWAAAGILNSVGKDFVAGSVGGMSSIMAGHPFDTIKVMLQDASGNLPKFKNGFQALKYIMKVDGIKGIYRGLSVPLFSVSFTNSVFFATNNFCQSYFHPPCKDENGEDILIPYHKAAAAGAIAGGVISLLITPRDLVKSKLQVQCRPFGSTNVSLQYKGPIDVIRQTIKRDGIKGMFKGIRSTFCRDIPGDAVYFVVYEFMKRKLLALSKNNNNNNNNNDNNDNSSPKAGVPAWVAIGAGGCAGMSFWMSIYPMDVVKTRIQTQPDHLPPQYTSVLQTITKIYREEGISVFFRGFSATILRAFPTSAVNFLM... | Function: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37959
Sequence Length: 344
Subcellular Location: Mitochondr... |
Q55E45 | MENKKESSLLYILTGATSGLLADSIMHPVDTVRARVQIEKVGKSQYKGTFNALNQIIKNEGVSYLYKGFPIVATATVPAHALYFLGYEYSKQWVTDRYGKKWGESTITHFSAGFVADALGSLIWVPMDIIKQRLQVQTNTQKLNPNQTYYKGSFHAGKIILQEEGIRGLYRGFMPALATYGPFVGIYFSVYEKCKSTISSLLSKEKDQYLPIPYQLGSGFFAGAFAAAVTCPLDVIKTRIQVQRSTEKQIYKGMWDSFKTILKEEGPKAFVKGMGARIWWIAPGNALTIASYEQLKYLFKDLI | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34018
Sequence Length: 303
Subcellular Location: Mitochondrion inner membrane
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Q54BM3 | MASNNKDSQLMIALKDIVAGSIGGVGQVFTGHPLDTIKVRLQTQSVGNPIYSGTMDCLKKTISQEGFAGLYKGVASPLVGLSIMNSVMFLAYGQSKTLIQKLSDNPNEALDLKGLTAAGALAGIAIGFVDAPVDLFKSQMQVQQGDKNQYKSTADCAKQIWKVGGVRGVFQGLGATLVRDIPANACYFGAYELCRDFLASKDNISVNQLSSLQIMAAGGAGGVSYWTLTYPADVVKSTMQTDAIVKSQRKYKNMIDCASKIYKQQGIAGFYKGFTPCFIRSVPANAACFVLYEKARQIMS | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Mediates the transport of acylcarnitines of different length across the mitochondrial inner membrane from the cytosol to the mitochondrial matrix for their oxidation by the mitochondrial fat... |
Q86I81 | MVNGEEYVETPNLIHDEETRKDVKFNLGIELLAGTLAGVSSCILFYPLECVEAKLQVQSSSTAVAATMLGLKKNGGSGSGSSSSSSISHQTPNGPIAMAKSILRNEGFKGFYQGVSPTILGNAVNWGVYFSIYRATNHWWNSTDINGNQYQGPAWVGHSVSAITAGVITTAIVNPFWVLKIRLATSKKYSGMKHAFQSILRSEGVGGFWKGVGVSFIGVSEGLFQFVSYEYILNQMKESNLKMNGGELSVGNYLFAGGTARLIAGVLTYPYLLIRSSLQSETCPYKSMSEAVKGIYKTNGIKGFYKGIGPNLARSIPPAA... | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Transports folate across the inner membranes of mitochondria (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36655
Sequence Length: 338
Subcellular Locati... |
Q54VX4 | MSSSHTIQETKEVHTKTNKRIQWDDLDPKRYYFYNFLLGGSIDLLMFPLDVIRTRLQVQGSQNVIQSFPQYNGTFDGFKKLIRLEGKRALYKGFLTSECGYLCSRAIYFGSYEFVKQGFLKGRSDSDSDLLFVTTISGAISEALASVIWVPFDVATQSVQIQGSLSKPKYKGGSDVFKKIYGERGIKGLYKGFGATIIRNVPYSGIWWGTYEISKSKLTQFNIRQKLGLKERSSHSLAVSAEIDKNNPSHEVENEDPIIHFISGFFAAVFATSITNPLDVAKTRLQTGVFPENEKPNFYTIIKSTIRKEGIRALWKGLVP... | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39012
Sequence Length: 345
Subcellular Location: Mitochondrion inner membrane
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Q54W11 | MIASKETKEKIRNFIGGFASGAASTLAGHPFDTLKVRLQTEGSTGRFRGLAHCFTTTIKEEGFFALYKGVTPPLLGMSIINSCMFGAMNIVKSKIHTDKSTPISLGEIMVSGAITGWIVSFVACPIETVKSKLQVQYTGVKLYNGPIDCIKKIGIRGLYKALIPTGFQRNSLYAYFGCYELAQRYLRREDGSMTMGRSFIAGGIAGTGFWLTNFPFDVIRSRIMTMPYNESPPRYKGMIDCAKHIYRVDGLKGFWKGFSPCLLRTFPANGATFVAYECVMKFFPM | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31583
Sequence Length: 285
Subcellular Location: Mitochondrion inner membrane
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Q54QN2 | MRYILNNNVEGTSALLGSTVATAFLQPFDFLKIRLQGSGFASGGDLNKFKRVGVIDTCKNVLKNEGIKQFWRGSSPTIVASGIAWGTYMHFYEAYKNILKSKYNVTQLNTFDHFICAVGASATQVFITNPIFLIKTRMQLQTPGSANYYTGIFDGIKKTVKVEGFKGLYKGVIPSLWLTFHGGIQMSSYEHIKFYFSSNSGKSLDSLNASEIFIASSISKFLASTILYPFQVVKTRLQDERNIPNQNNVRVYNGTKDVIFKILKNEGIIGFYRGLVPNTLKVIPNTSITLLLYEEIKKSFNYIINE | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Transports folate across the inner membranes of mitochondria (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34343
Sequence Length: 306
Subcellular Locati... |
Q54BF6 | MAGDLTPSLFLKYGFGGALSCSITHSLVVPLDVVKTLLQTNPGKYTGMMNGFSTVIKEQGPSGLLQGLGPTAVGYALQGFLKFGFYEVFKKTYADAVGEKADQFRIPIWLAASATAEVIADIALCPNEAVRIRLVAEPTFAKSPVEAFGKIFKQEGVLGFYKGLPPILLKQVPYTMAKFAVFEFTAENVYKGLAASGKPKESLTDGQKLSVSLGSGIVAGIVAAIVSQPADTILSKINQEKTDGGVVKAIGNIMRRLGVRGLFLGLPTRCFMVGTLTAGQFFIYDGIKQMLGLTPAKK | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Transports phosphate groups from the cytosol to the mitochondrial matrix. Phosphate is cotransported with H(+) (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
