ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q67X45 | MAMAGADGPTAGAAAAVRWRGGESLLLLLLRWPSSAELVAAWGAARASAVAPALAAASAACLALSAMLLADAVLMAAACFARRRPDRRYRATPLGAGAGADDDDDDEEAGRVAYPMVLVQIPMYNEREVYKLSIGAACGLSWPSDRLIVQVLDDSTDPTVKGLVELECKSWGNKGKNVKYEVRNTRKGYKAGALKEGLLRDYVQQCNYVAIFDADFQPEPDFLLRTIPYLVRNPQIGLVQAHWEFVNTSECLMTRIQKMTLHYHFKVEQEGGSSTFAFFGFNGTAGVWRISALEEAGGWKDRTTVEDMDLAVRAGLKGWK... | Function: Probable mannan synthase which consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall.
Catalytic Activity:... |
Q8S7W0 | MEGQWGRWRLAAAAAASSSGDQIAAAWAVVRARAVAPVLQFAVWACMAMSVMLVLEVAYMSLVSLVAVKLLRRVPERRYKWEPITTGSGGVGGGDGEDEEAATGGREAAAFPMVLVQIPMYNEKEVYKLSIGAACALTWPPDRIIIQVLDDSTDPAIKDLVELECKDWARKEINIKYEIRDNRKGYKAGALKKGMEHIYTQQCDFVAIFDADFQPESDFLLKTIPFLVHNPKIGLVQTRWEFVNYDVCLMTRIQKMSLDYHFKVEQESGSSMHSFFGFNGTAGVWRVSAINEAGGWKDRTTVEDMDLAVRASLKGWQFLY... | Function: Probable mannan synthase which consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall.
Catalytic Activity:... |
Q6Z2T9 | MQGSSTSILHFVPSDPTSTSVLDFLSPTPRGTSPVHDRRLHAGDLALRAGGDRLLVADTVAAVVESLVQAWRQVRMELLVPLLRGAVVACMVMSVIVLAEKVFLGVVSAVVKLLRRRPARLYRCDPVVVEDDDEAGRASFPMVLVQIPMYNEKEVYQLSIGAACRLTWPADRLIVQVLDDSTDAIVKELVRKECERWGKKGINVKYETRKDRAGYKAGNLREGMRRGYVQGCEFVAMLDADFQPPPDFLLKTVPFLVHNPRLALVQTRWEFVNANDCLLTRMQEMSMDYHFKVEQEAGSSLCNFFGYNGTAGVWRRQVID... | Function: Probable mannan synthase which consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall.
Catalytic Activity:... |
Q9ZQN8 | MSPLPIFHRLPHATFSSFLLSLSQAGSSKTSVAFLNAFKSEDIIARIGLWWQLIRAVVVVPVFKFLVLLCLVMSVMFFVEVMYMGIVVLYVKLFKRKPEKFYKWEAMEDDVECGSASYPMVLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIQVLDDSTDPASKELVKKECDRWSKEGVNITFEIRDNRNGYKAGALREGMRHSYVKQCDYVAIFDADFQPDPDFLHRTVPFLIHNPKLALVQGRWEFVNAGQCMMTRLQEMSLSYHFTIEQQVGSSTFAFFGFNGTAGVWRISALNESGGWNDQTTVEDMDLAVRATL... | Function: Probable mannan synthase which consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall . Required for synth... |
Q7XIF5 | MVEAGEIGGAAVFALAAAAALSAASSLGAVDFRRPLAAVGGGGAFEWDGVVPWLIGVLGGGDEAAAGGVSVGVAAWYEVWVRVRGGVIAPTLQVAVWVCMVMSVMLVVEATFNSAVSLGVKAIGWRPEWRFKWEPLAGADEEKGRGEYPMVMVQIPMYNELEVYKLSIGAACELKWPKDKLIVQVLDDSTDPFIKNLVELECESWASKGVNIKYVTRSSRKGFKAGALKKGMECDYTKQCEYIAIFDADFQPEPNFLLRTVPFLMHNPNVALVQARWAFVNDTTSLLTRVQKMFFDYHFKVEQEAGSATFAFFSFNGTAG... | Function: Probable mannan synthase which consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall.
Catalytic Activity:... |
Q9LZR3 | MELGDTTSVIPDSFMGYRDDITMQMSMVLDQIRAPLIVPALRLGVYICLTMSVMLFVERVYMGIVISLVKLFGRKPDKRFKYEPIKDDIELGNSAYPMVLIQIPMFNEREVYQLSIGAACGLSWPSDRIVIQVLDDSTDPTIKDLVEMECSRWASKGVNIKYEIRDNRNGYKAGALKEGMKKSYVKSCDYVAIFDADFQPEADFLWRTVPYLLHNPKLALVQARWKFVNSDECLMTRMQEMSLDYHFTVEQEVGSSTYAFFGFNGTAGIWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFLYLGSLKVKNELPSTFK... | Function: Possesses glucomannan synthase and mannan synthase activities in vitro. Mannan synthase consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosi... |
Q9LR87 | MTTFLKSLIFLQDSCLAFLSLMFHRGSSEDAAEALKKLETSINGARISFDTTWTREFRSLFIVPLFKCLVAFCLIISLLVFIEGIYMNLVVLYVKVFERKPEKVYRWEAMQEDIELGHETYPMVLVQIPMYNEKEVLQLSIGAACRLIWPLDRLIVQVLDDSTDQTIKELVNTECAKWESKGVNIKCERRDNRNGYKAGALKEGMKHNYVKLCNYVVIFDADFQPEPDYLQHSVPFLVHNPEVALVQARWRFMNANKCLMTRMQEMSLNYHFMAEQESGSTRHAFFSFNGTAGVWRMAAMEEAGGWHDRTTVEDMDLAVR... | Function: Probable mannan synthase which consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall.
Catalytic Activity:... |
Q6YWK8 | MSSSGGGGVAEEVARLWGELPVRVVWAAVAAQWAAAAAAARAAVVVPAVRALVAVSLAMTVMILAEKLFVAAVCLAVRAFRLRPDRRYKWLPIGAAAAAASSEDDEESGLVAAAAAFPMVLVQIPMFNEREVYKLSIGAACSLDWPSDRVVIQVLDDSTDLVVKDLVEKECQKWQGKGVNIKYEVRGNRKGYKAGALKEGLKHDYVKECEYIAMFDADFQPESDFLLRTVPFLVHNSEIALVQTRWKFVNANECLLTRFQEMSLDYHFKYEQEAGSSVYSFFGFNGTAGVWRIAAIDDAGGWKDRTTVEDMDLAVRATLQ... | Function: Probable mannan synthase which consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall.
Catalytic Activity:... |
Q59288 | MKKLFVTCIVFFSILSPALLIAQQTGTAELIMKRVMLDLKKPLRNMDKVAEKNLNTLQPDGSWKDVPYKDDAMTNWLPNNHLLQLETIIQAYIEKDSHYYGDDKVFDQISKAFKYWYDSDPKSRNWWHNEIATPQALGEMLILMRYGKKPLDEALVHKLTERMKRGEPEKKTGANKTDIALHYFYRALLTSDEALLSFAVKELFYPVQFVHYEEGLQYDYSYLQHGPQLQISSYGAVFITGVLKLANYVRDTPYALSTEKLAIFSKYYRDSYLKAIRGSYMDFNVEGRGVSRPDILNKKAEKKRLLVAKMIDLKHTEEWA... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.
