ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8H5T6 | MADSTATCIDIILAIILPPLGVFFKFGCGIEFWICLLLTFFGYLPGIIYAVWVITK | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6230
Sequence Length: 56
Subcellular Location: Membrane
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Q7T0T2 | MAEELKRFLYKKLPSIEGLHAIVVSDRDGVPVIKVANENAPELALRPSFLSTFALATDQGSKLGLSKNKSIICYYDTCQVVQFNRLPLVVSFIASSDANTGLLLSLNEELGDLFEELQHAVEI | Function: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator plays a dual rol... |
Q9KLK7 | MNIRPSQIKHKQRIASFITHAVVVVMGVLIVSVLFQSYQISSRLMAQEGQRTSVQTSSLIQSLFDFRLAALRIHQDSTAKNASLINALVSRDSSRLDEFFSSVDELELSNAPDLRFISSHDNILWDDGNASFYGIAQQELNKLIRRVAISGNWHLVQTPSEGKSVHILMRRSSLIEAGTGQVVGYLYVGIVLNDNFALLENIRSGSNSENLVLAVDTTPLVSTLKGNEPYSLDYVVHSAKDAMRDSFIVGQTFLEVESVPTYLCVYSIQTNQNVLTLRDNFYFWMAFALISMIGVSIASRWWLQKRIQREIETLMNYTHK... | Function: At low cell density, in absence of AI-2 (autoinducer 2), LuxQ has a kinase activity and autophosphorylates on a histidine residue. The phosphoryl group is then transferred to an aspartate residue in the response regulator domain. The phosphoryl group is transferred to LuxU, and ultimately to LuxO. At high cel... |
P54302 | MTTTRSNIKKRRSLATLITKIIILVLAPIILGIFIQSYYFSKQIIWQEVDRTKQQTSALIHNIFDSHFAAIQIHHDSNSKSEVIRDFYTDRDTDVLNFFFLSIDQSDPSHTPEFRFLTDHKGIIWDDGNAHFYGVNDLILDSLANRVSFSNNWYYINVMTSIGSRHMLVRRVPILDPSTGEVLGFSFNAVVLDNNFALMEKLKSESNVDNVVLVANSVPLANSLIGDEPYNVADVLQRKSSDKRLDKLLVIETPIVVNAVTTELCLLTVQDNQSVVTLQIQHILAMLASIIGMIMIALMSREWIESKVSAQLESLMSYTR... | Function: At low cell density, in absence of AI-2 (autoinducer 2), LuxQ has a kinase activity and autophosphorylates on a histidine residue. The phosphoryl group is then transferred to an aspartate residue in the response regulator domain. The phosphoryl group is transferred to LuxU, and ultimately to LuxO. At high cel... |
Q4R5M8 | MLPAAMKGLGLALLAVLLCSAPAHGLWCQDCTLTTNSSHCTPKQCQPSDTVCASVRITDPSSSRKDHSVNKMCASSCDFVKRHFFSDYLMGFINSGILKVDVDCYEKDLCNGVAGAGHSPWALAGGLLLSLGPALLWAGP | Function: Believed to act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response. May play a role in the intracellular trafficking of alpha-7-containing nAChRs and may inhibit their expression at the cell surface. Seems to inhibit alpha... |
Q9WUC3 | MLPAAMKSLGLALLALLLCPSPAHGLWCQDCTLANSSHCAPKQCQPTDTVCASVRITDPSSSRKDHSVNKMCASSCDFVKRHFFSDYLMGFINSGILKVDVDCCEKDLCNGASVAGRSPWALAGGLLLSLGPALLWAGP | Function: Believed to act as modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response . May play a role in the intracellular trafficking of alpha-7-containing nAChRs and may ... |
Q17RY6 | MALLALLLVVALPRVWTDANLTARQRDPEDSQRTDEGDNRVWCHVCERENTFECQNPRRCKWTEPYCVIAAVKIFPRFFMVAKQCSAGCAAMERPKPEEKRFLLEEPMPFFYLKCCKIRYCNLEGPPINSSVFKEYAGSMGESCGGLWLAILLLLASIAAGLSLS | Function: Required for sperm migration into the oviduct and male fertility by controlling binding of sperm to zona pellucida (By similarity). May play a role in cell growth .