Q54DU1 | MATTSVSSPKSKPSWVSFLSGGLAGVTAKSAVAPLERVKILYQIKSELYSLNSVYGSMLKIVENEGIKGLWRGNSATILRVFPYAAVQFLSYETIKNHLVADKSSSFQIFLAGSAAGGIAVCATYPLDLLRARLAIEIHKKPTKPHHLLKSTFTKDGVKGIYRGIQPTLIGILPYGGISFSTFEFLKRIAPLNEIDENGQISGTYKLIAGGIAGGVAQTVAYPFDVVRRRVQTHGFGDAKAVVNLEHGTLRTIAHILKEEGILALYKGLSINYVKVIPTASIAFYTYEYLSNFFNKL | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Required for the accumulation of coenzyme A in the mitochondrial matrix (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32323
Sequence Length: 297
Subcell... |
Q54QI8 | MTVHGNTKTSPMVTLLAGGVSGVIAKSTIAPLERVKILYQVKSKMYSFNSVYGLMKNIIKNEGLAGLWKGNTATILRIFPYSAIQWTSYDYLKNNFVTDKKSSVQIFIAGSLGFSCAILLTYPLDVIRARLALSYSNNNNNNSINSKNLNSSTQPPKVLKNGIGAVNIEKSIDFNGYKTKGLFKGIWRGILPTLYGSIPYAGVGYSSFEYFKRIAPDSFRNEKGDVIGIYKLISGGVAGGLGQTAAYPLDVVRRRIQTTGYGDGKGVENLKHSTLKTMFTIFQKEGIYALFKGISINYIKVIPTNGVAFLTYETLCDYFN... | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May be involved in the accumulation of coenzyme A in the mitochondrial matrix (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35861
Sequence Length: 326
S... |
O86028 | MTEKTIKDWEALAEKELRVSPEGLVWHTPEGIDVKPLYTSDDMSGIGHLNSLPGFEPFVRGPRATMYAGRPWTVRQYAGFSTAEASNAFYRRNLAAGQQGVSVAFDLATHRGYDSDHPRVQGDVGKAGVAIDSVEDMKILFDGIPLDRISVSMTMNGAVIPILASFIVAGEEQGVSRDKLSGTIQNDILKEFMVRNTYIYPPEPSMRIVADIIEYTAKEMPKFNSISISGYHMQEAGATLVQELAFTLADGREYVRAALAKGLNVDDFAGRLSFFFAIGMNFFMEAAKLRAARLLWTRIMQEFKPEKASSLMLRTHCQTS... | Cofactor: Monovalent cations such as NH4(+), Rb(+), Cs(+), K(+), Li(+) or Na(+) are required for enzyme activity.
Function: Radical enzyme that catalyzes the transformation of methylmalonyl-CoA to succinyl-CoA. Is required for growth on the polyhydroxyalkanoate degradation pathway intermediates 3-hydroxybutyrate and ac... |
Q9UXG1 | MEIPSKQIDYRDVFIEFLTTFKGNNNQNKYIERINELVAYRKKSLIIEFSDVLSFNENLAYEIINNTKIILPILEGALYDHILQLDPTYQRDIEKVHVRIVGIPRVIELRKIRSTDIGKLITIDGILVKVTPVKERIYKATYKHIHPDCMQEFEWPEDEEMPEVLEMPTICPKCGKPGQFRLIPEKTKLIDWQKAVIQERPEEVPSGQLPRQLEIILEDDLVDSARPGDRVKVTGILDIKQDSPVKRGSRAVFDIYMKVSSIEVSQKVLDEVIISEEDEKKIKDLAKDPWIRDRIISSIAPSIYGHWELKEALALALFGG... | Function: Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighborin... |
Q46970 | MSFLNFAFSPVFFSIMACYFIVWRNKRNEFVCNRLLSIIIISFLICFIYPWLNYKIEVKYYIFEQFYLFCFLSSLVAVVINLIVYFILYRRCI | Function: Probably able to protect the producing cell against microcin N (microcin 24).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11426
Sequence Length: 93
Subcellular Location: Cell inner membrane
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Q46971 | MRELDREELNCVGGAGDPLADPNSQIVRQIMSNAAWGAAFGARGGLGGMAVGAAGGVTQTVLQGAAAHMPVNVPIPKVPMGPSWNGSKG | Function: Active against E.coli and Salmonella, but not Listeria or Campylobacter . Channel-forming microcin (By similarity). Probably neutralized by its immunity protein McnI (Probable).
PTM: Mass spectrometry suggests 3 of the 4 Met residues of the mature peptide are oxidized.
Sequence Mass (Da): 8896
Sequence Length... |
Q69HT9 | MMDMKENDQKRNDMMDMKSHDERKNLNSSQGKNEITFPKVLDPKKDNNGYKSYTLKAQKGKTEFYKGNFSNTLGYNGNLLGPTLKLKKGDKVKIKLVNNLDENTTFHWHGLEIDGKVDGGPSQVIKPGKEKTIKFEVKQEAATLWYHPHPSPNTAKQVYNGLSGLLYIEDDKKNNYPSNYGKNDLPIIIQDKTFVSKKLNYTKTKDEDGTQGDTVLVNGKVDPKLTTKEGKIRLRLLNGSNARDLNLKLSNNQSFEYIASEGGHLEKTKKLKEINLAPSARKEIVIDLSKMKEDKVNLVDNDETVILPIINKEKSTNKDT... | Cofactor: Binds 4 Cu cations per monomer.
Function: May be involved in copper homeostasis and oxidative stress response. Oxidizes the substrate 3,3'-dimethoxybenzidine in vitro. Also possesses low levels of phenoloxidase and ferroxidase activities.
Sequence Mass (Da): 50840
Sequence Length: 447
Subcellular Location: Cy... |
Q8CQF6 | MMNMKEDKKNTMDMKNMKHHDERKKLNSSQGKNEIIFPEVAESKKDNNGYKNYTLKAQEGKTEFYKNNFSNTLGYNGNLLGPTLKLKKGDKVKIKLINNLDENTTFHWHGLEINGKVDGGPSQVIKPGKEKTIKFEVNQDSATLWYHPHPSPNTAKQVYNGLSGLLYIEDSKKNNYPSNYGKNDLPIIIQDKTFVSKKLNYSKTKDEDGTQGDTVLVNGIVNPKLTAKEEKIRLRLLNGSNARDLNLKLSNNQSFEYIASDGGQLKNAKKLKEINLAPSERKEIVIDLSKMKGEKISLVDNDKTVILPISNKEKSSNKGN... | Cofactor: Binds 4 Cu cations per monomer.
Function: May be involved in copper homeostasis and oxidative stress response.
