ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8VYY4 | MSVITTPIETLHLKSTLRLLPRAVYRSQRIQVFPPNIFSNTSLSSPLRIDPISQVGGSRNLWRRYASDNFSEMGLDPGADPFKVIEKPSIVDRMKKANSILPHVVLASTILALIYPPSFTWFTSRYFVPALGFLMFAVGINSNEKDFLEAFKRPKAILLGYVGQYLVKPVLGFIFGLAAVSLFQLPTPIGAGIMLVSCVSGAQLSNYATFLTDPALAPLSIVMTSLSTATAVLVTPMLSLLLIGKKLPVDVKGMISSILQVVIAPIAAGLLLNKLFPKVSNAIRPFLPILSVLDTACCVGAPLALNINSVMSPFGATILL... | Function: May function as sodium-coupled metabolite transporter across the chloroplast envelope.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44207
Sequence Length: 409
Subcellular Location: Membrane
|
P30844 | MHFLRRPISLRQRLILTIGAILLVFELISVFWLWHESTEQIQLFEQALRDNRNNDRHIMREIREAVASLIVPGVFMVSLTLFICYQAVRRITRPLAELQKELEARTADNLTPIAIHSATLEIEAVVSALNDLVSRLTSTLDNERLFTADVAHELRTPLAGVRLHLELLAKTHHIDVAPLVARLDQMMESVSQLLQLARAGQSFSSGNYQHVKLLEDVILPSYDELSTMLDQRQQTLLLPESAADITVQGDATLLRMLLRNLVENAHRYSPQGSNIMIKLQEDDGAVMAVEDEGPGIDESKCGELSKAFVRMDSRYGGIGL... | Function: Member of the two-component regulatory system BasS/BasR Autophosphorylates and activates BasR by phosphorylation.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 41029
Sequence Leng... |
P36557 | MRFQRRAMTLRQRLMLTIGLILLVFQLISTFWLWHESTEQIQLFEQALRDNRNNDRHIMHEIREAVASLIVPGVFMVSLTLLICYQAVRRITRPLAELQKELEARTADNLAPIAIHSSTLEIESVVSAINQLVTRLTTTLDNERLFTADVAHELRTPLSGVRLHLELLSKTHNVDVAPLIARLDQMMDSVSQLLQLARVGQSFSSGNYQEVKLLEDVILPSYDELNTMLETRQQTLLLPESAADVVVRGDATLLRMLLRNLVENAHRYSPEGTHITIHISADPDAIMAVEDEGPGIDESKCGKLSEAFVRMDSRYGGIGL... | Function: Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well.
PTM: Autophosphorylated.
Location Topolog... |
B0R6I4 | MSDIDRGLFERVLPARIRGSYAAKFNVLLLVVVIIVAAAGGYIHLQTQSTVGENTERRVSGIAEQQAATLHDWLTQKESTTTFLASNIGGDAVRTSDVKPQLERQLATLQQDVRAIHVVSTSQDTVVASTDDARSGTTLQAGDAPWLSTIEDGTTDVSVSDPYEVDDSPVVAMTAPTDKPGWVLVMTMSLAQHSQSFNSPIATGDVKVVNGDGVITLDNRNRALLEQYTDTAGNVPAAVATARSGQTVYNTEPERTGMDDGRYATAYTPVAGTDWVLTYHVPRGQAYALQSEVTQNLAGLVVVALVGLLLVGLTVGRRTS... | Function: Mediates chemotaxis towards five attractant amino acids (leucine, isoleucine, valine, methionine and cysteine). Probably transduces the signal from the substrate-binding protein BasB to the histidine kinase CheA.
PTM: Methylated by CheR.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84831... |
Q94FV7 | MATEEMKKLATVMAIGTANPPNCYYQADFPDFYFRVTNSDHLINLKQKFKRLCENSRIEKRYLHVTEEILKENPNIAAYEATSLNVRHKMQVKGVAELGKEAALKAIKEWGQPKSKITHLIVCCLAGVDMPGADYQLTKLLDLDPSVKRFMFYHLGCYAGGTVLRLAKDIAENNKGARVLIVCSEMTTTCFRGPSETHLDSMIGQAILGDGAAAVIVGADPDLTVERPIFELVSTAQTIVPESHGAIEGHLLESGLSFHLYKTVPTLISNNIKTCLSDAFTPLNISDWNSLFWIAHPGGPAILDQVTAKVGLEKEKLKVT... | Function: Polyketide synthase producing 4-hydroxybenzalacetone. Can use p-coumaryl-CoA as substrate but does not accept hexanoyl-CoA, isobutyryl-CoA, isovaleryl-CoA, and acetyl-CoA as a substrates. Catalyzes the initial key reaction step in the biosynthesis of phenylbutanoids.
Catalytic Activity: 4-coumaroyl-CoA + H(+)... |
Q9ZU50 | MGLGGDQSFVPVMDSGQVRLKELGYKQELKRDLSVFSNFAISFSIISVLTGITTTYNTGLRFGGTVTLVYGWFLAGSFTMCVGLSMAEICSSYPTSGGLYYWSAMLAGPRWAPLASWMTGWFNIVGQWAVTASVDFSLAQLIQVIVLLSTGGRNGGGYKGSDFVVIGIHGGILFIHALLNSLPISVLSFIGQLAALWNLLGVLVLMILIPLVSTERATTKFVFTNFNTDNGLGITSYAYIFVLGLLMSQYTITGYDASAHMTEETVDADKNGPRGIISAIGISILFGWGYILGISYAVTDIPSLLSETNNSGGYAIAEIF... | Function: May play a role in primary carbon metabolism and plant growth, by mediating the transport of GABA from the cytosol to mitochondria. When expressed in a heterologous system (yeast), imports Arg and Ala across the plasma membrane and exports Lys and Glu, but does not transport proline.
Location Topology: Multi-... |
P82251 | MGDTGLRKRREDEKSIQSQEPKTTSLQKELGLISGISIIVGTIIGSGIFVSPKSVLSNTEAVGPCLIIWAACGVLATLGALCFAELGTMITKSGGEYPYLMEAYGPIPAYLFSWASLIVIKPTSFAIICLSFSEYVCAPFYVGCKPPQIVVKCLAAAAILFISTVNSLSVRLGSYVQNIFTAAKLVIVAIIIISGLVLLAQGNTKNFDNSFEGAQLSVGAISLAFYNGLWAYDGWNQLNYITEELRNPYRNLPLAIIIGIPLVTACYILMNVSYFTVMTATELLQSQAVAVTFGDRVLYPASWIVPLFVAFSTIGAANGT... | Function: Associates with SLC3A1 to form a functional transporter complex that mediates the electrogenic exchange between cationic amino acids and neutral amino acids, with a stoichiometry of 1:1 . Has system b(0,+)-like activity with high affinity for extracellular cationic amino acids and L-cystine and lower affinity... |
B9EXZ6 | MTWNKAPAADAEAGGGGDTGHARLRELGYKQELKRDLSVLSNFAFSFSIISVLTGITTLYNTGLSFGGPATMTFGWFVAGAFTMTVGLSMAEICSSFPTSGGLYYWSARLSGKRWAPFASWITGWFNIVGQWAVTTSVDFSLAQLIQVIILLSTGGNNGGGYMASKYVVIAFHAAILLSHAAINSLPITWLSFFGQFAAAWNMLGVFVLMIAVPTVATERASAKFVFTHFNTENNAGIHSNFYIFVLGLLMSQYTLTGYDASAHMTEETKNADRNGPIGIISAIGISIIVGWGYILGITFAVKDIPYLLNPENDAGGYAI... | Function: May be involved in the transport of amino acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55810
Sequence Length: 520
Subcellular Location: Membrane
|
P82252 | MEETSPRRRREDEKSVHSTEPKTTSLQKEVGLLSGICIIVGTIIGSGIFISPKSVLANTESVGPCLIIWAACGVLATLGALCFAELGTMITKSGGEYPYLMEAFGPIPAYLFSWTSLIVMKPSSFAIICLSFSEYVCAAFYLGCRPPAVVVKLLAAAAILLITTVNALSVRLGSYVQNVFTAAKLVIVAIIIISGLVLLAQGNVKNFQNSFEGSQTSVGSISLAFYNGLWAYDGWNQLNYITEELRNPYRNLPMAIVIGIPLVTVCYILMNIAYFTVMTPTELLQSQAVAVTFGDRVLYPASWVVPLFVAFSTIGAANGT... | Function: Associates with SLC3A1 to form a functional transporter complex that mediates the electrogenic exchange between cationic amino acids and neutral amino acids, with a stoichiometry of 1:1 (By similarity). Has system b(0,+)-like activity with high affinity for extracellular cationic amino acids and L-cystine an... |
Q9SID1 | MKIQCDVCEKAPATLICCADEAALCAKCDVEVHAANKLASKHQRLFLDSLSTKFPPCDICLEKAAFIFCVEDRALLCRDCDEATHAPNTRSANHQRFLATGIRVALSSTSCNQEVEKNHFDPSNQQSLSKPPTQQPAAPSPLWATDEFFSYSDLDCSNKEKEQLDLGELDWLAEMGLFGDQPDQEALPVAEVPELSFSHLAHAHSYNRPMKSNVPNKKQRLEYRYDDEEEHFLVPDLG | Function: Acts as negative regulator of seedling photomorphogenesis . BBX25/STH and BBX24/STO function as transcriptional corepressors of HY5 activity, leading to the down-regulation of BBX22 expression. BBX25/STH acts additively with BBX24/STO during de-etiolation and the hypocotyl shade avoidance response .