Location Topology: Lipid-anchor
Sequence Mass (Da): 18673
Sequence Length: 165
Subcellular Location: Secreted
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Q9CWP4 | MAFLVALLVVLGLQLVQSNALTCHVCEAQNSYACSNPSQCPGEKKFCLLAVTRIFERFFYVSKQCTRRCPTPVVSPPSTNPPSEPKEFLIEKPMPFLFYKCCQWDSCNGEGPPTDQLLKEQPGKASGRRHRYIELLLTGFMVLTANGLSALCLL | Function: Required for sperm migration into the oviduct and male fertility by controlling binding of sperm to zona pellucida . May play a role in cell growth (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 17134
Sequence Length: 154
Subcellular Location: Secreted
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Q86Y78 | MEPGPALAWLLLLSLLADCLKAAQSRDFTVKDIIYLHPSTTPYPGGFKCFTCEKAADNYECNRWAPDIYCPRETRYCYTQHTMEVTGNSISVTKRCVPLEECLSTGCRDSEHEGHKVCTSCCEGNICNLPLPRNETDATFATTSPINQTNGHPRCMSVIVSCLWLWLGLML | Function: Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain . Inhibits nicotine-induced Ca(2+) influx through nAChRs . In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner . Acts as a positive regulator of Wnt/beta-catenin signaling (By ... |
D3ZTT2 | MEPSPALAWLLLLSLVADCLKAAQSRDFTVKDIIYLHPSTTPYPGGFKCFTCEKAADNYECNRWAPDIYCPRDTRYCYTQHTMEVTGNSISVTKRCVPLEECLSTGCRDSEHEGYKICTSCCEGNICNLPLPRNDTDATFATTSPINQTNGHPHCVSVIVSCLWVWLGLTL | Function: Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain . Inhibits nicotine-induced Ca(2+) influx through nAChRs (By similarity). In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner (By similarity). Acts as a positive regulator of W... |
A2VE33 | MKSFLFAGIVVVLTVAAVDTLRCIQCNSLKDSCVAKNATECPSNATTSCTSFSTNFYHGEHPTWYEDHACSEENCSNTTVESFTVSVSENETFHFESQCCLGEPCNQTSNTTASPHQVGSGNMECPACYGNNETSCNETRKCYGERCVSIIAEFTNETKTLVLKGCSNVSISTCESLGAGNQTFRGVTFRKFECGDNFSTTTPLATTDTGSQASFTPLALASILLLSLLL | Function: Secreted protein specifically required to prevent invasion of Gram-negative bacteria in the inner mucus layer of the colon epithelium, a portion of the large intestine which is free of commensal microbiota. Prevents invasion of flagellated microbiota by binding to the flagellum of bacteria, such as P.mirabili... |
Q6UX82 | MKGILVAGITAVLVAAVESLSCVQCNSWEKSCVNSIASECPSHANTSCISSSASSSLETPVRLYQNMFCSAENCSEETHITAFTVHVSAEEHFHFVSQCCQGKECSNTSDALDPPLKNVSSNAECPACYESNGTSCHGKPWKCYEEEQCVFLVAELKNDIESKSLVLKGCSNVSNATCQFLSGENKTLGGVIFRKFECANVNSLTPTSAPTTSHNVGSKASLYLLALASLLLRGLLP | Function: Secreted protein specifically required to prevent invasion of Gram-negative bacteria in the inner mucus layer of the colon epithelium, a portion of the large intestine which is free of commensal microbiota. Prevents invasion of flagellated microbiota by binding to the flagellum of bacteria, such as P.mirabili... |