Sequence Mass (Da): 50683
Sequence Length: 447
Subcellular Location: Cytoplasm
EC: 1.-.-.-
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Q2W8M7 | METTLGSYARTLSLGMLVPSAICLLAGTFGLLGGSSIALWVVIAVSLLGVVGGVKIGGSARRMAGDLSTAIHVLSRSASGDLNARILDVRGSGGIGALQHSINRLLDLAEAFGKEAFAAVESANHGRYYRRIITTGLRGDFVLYAKTINQALKRMEARDAEFIAFANNQVKPVVNAVAAAATELEASSGAMSAQSTDTSHQAMTVAAAAEQASVNVQAVASAVEEFSASIKEISTQVHRAAAVASEAAGVASRTDTTVHGLSDAAQRIGAIVSLINDIAAQTNLLALNATIEAARAGDAGKGFAVVANEVKNLANQTARA... | Function: Probable methyl-accepting taxis protein. May be the receptor that senses the torque generated from the interaction between the magnetosome dipole moment and the external magnetic field (Probable). Overproduction interferes with magnetotaxis, cells respond more slowly to changes in the magnetic field; requires... |
P02942 | MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA... | Function: Receptor for the attractant L-serine and related amino acids. Is also responsible for chemotaxis away from a wide range of repellents, including leucine, indole, and weak acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59443
Sequence Length: 551
Subcellular Location: Cell inner membr... |
Q9WYR0 | MSLRKKVFLLMIVVVAGLLLSFFLIYRSVSNSIINSVRSNTENQAKALSKFVVEKLNNVTNVARSAATYLGSQFFEAYMITNQLKTTVEKEKSTFAFAFSALSFNKSAALTDGNRVDRVDFADYEKYIKAVEGKDIFFMPETFQGTPVLTVVVPIETMNTRTGIVGFGINLSENSDLWKAVVEEGKASKSGYGLLVTSDGKVLIHKDMGNFMKDVKELGGFEKAFEEAKSGGEKYVEYEYNGEKKYTVWEKVPGYDFYIFSTGYLEELLAEGRKATLGTIVTYVVFGGVIFAVLFVSMMPVVKRMRQQVEKVKRFGEGDL... | 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.
Location Topology: Multi-pass membrane pr... |
Q9HUB1 | MYDWWVLQLAKLSVSRKLMVGFGVLLALLLLVVISSNRTLTHQTALSEQLAEVASLMEQTQQAEQGRLAFEAGSDPRQAEQVRQTLAGMLQRLQALRDSELDPAALAHQVEAIEAYRKAFDDLAAADQQRSAARGVLVGTAQQALDSFARLEELMDASLAQQAGDPQALQRSRAVADLHQQLLMVRYQVRGYVFERSDKAEQAAFAAFDALRQAATTLRGQLPGEADAALEQAMGSLQGYRGGIEQFRAGVIRTRQAQQAMQSSTQDMARAGRTLTEAGRQLRESTASRDRASLWLIAALALAFGCVAGWAINRQIVRPL... | 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. McpK is a chemoreceptor that specifically... |
Q9I055 | MNESVARVFDRILRGLGLKTLNAQFLLSYALMFGLAACASVALYLSMSISPETINVAGAQRMLSQKMAREALQLRLGAGDPKALAATIAQYERSAADLDAGNAERNVSRMGAPEIAAQRQKVAQIWGRYRAMLDQVAQPASQVDLRGFSQYSTELLGELNNLVSLMSARADSVQHTQMWIAFGCLLAILVLVVLGRQFGLAPLMRQLRGLEVALTEVGAANFTHALAAGHADNEIGRIVAGYERMRQDVSGLLANVKRSAAETDKDVAEALEQALGAGDQVARQHQDLDQVATAMNEMSATVAEVARHANHAAHSTRDAA... | 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. McpN is a chemoreceptor that recognizes s... |
Q88IY8 | MNTLRSMSISRRLWLILVVAVAMLVVLGLLMLRQIHGDLYQAKAEKTRHVVQTAAGVLAYYQGLEAAGTLSREAAQQQALQVVRALRYDHDDYFWINDLGPKMIMHPANPKLDDQDLSAIRDPDGFAVFNEMVALARQQDAGPVNYRWPKPGASEPVAKTSYIQLFKPWGWIIGSGVYVDDVQAEFARQLRDASLVGVGIALLMALVVMLIARSIARPLQEAVQAMGNIASGESDLTRRLDTHGSDEITHLGEHFNRFNGKLQGVVGQLQGAAHALAQSAGHVGDNAGAAQQRSAQQSLQMDQVATAVNEVTYAVQDVAK... | 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. McpP is a chemoreceptor that responds spe... |
Q88D09 | MYQWLAQSLGNVSVNRKLGLGFGLVLLLTLAITLTGWHGMDSIIDRGDKLGNISVIQQYTQELRIARQQYDRRRDDASLAELEKALSNLDRQVQLMLGQIEQPADHQRLEQQREAVRIYQQAFNELKQADQRREASRDVLGSSADKAVDLIGRVQRSLLQGANINQYQHAVDVSALLQQARFQVRGYTYSGNADYQQTALKAIDQALAELRALPAKVPAEHAASLDDAATAMGGYRDAVTQFGNAQLASEQALQRMVEQGTVLLQASQMMTASQTEVRDAAAAQAKTLLTVATVLALALGLLAAWAITRQIIIPLRQTLR... | 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. McpQ recognizes specifically citrate and ... |
P21822 | MFNRIKVVTSLLLVLVLFGALQLISGGLFFSSLKSDKENFTVLQTIRQQQLLLSESRVDLLQARNSLNRAGIRYMMDTNKIGSGATIDELLAKAKEELARAERNYTAYEKIPQDPRQDPQATEKLKQQYGILYGALSELIQLLGEGKINAFFDQPTQKYQDDFEQTYNAYLQQNGKLYQIAVDASNSSYSSAIWTLIVVIIVVLAAIVGVWMGIHHILVRPLNRMIEHIKRIASGDLTQPIPVTSRNEIGVLAASLKHMQNELIETVSGVRQGADAIYSGASEIAAGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA... | Function: Receptor for the attractant L-serine and related amino acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60038
Sequence Length: 556
Subcellular Location: Cell inner membrane