PTM: COP1... |
Q8L649 | MNGDNRPVEDAHYTETGFPYAATGSYMDFYGGAAQGPLNYDHAATMHPQDNLYWTMNTNAYKFGFSGSDNASFYGSYDMNDHLSRMSIGRTNWDYHPMVNVADDPENTVARSVQIGDTDEHSEAEECIANEHDPDSPQVSWQDDIDPDTMTYEELVELGEAVGTESRGLSQELIETLPTKKYKFGSIFSRKRAGERCVICQLKYKIGERQMNLPCKHVYHSECISKWLSINKVCPVCNSEVFGEPSIH | Function: E3 ubiquitin-protein ligase that limits organ size, and possibly seed size, in a dose-dependent manner. Negatively regulates the duration of cell proliferation in leaves and petals independently of the major phytohormones (e.g. auxin, cytokinin, gibberellin, brassinosteroids, ethylene, abscisic acid, jasmonic... |
Q65XS5 | MKPPRRWMYGRGGGKGKPAGLLLLGVFLCLSVVLLLLLHGSSPSLEGEGRKPEAVEAAGGGGEEEEVAVARAEVEEAPLPPGNARLAFLFIARNRLPLDLVWDAFFRGDKEGRFSIFVHSRPGFVLTRATTRSGFFYNRQVNNSVQVDWGEASMIEAERVLLAHALKDPLNERFVFVSDSCVPLYNFNYTYDYIMSSSTSFVDSFADTKAGRYNPRMDPIIPVENWRKGSQWAVLTRKHAEVVVEDEEVLPEFQKHCRRRPLPEFWRDWDRPIPAEAWKAHNCIPDEHYVQTLLAQHGLEEELTRRSVTHSAWDLSSSKD... | Function: Glycosyltransferase required for the regulation of cellulose biosynthesis in the cell wall . Required for the biosynthesis of hexoses (glucose, mannose and galactose) in both cellulosic and non-cellulosic (pectins and hemicelluloses) components of cell walls . Required for the formation of arabinogalactan pro... |
Q9H165 | MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLR... | Function: Transcription factor . Associated with the BAF SWI/SNF chromatin remodeling complex . Binds to the 5'-TGACCA-3' sequence motif in regulatory regions of target genes, including a distal promoter of the HBG1 hemoglobin subunit gamma-1 gene . Involved in regulation of the developmental switch from gamma- to beta... |
Q9QYE3 | MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKGVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLR... | Function: Transcription factor (By similarity). Associated with the BAF SWI/SNF chromatin remodeling complex . Binds to the 5'-TGACCA-3' sequence motif in regulatory regions of target genes (By similarity). May play a role in hematopoiesis . Essential factor in lymphopoiesis, required for B-cell formation in fetal live... |
Q99PV8 | MSRRKQGNPQHLSQRELITPEADHVEATILEEDEGLEIEEPSSLGLMVGGPDPDLLTCGQCQMNFPLGDILVFIEHKKKQCGGLGPCYDKVLDKSSPPPSSRSELRRVSEPVEIGIQVTPDEDDHLLSPTKGICPKQENIAGPCRPAQLPSMAPIAASSSHPPTSVITSPLRALGVLPPCFPLPCCGARPISGDGTQGEGQMEAPFGCQCELSGKDEPSSYICTTCKQPFNSAWFLLQHAQNTHGFRIYLEPGPASTSLTPRLTIPPPLGPETVAQSPLMNFLGDSNPFNLLRMTGPILRDHPGFGEGRLPGTPPLFSPP... | Function: Key regulator of both differentiation and survival of T-lymphocytes during thymocyte development in mammals . Essential in controlling the responsiveness of hematopoietic stem cells to chemotactic signals by modulating the expression of receptors CCR7 and CCR9, which direct the movement of progenitor cells fr... |
P27140 | MSTAPLSGFFLTSLSPSQSSLQKLSLRTSSTVACLPPASSSSSSSSSSSSRSVPTLIRNEPVFAAPAPIIAPYWSEEMGTEAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGA... | Function: Reversible hydration of carbon dioxide. Required for photosynthesis in cotyledons. Binds salicylic acid. Together with BCA4, involved in the CO(2) signaling pathway which controls gas-exchange between plants and the atmosphere by modulating stomatal development and movements. Promotes water use efficiency.
PT... |
Q22460 | MNKILRGVIQFRNTIRKDLVKQFEEIKNNPSPTAVMFTCMDSRMLPTRFTQSQVGDMFVVRNAGNMIPDAPNYGAFSEVSVNTEPAALELAVKRGGIRHIVVCGHSDCKAINTLYGLHQCPKNFDVTSPMDHWVRRNGFASVKRLNERLHRGPSSMKFESEVAPSQSFDAIIDPMDTLAMEDKLSQINVLQQLINICSHEFLKEYLESGRLHIHGMWFDIYKGEDYLFSKDKKRFVVIDEKTVTDLLAELNARYPVPEDQDGPVAFAKSN | Cofactor: Binds 1 zinc ion per subunit.
Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 30686
Sequence Length: 270
EC: 4.2.1.1
|
O14370 | MSLMFLRRAGNIKGRNIRFALQRGSVGYSQQSSEACKNFLNTTQLRTMVQTAALHGPKPMDSSHIKVTNVKELKPLPEWKSLKFGENFTDHMLIMKWNREKGWSTPEIVPFGKLCFHPASSVFHYGFECFEGMKAFRDEKGVPRLFRPIKNAERMLSTGTRISLPSFDPAELAEIIRKFVAHENRWVPDQRGYSLYIRPTFIGTDEALGVHHCDNAMLYVIASPVGPYYSSGFKAVKLCCSEESVRAWPGGTGHYKLGGNYAPSVLPQKEAAKKGYAQILWLYGDEDYITEVGTMNCFTVWINKNGEKEIITAPLDGMIL... | Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 47855
Sequence Length: 427
Subcellular Location: Mitochondrion
EC: 2.6.1.42
|
Q9F714 | MSLVLAVYGKGGIGKSTTSANISAALALKGAKVLQIGCDPKHDSTFPITGKLQKTVIEALEEVDFHHEELSPEDIVETGFAGIDGLEAGGPPAGSGCGGYVVGESVTLLQEMGVYDKYDVILFDVLGDVVCGGFSAPLNYADYAVIIATNDFDSIFAANRLCMAIQQKSVRYKVQLAGIVANRVDYTKGGGTNMLDQFAEQVGTRLLAKVPYHELIRKSRFAGKTLFAMDPNEPELAECLAPYNEIADQILSEKPIASVPKPIGDREIFDIVGGWQ | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique... |
Q7ZV60 | MTLSDFIGALKDNPYFGAGFGLVGVGTALAVARKGAQVGMIFFRRHYMITLEVPSKDKSYHWLLSWITKHAKHTQHLSVETSYMQHESGKVHTQFDFHPSPGNHIIWYGRKWIRVERVREKQMMDLHTGTPWESVTFTALGRDRQTFFNILQEARELALKQEEGRTVMYTAMGAEWRPFGFPRRRRPLSSVVLESGVAERIVDDVKEFIGNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELGYSICLMSLSDRSLSDDRLNHLLSVAPQQSIILLEDVDAAFVSRELLPTENPLAYQGMGRLTFSGLLNALDGV... | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47492
Sequence Length: 420
Subcellular Location: Mitochondrion inner membrane
|
Q48230 | MNKNKNIGIILAGGVGSRMGLGYPKQFSKIAGKTALEHTLAIFQEHKEIDEIIIVSERTSYRRIEDIVSKLDFSKVNRIIFGGKERSDSTLSAITALQDEPENTKLIIHDAVRPLLATEIISECIAKLDKYNAVDVAIPAVDTIVHVNNDTQEIIKIPKRAEYYQGQTPQAFKLGTLKKAYDIYTQGGIEGTCDCSIVLKTLPEERVGIVSGSETNIKLTRPVDLFIADKLFQSRSHFSLRNITSIDRLYDMKDQVLVVIGGSYGIGAHIIDIAKKFGIKTYSLSRSNGVDVGDVKSIEKAFAEIYAKEHKIDHIVNTAA... | Function: Catalyzes the NADPH-dependent reduction of D-ribulose 5-phosphate to D-ribitol 5-phosphate and the further reaction of D-ribitol 5-phosphate with CTP to form CDP-ribitol.