Q9D7S0 | MRGVFIAGVIAAFAITVVDSLNCTQCYTYNSTCDGQATECNEQSFSCVESSINSTLGGFLHVYQNKFCSASNCTENSTEVAFTVHLFDDQRYHFASQCCQGESCNATHSESGTQNVTDMQCMSCYGHNKTLCEEKPQKCYEGEQCVFIIAEMVNGSGRVELKGCSDISNSTCQFLSPGNTTVGEFVFKSVECTQPTEYTNSTTTIPPITNTSLTSVTRPGIKTSPASVTPQASMGTKASFTSSIFGSLLLLKLLF | Function: Secreted protein specifically required to prevent invasion of Gram-negative bacteria in the inner mucus layer of the colon epithelium, a portion of the large intestine which is free of commensal microbiota. Prevents invasion of flagellated microbiota by binding to the flagellum of bacteria, such as P.mirabili... |
Q5ZU17 | MTYSFSKPVSWVFLFTAVIYLVSLSFIQYPATTVLKPIPIVCLIVGVFRTSLSSSAKILLILALVFSLAGDVVLTLPFSLQLELGIACFLLAHCFYITLFLKSFEFNRLHLFYYLPIFLFMGFAAFTMIPYLGNLLIPVMIYFCVLMLMVFSAFQVKKETLTISSGALFFLISDLTLALNLFIYTQADVRIFVMFTYYVAQFLLTFGLVRLYEKGG | Function: Specifically hydrolyzes the vinyl ether bond of lysoplasmenylcholine (pLPC) and lysoplasmenylethanolamine (pLPE) to release a fatty aldehyde and glycerophospho-choline or glycerophospho-ethanolamine . Has no activity on diradyl plasmalogen, 1-alkenyl-glycerol, and monoacylglycerophospho-ethanolamine or monoac... |
P64838 | MGSIAGFSSAVLSKLGIPVPYAPRLLAGGWVVAGWAGLAYGVYLTVIALRLPPGSELTGHAMLQPAFKASMAVLLAAAAVAHPIGRERRWLVPALLLSATGDWLLAIPWWTWAFVFGLGAFLLAHLCFIGALLPLARQAAPSRGRVAAVVAMCVASAGLLVWFWPHLGKDNLTIPVTVYIVALSAMVCTALLARLPTIWTAVGAVCFAASDSMIGIGRFILGNEALAVPIWWSYAAAEILITAGFFFGREVPDNAAAPTDS | Function: Specifically hydrolyzes the vinyl ether bond of lysoplasmenylcholine (pLPC) and lysoplasmenylethanolamine (pLPE) to release a fatty aldehyde and glycerophospho-choline or glycerophospho-ethanolamine.
Catalytic Activity: 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = a 2,3-saturated aldehyde + sn-glycero... |
Q5VWZ2 | MAAASGSVLQRCIVSPAGRHSASLIFLHGSGDSGQGLRMWIKQVLNQDLTFQHIKIIYPTAPPRSYTPMKGGISNVWFDRFKITNDCPEHLESIDVMCQVLTDLIDEEVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQKSNGVLPELFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPNVYHELSKTELDILKLWILTKLPGEMEKQK | Function: Has depalmitoylating activity toward KCNMA1. Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site.
Catalytic Activity: H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]
Sequence ... |
Q9DD65 | MRTLVVLLLVAVANARVYERCEWARLLRNQGMDGYRGISLANWVCLTEWESHYNTRATNHNTDGSTDYGIFQINSRWWCNDSQTPTSNACNIRCSELLTDDVIVAIKCAKRVVRDPNGIGAWVAWRQHCQGQDLSSYLAGCGL | Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidog... |
C1IIX1 | MRVLPLALLVGLLAVSDAKVLGKCEFARLLETRYNLSRNDIKNWVCIAEFESSFNTAATNRNRNRSTDYGIFQINNKYWCGSDYGKNVCGIPCSDLMSDDITAALRCAETVRRATERYRGRGKGYTAWVAYNSKCKKRDLDQYMAECWSRGSNSIFPF | Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents (By similarity). Has bacteriolytic activity against Gram-positive bacterium M.luteus, and Gram-negative shrimp pathogenic bacteria V.a... |
Q9HWK6 | MHKRTYLNACLVLALAAGASQALAAPGASEMAGDVAVLQASPASTGHARFANPNAAISAAGIHFAAPPARRVARAAPLAPKPGTPLQVGVGLKTATPEIDLTTLEWIDTPDGRHTARFPISAAGAASLRAAIRLETHSGSLPDDVLLHFAGAGKEIFEASGKDLSVNRPYWSPVIEGDTLTVELVLPANLQPGDLRLSVPQVSYFADSLYKAGYRDGFGASGSCEVDAVCATQSGTRAYDNATAAVAKMVFTSSADGGSYICTGTLLNNGNSPKRQLFWSAAHCIEDQATAATLQTIWFYNTTQCYGDASTINQSVTVLT... | Function: Lysine-specific endoprotease . Involved in corneal virulence.