Sequence Mass (Da): 79694
Sequence Length: 700
EC: 4.2.2.5
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O80898 | MADSSFSLPPLCERISYTNYFLRAVYLTVLGLFFSLLLHRIRHTSEYDNVWLVAFFCESCFFLVCLLITCLKWSPADTKPFPDRLDERVHDLPSVDMFVPTADPVREPPIMVVDTVLSLLAVNYPANKLACYVSDDGCSPLTYFSLKEASKFAKIWVPFCKKYNTRVRAPSRYFLKPISVATEDYEFNRDWEKTKREYEKLRRKVEDATGDSHMLDVEDDFEAFSNTKPNDHSTLVKVVWENKGGVGDEKEIPHIIYISREKRPNYVHNQKCGAMNFLARVSGLMTNAPYILNVDCDMYANDADVVRQAMCILLQESLNM... | Function: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85061
Sequence Length: 757
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q8RX83 | MADSSSSLPPLCEKISYKNYFLRVVDLTILGFLFSLLLYRILLMNQNNSVWVVAFLCESFFSFIWLLITSIKWSPASYKSYPERLDERVHDLPSVDMFVTTADPVREPPILVANTLLSLLAVNYPANKLACYVSDDGCSPLTYFSLKEASKFAKIWVPFCKKYNIKVRAPFRYFLNPPAATESSEFSKDWEITKREYEKLSRRVEDATGDSHWLDAEDDFEDFSNTKPNDHSTIVKVVWENKGGVGVENEVPHFVYISREKRPNYLHHYKAGAMNFLVRVSGLMTNAPYMLNVDCDMYANEADVVRQAMCIFLQKSMNSN... | Function: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84889
Sequence Length: 755
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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P61201 | MSDMEDDFMCDDEEDYDLEYSEDSNSEPNVDLENQYYNSKALKEDDPKAALSSFQKVLELEGEKGEWGFKALKQMIKINFKLTNFPEMMNRYKQLLTYIRSAVTRNYSEKSINSILDYISTSKQMDLLQEFYETTLEALKDAKNDRLWFKTNTKLGKLYLEREEYGKLQKILRQLHQSCQTDDGEDDLKKGTQLLEIYALEIQMYTAQKNNKKLKALYEQSLHIKSAIPHPLIMGVIRECGGKMHLREGEFEKAHTDFFEAFKNYDESGSPRRTTCLKYLVLANMLMKSGINPFDSQEAKPYKNDPEILAMTNLVSAYQN... | Function: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to ... |
Q7V2C8 | MSTKTSREIALERRKAMSDGGKKAALHSSSTKDRVRSSQDINSTGATSSNKKVLTSPSKSNIPANKIARKSTSSKLSSKELGIERRKAMSTHGKSAINSSDRTRTDVKSDIKVNKVISTEKPQALKDHNNNIKDNQVVKQNIKRRINQKRKPITNTSRDIVLARREAQSKHGKSASKQNTSAASLARRGDPDLSSREISQRVRELRSKTGSTSKQGNGKCRPCGPNKNGSKLNIADASWKVGKSETDSGQTVTGTQANRSLKTTGNEASTCRTVTGTQYMGAEVTGQFCQDKPKYKQPIRASVTTTTSGNKVTGNEVGRS... | Function: Required for alpha-carboxysome (Cb) assembly, mediates interaction between RuBisCO and the Cb shell. The protein is probably highly flexible (Probable). The C-terminal repeats act as the encapsulation signal to target proteins to the Cb; they are necessary and sufficient to target both CsoS2 and foreign prote... |
P45689 | MADVTGIALGMIETRGLVPAIEAADAMTKAAEVRLVGRQFVGGGYVTVLVRGETGAVNAAVRAGADACERVGDGLVAAHIIARVHSEVENILPKAPQA | Function: The major shell protein of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, ccbL-ccbS) is sequestered . Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome . The shell probably limits the diffusion of CO(2) into and out of the c... |
P45690 | MATTHGIALGMIETRGLVPAIEAADAMTKAAEVRLVGRSFVGGGYVTVMVRGETGAVNAAVRAGADACERVGDGLVAAHIIARVHSEVEIILPETPEDSDSAWCIANLNS | Function: One of shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, ccbL-ccbS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome (By similarity). The shell probably limits the diffusion of CO(2) into and ... |
Q31HD1 | MSTEYGIALGMIETRGLVPAIEAADAMTKAAEVRLVSREFVGGGYVTVLVRGETGAVNAAVRAGADACERVGDGLVAAHIIARPHKEVEPVLALGNSSPDRS | Function: One of shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, ccbL-ccbS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome. The shell probably limits the diffusion of CO(2) into and out of the carbo... |
D0KZ73 | MNNIDLRVYSFIDSLQPQLASYLATSSQGFLPVPGDACLWIEVAPGMAVHRLSDIALKATNVRLGEQVVERAFGSMEIHYRNQSDVLASGEAVLREINHAQEDRLPCRIAWKEIIRAITPDHATLINRQLRKGSMLLPGKSMFILETEPAGYIVQAANEAEKAAHVTLIDVRAFGNFGRLTMMGSEAETEEAMRAAEATIASINARARRAEGF | Function: Part of the carboxysome shell, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered. It may control transport of RuBisCO reactants in and out of the carboxysome (By similarity). In an E.coli expression system not absolutely necessary, its presence leads to fewer d... |
Q31HC6 | MIELRTYVFLDSLQPQLASYMATASMGFLPVPGDSSLWIEVAPGMAVHRLSDIALKASNVRLGQQIVERAYGSMVIHHRDQSDVLEAGQRILDHLQTREYDRQQCVVMWNEIIRGVTADHATLINRDNRKGSMILPGQSMFIMETEPAGYIIYAANEAEKAADVTLVEARAVGAYGRLVMCGKEGDITEAARAANEALKRLTCRS | Function: Part of the carboxysome shell, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered. It may control transport of RuBisCO reactants in and out of the carboxysome.
Sequence Mass (Da): 22682
Sequence Length: 205
Domain: Contains 2 BMC domains, trimerizes in a stagger... |
Q7V2D3 | MEPTSSLNRGDRKKGSSLVTGSEVQSQSNGASCFITTDSEKSLVSRQASQVEQIELRTYVFLDSLQPQLAAYMGTVSRGFLPIPGDSCLWMEVSPGMAVHRVTDIALKASNVRLGQMIVERAFGSLALYHKDQSTVLHSGDVVLDAIGSEVRKRTKPSTSWTEVICAITPDHAVLINRQNRSGSMIQSGMSMFILETEPAGYVLKAANEAEKSANITIIDVKAVGAFGRLTLAGKEGDVEEAAAAAIRAIDQISNY | Function: Part of the carboxysome shell, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered (Probable) . It may control transport of RuBisCO reactants in and out of the carboxysome (Probable). There are estimated to be 6 CsoS1D hexamers per carboxysome .
Sequence Mass (Da... |
G5EBM1 | MVLKTIEDNCKSQFDDDLVEDFNNFQTTSSMSSSTTISTEDFNTIEIESTFEICRSGSYTEEPILGENDEFLIDFEMERFLKFLKDKTKQVEKRKEPFSQKEIYAVFQRRIKSELCIETVKKKFQPLLPNAIQTCEFDEETMIRMIYGAGIRIDSVDFWNRFTSKATISLDCYSRLISYSSDSLTLSGTHRSGFTYHWISTPPVTYHRTENKDPNIQEPSPVEFLDVQSSLGSSMKPPILDKPTKLDDPAETRHDCSYSLEEYDSQSRMPRTDAKKSNHKHKYCYEMNSNPRGTVLILSNENFKNMERRVGTKQDEVNLT... | Function: Cysteine protease which, in vitro, cleaves itself and caspase ced-3 into their mature active forms . Also cleaves, in vitro, inactive caspase csp-2 isoform b . Required maternally to induce apoptosis in a subset of cells fated to die during embryogenesis, mostly independently of the ced-9, ced-4 and ced-3 can... |
P23093 | MKKCTILVVASLLLVNSLLPGYGQNKSIQAQRNLNELCYNEGNDNKLYHVLNSKNGKIYNRNTVNRLLADAPEGKKNEKKNEKIERNNKLKQPPPPPNPNDPPPPNPNDPPPPNPNDPPPPNPNDPPPPNANDPPPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPPPPNPNDPAPPNANDPPPPNPNDPAPPQGNNNPQPQPRPQPQPQPQPQPQPQPQPQPRPQPQPQPGGNNNNKNNNNDDSYIPSAEKILEFVKQIRDSITEEWSQCNVTCGSGIRVRKRKGSNKKAEDLTLEDIDTEICKMDKCSSI... | Function: Essential sporozoite protein . In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands . In the vertebrate host, required for sporozoite migration through the host dermis and infection of host hepatocytes . Bin... |
P06915 | MKKCTILVVASLLLVNSLLPGYGQNKIIQAQRNLNELCYNEGNDNKLYHVLNSKNGKIYNRNTVNRLLPMLRRKKNEKKNEKIERNNKLKQPPPPPNPNDPPPPNPNDPPPPNPNDPPPPNPNDPPPPNANDPPPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPPPPNPNDPAPPQGNNNPQPQPRPQPQPQPQPQPQPQPQPQPRPQPQPQPGGNNNNKNNNNDDSYIPSAEKILEFVKQIRDSITEEWSQCNVTCGSGIRVRKRKGSNKKAEDLTLEDIDTEICKMDKCSSIF... | Function: Essential sporozoite protein . In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands . In the vertebrate host, required for sporozoite migration through the host dermis and infection of host hepatocytes (By s... |