Catalytic Activity: CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol + diphosphate
Sequence Mass (Da): 52467
Sequence Length: 474
Pathway... |
Q9Y276 | MPLSDFILALKDNPYFGAGFGLVGVGTALALARKGVQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRHSTRTQHLSVETSYLQHESGRISTKFEFVPSPGNHFIWYRGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAVGSEWRPFGYPRRRRPLNSVVLQQGLADRIVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVLLEDVDAAFLSRDLAVENPVKYQGLGRLTFSGLLNALDGVA... | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47534
Sequence L... |
Q9P6Q3 | MDNIGAADAATSSGISGLLSGNSFLGAGIGLMGFGAGLAILRRGLISGASLVKRRMLVSVEIPSKEKSYNAFLHWMSTVPKRYSNQLAVESNRQLKMPQNAREKPDKQVANRIFSLVPGPGKHYIKYKKCWIQVERERSNRLQDLTTGTPWETITLTTLSRDRGIFSELLLEAQKFMQSAQKNKTTIYTAWATEWKPFGHPRSKRMLSSVVLESNVKKMITDDVHDFLRNSQWYDTRGIPYRRGYLLYGPPGSGKTSFLYALAGELDYDICVLNLAEKGLTDDRLNHLLSNVPPKAVVLLEDVDSAFQGRERSGEVGFHA... | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 49856
Sequence Length: 449
Subcellular Location: Mitochondrion inner membrane
|
P32839 | MSDKPIDIQYDKQATPNLSGVITPPTNETGNDSVREKLSKLVGDAMSNNPYFAAGGGLMILGTGLAVARSGIIKASRVLYRQMIVDLEIQSKDKSYAWFLTWMAKHPQRVSRHLSVRTNYIQHDNGSVSTKFSLVPGPGNHWIRYKGAFILIKRERSAKMIDIANGSPFETVTLTTLYRDKHLFDDILNEAKDIALKTTEGKTVIYTSFGPEWRKFGQPKAKRMLPSVILDSGIKEGILDDVYDFMKNGKWYSDRGIPYRRGYLLYGPPGSGKTSFIQALAGELDYNICILNLSENNLTDDRLNHLMNNMPERSILLLED... | Function: Essential for the expression of the Rieske iron-sulfur protein.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 51107
Sequence Length: 456
Subcellular Location: Mitochondrion inner membrane
|
P19449 | MSEVQSPVPAESRLDRFSNKILSLRGANYIVGALGLCALIAATTVTLSINEQLIVALVCVLVFFIVGRGKSRRTQIFLEVLSALVSLRYLTWRLTETLDFDTWIQGGLGVTLLMAELYALYMLFLSYFQTIQPLHRAPLPLPDNVDDWPTVDIFIPTYDEQLSIVRLTVLGALGIDWPPDKVNVYILDDGVRPEFEQFAKDCGALYIGRVDSSHAKAGNLNHAIKRTSGDYILILDCDHIPTRAFLQIAMGWMVADRKIALMQTPHHFYSPDPFQRNLAVGYRTPPEGNLFYGVIQDGNDFWDATFFCGSCAILRREAIE... | Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose in a processive way. The thick cellulosic mats generated by this enzyme probably provide a specialized protective environment to the bacterium. Binds c-di-GMP with a dissociation constant of 30 uM.
Catalytic Ac... |
P37653 | MSILTRWLLIPPVNARLIGRYRDYRRHGASAFSATLGCFWMILAWIFIPLEHPRWQRIRAEHKNLYPHINASRPRPLDPVRYLIQTCWLLIGASRKETPKPRRRAFSGLQNIRGRYHQWMNELPERVSHKTQHLDEKKELGHLSAGARRLILGIIVTFSLILALICVTQPFNPLAQFIFLMLLWGVALIVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKDMSLWPSVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFR... | Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection at the onset of the stationary phase, when the cells exhibit multicellular behavior (rdar morphotype). Coexpression of cel... |
P58931 | MTDTTSSTPFVEGRAEQRLNGAIARFNRWPSAPRTVLVVASCVLGAMLLLGIISAPLDLYSQCLFAAVCFLAVLVLRKIPGRLAILALVVLSLVASLRYMFWRLTSTLGFETWVDMFFGYGLVAAEFYALIVLIFGYVQTAWPLRRTPVWLKTEPEEWPTVDVFIPTYNEALSIVKLTIFAAQAMDWPKDKLRVHVLDDGRRDDFREFCRKVGVNYIRRDNNFHAKAGNLNEALKVTDGEYIALFDADHVPTRSFLQVSLGWFLKDPKLAMLQTPHFFFSPDPFEKNLDTFRAVPNEGELFYGLVQDGNDLWNATFFCGS... | Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component responsible for the structural integrity and rigidity of self-supporting mats characteristic of the 'wrinkly spreader' phenotype.
Catalytic Activity: [(1->4)-bet... |
Q93IN2 | MSALSRWLLIPPVSARLSERYQGYRRHGASPFSAALGCLWTILAWIVFPLEHPRWQRIRDGHKALYPHINAARPRPLDPARYLIQTLWLVMISSTKERHEPRWRSFARLKDVRGRYHQWMDTLPERVRQKTTHLEKEKELGHLSNGARRFILGVIVTFSLILALICITQPFNPLSQFIFLLLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKEMSQWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGRESFR... | Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection at the onset of the stationary phase, when the cells exhibit multicellular behavior (rdar morphotype). Coexpression of cel... |
P58932 | MPLVVPHAAMPEGRLMTAASRRSASPLPTLATWALWLLGALLLVFVVAVPMDVTQQLVFSGVLFAVALAVRNRGGRVVILMMMGMSLAVSCRYIWWRMTQTMGVGSAVDFILGLGLLGAELYAFVILVLGYFQVLWPLNRKPVPLPADQRLWPSVDVFIPTYNEPLSVVRTTVLAASVIDWPAGKITIHLLDDGRRDEFRAFCAEVGINYVTRTNNAHAKAGNINAALKKCSGDYVAIFDCDHIPTRSFLQVAMGWFLHDTKLALVQMPHYFFSPDPFERNLDTHGKVPNEGELFYGLLQDGNDQWNATFFCGSCAVIKR... | Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection (By similarity).
Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H... |
P37716 | MKMVSLIALLVFATGAQAAPVASKAPAPQPAGSDLPPLPAAASQAATPAAASADQPATTAPAADAASASAADAVVDNAENAIAASDVATVHTYSLKELGAQSALKMQGAATLQGLQFGIPADQLVTSARLIVSGAMSPSLQPDTSAVTITLNEQFIGTLRPDPTHPTFGPLSFDINPIFFITGNRLNFSFASSSKGCTDPSNGLLWASVSEHSELQITTIPLPPRRQLSRLPQPFFDKNVKQKIVIPFVLAQTFDPEVLKATGILASWFGQQTDFRGVTFPVFSTIPQTGNAVVVGVADELPSALGRQAVNGPTLMEVAN... | Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85382
Sequence Length: 802
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Cell inner membrane
|
Q8N1M1 | MTVTYSSKVANATFFGFHRLLLKWRGSIYKLLYREFIVFAVLYTAISLVYRLLLTGVQKRYFEKLSIYCDRYAEQIPVTFVLGFYVTLVVNRWWNQFVNLPWPDRLMFLISSSVHGSDEHGRLLRRTLMRYVNLTSLLIFRSVSTAVYKRFPTMDHVVEAGFMTTDERKLFNHLKSPHLKYWVPFIWFGNLATKARNEGRIRDSVDLQSLMTEMNRYRSWCSLLFGYDWVGIPLVYTQVVTLAVYTFFFACLIGRQFLDPTKGYAGHDLDLYIPIFTLLQFFFYAGWLKVAEQLINPFGEDDDDFETNWCIDRNLQVSLL... | Function: Forms calcium-sensitive chloride channels. Permeable to bicarbonate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76107
Sequence Length: 668
Subcellular Location: Cell membrane
|
Q8NFU0 | MTVSYTLKVAEARFGGFSGLLLRWRGSIYKLLYKEFLLFGALYAVLSITYRLLLTQEQRYVYAQVARYCNRSADLIPLSFVLGFYVTLVVNRWWSQYTSIPLPDQLMCVISASVHGVDQRGRLLRRTLIRYANLASVLVLRSVSTRVLKRFPTMEHVVDAGFMSQEERKKFESLKSDFNKYWVPCVWFTNLAAQARRDGRIRDDIALCLLLEELNKYRAKCSMLFHYDWISIPLVYTQVVTIAVYSFFALSLVGRQFVEPEAGAAKPQKLLKPGQEPAPALGDPDMYVPLTTLLQFFFYAGWLKVAEQIINPFGEDDDDF... | Function: Forms calcium-sensitive chloride channels. Permeable to bicarbonate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53497
Sequence Length: 473
Subcellular Location: Cell membrane
|
P34319 | MTNNNDPKCVVIEEPDDVPVKPPKIFDFTDWPFEIPDIFKRKELSYNYNYDLATSKSLMIVRMIFKWRGSLWQAVYKELIVWICAYSLVSVIYRFALTRSQKDIFERFGEYCDARMGYLPLNFVLGFFCNIIIRRWLKLYTSLGNIDNIALFVSAYVRGTDDRARQIRRNIIRYCVISQCLVFRDIHVGVRRRFPTLEAVAQAGIMLPHELEKFNSIKSRYQKYWVSFNWALELLNVAKTEKSIDGDNARNAIAQEISKFRSALTTVSMYDWVPIPLMYPQLVNMAVHTYFFLCIFTRQFFISADAHNKTEVDLYIPFMT... | Function: Forms chloride channels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52830
Sequence Length: 453
Subcellular Location: Cell membrane
|