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Q88E10 | MNSWFANISVNLKLGLGFGLVLVLTGLLALTGWTSLGSLIDRSNWMGDIGQLNKDLTDLRIARLQYMIANGDDTAAANTLAKLDAFSKQQAYLATTFKSPENVKLLGELGDTISAYKLSLNKMRQGYDATRAARVSMDSSAIRADQAMDALSQEVMARPEADSVRLAQYQLISKARQQLLQVRIDVRGYIAENSSANEQAALRQLDAALADTDNLKRQLPSEDARLQQFENAVLAYRDAVRQFRDAVANITTSRAEMTVQGADIVKRSDALYQIQLERRDIESTQARSLQAIATLLALLVGVLAAVLITRQITRPLQDTL... | 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. McpS is a specific chemoreceptor for 6 tr... |
Q0TML0 | MVQWISPLDNSIVIASKVKILRNIKGIKFTKLLNEEEFNDLLSMVLGRLKEIDILDKCYVVKLKDGEEKIIDYYKENFGLIKYFENKDNLIFIMNKNGEFNILLNEEEHIGIECTNSGLSLREVYSKVDNLDDLIEEKIHYSFDSELGYLTSNIKNLGTALRAKVFIHLPLLSSNNLIRIIKNALKEEGITLKSIYNSGNKDVGNIYEVSNIKTLGMSEKDILDSLISITNKLILREKNQRDNLSKDEYIELKDDILRSLGVLRNTYSIDRDEALKYLSYVRLGVELGIIEDLSLKSVNSAMIEIQPDMINNSSIKKRDI... | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 38686
Sequence Length: 337
EC: 2.7.14.1
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A4J0X5 | MSLKETVSNPYSKWLEATGPENDVIISSRVRLARNLMGYPFPHVLGHENADKVLYAVQSAVAQKSLQEAVGNLELSRMTELSSIERQILVEKHLISPDMLEQPEKRGVVLRDDEVISIMVNEEDHLRIQCLLPGLQLKECWDLANTVDDGLEQIIDYAFAKEQGYLTSCPTNIGTGLRASVMLHLPALVMTRQINAVLTTLSKLGLTVRGLYGEGTQATGNLFQVSNQVTLGLTEEEIIDNLITVALQLVTQERAARRALHKEQLHQIEDKVWRAYGLLKYARTMTSNETMTLLSDMRLGVDLGVITGIPPGIIMELIIL... | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 39884
Sequence Length: 357
EC: 2.7.14.1
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C4KZS5 | METFLTHPLGPKMKERAKLDDLVVSTRIRLARNVKDTVFSPVLSKEGERQLCDRLEGRLRGLKGFEYLHMRDYDEVTRQALMEKHLISPAVAANEESAVFLSEDETISVLINEEDHLRIQTLLPGYQVKEAFELANQVDALCAESLSYAFDEQLGYLTTCPSNIGTGLRASVMLHLPGLTLTGRISPILRELRKLGYTIRGRYGEGSDAAGRLFQLSNQRTLGSHESQLLADFMEVTEQVIQAERHAREELIAHRQEELEDRFYRSYGILRYAKLLSSTEAIERLSDLHLASDLGILSDWSPPKFHELIVRLQSGFLQKH... | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 39508
Sequence Length: 347
EC: 2.7.14.1
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P0DMM5 | MSFGKFFNTAVSAWMSQEGPNSDIVLSSRIRLARNIVDFRFPTLFSSEEAKQIVALFERAFVHRPYGEAGRFELLKMSELQPIEKRVLVEKHLISPHLAEDSPFGACLLSENEEISIMINEEDHIRIQCLFPGLQLAEALEAASELDDWIEGHVNYAFDERLGYLTSCPTNVGTGLRASVMMHLPALVLTQQINRIIPAINQLGLVVRGTYGEGSEALGNIFQISNQITLGKSEEDIVADLHTIVEQLIAQERAARQALVKTLGIQLEDKVFRSYGILANCRVIDSKEAAQCLSDVRLGIDLGYIKNVSRNILNELMILT... | Function: Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventin... |
B8D093 | MSLKDLINKNLSHWVAGQGPERDIVLSSRIRLARNLDTIPYPNRADKDSKEEVTKRVLDATSKQGKIKLHYIKMDDLPEVEREVLVEKHLISPAHAKAGEGKGVLLNDNETISIMINEEDHLRLQVLIPGLQLEGAWETASELDDLLEEKLDFAFSQKWGYLSACPTNVGTGLRASVMVHLPALNLTNNINKMLGAISKVGLTVRGIYGEGSEYVGNLYQISNQVTLGHTEKEIIANLKSVTSQIIEQERQARNLLLKEKEIEVRDRVNRSFGILSHAYQISSEEALRMLSNVKLGIDMGIITDVDTGVLSELMVLIRPA... | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 39109
Sequence Length: 349
EC: 2.7.14.1
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Q48759 | MNVFEPRLSSWLENAGDDDDVVLSSRIRLARNLKDEQFPIYEQKEEIVDNIAEVFDDNFILIKMNQISLLQKALLVEKHLISPYMMNKSEYGAVLLNEEENVSIMLNEEDHLRIQCMTPGLRLFDALEAALQIDGYVEEKLSYAFDKEFGYLTSCVTNIGTGMRASVMVHLPGLVTTKRIKSVIEAIRSLGFVVRGIYGEGSMPASNIFQVSNQVTLGKTEAEIVEDLTQVMEQIIMQERVARTTLKQKFHIALEDRVFRSYGLLMNCRIISMKEAADAISDIRFGVELGFFEHISRQKMNELVLFSQPAFLRREAGRDM... | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 38855
Sequence Length: 340
EC: 2.7.14.1
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Q89XN9 | MEDLSFRHPVRARADGARRSAIVGIVASGNLEVLVERVLPDAECAIDIKTAAVGFGEVWRAVIGDFVERYSPGGLKFSINDGGARPDTVSLRLAQAVRSIAENGQ | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence... |
O32712 | MEQITLSFPASRALSGRALAGVVGSGDMEVLYTAAQSATLNVQITTSVDNSQARWQALFDRLNLINGLPAGQLIIHDFGATPGVARIRIEQVFEEAAHA | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence... |
O06925 | MEGMLNELNFKFKSENPVDVVLPKHHYGVVGSGDLEVLLKKHELEGAVEIRVVSPVRGFDHVWEKVLEKVISDAEVGNVAIEINDNNATPVVVALRLAQALSEAKSAEQSVN | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence... |
Q48PD1 | METLSFEFPAGQPPKGRALVGVVGSGDLEVLLEPGSPGKLSIQVVTSVNGASLRWKHLFERMFDGQTPPALSIDIHDFGATPGVVRLRLEQGFEEIGHD | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence... |