P08672 | MKNFNLLVVSSILLVDLFPTNCGHNVHFSRAINLNGVSFNNVDASSLGAAQVRQSASRGRGLGENPKDEEGADKPKKKEEKKVEPKKPRENKLKQPPAGDGAPEGDGAPAAPAGDGAPAAPAGDGAPAAPAGDGAPAAPAGDGAPAAPAGDGAPAAPAGDGAPAAPAGDGAPAAPAGDGAPAAPAGDGAPAGNRAGGQPAAGGNQAGGNRAGGQPAAGGNQAGGNRAGGQPAAGGNQAGGQPAAGGNQAGAQAGGNQAGAQAGGANAGNKKAGEAGGNAGAGQGQNNEAANVPNAKLVKEYLDKIRSTLGVEWSPCSVTC... | Function: Essential sporozoite protein (By similarity). In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (By similarity). In the vertebrate host, required for sporozoite migration through the host dermis and infec... |
Q7K740 | MMRKLAILSVSSFLFVEALFQEYQCYGSSSNTRVLNELNYDNAGTNLYNELEMNYYGKQENWYSLKKNSRSLGENDDGNNEDNEKLRKPKHKKLKQPADGNPDPNANPNVDPNANPNVDPNANPNVDPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNVDPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNKNNQGNGQGHNMPNDPNRNVDENANANSAVKNNNNEEPSDKHIKEYL... | Function: Essential sporozoite protein . In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (By similarity). In the vertebrate host, required for sporozoite migration through the host dermis and infection of host he... |
P04922 | MKNFILLAVSSILLVDLLPTHFEHNVDLSRAINVNGVSFNNVDTSSLGAAQVRQSASRGRGLGEKPKEGADKEKKKEKEKEKEEEPKKPNENKLKQPEQPAAGAGGEQPAAGAGGEQPAAGAGGEQPAAGARGEQPAAGAGGEQPAAGAGGEQPAAGAGGEQPAAGAGGEQPAAGAGGEQPAAGARGEQPAAGAGGEQPAAGAGGEQPAAGARGEQPAAGAGGEQPAPAPRREQPAPGAVAGDGARGGNAGAGKGQGQNNQGANVPNEKVVNDYLHKIRSSVTTEWTPCSVTCGNGVRIRRKGHAGNKKAEDLTMDDLEV... | Function: Essential sporozoite protein (By similarity). In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (By similarity). In the vertebrate host, required for sporozoite migration through the host dermis and infec... |
P13815 | MKKLSVLAISSFLIVDFLFPGYHHNSNSTKSRNLSELCYNNVDTKLFNELEVRYSTNQDHFYNYNKTIRLLNENNNEKDGNVTNERKKKPTKAVENKLKQPPGDDDGAGNDAGNDAGNDAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNDAGNAAGNAAGNAAGNAAGNAAGNDAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNDAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNAAGNEKAKNK... | Function: Essential sporozoite protein (By similarity). In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (By similarity). In the vertebrate host, required for sporozoite migration through the host dermis and infec... |
P26694 | MMRKLAILSVSSFLFVEALFQEYQCYGSSSNTRVLNELNYDNAGTNLYNELEMNYYGKQENWYSLKKNSRSLGENDDADNGDADNGDEGIDENRRHRNKEGKEKLKKPKHNKLKQPGNDNVDPNANPNVDPNANPNVDPNANPNVDPNANPNVDPNANPNVNPNANPNVDPNANPNVNPNANPNVNPNANPNVNPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNRNNEANGQGHNKPNDQNRNVNENANANNAGRNNNNEEPSDKHIEEFLKQIQNNLST... | Function: Essential sporozoite protein (By similarity). In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (By similarity). In the vertebrate host, required for sporozoite migration through the host dermis and infec... |
P08677 | MKNFILLAVSSILLVDLFPTHCGHNVDLSKAINLNGVNFNNVDASSLGAAHVGQSASRGRGLGENPDDEEGDAKKKKDGKKAEPKNPRENKLKQPGDRADGQPAGDRADGQPAGDRADGQPAGDRAAGQPAGDRADGQPAGDRADGQPAGDRADGQPAGDRADGQPAGDRAAGQPAGDRAAGQPAGDRADGQPAGDRAAGQPAGDRADGQPAGDRAAGQPAGDRADGQPAGDRAAGQPAGDRAAGQPAGDRAAGQPAGDRAAGQPAGNGAGGQAAGGNAGGGQGQNNEGANAPNEKSVKEYLDKVRATVGTEWTPCSVTC... | Function: Essential sporozoite protein (By similarity). In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (By similarity). In the vertebrate host, required for sporozoite migration through the host dermis and infec... |
P50461 | MPNWGGGAKCGACEKTVYHAEEIQCNGRSFHKTCFHCMACRKALDSTTVAAHESEIYCKVCYGRRYGPKGIGYGQGAGCLSTDTGEHLGLQFQQSPKPARSVTTSNPSKFTAKFGESEKCPRCGKSVYAAEKVMGGGKPWHKTCFRCAICGKSLESTNVTDKDGELYCKVCYAKNFGPTGIGFGGLTQQVEKKE | Function: Positive regulator of myogenesis. Acts as cofactor for myogenic bHLH transcription factors such as MYOD1, and probably MYOG and MYF6. Enhances the DNA-binding activity of the MYOD1:TCF3 isoform E47 complex and may promote formation of a functional MYOD1:TCF3 isoform E47:MEF2A complex involved in myogenesis (B... |
O74369 | MSVEKAPELRVLSFNCWGLRFVSKYRTERLKAVGEKLAKCDYDIVLLQEVWSIYDFQEIRNLVSCNLVYSRFFHSAAMGAGLAMFSKFPIIESSMNKYPLNGRPQAFWRGDWYVGKGVATASLQHPSGRIISLFNTHLHAPYGKGADTYLCHRLSQAWYISKLLRAAVQRGHIVIAAGDFNIQPLSVPHEIITSYGLVNDAWLSVYPDQVEHPPNRFSMNDKELVEIAGTTCDSRLNTWRENISSKDMDDFVAKRLDYVFHSPSTCEAKNAKVVFLERVPKLDCSYSDHFAIETVLSIKLQPIPVQETRVSYSIIDDTLG... | Function: Inositol phosphosphingolipids phospholipase essential for the coordination of cell wall formation. Responsible for the hydrolysis of the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol phosphorylceramide (M(IP)2C).
Location Topo... |
O85043 | MKIMQVEKTLVSTNRIADMGHKPLLVVWEKPGAPRQVAVDAIGCIPGDWVLCVGSSAAREAAGSKSYPSDLTIIGIIDQWNGE | Function: Probably forms vertices in the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered. Has been modeled to induce curvature upon insertion into an otherwise flat hexagonal layer of major carboxysome subunits (Probable). A minor shell protein, only 12 pe... |
Q9BPE1 | MLCLPVFIILLLLASPAAPNPLEKRIQSDLIRAALEDADMKTDEREIVNIIDSISDVAKQICCEITVQCCVLDEE | PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or 'C1-C4, C2-C3', since these disulfide connectivities have been observed for conotoxins with cysteine framework V (for examples, see AC P0DQQ7 and AC P81755).
Sequence Mass (Da): 8314
Sequence Length: 75
Domain: The cysteine framework is V (CC-CC).
Sub... |
Q1A3Q7 | MLCLPVFIILLLLASPAAPKSFETKVQSDLTRTDGNMETEENLGEVRKVYCCLGVRDDWCCAGQIQI | PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or 'C1-C4, C2-C3', since these disulfide connectivities have been observed for conotoxins with cysteine framework V (for examples, see AC P0DQQ7 and AC P81755).
Sequence Mass (Da): 7448
Sequence Length: 67
Domain: The cysteine framework is V (CC-CC).
Sub... |
P81755 | MRCFPVFIILLLLIASAPCFDARTKTDDDVPLSSLRDNLKRTIRTRLNIRECCEDGWCCTAAPLTGR | Function: Epsilon-conotoxins act at presynaptic membranes, blocking the calcium channels or G protein-coupled receptors. Causes hyperactivity upon intracranial injection into mice. Causes dorsal fins drooping in fish.
PTM: O-glycan consists of the disaccharide Gal-GalNAc.
Sequence Mass (Da): 7587
Sequence Length: 67
Do... |
P58848 | FCCPFIRYCCW | Function: Causes dorsal fins drooping in fish. No effect is observed when injected into mice.
Sequence Mass (Da): 1441
Sequence Length: 11
Domain: The cysteine framework is V (CC-CC).
Subcellular Location: Secreted
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P0DJL6 | ECCHRQLLCCLRFV | Function: Interacts selectively with the G-coupled somatostatin sst3 receptor (SSTR3). It displays antagonist property for SSTR3 (Ki=1.5 uM). Other somatostatin receptors are also affected, but with a lower selectivity: SSTR5 (Ki=80.2 uM), SSTR1 (Ki=169 uM), SSTR2 (KI=159 uM), SSTR4 (Ki>100 uM).