Q9M2J9 | MNPRREPRGGRSSLFDGIEEGGIRAASSYSHEINEHENERALEGLQDRVILLKRLSGDINEEVDTHNRMLDRMGNDMDSSRGFLSGTMDRFKTVFETKSSRRMLTLVASFVGLFLVIYYLTR | Function: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE associated with ER-derived vesicles (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 13973
Sequence Length: 122
Subcellular Location: Golgi apparatus membrane
|
Q94CG2 | MNFRRENRASRTSLFDGLDGLEEGRLRASSSYAHDERDNDEALENLQDRVSFLKRVTGDIHEEVENHNRLLDKVGNKMDSARGIMSGTINRFKLVFEKKSNRKSCKLIAYFVLLFLIMYYLIRLLNYIKG | Function: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE associated with ER-derived vesicles (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 15207
Sequence Length: 130
Subcellular Location: Golgi apparatus membrane
|
Q3MHP8 | MADWARAQSPGAVEEILDRENKRMADSLASKVTRLKSLALDIDRDAEDQNRYLDGMDSDFTSMTGLLTGSVKRFSTMARSGRDNRKLLCGVAVGLIVAFFILSYLLSRART | Function: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 12320
Sequence Length: 111
Subcellular Location: Golgi apparatus... |
O35153 | MADWTRAQSSGAVEDILDRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFSTMARSGRDNRKLLCGMAVVLIVAFFILSYLLSRTRT | Function: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 12428
Sequence Length: 111
Subcellular Location: Golgi apparatus... |
Q5RBX2 | MADWARAQSPGAVEEILDRENKRMADNLASKVTRLKSLALDIDKDAEDQNRYLDGMDSDFTSMTGLLTGSVKRFSTMARSGRDNRKLLCGMAVGLIVAFFILSYFLSRART | Function: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 12385
Sequence Length: 111
Subcellular Location: Golgi apparatus... |
O35152 | MADWTRAQSSGAVEEIVDRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFSTVARSGRDTRKLLCGMAVVLIVAFFILSYLFSRTRT | Function: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 12417
Sequence Length: 111
Subcellular Location: Golgi apparatus membrane
|
Q95Y80 | MSEGSGDQSQQRPWASPRQQPIKGIVQPRVLPPFGKPTRHTNKLDYIMTTVLKEAGKHKHVWPFQKPVDAVALCIPLYHERVARPMDLKTIENRLKSTYYTCAQECIDDIETVFQNCYTFNGKEDDVTIMAQNVHEVIKKSLEQAPREEHDMDVYWGKNKKKPAKSDGGSKSSSSKKNDARGPSEAPSEAGSEVSSVTTASAAAPTVSESASVAAKPERKVAGKKTGKRKAESEDDEKPEPLRAKREVAVVKKEVHQPLLPSMKPCLKLLNDFSTKKYQEFAWPFNEPVDAEQLGLHDYHKIIKEPMDLKSMKAKMESGA... | Function: Required for the establishment and maintenance of stable cell fate in several lineages including V5.pa, T, Z1/Z4 and QR lineages probably by repressing the expression of cell fate determinants . Required to maintain non-distal tip cell (DTC) fate of somatic gonadal cells through the htz-1-mediated repression ... |
O15155 | MRRAGLGEGVPPGNYGNYGYANSGYSACEEENERLTESLRSKVTAIKSLSIEIGHEVKTQNKLLAEMDSQFDSTTGFLGKTMGKLKILSRGSQTKLLCYMMLFSLFVFFIIYWIIKLR | Function: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 13289
Sequence Length: 118
Subcellular Locatio... |
Q62896 | MRRAGLGDGAPPGGYGNYGYANSGYNACEEENDRLTESLRSKVTAIKSLSIEIGHEVKNQNKLLAEMDSQFDSTTGFLGKTMGRLKILSRGSQTKLLCYMMLFSLFVFFVIYWIIKLR | Function: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 13230
Sequence Length: 118
Subcellular Location: Endoplasmic r... |
P0ABD4 | MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activ... |
P63698 | MQGDPDVLRLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRAESFDEMRHAEEITDRILLLDGLPNYQRIGSLRIGQTLREQFEADLAIEYDVLNRLKPGIVMCREKQDTTSAVLLEKIVADEEEHIDYLETQLELMDKLGEELYSAQCVSRPPT | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activ... |
P43315 | MQGDPDVLRLLNEQLTSELTAINQYFLHSKMQENWGFTELAERTRVESFDEMRHAEAITDRILLLDGLPNYQRIGSLRVGQTLREQFEADLAIEYEVMSRLKPGIIMCREKQDSTSAVLLEKIVADEEEHIDYLETQLALMGQLGEELYSAQCVSRPPS | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex (By similarity).... |
Q9HWF9 | MQGHPEVIDYLNTLLTGELAARDQYFIHSRMYEDWGFSKLYERLNHEMEEETQHADALLRRILLLEGTPRMRPDDIHPGTTVPEMLEADLKLERHVRAALAKGIALCEQHKDFVSRDILKAQLADTEEDHAYWLEQQLGLIARMGLENYLQSQI | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activ... |
P77930 | MQGHPDVINYLVTLLKGELAARDQYFIHSRMYEDWGLTKLYERINHEMEEETQHADALMRRILMLEGTPDMRADDLEVGSTVPEMIEADLKLEYKVRGALCKGIELCELHKDYISRDILRAQLADTEEDHTYWLEKQQGLIKAIGLENYLQSQM | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activ... |
Q59738 | MKGDAKVIEFLNAALRSELTAISQYWVHFRLQEDWGLAKMAKKSREESIEEMGHADKIIARILFLEGHPNLQKLDPLRIGEGPRETLECDLAGEHDALKLYREARDYCAEVGDIVSKNIFESLITDEEGHVDFLETQISLYDRLGPQGFALLNAAPMDAAE | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activ... |
O68926 | MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLTRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLGIGEDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIAKLGMQNYLQSQIKVTD | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activ... |
P24602 | MKGKPAVLAQLHKLLRGELAARDQYFIHSRMYQDWGLEKLYSRIDHEMQDETAHASLLIERILFLEETPDLSQQDPIRVGKTVPEMLQYDLDYEYEVIANLKEAMAVCEQEQDYQSRDLLLKILADTEEDHAYWLEKQLGLIEKIGLQNYLQSQMS | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activ... |
Q06002 | MYRRSYVFQTRKEQYERAEEAPRAAEPDRLAEARAAAPNLAALQGLGERVAAHVQRARALEQRHAVLRRQLDAFQRLDELAGPEDALARHVEGNRQRARDLAAERTRLERQGAEAQRALDEFRSKYENECECQLLLKEMLERLNKEADEALLRNLRLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIIQTTPQAAAITSGMREEKLLTEREAAALQCQLEDGREMICLLQAQRTELQAQTAALEQAIRDAHECYDDEIQLYNEQIDTLRKEIEEAERSLERSSYDCRQLVVVQQTLRNELDRYHRIIENEGNRLS... | Function: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity).
PTM: Proteolytically cleaved during lens cell fiber differentiation with increased f... |
Q06637 | MYRSSFLREVRKEKYERSDAYDELRGSPEFDSLAQAQGLENLQELNERFASYINRARVLEQRNTILRKQLETFQRMDELVGLDEAFAGQIEFNRQRMRELASDRAKLEREEKDAQRMLDEYHNKYRNEREYQQKLKETLERLNKEADEALLCNLELQIESQFLQDDINATKDRYKKNLMEIQTYVNILQQIIQTTPRVSPITTGISEEKLVAERRIPVLQSQLEEYKSILCQLQAQKYKLQTETTMLEQAIKNTQESYDDEIQLYNEQIENLRKGIEEAERTLEKYTTDCRQLVIYQQSLENELERYKRIIENEDSRLNS... | Function: Required for the correct formation of lens intermediate filaments.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76105
Sequence Length: 657
Subcellular Location: Cell membrane
|
Q12934 | MYRRSYVFQTRKEQYEHADEASRAAEPERPADEGWAGATSLAALQGLGERVAAHVQRARALEQRHAGLRRQLDAFQRLGELAGPEDALARQVESNRQRVRDLEAERARLERQGTEAQRALDEFRSKYENECECQLLLKEMLERLNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKKNLLEVQTYISILQQIIHTTPPASIVTSGMREEKLLTEREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHECYDDEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLAVAQQTLKNELDRYHRIIEIEGNRL... | Function: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA . Involved in altering the calcium regulation of MIP water permeability .