A6UY05 | METLTFEFPAGAPARGRALAGCVGSGDLEVLLEPAAGGALSIEVVTSVNGSGPRWQQLFARVFAAATAPAAAIRIHDFGATPGVVRLRLEQALEEAGHD | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence... |
Q87V56 | METLSFEFPAGQPPKGRALVGVVGSGDLEVLLEPGQPGKLSIQVVTSVNGASLRWKHLFERMFDGQTPPALSIDIHDFGATPGVVRLRLEQGFEEIGHD | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence... |
B4SNX3 | METLDYRFDGTTHAHFPTNAVLVGVLASGNLEILLEPAALDGAMTVRIITAAQGFGSVWQAVITDFARRHPLRDVRISINDAGATPAVVSLRLDQAVETLLGGGTP | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence... |
Q5HM62 | MKFLKNKSYHLLVTLIVLTIFVISGAIFLTFLGFGLYGLSRILIYLHLGDFSYNKGFYDNLIYYGSYIVLGYFTLFSIEHLMDYFKKNLPKNPYFQGINFHLISYIVTTIMFYFIVHIHYVHVNIHFWVIMIIIGFLFVCKEVFYPESKNLNNKK | Function: Involved in multidrug efflux.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18447
Sequence Length: 155
Subcellular Location: Cell membrane
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P17505 | MLSRVAKRAFSSTVANPYKVTVLGAGGGIGQPLSLLLKLNHKVTDLRLYDLKGAKGVATDLSHIPTNSVVKGFTPEEPDGLNNALKDTDMVLIPAGVPRKPGMTRDDLFAINASIVRDLAAATAESAPNAAILVISNPVNSTVPIVAQVLKNKGVYNPKKLFGVTTLDSIRAARFISEVENTDPTQERVNVIGGHSGITIIPLISQTNHKLMSDDKRHELIHRIQFGGDEVVKAKNGAGSATLSMAHAGAKFANAVLSGFKGERDVIEPSFVDSPLFKSEGIEFFASPVTLGPDGIEKIHPIGELSSEEEEMLQKCKETL... | Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 35650
Sequence Length: 334
Subcellular Location: Mitochondrion matrix
EC: 1.1.1.37
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Q8H1E2 | MAMAELSTPKTTSPFLNSSSRLRLSSKLHLSNHFRHLLLPPLHTTTPNSKISCSVSQNSQAPVAVQENGLVKTKKECYGVFCLTYDLKAEEETRSWKKLINIAVSGAAGMISNHLLFKLASGEVFGPDQPIALKLLGSERSIQALEGVAMELEDSLFPLLREVDIGTDPNEVFQDVEWAILIGAKPRGPGMERADLLDINGQIFAEQGKALNKAASPNVKVLVVGNPCNTNALICLKNAPNIPAKNFHALTRLDENRAKCQLALKAGVFYDKVSNMTIWGNHSTTQVPDFLNARINGLPVKEVITDHKWLEEGFTESVQK... | Function: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells (Probable).... |
Q9SN86 | MATATSASLFSTVSSSYSKASSIPHSRLQSVKFNSVPSFTGLKSTSLISGSDSSSLAKTLRGSVTKAQTSDKKPYGFKINASYKVAVLGAAGGIGQPLSLLIKMSPLVSTLHLYDIANVKGVAADLSHCNTPSQVRDFTGPSELADCLKDVNVVVIPAGVPRKPGMTRDDLFNINANIVKTLVEAVAENCPNAFIHIISNPVNSTVPIAAEVLKKKGVYDPKKLFGVTTLDVVRANTFVSQKKNLKLIDVDVPVIGGHAGITILPLLSKTKPSVNFTDEEIQELTVRIQNAGTEVVDAKAGAGSATLSMAYAAARFVESS... | Function: Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments (Probable). Plays a key role in the metabolism of dark chloroplasts and non-green plastids. Essential for embryo viability . Plays an essential role in heterotrophic ... |
P46489 | MAVVKLSPWANYSSSKSEIKSSSSSSSSKSSLSAYVINVSSSPRLSFYNPYPRRLHHQRLSSPASIRCSVTSSDQIQAPLPAKQKPECFGVFCLTYDLKAEEETKSWKKIINVAVSGAAGMISNHLLFKLASGEVFGPDQPISLKLLGSERSFAALEGVAMELEDSLYPLLRQVSIGIDPYEIFQDAEWALLIGAKPRGPGMERADLLDINGQIFAEQGKALNAVASPNVKVMVVGNPCNTNALICLKNAPNIPPKNFHALTRLDENRAKCQLALKAGVFYDKVSNVTIWGNHSTTQVPDFLNAKIHGIPVTEVIRDRKW... | Function: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells.
Catalytic ... |
P15719 | MGLSTVYSPAGPRLVPAPLGRCRSAQPRRPRRAPLATVRCSVDATKQAQDGVATAVATEAPASRKECFGVFCTTYDLKAEDKTKSWRKLVNVAVSGAAGMISNHLLFKLASGEVFGQDQPIALKLLGSERSFQALEGVAMELEDSLYPLLREVSIGIDPYVVFQDVDWALLIGAKPRGPGMERAALLDINGQIFADQGKALNAVASRNDEVLVVGNPCNTNALICLKNAPNIPAKNFHALTRLDENRAKCQLALKAGVFYDKVSNVTIWGNHSTTQVPDFLNAKIDGRPVKEVIKDTKWLEEEFTLTVQKRGGVLIQKWG... | Function: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells.
Catalytic ... |
O48902 | MALTQLNNTCSKTQLHSSSQLSFLSRTLPRHHHCTLAPLHRTQHARISCSVAPNQVQAPAVQTQDPKSKPDCYGVFCLTYDLKAEEETKSWKKLITIAVSGAAGMISNHLLFKLASGEVFGPNQPIALKLLGSERSLQALEGVAMELEDSLFPLLREVVISIDPYEVFQDAEWALLIGAKPRGPGMERAALLDINGQIFAEQGKALNAVASRNVKVIVVGNPCNTNALICLKNAPNIPAKNFHALTRLDENRAKCQLALKAGVFYDKVSNMTIWGNHSTTQVPDFLNARIDGLPVKEVIKDHKWLEEEFTEKVQKRGGAL... | Function: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells (By similar... |
P32419 | MVKVAILGASGGVGQPLSLLLKLSPYVSELALYDIRAAEGIGKDLSHINTNSSCVGYDKDSIENTLSNAQVVLIPAGVPRKPGLTRDDLFKMNAGIVKSLVTAVGKFAPNARILVISNPVNSLVPIAVETLKKMGKFKPGNVMGVTNLDLVRAETFLVDYLMLKNPKIGQEQDKTTMHRKVTVIGGHSGETIIPIITDKSLVFQLDKQYEHFIHRVQFGGDEIVKAKQGAGSATLSMAFAGAKFAEEVLRSFHNEKPETESLSAFVYLPGLKNGKKAQQLVGDNSIEYFSLPIVLRNGSVVSIDTSVLEKLSPREEQLVN... | Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 37186