PTM: Contains 2 disulfi... |
Q9U6Z6 | MRCLPVFVILLLLIPSAPCVDAHPKTKDDMPLASFHDNAKGTLQRFWKKRGCCPKQMRCCTLG | Function: In vivo, low levels of the peptide injected into male specimens of the Siamese fighting fish causes an immediate aggressive display in this fish in response to their reflection when placed in a mirrored aquarium; High levels of the peptide suppressed this behavior. No effect is observed when injected into mic... |
A0ST41 | MVKRIEADNLFELTAELVSASSKLHKFLDQKNLPQPSFDAPAPSVALNSANKPYYDARSAIVEAAEQLIRLVRGPRDTLLALSFEHCATASMQVVFKYKFANHIPLHGSTTYSKIAEAVGDGVTTALVERTIQHCASFGLFETIPGAMLLQCYLVLLVTDPDLEAWMYLSAVIAYPAGAAIPKAVEQYGVSHEADESGYGASIGRKIAQFQRFREPDGKKDHEMFARAMRGIAAGGAYDFRHAVDGGYPWHLLAEGAGHLVVDVGGGPGHVAMALAEKYPSLRFQVQDLPETVQVGAKNCPEHLKSRVSFQSHDFFTSQP... | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin . The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydr... |
Q2I0M6 | MMQFQRDLEASLEAVSANAQELLKSLKSRKDVQDLNASLPKDPLDNCDAQTQAARAQLAEAATRILQLSIRPQEYLEHLQNGYQHLTCFRWLVELNILDHLPHSGTISYTDLARKASVPPMQLRSICRMAICNGFLEEPEANQVRHSRISALFARDESYLGWARWMVNYSVPAAYKLSDATRSWGETVAKDQTAFNLGMDVKVPFFDHLRQTPAMKDAFAAYMRNVTSNATWGLQHAVTGFDWASLPRGAKVVDVGGSLGHGSIAIAKEHTHLTFVIQDLPETVAGARKEMAQNDKIEASVKSRITFQEHDFFGPQTVKD... | Function: Dual O-methyltransferase/FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin . The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces activ... |
A0ST42 | MAPPITDDDLDGLKQPYVTFSSGSASPPRSTAEAMDFEEQILEAIKSDAFLVDWIGEDDKGNPQNLPYWRKWVITMSLALYALSTTFSSSVFGAATHVLAEEFALPAETVVLGCTSLFMVGFATGPIFWGPFSEAFGRTRPLLAGYLGFAVLQLPIADARSLTSICILRFLGGFFGAAPSSILSGILADIWSPRERGFAMPTVGAFLTIGPILGPLIGSVLVQSVLGWRWIANVVAIASFLIALSTFPFLPETYTPLLLARRAERMRHMTRNWAYRSKSEEAQSSIGDFAERYLLRPARMLALEPILLMMTLYVSVSFGL... | Function: MFS transporter; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin . The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydroxyl... |
A0ST43 | MGSYFSLKNSDLHPSCIALPRSAEEVSKAVRTLSLGAHKWEGQCQFGVRGGGHTPFKGAASTDNGIVLDLLHMPSAGISPDYETITVSPSTTWDLVYEVLDAHNRSTLGTKVAGIGVGGASTSCGVSYFSPRYGYICDMVENWEVVLATGDIVNANANENADLWKALRGGINNFGIVTAVTLKAFEQGPFWGGQTFHSIETRQEHFKNHAKLASAHPYDPYAHYINTLVLANGGHWFIGNSIQYTKSDPPVAEPEVFKPFLKTERTPIFPGLPEDTLRVDNVTSFSREYAANTLYPQRWQFACISFAPDADFMETFFQMA... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin . The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as ... |
A0ST44 | MADSLVLLTGATGFIGFRILVELLRQGYSVRAVIRSAAKGQWLESRLTAVMKGSDYKDRFQTTIVADFVTDGAFDQAAENTSYIIHVASPIVSSDNPDDWEHDFKRVAVKGSIGVLEAAKRSGTVRRVVITSSMVGLFSPKALFAEPSEVPLNAESRIPEMEPPYAHKMLAYQAGKIASINSAEAWIKHEKPAFDLIHMHPSFVTGRDDLATTREDLRKFSSNWHSMQIVLGHKNPIGKPILTCHNDDVARCHVSALDPKVAGNQSFLISCSPEDGSEWDNVKKIVQREFPEAVAQGVLPNDGHMPTVNKGVRFDVRKTE... | Function: Ketoreductase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin . The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydroxyl r... |
A0ST45 | MASSNRRVLVNGGGPAGAVTAFWLAKGGFEVVVTERSMSRPYGQGVDVMGRAVDIIKKMGLEQRIRDSTTGEAGLTVVDDQGEDVAPPLGTAPIEGGTASVTQEIEIMRRDLTKIFVDAAEALPNVTFRYGCTVDEVQQHEKSITAVLSDTGDPEDFTAIIGADGLGSAIRKLTFDPEINRRSVSPTNTYVAFFSIPGDPKYVSSAARRLSPAPSLCPRSELCDSEGGHDANAYDTPVGKLQHANKGRGILVRPIDKKGTQRSCYLMSQSDSQELAQVARTGSQEDQKALLDNRFREFTGPLGKRAVEGMHSADDFYFTR... | Function: Monooxygenase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin . The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydroxyl r... |
A0A2G5I8W0 | MTSTITTTETLQDAVPFVAPPSPPEDTSNKELPEKPYYDVEFNYRLDPRDGGDEVIWGGTVGLMRRKYETRTVRINNERGNEHNFNLDTHGFAWVKHKTSVTEFADYLAIRQGPYFGEVAEMLKRVTGATKVHVIGHLHRSLNYNDTTEEEKNAPDMTMTKGQTPGRFVHVDQSYQGAVRRLYLDLPQEEARRLEKTRWAIINVWRPVRKVTNEPLAVCDARSVREDELFNTLHLVPMRWPDAAPQENQMWAVAPPKTPTQHKWHYVSGMTEDEALLIKMFDSKKDGTARRVPHSSFPTPDDFGEPRASTETRCFVFWED... | Function: Hydroxylase/desaturase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin . The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the h... |
Q8WYA6 | MDVGELLSYQPNRGTKRPRDDEEEEQKMRRKQTGTRERGRYREEEMTVVEEADDDKKRLLQIIDRDGEEEEEEEEPLDESSVKKMILTFEKRSYKNQELRIKFPDNPEKFMESELDLNDIIQEMHVVATMPDLYHLLVELNAVQSLLGLLGHDNTDVSIAVVDLLQELTDIDTLHESEEGAEVLIDALVDGQVVALLVQNLERLDESVKEEADGVHNTLAIVENMAEFRPEMCTEGAQQGLLQWLLKRLKAKMPFDANKLYCSEVLAILLQDNDENRELLGELDGIDVLLQQLSVFKRHNPSTAEEQEMMENLFDSLCSC... | Function: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Participates in AID/AICDA-mediated somatic hypermutation (SHM) and class-switch recombination (CSR), 2 processes resulting in the production of high-affinity, mutated isotype-s... |
Q6IP59 | MEDDGKSPPDSAYGEPKKYDPNFKGPIQNRGCTDILCCILIVLGIIAYVAVGIVAWTYGDPRKVIYPTDSKGQFCGQVGTPNEKKPFLFYFNIMKCASPLVLLQFQCPTTQICVENCPDRFLTYLSVATTQQNFDYYKQFCRDGFNNFTKSPVEVLRDRDCPAMITPSKPFTRRCFPAINTQKGVVMVGNSTTFDDGRGDKQRNVTDLLEGAKKANVVLEARQVAMKIFEDYTVSWYWIIIGLIIAMVISLIFVVLLRFLAGIMVWVMIVLVIAVMGYGIFHCYMEYARLKGQSGSDVTLKDIGFQTDIRVYLHLRQTWL... | Function: Choline/H+ antiporter, mainly in mitochodria. Also acts as a low-affinity ethanolamine/H+ antiporter, regulating the supply of extracellular ethanolamine (Etn) for the CDP-Etn pathway, redistribute intracellular Etn and balance the CDP-Cho and CDP-Etn arms of the Kennedy pathway.
Catalytic Activity: choline(o... |
Q7T2B0 | MGKKKQEEEQNSSEYGAPAQYDPTFNGPIHKRSCTDIICCVLFMLVITGYMVVGILAWLYGDPRHVLYPRNSTGMFCGIGQNQNKPSVLYFDILKCATATNIMAAALQGLQCPTTQVCVSSCPSGFWALSPLAYLPNAKPADYFQQELCVPSLQLKDTTYTVMEIINKELCPYYYTPTTSVLDRCLPSLGGSAYNPSNIPANFSLPGLSINQTLSTIANATSDLTNSFNMKDVGLRIFEDFAKTWQWIVAGLVIAMVVSVLFLLLLRFTAPVLIWILIFGVLAVGAFGIWYCYNDYMSLASSNLTFSNVGFTTNVQVYLQ... | Function: Choline transporter that seems to play a role in the choline-acetylcholine system and is required to the efferent innervation of hair cells in the olivocochlear bundle for the maintenance of physiological function of outer hair cells and the protection of hair cells from acoustic injury. Also described as a t... |
Q53GD3 | MGGKQRDEDDEAYGKPVKYDPSFRGPIKNRSCTDVICCVLFLLFILGYIVVGIVAWLYGDPRQVLYPRNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLQCPTPQVCVSSCPEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNMTVITSLQQELCPSFLLPSAPALGRCFPWTNVTPPALPGITNDTTIQQGISGLIDSLNARDISVKIFEDFAQSWYWILVALGVALVLSLLFILLLRLVAGPLVLVLILGVLGVLAYGIYYCWEEYRVLRDKGASISQLGFTTNLSAYQSVQETWLAALIVLAVLE... | Function: Choline transporter that plays a role in the choline-acetylcholine system and is required to the efferent innervation of hair cells in the olivocochlear bundle for the maintenance of physiological function of outer hair cells and the protection of hair cells from acoustic injury (By similarity) . Also describ... |
A5PMW0 | EPRKFDPTFRGPVYNRGCTDVLCCVLFVIVILGYIALGTVAWIHGDPRKVIYPTDSTGQFCGQKGTPNAKKAILFYFNILKCASPAVLINLQCPTTQMCVSKCPDRFATYTDMQLLYRFNKSHWDYYKQFCKPGFNNPQKSVAQVLRDEDCPSMIVPSRPFLQRCFPDFITRNGTLTVANKTAFKDALDTARSVTELRDAANGITSIHEAKEVGMKIVEDYASCWYWIVIGLFIALVISLIFILLLRFTAGFLLWFIIFAVILLVAYGIWHCYWEFAVLRETPGADVTISDIGFQTDLHVYLQLSQTWLVFMVTLGLTEA... | Function: Choline/H+ antiporter.
Catalytic Activity: choline(out) + n H(+)(in) = choline(in) + n H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79471
Sequence Length: 702
Subcellular Location: Cell membrane
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B0S5A7 | GCTDVLCCVIFVIVILGYIVLGTVAWMHGDPRKVVYPTDSYGQFCGQQETPNANKAILFYFNILQCANPSVLINLQCPTTQLCVSKCPDRFATYIDMQYSYRRNKGSWEYYKQFCKPGFNNPDKPISQVLRDEDCPSMIVPSRPFLQRCFPDFITRNGTLTVANQTSFKDGHGKIRSVVDLRDAANGITSLLDAKEVGTKIFEDYASSWFWILIGLVISMLVSLVFILLLRFTAGVLFWLVIFGVIAAVGYGIWHCYWEYSSLKGKPDSDVTISDIGFQTDFRVYLQLSQTWLIFMTSLAVIEAIIILVLIFLRNRVRIA... | Function: Choline/H+ antiporter.