PTM: Experiments performed in E.coli. Processing of pro-endopeptidase to mature endopeptidase is probably autocatalytic, as mutations in the probable active site residues prevent processing, and purified inactive pro-endopeptidase disappears in the... |
P21776 | SKMKKCEFAKIAKEQHMDGYHGVSLADWVCLVNNESDFNTKAINRNKGI | Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidog... |
Q976J8 | MVVLKCPVCNGDVNVPDDALPGEIVEHECGAQLEVYNDHGRLALRLAEQVGEDWGE | Function: Carrier protein that bears the covalently bound substrates for arginine and lysine biosynthesis; bound L-glutamate is sequentially converted to L-ornithine, while bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.
PTM: Formation of an isopeptide bond between the gamma-carboxyl group of the ... |
Q5SH22 | MVGTCPECGAELRLENPELGELVVCEDCGAELEVVGLDPLRLEPAPEEAEDWGE | Function: Carrier protein that bears the covalently bound substrates for lysine biosynthesis; the bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.
PTM: Formation of an isopeptide bond between the gamma-carboxyl group of the C-terminal glutamate and the amino group of alpha-aminoadipate (AAA) is cat... |
O06136 | MVAAAGEPLNCQRANPEVTVKLPSADVVPRLRGRQRVVVHVDSRTARCVGALALVCAACWLIALLAGDYRHAQWAVAGRLGWSLTVLAAVAFIARGIFLGRPVTAMHATAAGLFLLAGLAAHVLVADLLGEILIAGSGWALMWPTSAHPRPEDLPRVWALINATRADSLAPFAMQAGKSHHFSAAGTAALAYRTRIGYAVVSGDPIGDEAQFPQLVADFAAMCHMHGWRIVVVGCSERRLGLWSDPMVVGQSLRPIPIGRDVVIDVSNFEMTGRRFRNLRQAVKRTHNFGVTTEIVAEQQLDDQRQAELAEVLAASPSGA... | Function: Plays a role in mycobacterial fitness . Likely enhances survival of pathogenic strains . Considerably reduces the overall net negative charge on bacterial surface when bacteria are exposed to an acidic environment .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52642
Sequence Length: 484
... |
P37161 | MRALLGICVLALVTPAVLGRTMDRCSLAREMANMGVSRDQLSKWACIAEHESSYRTGVVGPPNTDGSNDYGIFQINDMYWCQPSSGKFSHNGCDVSCNALLTDDIKSSVRCALKVLGQQGWSAWSTWHYCSGYLPPIDDCFV | Function: Unlikely to play an active role in the humoral immune defense. May have a function in the digestion of bacteria in the food. May be involved in the clearance of bacteria from the larval gut before metamorphosis.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D... |
Q02978 | MAATASAGAGGIDGKPRTSPKSVKFLFGGLAGMGATVFVQPLDLVKNRMQLSGEGAKTREYKTSFHALTSILKAEGLRGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFLLKAVIGMTAGATGAFVGTPAEVALIRMTADGRLPADQRRGYKNVFNALIRITREEGVLTLWRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIAKTRIQNMRMIDGKPEYKNGLDVLFKVVRYEGFFSLWKGFTPYYARLGPHTVLTFIFLEQMNKAYKRLFLSG | Function: Catalyzes the transport of 2-oxoglutarate (alpha-oxoglutarate) across the inner mitochondrial membrane in an electroneutral exchange for malate. Can also exchange 2-oxoglutarate for other dicarboxylic acids such as malonate, succinate, maleate and oxaloacetate, although with lower affinity. Contributes to sev... |