Sequence Length: 343
Subcellular Location: Peroxisome
EC: 1.1.1.37
|
O82399 | MDPNQRIARISAHLNPPNLHNQIADGSGLNRVACRAKGGSPGFKVAILGAAGGIGQPLAMLMKMNPLVSVLHLYDVANAPGVTADISHMDTSAVVRGFLGQPQLEEALTGMDLVIIPAGVPRKPGMTRDDLFNINAGIVRTLSEAIAKCCPKAIVNIISNPVNSTVPIAAEVFKKAGTFDPKKLMGVTMLDVVRANTFVAEVMSLDPREVEVPVVGGHAGVTILPLLSQVKPPCSFTQKEIEYLTDRIQNGGTEVVEAKAGAGSATLSMAYAAVEFADACLRGLRGDANIVECAYVASHVTELPFFASKVRLGRCGIDEV... | Function: Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments (Probable). Peroxisomal NAD-dependent malate dehydrogenase involved in fatty acid beta-oxidation. Reoxidizes NADH from the beta-oxidation and provides NAD for the con... |
Q9ZP05 | MEFRGDANQRIARISAHLTPQMEAKNSVIGRENCRAKGGNPGFKVAILGAAGGIGQSLSLLMKMNPLVSLLHLYDVVNAPGVTADVSHMDTGAVVRGFLGAKQLEDALTGMDLVIIPAGIPRKPGMTRDDLFKINAGIVKTLCEGVAKCCPNAIVNLISNPVNSTVPIAAEVFKKAGTYDPKKLLGVTTLDVARANTFVAEVLGLDPREVDVPVVGGHAGVTILPLLSQVKPPSSFTPQEIEYLTNRIQNGGTEVVEAKAGAGSATLSMAYAAAKFADACLRGLRGDANVVECSFVASQVTELAFFATKVRLGRTGAEEV... | Function: Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments (Probable). Peroxisomal NAD-dependent malate dehydrogenase involved in fatty acid beta-oxidation. Reoxidizes NADH from the beta-oxidation and provides NAD for the con... |
A0L5T9 | MADPIRVAVTGAAGQIAYSLLVRLASGQLFGKDRKVELKLLEIPQAMGPLEGVMMELQDCAFPTLAKVEAFDNPEQAFDGINWCLMVGSRPRGPGMERSDLIKINGPIFVNQGKALNRAAQDVRAVVVGNPCNTNCMIAAHNSDVPHERFSAMMRLDQNRAKYLLASKAGAQVIDVTNVVIWGNHSNNQVPDFEFAKIGGKPVPEVIADAAWLENAFMPTVQNRGAAVIKARGASSAASAANAALDHVRSLITPTPAGDTFCAAVMANGAYGVDAGLIAGMPLTSTGHGDWSIVEGVPMSPFIKGKFDAVLDELRREREM... | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 34833
Sequence Length: 327
EC: 1.1.1.37
|
P16142 | MIISPEEERSLIIKILNALGVSEEHAKITADVIVDADLKGFTSHGIGRFPQYVEGIKLGTIKTSGNIEIEKETDSVALINGNHLLGQVVAYKGMKLAIEKAKNTGVGIVGIHDSNHFGIAGYYSDMAMKNDMIGITMTNTEPAVAPLGGKIPVLGTNPIAISIPSNEYYVAVDMSTAAVARGKLLEAARKNEKIPEGIAVDKNGNPTTDPNEALNGSILPFGGHKGYALCFMIEILAGPLVKAEFGSKVKGTVDPSQMCTKGDLLIAIDPSKFYDIEEFKRNVDEFVKEIKSTGKDVLIPGDRERMNIKKREKEGIELDK... | Function: Acts on oxaloacetate, sulfopyruvate but not on pyruvate. Has a higher selectivity for the coenzyme NADH than for NADPH.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 36762
Sequence Length: 339
Subcellular Location: Cytoplasm
EC: 1.1.1.310
|
Q60176 | MKVTIIGASGRVGSATALLLAKEPFMKDLVLIGREHSINKLEGLREDIYDALAGTRSDANIYVESDENLRIIDESDVVIITSGVPRKEGMSRMDLAKTNAKIVGKYAKKIAEICDTKIFVITNPVDVMTYKALVDSKFERNQVFGLGTHLDSLRFKVAIAKFFGVHIDEVRTRIIGEHGDSMVPLLSATSIGGIPIQKFERFKELPIDEIIEDVKTKGEQIIRLKGGSEFGPAAAILNVVRCIVNNEKRLLTLSAYVDGEFDGIRDVCIGVPVKIGRDGIEEVVSIELDKDEIIAFRKSAEIIKKYCEEVKNL | Function: Catalyzes the reversible oxidation of (S)-malate and (S)-sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruva... |
Q8TWG5 | MSKVAVIGATGRVGSTAAARLALLDCVNEVTLIARPKSVDKLRGLRRDILDSLAAAQKDAEITIGCERDDYVDADVIVMTAGIPRKPGQTRLDLTKDNAAIIKKYLEGVAEENPEAIVLVVTNPVDVLTYVALKVSGLPKNRVIGLGTHLDSMRFKVLIAKHFNVHMSEVHTRIIGEHGDTMVPVISSTSVGGIPVTRMPGWEDFDVEEAVREVKEAGQRIIETWGGSQFGPAQAITNLVRTILQDERRVLTVSAYLDGEIDGIRDVCIGVPARLGREGVLEIVPIELEEDEMRAFRRSVKVVKEATREAMEAISER | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate
Sequence Mass (Da): 34609
Sequence Length: 317
EC: 1.1.1.299
|
Q8PVJ7 | MVKISVIGAGNVGSTTVQRLAELEPGEIVMTDIVEGMPQGKALDLMQAGAINGYDTRITGTNDYADIANSDLVIITAGIARKPGMSREDLIKTNSKIIGDVAGNIAKYAPNSIVINVTNPLDIITYVAMKATGFDPEKVFGMSGVLDAGRFASFIAEELKCSKRDVEAMVIGGHGDLMVPLPQYTTVSGIPLPELLPEKTIDRLVERTVNGGAEIVELLKQGSAFYAPSAAIVRMAEAVIKDSRRVLPASAYLEGQYGQKGIYFGVPVKLGANGIEEILELKLEDSQCEILKKSSETIRKGISKLEI | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 32786
Sequence Length: 307
EC: 1.1.1.37
|
Q55383 | MNILEYAPIACQSWQVTVVGAGNVGRTLAQRLVQQNVANVVLLDIVPGLPQGIALDLMAAQSVEEYDSKIIGTNEYEATAGSDVVVITAGLPRRPGMSRDDLLGKNANIVAQGAREALRYSPNAILIVVTNPLDVMTYLAWKVTGLPSQRVMGMAGVLDSARLKAFIAMKLGACPSDINTLVLGGHGDLMLPLPRYCTVSGVPITELIPPQTIEELVERTRNGGAEIAALLQTGTAYYAPASSAAVMVESILRNQSRILPAATYLDGAYGLKDIFLGVPCRLGCRGVEDILEVQLTPEEKAALHLSAEAVRLNIDVALAM... | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 34346
Sequence Length: 324