Catalytic Activity: choline(out) + n H(+)(in) = choline(in) + n H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79503
Sequence Length: 700
Subcellular Location: Cell membrane
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Q8NCS7 | MNDTEKPADTPSEEEDFGDPRTYDPDFKGPVANRSCTDVLCCMIFLLCIIGYIVLGLVAWVHGDPRRAAYPTDSQGHFCGQKGTPNENKTILFYFNLLRCTSPSVLLNLQCPTTQICVSKCPEKFLTYVEMQLLYTKDKSYWEDYRQFCKTTAKPVKSLTQLLLDDDCPTAIFPSKPFLQRCFPDFSTKNGTLTIGSKMMFQDGNGGTRSVVELGIAANGINKLLDAKSLGLKVFEDYARTWYWILIGLTIAMVLSWIFLILLRFIAGCLFWVFMIGVIGIIGYGIWHCYQQYTNLQERPSSVLTIYDIGIQTNISMYFE... | Function: Choline/H+ antiporter.
Catalytic Activity: choline(out) + n H(+)(in) = choline(in) + n H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81694
Sequence Length: 719
Subcellular Location: Cell membrane
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Q5RJI2 | MARKRKPPSSQGDPRRYDPDFQGPTAKRTCTDVLCCLIFLLFILGYVLLGLLAWAHGDPRKMAYPTDSQGHFCGQKGTPNENKTVLFYFNIFRCTSPSMMLRLQCSTTQICVSRCPERFLTYLDMQFLNKEDKNYWEYYRQFCKAKAKPVETLRDLLISGDCPLAVYPSRPFLQRCIPDLSALNGTWTPGSRMKFEDGSGQTRTMLEFREAANGISDLINARTIGLKLLEDYATSWKWILIGLTVAMALSWTFLILLRFTAGFLFWFFIFGVLGIIGYGIWYCFLEYSSIQQRPQSTFWMYGFGIQRRVNMFFHLKETWF... | Function: Choline/H+ antiporter.
Catalytic Activity: choline(out) + n H(+)(in) = choline(in) + n H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81429
Sequence Length: 710
Subcellular Location: Cell membrane
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Q06686 | MNMGGSSSTAAKKATCKISMLWNWYTIDTCFIARSWRNDTKGKFAGSCIGCFALVVVAQWLTRFSRQFDVELLKRQKIKHLASYSPEEYVVKCGEEDAKSDIEELQGFYNEPSWKTTLISLQKSFIYSFYVWGPRRLNEPEDDLLKKVLSCCTLITPVDLYPTFLDHMIRVTIFVLQWGLSYIIMLLFMYYNGYIIISCLIGAIVGRFIFCYEPLGSLGANGSAQGTVSYDKESDDRKCCL | Function: Required for high affinity copper (probably reduced Cu I) transport into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27534
Sequence Length: 241
Subcellular Location: Cytoplasmic vesicle membrane
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J9VLN4 | MDMGNMGMGMGMGMDSGHNHSHMNMGSGHGADSGHACRISMLLNFNTVDACFLSPNWHIRSKGMFAGSIIGIFFLCVLIELIRRLGREFDRWLVKRAGVNSTCGELSSVAEYGKDGAQGGAVVRVAPRFRYVPSWPHQILRGFIYGSQFTAAFFVMLLGMYFNVIVLIFIFLGQTVGYMLFGRDTCGGGFDFGAQGRCC | Function: Required for high affinity copper (probably reduced Cu I) transport into the cell (By similarity). Plays a role in fungal pathogenesis during host infection .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21810
Sequence Length: 199
Subcellular Location: Membrane
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O43246 | MARGLPTIASLARLCQKLNRLKPLEDSTMETSLRRCLSTLDLTLLGVGGMVGSGLYVLTGAVAKEVAGPAVLLSFGVAAVASLLAALCYAEFGARVPRTGSAYLFTYVSMGELWAFLIGWNVLLEYIIGGAAVARAWSGYLDSMFSHSIRNFTETHVGSWQVPLLGHYPDFLAAGIILLASAFVSCGARVSSWLNHTFSAISLLVILFIVILGFILAQPHNWSADEGGFAPFGFSGVMAGTASCFYAFVGFDVIAASSEEAQNPRRSVPLAIAISLAIAAGAYILVSTVLTLMVPWHSLDPDSALADAFYQRGYRWAGFI... | Function: Involved in the transport of the cationic amino acids (arginine, lysine and ornithine).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68268
Sequence Length: 635
Subcellular Location: Membrane
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Q8BLQ7 | MARGLPSTACLARFCQKLNRLKPLEESSMETSLRRCLSTLDLTLLGVGGMVGSGLYVLTGTVAKDMAGPAVLLSFLVAAVASLLAALCYAEFGARVPRTGSAYLFTYVSMGEIWAFLIGWNVLLEYLIGGAAVARAWSGYLDAIFNHSIRNFTESHLGVWQVPFLAHYPDFLAAGILLVASAFVSCGARVSSWLNHTFSAISLIVILFIIVLGFILARPHNWSAEEGGFAPFGFSGILAGTATCFYAFVGFDVIAASSEEAKNPRWAVPMAIAISLSLAAGAYILVSTVLTLMVPWHSLDPDSALADAFYRRGYSWAGFI... | Function: Involved in the transport of the cationic amino acids (arginine, lysine and ornithine).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68350
Sequence Length: 635
Subcellular Location: Membrane
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O94722 | MSFFSAAKQSLGNSLIKLGTSMAQNSQGPVDDSSLSQLENLLPPLQILTARAAMAAMNMSNDTSMSGMNMTNSTTPMSGMNMTNSTTSMSGMNMSNSTTSMSGMNMTNTTTTAKASSCKLSMYWNWYTIDACFITKHWHITSKHMFVGSIFGIIFMMMALELVRRGQREFDRWCVRRFSPASNSCCHSGAPVHSGPSMALRIFLHFLRSCFYLVQYIVAYIAMLLAMYYNGYVILFLFCGTFFGYFLFGADTISTKASSSVQTKTIVQVADEKHEHDSSQYSDTTPTTE | Function: Required for high affinity copper (probably reduced Cu I) transport into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32020
Sequence Length: 289
Subcellular Location: Membrane
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Q9P7F9 | MSLSKMSMSGMSGMGMGSSSNSSAATCRMSMLWNWYIHDSCFLAKSWHINTGNKFAGSIIGIFFFAVAIEGLSLVQRMFDRWIVAHSNGKTLSGPLRIFFPSSTVHVTVWQQLIRAAMYSSFYLSATILMLIVMSFNGYAILFGFVGAWIGFFLFASDTYGTPSTGTGCCESR | Function: Required for high affinity copper (probably reduced Cu I) transport into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19012
Sequence Length: 173
Subcellular Location: Membrane
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Q9USV7 | MNHGGNSTMRHCSMKMTFNTDYDNLCIVFKSWHIGNLSQFLLSLLAIAILGYLFERLRSFTSLKETEFQRGYAGQQSEGLLTHHSKSLKSGRPFRLCALYAVQLVFSYFLMLVAMTYNAYVILAIAIGAAFGYRRSHCDTVQTVGLCH | Function: Mobilizes stored copper from the vacuole to the cytoplasm under conditions of copper limitation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16747
Sequence Length: 148
Subcellular Location: Vacuole membrane
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Q4WCY0 | MNMDHSSHSTMSSSSSMTMTMVFTNSHDTPLFSSAWTPSSSGAYAGTCIFLVVLAIINRCLVAFKASMEHYWFATHLNRRYIAIAGKSSEAGRIDTDPDAKVASLVTAQGVEESVKVVRRVSREPIPWRFSVDLPRAAIFLCITGVSYLLMLAVMTMNVGYFCSVLAGAFLGELAVGRYIQWNEHDH | Function: High-affinity copper transporter of plasma membrane that mediates copper uptake under low copper conditions . The mechanism driving the transmembrane transport of copper has still to be determined (Probable). Acts as a potential virulence factor .
Catalytic Activity: Cu(2+)(in) = Cu(2+)(out)
Location Topology... |
Q32NV1 | MCEEGETYCPEVKDAKQAKSLGKICMKCKESSAALLIRAGDAFCKSCFKEYFVHKFRATLGKNRVIYPGEKVLLAYSGGPSSSAMVRQVQEGLSRDAPKKLRFVPGILFIDEGTACGMSWEERQQILSEICSVLQQTKIPFHIVSLEQVFSLPGSVLQRGAPEQRPNYKEEVDRFLVQEREQGDAGCSEMLERLEVTDSDSPGSSDKMYQSTCSRPPDMHTQKLKQLFASAKTLTAKQQLLHTLRSHLILHIARTCGYSKVMTGESCTRLSIRLLSNVSLGRGAFLPLDTGFCDSRYGDVDIIRPMREYSSKEIAYYNRF... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with ctu1/atpbd3 that ligates sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position.