PTM: Proteolytically cleaved during lens cell fiber differentiation with increased fragmentation as fiber cell age... |
P77989 | MGRDVLNFNVDWLYIPEDLNDAYKFDFDESNFEVVSLPHANKTFPHHYFKEEDYRFVSWYRKHFKVDERYKGKKVYIHFEGVITVAKVYVNGEFVGEHKGGYTPFEFDITEYIKYGNFENLIAVQVDSREHKDIPPEGHLVDYMLFGGIYRNVWLKILNDTHIKDVYFVVDKLQDSVAEISITTTIAGKEISNGKILTEVINKEGVVCSSVVTDIKEMQKEIVQQIKMDNPLTWHPDHPYLYNVSVKLIAENEILDNYTFKTGIRTVEFRDDGKFYINGEPLKLRGLNRHQTFPYVGGAMPDRVQRKDADILKYELGLNY... | Function: Beta-galactosidase.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 85765
Sequence Length: 743
EC: 3.2.1.23
|
P26257 | MRKIIPINNNWYFKADYEEGYEKVDDLRSFENVNLPHTNIELPYNYFDEKMYQIKSCYKYPLHISEKYRDKVIYIHFEGVMAYAQVYLNGLYIGEHKGGYTPFDIRIDEVYDWKKELNMLTVVVDSTERSDIPPKGGQIDYLTYGGIYREVSLGIYDDVFIKNIKVETHGIYDNEKSLNLIVHLENLNHQSGNVKFKVKINDKNGKEVFYKEFNTYLDAVKDVYSFNIENLKDIKLWDVDNPNLYEIKVGMKINNFSDEYDNKFGFREAVFKPDGFYLNGRKLKLRGLNRHQSYPYVGYAMPRRVQEKDAEILKNELHLN... | Function: Displays beta-galactosidase activity with the artificial chromogenic substrate o-nitrophenyl-beta-D-galactopyranoside (ONPG).
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 83781
Sequence Length: 716
EC: 3.2.1.23
|
P48982 | MLRTTLAPLVLALALALPAAAATPESWPTFGTQGTQFVRDGKPYQLLSGAIHFQRIPRAYWKDRLQKARALGLNTVETYVFWNLVEPQQGQFDFSGNNDVAAFVKEAAAQGLNVILRPGPYACAEWEAGGYPAWLFGKGNIRVRSRDPRFLAASQAYLDALAKQVQPLLNHNGGPIIAVQVENEYGSYADDHAYMADNRAMYVKAGFDKALLFTSDGADMLANGTLPDTLAVVNFAPGEAKSAFDKLIKFRPDQPRMVGEYWAGWFDHWGKPHAATDARQQAEEFEWILRQGHSANLYMFIGGTSFGFMNGANFQNNPSD... | Function: Preferentially hydrolyzes beta(1->3) galactosyl linkages over beta(1->4) linkages.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 66086
Sequence Length: 598
EC: 3.2.1.23
|
A2RAL4 | MRFTSIEAVALTAVSLASADELAYSPPYYPSPWANGQGDWAEAYQRAVDIVSQMTLAEKVNLTTGTGWELELCVGQTGGVPRLGIPGMCAQDSPLGVRDSDYNSAFPAGVNVAATWDKNLAYLRGQAMGQEFSDKGADIQLGPAAGPLGRSPDGGRNWEGFSPDPALSGVLFAETIKGIQDAGVVATAKHYIAYEQEHFRQAPEAQGYGFNITESGSANLDDKTMHELYLWPFADAIRAGAGAVMCSYNQINNSYGCQNSYTLNKLLKAELGFQGFVMSDWAAHHAGVSGALAGLDMSMPGDVDYDSGTSYWGTNLTISV... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
P42973 | MGNMPKDFLWGGALAAHQFEGGWNQGGKGPSVVDVMTAGAHGVPRKITDTIEENEFYPNHEAIDFYHRYKEDIALFAEMGLKCLRTSIGWSRIFPKGDEAEPNEAGLQFYDDVFDELLKHGIEPVITLSHFEMPLHLAREYGGFRNRKVVDFFVNFAEACFTRYKDKVKYWMTFNEINNQMDVNNPLFLWTNSGVVVGENENAKEVMYQTAHHELVASALAVAKGKDINPEFQIGAMVSHVPIYPFSSNPEDVMLAEEEMRQRYFFPDVQVRGYYPSYALKEFEREGYNITFEDGDDEILRNGTVDYLGFSYYMSTTVKS... | Function: Catalyzes the hydrolysis of aryl-phospho-beta-D-glucosides such as 4-methylumbelliferyl-phospho-beta-D-glucopyranoside (MUG-P), phosphoarbutin and phosphosalicin. Plays a major role in the utilization of arbutin or salicin as the sole carbon source. BglA and BglH are the major proteins contributing to hydroly... |
Q46829 | MIVKKLTLPKDFLWGGAVAAHQVEGGWNKGGKGPSICDVLTGGAHGVPREITKEVLPGKYYPNHEAVDFYGHYKEDIKLFAEMGFKCFRTSIAWTRIFPKGDEAQPNEEGLKFYDDMFDELLKYNIEPVITLSHFEMPLHLVQQYGSWTNRKVVDFFVRFAEVVFERYKHKVKYWMTFNEINNQRNWRAPLFGYCCSGVVYTEHENPEETMYQVLHHQFVASALAVKAARRINPEMKVGCMLAMVPLYPYSCNPDDVMFAQESMRERYVFTDVQLRGYYPSYVLNEWERRGFNIKMEDGDLDVLREGTCDYLGFSYYMTN... | Function: Catalyzes the hydrolysis of phosphorylated beta-glucosides into glucose-6-phosphate (G-6-P) and aglycone. It has a high affinity for phosphorylated aromatic beta-glucosides (p-nitrophenyl-beta-glucoside, phenyl beta-glucoside, arbutin), with the exception of phosphorylated salicin, and a low affinity for phos... |
Q5B5S8 | MKLGWLEAAALTAASVASAQVKQDDLPVSPPYYPSPWSNGEGEWAEAYNRAVQIVSQMTLDEKVNLTTGTGMSEKCVGQTGSVPRLGINSICLQDGPLGIRFTDYNSAFPAGVNVAATWDRQLAYIRGHAMGQEFSDKGIDVQLGPAAGPLGRFPDGGRNWEGFSPDPVLSGVLFAETIKGIQDAGVIATAKHYLLNEQEHFRQVPEANGYGYNITETLSENVDDKTLHELYLWPFADAVRAGVGAIMCSYQHLNNTQACQNSHLLNKLLKAELGFQGFVMSDWSATHSGVGSALAGMDMTMPGDIAFNDGLSYYGPNLT... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
P22073 | MTIFQFPQDFMWGTATAAYQIEGAYQEDGRGLSIWDTFAHTPGKVFNGDNGNVACDSYHRYEEDIRLMKELGIRTYRFSVSWPRIFPNGDGEVNQEGLDYYHRVVDLLNDNGIEPFCTLYHWDLPQALQDAGGWGNRRTIQAFVQFAETMFREFHGKIQHWLTFNEPWCIAFLSNMLGVHAPGLTNLQTAIDVGHHLLVAHGLSVRRFRELGTSGQIGIAPNVSWAVPYSTSEEDKAACARTISLHSDWFLQPIYQGSYPQFLVDWFAEQGATVPIQDGDMDIIGEPIDMIGINYYSMSVNRFNPEAGFLQSEEINMGLP... | Function: BglA is intracellular and cleaves cellobiose probably through inorganic phosphate mediated hydrolysis.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 51649
Sequence Length: 448
EC: 3.2.1.21
|
B9K7M5 | MKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGDVACDHYNRWKEDIEIIEKIGAKAYRFSISWPRILPEGTGKVNQKGLDFYNRIIDTLLEKNITPFITIYHWDLPFSLQLKGGWANRDIADWFAEYSRVLFENFGDRVKHWITLNEPWVVAIVGHLYGVHAPGMKDIYVAFHTVHNLLRAHAKSVKVFRETVKDGKIGIVFNNGYFEPASEREEDIRAARFMHQFNNYPLFLNPIYRGEYPDLVLEFAREYLPRNYEDDMEEIKQEIDFVGLNYYSGHMVKYDPNSPARVSFVERNLPKTAM... | Function: Broad substrate specificity glycosidase. Releases glucose from soluble glucooligomers, with a preference for longer oligomers; acts more readily on cellotetraose than on cellobiose. Displays similar activities towards the disaccharides lactose and cellobiose. Is also able to hydrolyze various aryl-beta-glycos... |
P14002 | MAVDIKKIIKQMTLEEKAGLCSGLDFWHTKPVERLGIPSIMMTDGPHGLRKQREDAEIADINNSVPATCFPSAAGLACSWDRELVERVGAALGEECQAENVSILLGPGANIKRSPLCGRNFEYFSEDPYLSSELAASHIKGVQSQGVGACLKHFAANNQEHRRMTVDTIVDERTLREIYFASFENAVKKARPWVVMCAYNKLNGEYCSENRYLLTEVLKNEWMHDGFVVSDWGAVNDRVSGLDAGLDLEMPTSHGITDKKIVEAVKSGKLSENILNRAVERILKVIFMALENKKENAQYDKDAHHRLARQAAAESMVLLK... | Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 83900