EC: 1.1.1.37
|
P33163 | MSILPLVHAMANVRGDIEYLTEA | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 2544
Sequence Length: 23
EC: 1.1.1.37
|
P61977 | MKAPVRVAVTGAAGQIGYSLLFRIAAGEMLGKDQPVILQLLEIPQAMKALEGVVMELEDCAFPLLAGLEATDDPKVAFKDADYALLVGAAPRKAGMERRDLLQVNGKIFTEQGRALAEVAKKDVKVLVVGNPANTNALIAYKNAPGLNPRNFTAMTRLDHNRAKAQLAKKTGTGVDRIRRMTVWGNHSSTMFPDLFHAEVDGRPALELVDMEWYEKVFIPTVAQRGAAIIQARGASSAASAANAAIEHIRDWALGTPEGDWVSMAVPSQGEYGIPEGIVYSFPVTAKDGAYRVVEGLEINEFARKRMEITAQELLDEMEQ... | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 35426
Sequence Length: 327
EC: 1.1.1.37
|
A0A0S3QTC6 | MGKRAKITVVGAGHVGEHVAMFCAIKELGDVVLIDIVEDMPQGKALDMFEATPLEGWDSRIVGTNDYADTADSDIVVITAGSPRKPGMSRDDLLEINAKIIKAVTEQVAKYSPNAVIIVVTNPLDAMTQLAWNVSGFPKNRVLGQAGNLDSARFRAFIAMELGVSVKEISAMVLGGHGDDMVPLPRFTTVSGIPITELIPPDRIEALVQRTRVGGGEIVKLLKTGSAYYAPALATVEMVEAILKDQKRIQPCAALCEGEYGINGVYCGVPCLLGANGVEKIIELKLTDDELKALQASAGRVKGLIDKLTEWGYIK | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 33717
Sequence Length: 315
EC: 1.1.1.37
|
Q8J0L4 | MLDFMDYIQLAFAEGTQRNCDNSYSSLTATTQNLLDFTTPERVRIHLSSLSTPNFATSYTLGTVGLIEGSISYLYSNISFDNTPSKSALIPLRKLAPGYRQVQAPIAPPSSKGQKATLLHATLHLPPPTTLNALFLRRISPTMQLSLAVSSTRGPPLSKSAPQATLLTQLTHDTGKYSNEYLFSTDNSLFGWRGLWNFGPDPRFNNNAQRLSLLSAGAEAYYSPVSSLIGMSTGLRFCTLPAATSSTPNPNTPISTFPYTLTLTLTPLTGSLSTSYSVRASPNLSFSSRFGFNVYSWESEMVAGFELWRQSRKAAIVDND... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly s... |
C4QWJ4 | MLEYMEYLEQCFAKNSQWDYNNLYEHVLDSSASILQFKIPHGFKFSVSSSSSPYNYNSISFENRGKGRLNGSLAYFYTTQELSNYKTSKNIPLQDVIDSYRLVNIPKNDRSYTDNEESKRPWLLYGRMYLPSQSMEAMAIKRLTANTQLMLKGVNILNPTPTPFNNKLTSLSFYLQSNYYKWSREAIFLSSDALFGLRFLYNFGNSTNPQCTPSIDSNNISTLSLGTELWYGAMNMTPGLSTTLRYTSFSVTGNPLTFTLACNPILGSVSTTYSIKTNVFTTLCSKFDFNFYSYESDLTIGCDLWRFGNNEDVPDSNPTP... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
B0DK33 | MHPFASYVLRSYYKATGWNEDNLYANLTRSSNAILDFTVPRGLHLTVSKSPNALFKTTYSMTAMPSLHGSVGYIFTSCDLDVKSSGNVRFKNMIERFKVYDQPRRPEPKEEEWLAGEQVQKRDYLLYGRFYLPTGRLDALYSTRLSPTVQALVAAISDPPSNIPSELRDRNGDPSNIMLNLQHDVGKWCTEYTWSAEDGMWGVRVLHNFGRLGMSDAVEDGGGGKGDRTVKVKRVDEEDAVEGGLKGRVSMGAELYFSAKERSAGVSTGIRFTTLPDATPPSFQVPSSSSSSSNPVSPSTSQPPTTITALFNPMLGHMSG... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
Q7SBE0 | MREFMNYITNAFYGATGWNEDNKYNELNATSRELIDFPLPRGLRLTLSSLATPHFATSYQLGSVGVVDGSISYLHSSIPLTHIAAQSDKIPLPALLRCYRRLHDLRSPGQQHYILDADPLSGLPPPPQSARALLGAASDAAVAGGALDGGNTDQDLGIYTHSLLYGRLYLPKSLLEGMIIKRFTQALQVQVRAVSEQSLRNGGTILGLVQYDKGKYGLEGLYSTDGGLLGFRGLYNFGGDASSSTCDPWTPTPGENNNNNNNNNNNNNGNAQAGEKERIYGRFSVGGELYYGTLNKSGGMSLGARFATLPAHRGTPLTAT... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly s... |
Q0TWV0 | MLDFMDNVQHAFYEASHWNVDNSYGALNATARALLDFDSPRGLRLQISSLAAPNFATSYTLGSVGVVDGSVSYLYSSLPLRKDFKSSRIDLHHVIRGFKHLQELRKPDEKWSWEQWHAGRRVDRKDTLLYGRIFLPQSRLEALYLRRLAPTRQLRIAAVSDSNLNNGGTILTLLQTDSGKYSTEYMYSTDSALMGLRGLYNFGPDPRVAPTEPTRPEQVEPVHGRFSAGAELYYGILNKSGGMSTGLRFTTLPNHPGFPYTMTLTLNPLMGNLSSTYAVKAGPSLALCSRFDFNFYSYESELQLGCELWRRRGNTDTEWA... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
A5DCL4 | MYTYMEYLQKCFFHATRWNEDNIYSNITASSHALLEFLVPSGLKMDVSSRSSPNSASSFTLSNHHSLNGSLAYMYSSTQLKGTPGTRRIPLQDAIAGFKIVEPNEMRPSASGTIAPSSLLYGRMYFPGAALEAMVIRRFSPHTQLLIKCIHNPQLDKNGTLIAYFQKNTQRYSREVIYSTNDALVGFRGLYNIGSTPSWSPSPPNFDRSVVSVGAELWYAARTMSPGLSTGLRYSTRSTSTGKPLTMTLACNPILGHISSTYTVKTSVASTFCSRYDFNLFSYASNLSLGFELFNFDKNAAVERNPQLPTPTTNPSASKQ... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
O13498 | MREFMQYVRNAFYGATGWSEDNSYKDLNVTARELIDFPLPRGIRLSLSSLATPHFATSYQLCNVGVVDGSISYLHSSVPLAAVPAQSNKIPLGALMRSYRGLHQLGSRGGTPWSWETGPQIGTIPQVPAVADMGQIPNKDKSSLLYGRLYLPQSLLEAMVIKRFSPALQVQISAVSEQSLRNGGTMLSVVQYDRGKYGVEGLYSTDGGLLGLRGLYNFGGDASVAVMSSQNGTGSPESTEKERIYGRFSAGGEMYYGTLNKSGGMSLGARFATLPTHKGTPLTATLTINPLMGNINTTYAVLAKDFLAMATRMEFNAYSY... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
B8P366 | MHPFASYVLRSYYRGTGWNEDNLYANLTRSSNAILDFSVPRGLHFSISKSPNPLFKTTYSMNALPSLNGSIGYIFTSCELDVKGSGDVRFKDMVDRFRVYDQPRRPEGKEEEWLAGERVDTRDYLLYGRVYIPTGRLDALYSTRLSPTLQAMVAAISDPRSSLFAESPRGIAAPSSNIMFSLQHDTGKWCTEYTWSAEDGMWGVRCLHNFGKVGGPSEPVEDSEKSTAAPTKTRSGVKRIDEEDAMEGGLKGRISAGAEFYFSAKEKSAGVSTGIRFTTLPDATPPSFQLPSSSPTQPSLLAHGAPSQPPTTITALFNPM... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... |