Sequence Mass (Da): 57315
Sequence Length: 512
Path... |
A6QYX4 | MTLDSRYGGEVYGGSKVVKRMEKYRPQNAPKNRQRKLLLPLSYGISSSTLLHILNLQLERQISSGLGRRAYDIHVLNIGTCEQSDSHRLGLFREAYPLHTYTQVPLHSIFKHDTTIKDVISEYGGPEFADDPSKTDQERLDIFRLSLSTATARADIDGILLTRLVVAIAKEQDCDGILWGDSDTRLASKALSNVAKGRGFSVPWDVCDGMSPWGIQFNFPMRDLFKFELSTYASLALPKSLNVVDSERPSVDNLSNKNMSIEDLLAHYVETQGQKYPGVMANIVRTINKLQPQSADTDHKCMLCGMPVDYSGEDPAIIGG... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is... |
A0NEF7 | MCSIVEDDFGDEGGAHAMKEDTPQPELGGNELCRKCNTEQAVLKLNQKEPQCRVCFLNYVRHKFRASLGSTKIVRRGSRVLIILTGEPANVTLLDMVRFGLEQDAFKQLRIVPVLLYVDDDFVGNTSEARLQQLAERLQVFKQFESFPAYYTVCGSSRHVALTFDGAFSPAGFEQDEARLLQVLDAVRSVSSKQDLLEQVRKQTYRQIGHALQCAYVFLSDIGVDLAKTLLSNVALGRGCSLAQDVAFCDDRYNTVKLVRPIRDLNPDEVSNYLQYSEQPLLSYSPAKHFEDKPSLQNLTAKFIDNLMQSFPSTVSTVYR... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6/CTU1 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Sequence Mass (Da): 46861
Sequence Length: 417
Pathwa... |
O65628 | MACNSSGCESGCYDREKDNGSKIVDDAVSGGGNHESVCVKCKCNAPMTFGDGGFDDGRFCADCFRNNVFGKFRLAVTSHAMITPSDNVLVAFSGGSSSRVSLQFVHELQIKALKNYEASRDRSLPVFGVGVAFVDETAAFPALSTEMIDAIEWVRYTVSCLSPPAKDLHVVPVESIFGSDSLDARDRLLKLLDSVPDDTGKEDLLLHLKMLSLQKVAAENGYNRLVLGSCTSRIASHVLTATVKGRGYSLSADIQHVDARWKVPIVLPLRDCVRLEITRLCLLDGLKTVELACRSQCGINDLVSSFVALLQEENPSRECT... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6/CTU1 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Sequence Mass (Da): 50399
Sequence Length: 458
Pathwa... |
Q75BK0 | MKCKRCTTSEGCLVSRNETFCGECFSRFVLLKFRKQMMMDEYCQQVFKVLYADKHRTAVEADEQNKRSVVLVPLSLGSSSLAMLDLLNQTLSEQRAAHNRTGFQVKVVLCGFSADMDELKRLAESLQTERLAMNSDCIKLYLLDLDRSFSTCEIHKLLLANDNHGSRKIATRENATLSSILDQFSRRSSRDDMLWFARQHLIKKFASQHQVKVIMWGHSVTRLADEVMSLVIKGRGAQIAATLDSTGMDVEYGALFKNLYPLRDVLLSEIDAYCSLSKLQRYIYNYSLQGSLFIKSQDEAAQANRAVPMAKNMTINELTR... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is... |
A1CBI6 | MPGKELTDPCVDCADAEAILTVRCRRLCQDCYARFVNFKVFKRMENYRLRRNMSRTGPCKLLLPLSYGTSSSVLLHILNAQIQHERAKSHPSPGFELHVLVIEPSTVSTSSPPHDEGFDLLQQTFPSHSFTRVSLHNVFELDPSIQDVLSQFSSEGFTDDATMSDKDRLDAFRASITTATSRVDVDYILITRLVVAFAKKIECRGVVWGDSDTRLAAKTLANVAKGRGSAITWQVCDGMSPFGLEFSFPLRDLYKAEVQNYASFFPELAKIIIPDEPPSENILTKNLSIDELMMRYVQTQGEKYPGIMANVTRTASKLQA... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with ncs6 that ligates sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is... |
Q3SZG9 | MCEMSEEYRESAPKGPPPPRLGTGDQKCVKCKEGLPVVVIRAGDAFCRDCFKALYVHKFRAMLGKSRLIFPGEKVLLAWSGGPSSSSMVWQVLEGLSRDSAKRLRFVPGVVYIDEGAACGQSPEDRARTLAEVKLALQTTGFPWHAVALEEVFSLPPSALRCSAQEAAGTEGAYKAAVDSFLQQQHALGTNGVERQSQHCAQDPQSPTGPPTTAQTQALSRLFDSVKTLTAKEELLQTLRTHLILHVARNHGYSKVMTGDSCTRLAIKLMTSLALGRGAFLAWDTGFSDERHGDVVVVRPMREHTLKEVAFYNRLFAVPS... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with CTU1/ATPBD3 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Sequence Mass (Da): 54353
Sequence Length: 501
Path... |
Q19906 | MELGNFVTDLNGKKCVKCDKDAKFTGVDPKKAWYCQECFVQMVRNKFRSSLSKKKIYKDADARDTLIVFDGTLSGTFLLHQINDALKQITYKRLMVKPTVLVLVSLTEDTEIQMVIKRIQEIKKSVLENVRWVVAHLACSMYDEDFKLKENECNGVEKISDYNQLIASCSVPTYRKELERVLKEKCLQKIACSMGILKCMVPDHADDLGRLAIDQLCLGRGGSISTLVTVTDKRPDFMLIRPLCDISKKELAVYNYLCDIDKHCIHIAQQNNQQKSVQTLTDAFICTLENEKFYSTINTVLSTAAKIHNTSIGKDDSKCS... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with tut-1/ctu-1 that ligates sulfur from thiocarboxylated urm-1 onto the uridine of tRNAs at wobble position.
Sequence Mass (Da): 39412
Sequence Length: 349
Pat... |
Q59ZY9 | MPEAIVYLTETEICQKCKTENAVVHARVEKLCSNCYIRFIRGKLRKQMHDERYKVKFGRAVEQYGTQRILLALSGGESSLVLLDIFGSLLQEQNELHKGKQGFELVVVNLDEYELDSLNNRIQKVFPELLAKYQPVKISLNVLSLDSYVDEESLHRILLTPDFRAMSKSIDPTRVTLTEILRLCPNKSSAEDLLTIVYNDLILRVAAKEDCQTVVYGHCMTRLANEIIALTVKGRGSIIHKSIADHTETIDDKEIKVMFPLREILQAEISAYVKLAELNKYVISSTVQKSKINKNLTIRDLTTNYFKQLDATGYASTAST... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is... |
Q6FLE5 | MTAEQCQRCNKNAVEVISRKELFCAECFRVFVMQKQRKQMMSDDYYRDIFKVMYKDKIRSAEEAEQQNKNSTILIPLSFGSSSLMMLDIVHLTLLEQKMQHQKTGFNVDVLICYRESNDELLTNIQSNIKELSTVRYSENKDNIRFHTLCLDSMFEIDKELIDQVVLHNVEFTGRQVSINESEHANLSLQTVLTSCPNRSTKEDIIDFVTKHLVKKYAYQNGQKAILWGHSMTRLADEIISCVVKGRGAQISSKLNTTNLDVNYGSRFKNLYPLKDILLTEVDAYCALFDLSKYLIKYELQDSLLVNKLKKEKHIGNQRL... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is... |
Q1DK31 | MSCVDCRFAPACVTVRTRNLCENCFIRFLQTKVLRRMERYRLRNAPKDRQRKLILPLSYGVSSLALLHIVSSLLLKQRTTGQKRTAFDLHVLIVDPVSLHPSKGAAASGRLAKIKEAYPDNTYSEVPLRSIFDYDPDIRGDISQHTGIPLGSNPSRSDEEILNLFRASFSTATARADIDGILLRRLIVAFAKSHKCDGILWGDSDSRLAAKTLANVAKGRGSSLVWNVCEGMSPWDIYFNFPLRDLYKSELEVYASYALRDLQQIIDQDPRNFEDLSNRHMSIEDLMSQYVLTQGAKYPGVMANIVRTVDKLTTPGVENA... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is... |
Q6DC53 | MCQVEEDYNGLECNQEKIPVSGLNRKCMKCKEGTAVLIIRVSDAFCRSCFKEYFIHKFRAMLGKNRVIFPQEKVLLAVSGGAASCTMLSQVQEGLSRDAPKKLRFMPGIVYIDDGGACGRSEDERQTSISQLKNIFTQTGFPYFIVPLEKVFSLPTSVLVPGTSDPDPSNPCYKQAVDKYLKEKQKLREEEAVCAVAQLNLEDSAYLPEHKLALQRLFSSLKTLSAKQEMLQTLRQHLILHVARENSYSKVMMGESCSRLAVKLLSNIALGRGAALASDTGFSDPRFGDVVIVRPMRDYSSKEITFYNRMFHVPSVFIPG... | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with ctu1/atpbd3 that ligates sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position.
Sequence Mass (Da): 55825
Sequence Length: 501
Path... |
A0A3G3C7T2 | MLSVQLITPSSHGTAHLPRDDTDAAAGEILEFLCPFFCIGGIGDEYCDCQEKRDLDLFTDQ | Function: Probable toxin that inhibits ion channels.
PTM: Mostly non-hydroxylated.
Sequence Mass (Da): 6721
Sequence Length: 61
Domain: The cysteine framework is XIV (C-C-C-C).