Sequence Length: 755
Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.21
|
P11988 | MKAFPETFLWGGATAANQVEGAWQEDGKGISTSDLQPHGVMGKMEPRILGKENIKDVAIDFYHRYPEDIALFAEMGFTCLRISIAWARIFPQGDEVEPNEAGLAFYDRLFDEMAQAGIKPLVTLSHYEMPYGLVKNYGGWANRAVIDHFEHYARTVFTRYQHKVALWLTFNEINMSLHAPFTGVGLAEESGEAEVYQAIHHQLVASARAVKACHSLLPEAKIGNMLLGGLVYPLTCQPQDMLQAMEENRRWMFFGDVQARGQYPGYMQRFFRDHNITIEMTESDAEDLKHTVDFISFSYYMTGCVSHDESINKNAQGNIL... | Function: Catalyzes the hydrolysis of phosphorylated beta-glucosides into glucose-6-phosphate (G-6-P) and aglycone. It has a high affinity for phosphorylated aromatic beta-glucosides (p-nitrophenyl-beta-glucoside, phenyl beta-glucoside, arbutin and phosphorylated salicin), and a low affinity for phosphorylated beta-met... |
Q5BFG8 | MSFQKVDPAQIESVLSKLTLEEKISLLAGKNFWETQDYPEKGVPPVKTSDGPNGARGATFKGGVTAACFPASSLLAATWDLDAAKHIGEALADETRSKGARVLLAPTVCIHRHPLGGRNFESFSEDPFLAGKLAAQYIKGLQGNGVAATIKHYAANEQETCRFTVNEHITERALREIYLKPFEIAIKESNPLAVMTAYNIVNGTHADSNNFLLRDVLRGEWGWKGLVMSDWGGTNSTADALNAGLDLEMPGPTRWRKVDEVLAVVKSGAVLEETIDERARNVLELLAKLNCFENPTIPEEKAINRPEHQKLIRSVGSQGL... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence ... |
P38645 | MTESAMTSRAGRGRGADLVAAVVQGHAAASDAAGDLSFPDGFIWGAATAAYQIEGAWREDGRGLWDVFSHTPGKVASGHTGDIACDHYHRYADDVRLMAGLGDRVYRFSVAWPRIVPDGSGPVNPAGLDFYDRLVDELLGHGITPYPTLYHWDLPQTLEDRGGWAARDTAYRFAEYALAVHRRLGDRVRCWITLNEPWVAAFLATHRGAPGAADVPRFRAVHHLLLGHGLGLRLRSAGAGQLGLTLSLSPVIEARPGVRGGGRRVDALANRQFLDPALRGRYPEEVLKIMAGHARLGHPGRDLETIHQPVDLLGVNYYSH... | Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 52228
Sequence Length: 473
Subcellular Location: Cytoplasm
EC: 3.2.1.21
|
Q5AWD4 | MLTSWGKTGFVLALALGGRAAENVITSDTFFYGESPPVYPSPEGTGAGDWASAYTKARAFVAQLSDDEKIQLTAGVSSNTACSGFIQPIDRLGFPGICMSDAGNGLRGTDYVNGWSSGISVGASWNRDLAHSRGAYMGQEYRKKGVNMILGPVVGPLGRVALGGRNWEGYAADPYLSGVLVSESVKGLQSQKVATSVKHFIANEQETNRNPTTDSERNVVQSVSSNIDDKTMHELYLWPFQDAVLAGATNLMCSYNRVNNSYACQNSKLLNGVLKTELGFQGYVVTDWGAQHAGIASANAGLDVVMPRSSTWNSNLTTAI... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
Q5B681 | MHSNILPVLTSVATLLGLVQGQSQQPYRDWAKAYEAAETLVLPWTLEQQANISVRDGTAPGFVPFEPSDGVRSVQGSGKDYDNPAMRTSSNLDDRTLHELYLWPWIDGVANGLGSVMCVMNRVNGIIGCENDHIMNGILKNETGFRGFIVPDVTAPVDKAAGLLGGLGWNSGYSVSEIMAAVKNGSIPESVMTEHALRIVATQLNLLQPPEEYAFPVETADLNVRDPSSKDFIRRAGSESIVLLKNKNNTLPLRSPMSLGIFGKDAANLATGPTPQSDFSNFAGDTYDGHLITGGGSYSPAPYVVSPLDALTARAADGQG... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
Q5BG51 | MTVLAPWALWEKTKDVMVLEQQYQSMCTWIAAIPENMKRHRHLCDPVVLQFAVAVRESNPWAVMTAYHKINGVHCSEDPRLIRDIPRSEWKYDGLVLCDWWGIYSTSELINAGMDLEMPGPTDWRCKILAWATRSRKVSIETIDSSVRRVLKLVNRVLAAQSEPVKDSDTEKNRALLRETTAVPVVLLKKNEANVLPLVKDSKTRYALIGDHWKNPAVAGDDSSEVTPYYVSTPYSAFVEAVGEDSFICAMGCYSHKFAPLLYSTITQPGSDAHGMLLEFFNKDPNGSSDAELLYTTTTEKTDLKFADSLPPDTVPEYTS... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
Q5LIC7 | MKQQKCNYFPSLWWRGREKGLSTFLFLLLFSISLHAQRQDILLNNNWNFRFSHQVQGDTRRVDLPHTWNAQDALAGKIDYKRGIGNYEKALYIRPEWKGKRLFLRFDGVNSIADVFINRKHIGEHRGGYGAFIFEITDLVKYGEKNSVLVRANNGEQLDIMPLVGDFNFYGGIYRDVHLLITDETCISPLDYASPGVYLVQEVVSPQEAKVCAKVNLSNRAADGTAELQVLVTDGTKVICKESRNVSLKQGADILEQLPLLIQKPRLWNGCEDPFMYQVSISLHKDGKQIDSVTQPLGLRYYHTDPDKGFFLNGKHLPLH... | Function: Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sou... |
Q8XP19 | MLYPIITESRQLIDLSGIWKFKLNEGNGLTEELSKAPLEDTIEMAVPSSYNDLVESQEVRDHVGWVWYERNFTIPKTLLNERIVLRFGSATHEAKVYLNGELLVEHKGGFTPFEAEINDLLVSGDNRLTVAVNNIIDETTLPVGLVKEVEVDGKKVIKNSVNFDFFNYAGIHRPVKIYTTPKSYIEDITIVTDFKENNGYVNYEVQAVGKCNIKVTIIDEENNIVAEGEGKEGKLTINNVHLWEPMNAYLYKLKVELLDDEEIIDTYFEEFGVRTVEVKDGKFLINNKPFYFKGFGKHEDSYVNGRGINEAINIKDFNLM... | Function: Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sou... |
P05804 | MLRPVETPTREIKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADIRNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTPYVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTPNTWVDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPHLWQPGEGYLYELCVTAKSQTECDIYPLRVGIRSVAVKGEQFLINHKPFYFTGFGRHEDADLRGKGFDNVLMVHDHALMDW... | Function: Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG) and with 4-methylumbelliferyl-glucuronide . Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tra... |
P08236 | MARGSAVAWAALGPLLWGCALGLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFEEQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVVLRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTTLPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPTTYIDDITVTTSVEQDSGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYLYSLEVQLTAQTSLGPVSDFY... | Function: Plays an important role in the degradation of dermatan and keratan sulfates.
PTM: N-linked glycosylated with 3 to 4 oligosaccharide chains.
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 74732
Sequence Length: 651
Subcellular Location: Lysosome
EC: 3.2.1.31
|
P12265 | MSLKWSACWVALGQLLCSCALALKGGMLFPKESPSRELKALDGLWHFRADLSNNRLQGFEQQWYRQPLRESGPVLDMPVPSSFNDITQEAALRDFIGWVWYEREAILPRRWTQDTDMRVVLRINSAHYYAVVWVNGIHVVEHEGGHLPFEADISKLVQSGPLTTCRITIAINNTLTPHTLPPGTIVYKTDTSMYPKGYFVQDTSFDFFNYAGLHRSVVLYTTPTTYIDDITVITNVEQDIGLVTYWISVQGSEHFQLEVQLLDEGGKVVAHGTGNQGQLQVPSANLWWPYLMHEHPAYMYSLEVKVTTTESVTDYYTLPI... | Function: Plays an important role in the degradation of dermatan and keratan sulfates.