B6K463 | MNSFTRALFDEYLRKTGWNRGNLYTNLTQSADEVLNLEIPSGINCDLSSIPSPNFASNWEIQMLPILNGSVSYLYSNVDLRLPQNVFGHFAQHQQKFQHLLPPYRHLKTELTDMGFERKPYLMFGKLHLPTAKLEAIFAKRISPPNNLIIRMCHTKRGILTSTSTLLHWQRDTGRSCTEILYSTDEAMIGFRKLWNSGRLQPSLFESANLTKFDPFWSVGAEVYYGALTKCVGASIGARLYSCANGVHNPYSVTCTLNPIVGHLVSTFATSHNDTRVLCSQFEFNLYSYESRLRLGMELFQRKRLLTNEDNHSDDIRQQG... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly s... |
O13814 | MMSFNDYIFYEYLKKTNWNIHNLYCNLTQTADNILNFEIPSGVSCQLSSLTSSNFASGCKISAMPILNGSMSYVYTNVNLENLNRNITYNLQHFYEGYKHVDVPFVHYVNEFQDKKLPLRPTLLYGRMHLPSQHLDAIFATRLSPWLLFFIQGVNEIEDGVGDNLCFNWQYDTGKRCLEFVYESSGAMLGVRGLWNLNYRELNTKINMENKAPSNMRWSLGFETYYGVLTKCAGASLGMRLHSGPSHPYAPFILTCTLNPIVGHITSTFSTAEPRTKAFSAQYDFNIYSYESQLKLGIELWRSKQEMSQSTNDPTANSMS... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly s... |
A7TES0 | MSFKFNEESFLDNSFNETLREKLTKMLNSRKSMDIKIDDHLSYANNRGSTSCSNNFDNSSSIKARDSKLDILKSDVKVCEVNFPTIPNLEILDLDVSGQPRALAKGICKISCRDALLQIQTEIEANSLLLYTNISPDFTTPLMIANDTFTIPITMTFSQIQLEAITNVFVKNSGVGISFNDVSLDFQFDCSIKLLQPHIAKRLRKSMQLVFKDVLPSALFNMSRSWFTHDGSSSQTTTDHSQEEGSRLIRLHRLTVEDLDLQDLSPVNMLKLSTLTSSRQTLSLHSTMPKYFSTIPGCLDRQNFRNFTSRMPCLSNYGGG... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
Q6C7W0 | MSFKFDWESLRDESFYERAKTILADALNSDSKPPIIVDDITVKDLDLGDESPFLEILEIGDMADDRFRGIFKLNYTGNASLTLTTKVQANPLNVYRQSFDQSSFVAPQFLAAGSSLAIPLNLTLSDIRLSGIIILVFSRAKGLTLVFRNDPLESIKVSSTFDAIPPLAKFLQVQIENQIRGLFRELLPGIIHRLSQKWVTRDETKSNSNTVMSPHVTQPPSPKLKPVSIMDINPDLPALSPTNMLKISALCASQRTLSLFTPSISDAVYRSNLEQFDVVDEESQFQSEDPYDIVRIQSRNYYRHNHQAPKRRTIKYKRKS... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
A6ZTX2 | MSFRFNEAVFGDNSFNERIREKLSTALNSPSKKKLDILKSGIKVQKVDFPTIPQLEILDLDIITQPKSLAKGICKISCKDAMLRIQTVIESNLLLINEQDTPSFTMPQLINNGSFTIPITMTFSSIELEAITNIFVKNPGIGISFNDVDLDFKFDCSVKILQSTIERRLKESMHVVFKDVLPSLIFNTSQNWFTNRGESTSTIPGKREHHHQQTTMSRNVILDGSDFQELSPINMLRLSSIVSSRSTLSLHSTVMNSLSAIPGCLERQNLYRFISRMPSLNNYYSSQSFPQPKSSTVSSKQLVKPFYCSHNLLPKTVLDS... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
C5E4T8 | MSFRFNSQAFEDNSFNEKIREKLTQALNSSSSDSRSPKVTKTTMGEGSTSKKDSGSGGKSRKFDILKSGITVSKVNFPTTPQLEILDLDISAQPRSLVKGICKISCKDAMLQIQTEVEANLLLVYSECSPSFATPNMICNDSFTIPITMVFSEIRLEAITNIFVKHSGIGISFNDVNLDFKFDCSMKILQSTIERRLKNSMHHLFKEVLPSVIFSMSQSLFLSEAARNQEMHNESRGDSRPSPRVVLEESDLQELSPANMLRLSTLISSRQTLSLHGTVLNVPSTIPGCLERQNLHRFNSRIPSLSNYYASYKEEEKSRQ... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
Q08179 | MLNFASRASCVTRRQASLYFVKNQGPRLIASTIPSCHWPLRAQGVQPNYPLSLRFYSTDKSKSVTKPVAPTSTDAPAKPKETLMVKVKHALKHYANGTKLLGYEIKVSTKLLIKFAQGYELSRRERNQLRRTMGDVFRLIPFSAFLIIPFAELFLPFALKLFPNLLPSTYESGKDKQAKRNKLIEIRKKTSEFLHETLEESNLITYNTIENAEKKQKFLNFFRKLYSAKEGKIMTFQHDEISAIAQMFKNDSVLDNLSRPQLAAMSKFMSLRPFGNDNMLRYQIRSKLKDIMNDDKTIDYEGVESLSQEELYQACVSRGM... | Function: Involved in mitochondrial potassium homeostasis through the mitochondrial K(+)/H(+) exchange regulation . With MBA1, plays a role in ribosomal translation and protein insertion into the inner membrane .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65005
Sequence Length: 573
Domain: The ... |
O15151 | MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLATATTDAAQTLALAQDHSMDIPSQDQLKQSAEESSTSRKRTTEDDIPTLPTSEHKCIHSREDEDLIENLAQDETSRLDLGFEEWDVAGLPWWFLGNLRSNYTPRSNGSTDLQTNQDVGTAIVSDTTDDLWFLNESVSEQLGVGIKVEAADTEQTSEEVGKVSDKKVIEVGKNDDLEDSKSLSDDTDVEVTSEDEWQCTECKKFNSPSKRYC... | Function: Along with MDM2, contributes to TP53 regulation . Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apo... |
O35618 | MTSHSTSAQCSASDSACRISSEQISQVRPKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLLGCQSFSVKDPSPLYDMLRKNLVTSASINTDAAQTLALAQDHTMDFPSQDRLKHGATEYSNPRKRTEEEDTHTLPTSRHKCRDSRADEDLIEHLSQDETSRLDLDFEEWDVAGLPWWFLGNLRNNCIPKSNGSTDLQTNQDIGTAIVSDTTDDLWFLNETVSEQLGVGIKVEAANSEQTSEVGKTSNKKTVEVGKDDDLEDSRSLSDDTDVELTSEDEWQCTECKKFNSPSKRYCF... | Function: Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. The short isoform is a more pote... |
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