Subcellular Location: Secreted
|
Q9H467 | MELERIVSAALLAFVQTHLPEADLSGLDEVIFSYVLGVLEDLGPSGPSEENFDMEAFTEMMEAYVPGFAHIPRGTIGDMMQKLSGQLSDARNKENLQPQSSGVQGQVPISPEPLQRPEMLKEETRSSAAAAADTQDEATGAEEELLPGVDVLLEVFPTCSVEQAQWVLAKARGDLEEAVQMLVEGKEEGPAAWEGPNQDLPRRLRGPQKDELKSFILQKYMMVDSAEDQKIHRPMAPKEAPKKLIRYIDNQVVSTKGERFKDVRNPEAEEMKATYINLKPARKYRFH | Function: Down-regulates ESR1 protein levels through the ubiquitination-proteasome pathway, regardless of the presence of 17 beta-estradiol. Also involved in 17 beta-estradiol-induced ESR1 degradation. Controls PGR protein levels through a similar mechanism.
Sequence Mass (Da): 32009
Sequence Length: 287
Domain: The CU... |
D2Y100 | MKLCVVIVLLMLAMPFNGGEASRFFNQHARSQRSGMKTRGIWCDPPCPKGETCRGGECSDEFNSDVGR | Function: Probable neurotoxin with unknown target. Possibly targets ion channels.
PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 7524
Sequence Length: 68
Domain: The cysteine framework is XIV (C-C-C-C).
Subcellular Location: Secreted
|
P0DTX5 | MFRLGVFLLTFLLLVSMATSEYSRGRIMARASECVNECVESGHNTFHCERHCSNT | Function: Probable neurotoxin.
Sequence Mass (Da): 6256
Sequence Length: 55
Domain: The cysteine framework is XIV (C-C-C-C).
Subcellular Location: Secreted
|
P36649 | MQRRDFLKYSVALGVASALPLWSRAVFAAERPTLPIPDLLTTDARNRIQLTIGAGQSTFGGKTATTWGYNGNLLGPAVKLQRGKAVTVDIYNQLTEETTLHWHGLEVPGEVDGGPQGIIPPGGKRSVTLNVDQPAATCWFHPHQHGKTGRQVAMGLAGLVVIEDDEILKLMLPKQWGIDDVPVIVQDKKFSADGQIDYQLDVMTAAVGWFGDTLLTNGAIYPQHAAPRGWLRLRLLNGCNARSLNFATSDNRPLYVIASDGGLLPEPVKVSELPVLMGERFEVLVEVNDNKPFDLVTLPVSQMGMAIAPFDKPHPVMRIQ... | Cofactor: Binds 4 Cu cations per monomer . Contains a mononuclear type 1 (T1) or 'blue' copper site, and a trinuclear copper center consisting of one type 2 (T2) or 'normal' copper site, and two type 3 (T3) or 'binuclear' copper sites .
Function: Multicopper oxidase involved in copper homeostasis and copper tolerance u... |
P0A9G4 | MNISDVAKITGLTSKAIRFYEEKGLVTPPMRSENGYRTYTQQHLNELTLLRQARQVGFNLEESGELVNLFNDPQRHSADVKRRTLEKVAEIERHIEELQSMRDQLLALANACPGDDSADCPIIENLSGCCHHRAG | Function: Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations.
Sequence Mass (Da): 15235
Sequence Length: 135
Domain: It contains an N-terminal DNA binding region and a C-terminal metal binding region.
S... |
Q4J6M6 | MYPPEFSYVRAESLQEALKFLEGNDNTRPLAGGQSLIPMLKLRVLSPDYILDINRLNELNYVKTSLNGVSIGALTRYHDILSNDIVKSKVPLMHHATRTIGDMQVRNMGTIGGAISNADPASDMPVVLTALNATIILSSASGSRSVKALDFFKGPFTTDTNKGELVTQIEVPVLDGYKTVYKKVVRRAGDYALASVALAIKLKGNEIEDIKLAYGGVHDKPFRAMEVEKNVIGKKLNDDLVKDIASKVSSQINPPSDHRGSSWYRREVVKVLTMKAFKEVA | Cofactor: Binds 1 FAD per subunit.
Function: Component of the glyceraldehyde dehydrogenase which is involved the nonphosphorylated Entner-Doudoroff pathway. Catalyzes the oxidation of D-glyceraldehyde to yield glycerate. When the artificial electron acceptor 2,6-dichlorophenol-indophenol (Cl2Ind) is used, the enzyme sh... |
P53008 | MLISKSKMFKTFWILTSIVLLASATVDISKLQEFEEYQKFTNESLLWAPYRSNCYFGMRPRYVHESPLIMGIMWFNSLSQDGLHSLRHFATPQDKLQKYGWEVYDPRIGGKEVFIDEKNNLNLTVYFVKSKNGENWSVRVQGEPLDPKRPSTASVVLYFSQNGGEIDGKSSLAMIGHDGPNDMKFFGYSKELGEYHLTVKDNFGHYFKNPEYETMEVAPGSDCSKTSHLSLQIPDKEVWKARDVFQSLVSDSIRDILEKEETKQRPADLIPSVLTIRNLYNFNPGNFHYIQKTFDLTKKDGFQFDITYNKLGTTQSISTR... | Function: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor highly specifically . Seems to play a role in beta-1,6-glucan synthesis .
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: H2O + N(4)-(alpha-D-Glc-(1->2)... |
Q9HDZ2 | MTEKTSSLVFSAQYVALVHTICSFAAFFIPLALALYTHYYQVVKNEFYGYPEEWFPSVSATIGDWYPERSVFQWLIALTATPRLLVLLLWFTLSGISRPSVIITTALGVLRTALCGGWVYVTSTDDHDWHDIFMIGYLISNAPWFILVSKCSPVNSMASRIRNIGSALFVLTIFPLIYWYIQHKFKHIPGAYTVYAFFEWSLILWDILFDSALYWDFKPLVFNLHTSKTYSNPSSFATRKKEKGEHLSYAEAAAVGTQAKNIKKDSNVKCSKKQILFSLLYFSSEVYLSFVFWSVLTSLGLLVWYFPLWHMGISGYEACI... | Function: Involved in the maintenance of cell wall integrity. Required for the replacement of the diacylglycerol moiety by ceramides during GPI-anchor maturation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 110034
Sequence Length: 971
Subcellular Location: Cell membrane
|
P25618 | MLIINGKIIPIAHTICAFSAFFAALVTGYSLHFHKIVTNAHYTYPDEWFPSVSATIGDRYPERSIFQILIALTAFPRFLLLLGHYYLNQSKVCFLVGVLRTVSCGGWVYITSTDDHDIHDIFMITYIVLTLPWDIMITRYSSPLTSKNKGLTATIFFGTLFPMIYWYIQHSVQQRAGAYSIYAYFEWSLILLDIAFDAFAYADFKKIDIVLAFNEKPGNTSFFQIRDSSPINYGEEKSSELQKSGEKKVEKEKPVARSATGSYFRFDSFFYLLTNIFNGFLFWSNVTSLLCSIWHFPLWYMGISGYEAAILGYLGPIFLY... | Function: Involved in the maintenance of cell wall integrity. Required for the replacement of the diacylglycerol moiety by ceramides during GPI-anchor maturation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 107883
Sequence Length: 953
Domain: The PGAP2-like region interacts with the PGAP2IP-like ... |
P81717 | AVDFGEAIWNPASSSNYSTASNQTSAVIMHTMEGSYAGSISWFQNPSAQVSAHYLIRKSDGQITQMVREYHQAWHAKNHNYYTIGIEHDGRAADAGNWSAAMVNASARLTKSICARRGVNCASAWKGPGYDTFHLVPDSVRVKGHGMLSGNENRYDPGKYFPWSNYYNLINGGGGNP | Function: Antibacterial activity against Gram-positive bacteria M.luteus, S.aureus, E.faecalis and P.acidilactici and Gram-negative bacterium E.coli.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 19395
Sequence... |
P14892 | MEIKQMLVPVSRYSVLCPYEMNPTEITFHNTYNDAPAINERNNVANNSTGTSFHIAVDDKEAIQLIPFNRNAWHAGDGTNGRGNRHSIGVEICYSQSGGARYRKAELNAVEVIAQLMIQFDIPISKVKTHQERNGKYCPHRMLDEGRVQWFKNQCANRASSIKNSNKTQETGKVEIIVNKFNKVVTYEFGTALVPEMLGMMDALGYESRIISYGDKQGLVRFETAYRQGNELDKATAWLDAKGLKYFYTKE | Function: Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall... |
P24808 | MAIKVVKNLVSKSKYGLKCPNPMKAEYITIHNTANDASAANEISYMKNNSSSTSFHFAVDDKQVIQGIPTNRNAWHTGDGTNGTGNRKSIGVEICYSKSGGVRYKAAEKLAIKFVAQLLKERGWGIDRVRKHQDWNGKYCPHRILSEGRWIQVKTAIEAELKKLGGKTNSSKASVAKKKTTNTSSKKTSYALPSGIFKVKSPMMRGEKVTQIQKALAALYFYPDKGAKNNGIDGVYGPKTADAIRRFQSMYGLTQDGIYGPKTKAKLEALLK | Function: Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall... |
Q06320 | MVKIFIDPGHGGSDPGATGNGLQEKTLTLQIALALRTILTNEYEGVSLLLSRTSDQYVSLNDRTNAANNWGADFFLSIHVNSGGGTGFESYIYPDVGAPTTTYQSTIHSEVIQAVDFADRGKKTANFHVLRESAMPALLTENGFIDTVSDANKLKTSSFIQSLARGHANGLEQAFNLKKTSSSGLYKVQIGAFKVKANADSLASNAEAKGFDSIVLLKDGLYKVQIGAFSSKDNADTLAARAKNAGFDAIVILES | Function: Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is... |
P50864 | MRKKLKWLSFLLGFIILLFLFKYQFSNNDSWKPWSLPLSGKIIYLDPGHGGPDGGAVGGKLLEKDVTLEVAFRVRDYLQEQGALVIMTRESDTDLAPEGTKGYSRRKAEDLRQRVKLINHSEAELYISIHLNAIPSQKWSGAQSFYYGKYAENEKVAKYIQDELRRNLENTTRKAKRIHGIYLMQNVTKPGALIEVGFLSNPSEATLLGKPKYQDKVASSIYKGILRYFTEKGDPPE | Function: Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequ... |
P54450 | MVTIKKDFIPVSNDNRPGYAMAPAYITVHNTANTAKGADAKMHAKFVKNPNTSESWHFTVDDSVIYQHLPIDENGWHAGDGTNGTGNRKSIGIEICENADGDFEKATSNAQWLIRKLMKENNIPLNRVVPHKKWSGKECPRKLLDHWNSFLNGISSSDTPPKETSPSYPLPSGVIKLTSPYRKGTNILQLQKALAVLHFYPDKGAKNNGIDGVYGPKTANAVKRFQLMNGLTADGIYGPKTKAKLKSKLK | Function: Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Could play a role in mother cell lysis with CwlC.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl resid... |
O34360 | MNLPAKTFVILCILFLLDLCFSYIRHEWHSQNALQDMPVPSDLHPIVKQNADALKAAAANKGIDVVITEGFRSFKEQDELYKQGRTKKGNIVTYARGGESYHNYGLAIDFALQKKDGSIIWDMEYDGNQNGKSDWLEVVEIAKTLGFEWGGDWKRFKDYPHLEMIPN | Function: Cleaves the linkage of the L-alanine-D-glutamic acid of B.subtilis cell wall.