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 74195
Sequence Length: 648
Subcellular Location: Lysosome
EC: 3.2.1.31
|
P06760 | MSPRRSVCWFVLGQLLCSCAVALQGGMLFPKETPSRELKVLDGLWSFRADYSNNRLQGFEKQWYRQPLRESGPTLDMPVPSSFNDITQEAELRNFIGWVWYEREAVLPQRWTQDTDRRVVLRINSAHYYAVVWVNGIHVVEHEGGHLPFEADITKLVQSGPLTTFRVTIAINNTLTPYTLPPGTIVYKTDPSMYPKGYFVQDISFDFFNYAGLHRSVVLYTTPTTYIDDITVTTDVDRDVGLVNYWISVQGSDHFQLEVRLLDEDGKIVARGTGNEGQLKVPRAHLWWPYLMHEHPAYLYSLEVTMTTPESVSDFYTLPV... | Function: Plays an important role in the degradation of dermatan and keratan sulfates.
PTM: Undergoes a post-transcriptional proteolytic cleavage near its C-terminal end, which reduces its size by approximately 3 kDa. The site of this cleavage has as yet not been determined.
Catalytic Activity: a beta-D-glucuronoside +... |
Q8E0N2 | MLYPLLTKTRNTYDLGGIWNFKLGEHNPNELLPSDEVMVIPTSFNDLMVSKEKRDYIGDFWYEKVIEVPKVSEDEEMVLRFGSVTHQAKIYVDGVLVGEHKGGFTPFEVLVPECKYNNEKIKVSICANNVLDYTTLPVGNYSEIIQEDGSIKKKVRENFDFFNYAGVHRPLKLMIRPKNHIFDITITSRLSDDLQSADLHFLVETNQKVDEVRISVFDEDNKLVGETKDSRLFLSDVHLWEVLNAYLYTARVEIFVDNQLQDVYEENFGLREIEVTNGQFLLNRKPIYFKGFGKHEDTFINGRGLNEAANLMDLNLLKDM... | Function: Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sou... |
P16084 | MEKWARIKYTPNLPLGENGERVTASQKHIELSCEAACEGMVLLKNDRNVLPIRKGTRVALFGKGVFDYVKGGGGSGDVTVPYIRNLYEGLSQYTSDISIYDKSVRFYQEYVADQYRLGIAPGMIKEPALPEDILADAAAYADTAIIAISRFSGEGWDRKVAGVDREIKCEAKDLVEQGNKIFDHGDFYLTNAEKKMVKMVKENFSSVIVVMNVGGVVDTTWFKKDDQISSVLMAWQGGIEGGLAAARILLGKVNPSGKLSDTFAARLEDYPSTEGFHEDDDYVDYTEDIYVGYRYFETIPGAKEKVNYPFGYGLSYTTFL... | Function: B.fibrisolvens beta-glucosidase hydrolyzes cellobiose to a limited extent, cellotriose to cellobiose and glucose, and cellotetraose and cellopentaose to predominantly glucose.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): ... |
P07337 | MSKFDVEQLLSELNQDEKISLLSAVDFWHTKKIERLGIPAVRVSDGPNGIRGTKFFDGVPSGCFPNGTGLASTFDRDLLETAGKLMAKESIAKNAAVILGPTTNMQRGPLGGRGFESFSEDPYLAGMATSSVVKGMQGEGIAATVKHFVCNDLEDQRFSSNSIVSERALREIYLEPFRLAVKHANPVCIMTAYNKVNGDHCSQSKKLLIDILRDEWKWDGMLMSDWFGTYTTAAAIKNGLDIEFPGPTRWRTRALVSHSLNSREQITTEDVDDRVRQVLKMIKFVVDNLEKTGIVENGPESTSNNTKETSDLLREIAADS... | Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 93917
Sequence Length: 845
Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.21
|
Q9LD45 | MDAFSSFFDSQPGSRSWSYDSLKNFRQISPAVQNHLKRVYLTLCCALVASAFGAYLHVLWNIGGILTTIGCIGTMIWLLSCPPYEHQKRLSLLFVSAVLEGASVGPLIKVAIDVDPSILITAFVGTAIAFVCFSAAAMLARRREYLYLGGLLSSGLSMLMWLQFASSIFGGSASIFKFELYFGLLIFVGYMVVDTQEIIEKAHLGDMDYVKHSLTLFTDFVAVFVRILIIMLKNSADKEEKKKKRRN | Function: Suppressor of apoptosis. Modulator of endoplasmic reticulum stress-mediated programmed cell death. Involved in methyl jasmonate-induced leaf senescence through regulating cytoplasmic calcium level.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27483
Sequence Length: 247
Subcellular Locati... |
Q9VSH3 | MADTANYINDRFQTFMNGLGDRYEPYVREHLSKVYMVLGSTAAATAMGAMLQMRDFLDLGVLAAVATLVLVLGLHFYKDDGKNYYTRLGMLYAFGFCSGQTLGPLLGYICSINPAIILSALTGTFVTFISLSLSALLAEQGKYLYLGGMLVSVINTMALLSLFNMVFKSYFVQVTQLYVGVFVMAAFIVYDTQNIVEKCRNGNRDVVQHALDLFFDVLSMFRRLLIILTQKEERKQNERRQNKTK | Function: Suppressor of apoptosis (By similarity). Modulates unfolded protein response signaling . Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da... |
P55061 | MNIFDRKINFDALLKFSHITPSTQQHLKKVYASFALCMFVAAAGAYVHMVTHFIQAGLLSALGSLILMIWLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALEFCIAVNPSILPTAFMGTAMIFTCFTLSALYARRRSYLFLGGILMSALSLLLLSSLGNVFFGSIWLFQANLYVGLVVMCGFVLFDTQLIIEKAEHGDQDYIWHCIDLFLDFITVFRKLMMILAMNEKDKKKEKK | Function: Suppressor of apoptosis . Modulates unfolded protein response signaling . Modulates ER calcium homeostasis by acting as a calcium-leak channel . Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation (By simila... |
Q9D2C7 | MNIFDRKINFDALLKFSHITPSTQQHLKKVYASFALCMFVAAAGAYVHVVTHFIQAGLLSALGSLALMIWLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALELCIAVNPSILPTAFMGTAMIFTCFSLSALYARRRSYLFLGGILMSAMSLMLLSSLGNLFFGSIWLFQANLYLGLLVMCGFVLFDTQLIIEKAEHGDKDYIWHCVDLFLDFVTLFRKLMLILAFNEKDKKKEKK | Function: Suppressor of apoptosis (By similarity). Modulates unfolded protein response signaling (By similarity). Modulates ER calcium homeostasis by acting as a calcium-leak channel (By similarity). Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduc... |
Q9MBD8 | MDAFYSTSSAYGAAASGWGYDSLKNFRQISPAVQSHLKLVYLTLCVALAASAVGAYLHVALNIGGMLTMLGCVGSIAWLFSVPVFEERKRFGILLAAALLEGASVGPLIKLAVDFDSSILVTAFVGTAIAFGCFTCAAIVAKRREYLYLGGLLSSGLSILLWLQFAASIFGHSTGSFMFEVYFGLLIFLGYMVYDTQEIIERAHHGDMDYIKHALTLFTDFVAVLVRILVIMLKNASDKSEEKKRKKRS | Function: Suppressor of apoptosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27114
Sequence Length: 249
Subcellular Location: Membrane
|
P55062 | MNIFDRKINFDALLKFSHITPSTQQHLKKVYASFALCMFVAAAGAYVHVVTRFIQAGLLSALGALALMICLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALELCIAINPSILPTAFMGTAMIFTCFSLSALYARRRSYLFLGGILMSAMSLMFVSSLGNLFFGSIWLFQANLYMGLLVMCGFVLFDTQLIIEKAEHGDKDYIWHCIDLFLDFVTLFRKLMLILAFNEKDKKKEKK | Function: Suppressor of apoptosis. Modulates unfolded protein response signaling. Modulates ER calcium homeostasis by acting as a calcium-leak channel. Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation.
Location Top... |
Q0H8X2 | MRLLKTHPILGLANSYLIDSPQPSNISYMWNFGSLLGVCLIIQILTGVFLAMHYTPSVDLAFISVEHIMRDVNYGWLIRYLHANTASFFFIFVYLHIGRGLYYGSYKSPRTLLWSIGVIILVLMMAIAFLGFNGQKYMCFYNIDITIIQYLSIPTLITPSTRLKPILDKHNIKPVLLFENLTNSETKKIAYQALKPFSGIYMIVNLITEKYYVGSAVTGNLYMRFHKHLFSFTGNKRVANAVNKYGLSEFAFLVLEIVPQKDKIDSTLLLNREDYYLETLKPEYNIAPLASNSLGWKHSEESLAKMRENYSEERRQQVAN... | Function: Mitochondrial DNA endonuclease involved in intron homing.
PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of COB exon 1 plus intron 1, containing the bI1 open reading frame.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46822
Sequence Length: 410
Sub... |
Q9UHR4 | MSRGPEEVNRLTESTYRNVMEQFNPGLRNLINLGKNYEKAVNAMILAGKAYYDGVAKIGEIATGSPVSTELGHVLIEISSTHKKLNESLDENFKKFHKEIIHELEKKIELDVKYMNATLKRYQTEHKNKLESLEKSQAELKKIRRKSQGSRNALKYEHKEIEYVETVTSRQSEIQKFIADGCKEALLEEKRRFCFLVDKHCGFANHIHYYHLQSAELLNSKLPRWQETCVDAIKVPEKIMNMIEEIKTPASTPVSGTPQASPMIERSNVVRKDYDTLSKCSPKMPPAPSGRAYTSPLIDMFNNPATAAPNSQRVNNSTGT... | Function: May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.
PTM: Phosphorylated on tyrosine in response to insulin.
Sequence Mass (Da): 56883
Sequence Length: 511
Domain: The IMD domai... |
B0CC69 | MSEETFPQASALTLLSDPNIDLLSLVAAAGEVRMTYFGRQVMLHRINDIQNGLCPEDCGYCAQSKISDAPIKKYPLKSEEDIIQEAYEAKAKGVYRYCMVSSGRGPTAERTEHLAHIIRRIKNEVGIQTCLSAGLMDHEQAAVLKEAGLDRLNHNLNTSESHTPDIVTTHTFQDRINTLKAARSAGLDLCSGMIAGMGETDQDIVDIAYQLHEYQVPSIPINFLIPISGNPIYDCNQLTPQRCLRILCLFRFVNPKAEIRIGGGREGHLRSLQALALYPANSLFVEGYLATRGHSVDQVYQLIHDAGFEVAGETSLTGDL... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
Q6FAP9 | MTLRNDWTRDEIQALYDQPFLDLVFQAQQVHREHFSANTIQVSTLLSIKTGKCPEDCKYCSQSAHYDSKLEAEKRIAVDKVISEAKAAKDSGSSRFCMGAAWRNPHERDMPYVLEMVREVKALGLETCMTLGMLNQSQAERLSDAGLDYYNHNLDTSREYYNNIISTRTFDDRLNTLDHVRSAGMKVCSGGIVGLGEQKQDRIGLLHELATLPIHPESVPINMLVPIEGTPLADVEKLDVTEWIRTIAVARIIMPYSYIRLSAGRESLSDSDQALAFMAGANSLFSGDKLLTTPNAGEGKDQVLFAKLGLVAEKPKVSVR... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
B7MGN3 | MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGVKAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKVREAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNPQQTAVLAG... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
Q2GHB1 | MNTCTTIRNNWQLDEILELFNTPFNDLILRSHLTHRQFFNNNEIQLAALLNIKTGGCPENCRYCSQSAHYKTDLQKEALLDVENIKKAIQTAKNSGADRFCFAAAWRQLRDKDIEYICNIINLIKSEKLESCASLGMITLDQAKKLKNAGLDFYNHNIDTSRDFYSNVTTTRNYDDRLASLNNIYEAGINICSGGILGLGESIEDRAKMLLTLANLKEHPRSVPINRLVPIKGTPFENNIKVDNIDFIKTIAVTRILMPKSYVRLAAGRKDMSEEMQALCLFAGANSIFYGEKLLTTPNSNCDDDKNLLSKLGIKTKEPV... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
Q47C02 | MTSAIKPKAGTRPSKARIRQSFERAAPTYDDAAAIQRRICIRLAEGLPDIAPTHLLDAGCGTGYAQANLQTRFPDAHRVALDLSPGMLQRVATPCCRVAGDLEHLPLADSSLDLYWSSLAVQWCDLAVALREAHRTLRPGGVIALASLGPATFHELRHAFADVDDHRHTLAFHSPGEIRQLASLAGLAAIDIKKSTEIAHYPDFKTLLRAVKAIGANQLGDGRRTSLMSRSSFQLAESACEQLRTPAGLPLTYDVIYLYARK | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
P12999 | MATVNKQAIAAAFGRAAAHYEQHADLQRQSADALLAMLPQRKYTHVLDAGCGPGWMSRHWRERHAQVTALDLSPPMLVQARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPKGVVAFTTLVQGSLPELHQAWQAVDERPHANRFLPPDEIEQSLNGVHYQHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWPQQQGRYPLTYHLFLGVIARE | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily ... |
D8MPW4 | MQTVNKQAIAQAFGRAAQSYNQHAGLQRLCGEELASYATRRQGQKVLDAGCGPGWFSQHWRAAGNHVTALDLSAEMLVQAQALHTADCYQPGDIEALPFSDASFDLCWSNLAVQWCSDLSLALTELYRVTSPGGQVLFSTLSADSLHELSAAWQPLDLPAPVNRFLPFDAIAHAGQHLPLTLMQQTLTVGFPDVLSALRSLKGIGATHLHQGRHGGLLSRRHLQQLEQHWPRDRRGYLLSYHLVYGVMHRE | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
D9SJ16 | MNEFVIDKKAMRQAFSRAAEGYDASAVLQREVCMRMLERLEYIKLQPARLLDAGSGTGWGGRQLAEKYPAAQVISLDIAIGMLQTSKSRSSWWQKLFGGCRQLPVCADVEALPLAANSLDMVWSNLAVQWCNDLPATFVELHRVLKTEGLLMFSTLGPDTLKELRQAFKGVDERSHLNRFADMHDIGDMLVQAGFAEPVMDMEYLTLTYEDVRGVLQDLKAIGAHNTTAGRGQGLMGKAAWARLLENYEKLRRDGKLPATYEVVYGHAWKPAPRVNRDGAAIIKTSFKIK | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
Q749W5 | MIDRRKVRNAFHRGAADYDAYAAVQKRVMERILSLLFAEGVEPARILDVGAGTGALALRLADRYPSAAITCVDLAHGMARQARDNLGRTMERLVAVADAEHLPLRDGVFDLVVSTSTFQWLTTLDRAFAEARRVLADDGLFAFALFGDGTFKELKASYRAALHSVPRGGRDRTHRFFTRDEVRAALARAGFRSVEVFDEDEVEYHPDVPAFLRSVKRIGAGNASPVAGRGLSGRRVMETMMRTYAERFGGADGIPATYTVVYGVGKR | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
Q7VL11 | MAKLAKQLIAKRFVSHLTEYDQYAIAQQQINHQLVDLLQANTDKTFQRALEIGCGTGNLTEKLLAKIPIEHLTLNDFNAIYYPTVLQKIKQKKPLVVVDFMQGDAEQLVFTRNFDLVSAASVVQWFDSPQQFLRNSAYALKPGGVVLFNSFSPLNLQEIRQLTGIGLNYPTRLQWQEWLAQDFEQCQLIEQPIKLTFDSPLAVLIHLKKTGVTAVSNKPWNRHQIKQFCMEYQAHFACEQGVYLTYTPILMLGIKKNG | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
P45249 | MGSLTSVDKSRIRQAFQKALNDYDRHALIQQKMTINLMAHLQDYLPNGSLDSVLELGCGSGMLSSLLQKQISADYWLFNDLCDVQTQLAEKLPQSFDFYCGDAEHFLFLQQFDLIASASAVQWFHQPDAFIAHCKTGLKTNGLLAVATFGEDNLKEVRQITNIGLNYPTLSQWQTWLAKDFELLWCEDFKVILDFDTPLDVLKHLKYTGVTATNQKNWTRKNLNGFIGDYLSAFGMPSGKVRLTYHPLFFIARYSHIENQ | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
Q2SBD7 | MNHAVTIKSFVSTSPLSDLERGAVDKSKVAESFSAAAATYDLLAGMQKEVGESLVSLSREGCPQDIIDVGCGTGWLTHRLKNSFPEARLCAYDLSPGMIEYALAHHDNVAEIWAVADMESLPVANASQDLVFSNMAMQWLDDPRAWFAEASRVLRPGGRLICSTLLTQTLFELEQAWHGVDGGRHVNRFLSAEQVAEAAVSCGLRGECRESLYVRFHDSALDVMKELKGIGAHNIQSERPQGLTGKRRLRRVIENYEKCRQEQGVPATYHVGVCVYSRI | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
Q9K623 | MFIDKQTVERHFSKSAHLYDGVNHVQRKMAHRLVQLLDEKRRDAKDEPRAILDIGCGTGWLTRECLKSFPQATIDAVDLSKQMLEVAEKNVSSHPNVQFIQGDIEKMVREKPSAKTYDVIVANAVFQWLDKPTETVAQLRSWLKPNGLLLFSTFGPDTFYELHDSFQLAAKQLGIIDERRGLDYLSKTEWKRTLDGLFAELTIHEEKAIESYATVEQFLHTVKKMGATYSQSSRPLSKRYYQLMKEIYEQRYRTEDSIPATYDCLYVLCQA | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
A1WVM4 | MNPGDAQSIDRRCVRRSFDASAERYDEVAVLQREVADRLLERLEPVRVHPRRVLDLGAGTGYATRGLLRRYRKAEVHAVDLAPAMLQRVRRRAPWLRRPRCVCADLHALPYPDDSFELVFSNLALQWAEDLPTALRELQRVTAPEGAVMFATFGPETLHELRGAWAEVGDQARVHRFADKHDVGDRMLEAGFVDPVLDGESFTLTYAQPREVMRDLKALGASNADPGRPRGLLSPHRLARVEAAYRLAWRQPDGRVPATYEVVYGHAWGMGGTPQRADDTGEVRLDVHGIRRRRR | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.