Sequence Mass (Da): 19113
Sequence Length: 167
Subcellular Location: Cell membrane
EC: 3.4.-.-
|
P36550 | MVKVVKNFVKVNQYTRPGLKLAGVKGIVMHYTATPGASALNERDYFNGTCIAIKRKASSAHYFVDRKEAQHIIPENEVAYHAHDKNRCYVSFLKPNANTKSISVEMCVEKDGMIHSETVQNAAELVADLCKRYGLSTNKIVRHYDVTNKICPAPWVSDSSQLTTFRKKVDSLLGNKTVSKTTSSTSQSSKSTGTILKKGASGSQVKALQKRLIAAGFSLPKYGADGSYENETVQAVKALQKKAGIAVDGIYGPATEKALAAIGAKKKKPSSNGKKTSYPLPSGIYKVKSPLMKGTGVRQIQEALAALYFYPDKGAKNNGI... | Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 38996
Sequence Length: 360
Subcellular Location: Secreted
EC: 3.5.1.28
|
Q9WUS4 | MGDWNLLGGILEEVHSHSTIVGKIWLTILFIFRMLVLGVAAEDVWDDEQSAFACNTQQPGCNNICYDDAFPISLIRFWVLQIIFVSSPSLVYMGHALYRLRDFEKQRQKKKLYLRAQMENPELDLEEQQRVDKELRRLEEQKRIHKVPLKGCLLRTYVLHILTRSVLEVGFMIGQYILYGFQMHPIYKCTQAPCPNSVDCFVSRPTEKTIFMLFMHSIAAISLLLNILEIFHLGIRKIMRALDGKSSSGNTENETGPPFHSTNYSGTQQCMICSSLPERISLLQANNKQQVIRVNIPRSKSMWQIPHPRQLEVDVSCGKR... | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Involved in tracer coupling between horizontal cells of the retina. May play a role in the regulation of horizontal cell patte... |
O57474 | MGDWSALGRLLDKVQAYSTAGGKVWLSVLFIFRILVLGTAVESAWGDEQSAFKCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSTPTLLYLAHVFYLMRKEEKLNRKEEELKAVQNDGGDVELHLKKIELKKFKHGLEEHGKVKMKGSLLRTYIFSIIFKSICEVVFLVIQWYLYGFSLSAVYTCERTPCPHRVDCFLSRPTEKTIFIIFMLVVSLFSLLLNIIELFYVLFKRIKDRVKSRQNTQFPTGTLSPTPKELSTTKYAYYNGCSSPTAPLSPMSPPGYKLATGERTNSCRNYNKQANEQNWANYSTEQNRLG... | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Plays an essential role in gap junction communication in the ventricles (By similarity).
Location Topology: Multi-pass membran... |
P23242 | MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGRSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRM... | Function: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Negative regulator of bladder functional capacity: acts by en... |
P0DL31 | CKGQSCSSCSTKEFCLSKGSRLMYDCCTGSCCGVKTAGVT | Function: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). This toxin inhibits rat Cav2.2/CACNA1B calcium channels in a dose-dependent manner (EC(50)=2.8 uM), whose effect is partially reversed after washing. In vivo, when injected into mice, it shows both an anal... |
A0A125S9G0 | MRLTTMHSVILMLLLVFAFDNVDGDEPGQTARDVDNRNFMSILRSEGKPVHFLRAIKKRDCTGQACTTGDNCPSECVCNEHHFCTGKCCYFLHA | Function: Probable neurotoxin.
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 10583
Sequence Length: 94
Domain: The cysteine framework is C-C-C-C-C-C-CC.
Subcellular Location: Secreted
|
E9QJ73 | MDNSTTAAEVSAPTDYDYNSTSYDDDNPYAAPCSLTETWNFLGRFAPVAYILVFILALVGNILVLCVIRRYRQSRHSPCSFSLTDTFLLHLAVSDLLLAATLPFFAVEWISEWVFGKVMCKITGALFSLNVYCGVLFLACISFDRYLAIVHAINISWRRKTCHAQLACAFIWVICLGLSMVDMHFRDLVEIPGMNRMVCQIVYSEQYSKQWQIGMQLVSMVLGFILPLLVMLYCYLHIFKALCHATRRQKRRSLRLIISLVIVFVISWAPYNALRMTDSLQMLGVIVKSCALNNVLDVGILVTESLGLAHCALNPLLYGL... | Function: Receptor for the C-X-C chemokines cxcl11.1 and cxcl11.6 . Promotes macrophage chemotaxis to sites of bacterial infection .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42263
Sequence Length: 378
Subcellular Location: Cell membrane
|
Q9YGC3 | MDGFSGGIDINIFDGNSTENGSGDFEDFIEPCFMHENSDFNRIFLPTIYSFIFLLGIIGNGLVVVVMGYQKKSRTMTDKYRLHLSVADLLFVFTLPFWSVDAAIGWYFKEFLCKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQGSRKMLADKVVYAGVWLPALLLTVPDLVFARVSDENGQFVCDRIYPIENRETWTVGFRFLHITVGLILPGLIILICYCVIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYVCLTTDTFMLLGLVKGDCIWENTLHMAISITEALAFFHCCLNPILYAFLGAKFKTSA... | Function: Receptor for the C-X-C chemokine cxcl12/sdf-1. Transduces a signal by increasing the intracellular level of calcium ions. Signaling with cxcl12/sdf-1 mediates the directional movement of mesodermal cells during gastrulation. May play a role in the migration of embryonic presumptive primordial germ cells (pPGC... |
A0A0R4I952 | DGECGDKDEPCCGRPDGAKVCNDPWVCILTSSRCENP | Function: This toxin reduces the outward currents that are due to the opening of voltage-gated potassium channels in DRG neurons. In addition, leftward shift in the presence of this toxin is observed in averaged normalized conductance-voltage plot of outward sodium currents (Nav1.2/SCN2A).
Sequence Mass (Da): 3970
Sequ... |
Q5K8R6 | MPLNLPFSSPLKLPLPRRFIILILSASILILFLHTFAPSTLPPVLTPNLPHHEPDASYFSPSKWLPPILNPNAPTRPLEFDEDGQCLFLSPFDALSAAEKARARVLSLDEISPGIVRADAPPAEGTDADPDFDDEFSELSNATRKMPAGLTHPILGLLRDGEAKWNSMVTMQSQTLEQAVDVYMDRWGRRPPKGFDEWWHFAKANNVLLPDEYDPIMNSLLPFYALPIDTLKERLVEAEKIPETFTLIVHDGKVELKWNDDYSRDTWWASRPRADSQINLMEPFIKHIGTFRATFTIHDQPSILLDHERQEELLTAARHG... | Function: Beta-1,2-xylosyltransferase that plays a key role in capsule polysaccharide synthesis by transferring xylose to alpha-1,3-dimannoside in a beta-1,2-linkage. Also mediates glycosylation of glycosphingolipids; constitutes the unique xylosyltransferase responsible for adding xylose to glycosphingolipids.
Locatio... |
Q9P0U4 | MEGDGSDPEPPDAGEDSKSENGENAPIYCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCRECREKDPKLEIRYRHKKSRERDGNERDSSEPRDEGGGRKRPVPDPDLQRRAGSGTGVGAMLARGSASPHKSSPQPLVATPSQHHQQQQQQIKRSARMCGECEACRRTEDCGHCDFCRDMKKFGGPNKIRQKCRLRQCQLRARESYKYFPSSLSPVTPSESLPRPRRPLPTQQQPQPSQKLGRIREDEGAVASSTVKEPPEATATPEPLSDEDLPLDPDLYQDFCAGAFDDHGLPWMSDTEESPFLDPAL... | Function: Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG.
PTM: May be regulated by proteolysis.
Sequence Mass (Da): 75712
Sequence Length: 656
Domain: The acidic domain carries the potential to activate transcription.
Subcellular Location:... |
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