Q9CR62 | MAATASPGAGRMDGKPRTSPKSVKFLFGGLAGMGATVFVQPLDLVKNRMQLSGEGAKTREYKTSFHALTSILKTEGLKGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFLLKALIGMTAGATGAFVGTPAEVALIRMTADGRLPADQRRGYKNVFNALVRIAREEGVPTLWRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIVKTRIQNMRMIDGKPEYKNGLDVLLKVVRYEGFFSLWKGFTPYYARLGPHTVLTFIFLEQMNKAYKRLFLSG | Function: Catalyzes the transport of 2-oxoglutarate (alpha-oxoglutarate) across the inner mitochondrial membrane in an electroneutral exchange for malate. Can also exchange 2-oxoglutarate for other dicarboxylic acids such as malonate, succinate, maleate and oxaloacetate, although with lower affinity. Contributes to sev... |
P0C582 | MSSVKQSAQAATSDVVDTAKNATAETVTAATDFLHTPAVRAALPFINGGLSGMVATTVIQPIDMIKVRIQLAGEGKAGGPKPTPLGVTRDIIASGKAMDLYTGLSAGLLRQAVYTTARIGCFDTFMSRLSARAKEKGQSVGFKERASAGLAAGGLAAMIGNPADLALIRMQSDGLKPVAERKNYKSVIDALGGIARNEGVAALWAGAAPTVVRAMALNFGQLAFFSEAKAQLKARTQWSSKVQTLSASAIAGFFASFFSLPFDFVKTRLQKQTRGPDGKLPYNGMVDCFAKVAKQEGVFRFYRGFGTYYVRIAPHAMVTL... | Function: Catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35047
Sequence Length: 331
Subcellular Location: Mitochondrion inner membrane
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F1RFX9 | MQSWDPCLTPLELHGALFLHGPYWTPGLFRLIALGTCGDSCTHVRQPPKTWMGATVFVQPLDLVKNRMQLSGEGAKTREYKTSFHALTSILRAEGLRGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFLLKALIGMTAGATGAFVGTPAEVALIRMTADGRLPPDQRRGYKNVFDALIRIVREEGVPTLWRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIAKTRIQNMRTIDGKPEYKNGLDVLVKVIRYEGFFSLWKGFTPYYARLGPHTVLTFIFLE... | Function: Catalyzes the transport of 2-oxoglutarate (alpha-oxoglutarate) across the inner mitochondrial membrane in an electroneutral exchange for malate . Can also exchange 2-oxoglutarate for other dicarboxylic acids such as malonate, succinate, maleate and oxaloacetate, although with lower affinity . Contributes to s... |
P16947 | MARKDTNKQYSLRKLKTGTASVAVAVAVLGAGFANQTEVKAAEKKVEAKVEVAENNVSSVARREKELYDQIADLTDKNGEYLERIGELEERQKNLEKLEHQSQVAADKHYQEQAKKHQEYKQEQEERQKNQEQLERKYQREVEKRYQEQLQKQQQLETEKQISEASRKSLSRDLEASREAKKKVEADLAALTAEHQKLKEEKQISDASRQGLSRDLEASREAKKKVEADLAALTAEHQKLKEEKQISDASRQGLSRDLEASREAKKKVEADLAEANSKLQALEKLNKELEEGKKLSEKEKAELQARLEAEAKALKEQLAK... | Function: This protein is one of the different antigenic serotypes of protein M. Protein M is closely associated with virulence of the bacterium and can render the organism resistant to phagocytosis.
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 43915
Sequence Length: 389
Subcellular Location: Secreted
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Q96PG2 | MKAEATVIPSRCARGLPSWQVLSPVQPWQTSAPQNTTQPKLLAPHQHEKSQKKSSLLKELGAFHITIALLHLVFGGYLASIVKNLHLVVLKSWYPFWGAASFLISGILAITMKTFSKTYLKMLCLMTNLISLFCVLSGLFVISKDLFLESPFESPIWRMYPNSTVHIQRLELALLCFTVLELFLPVPTAVTAWRGDCPSAKNDDACLVPNTPLHLKGLPVEPPPSYQSVIQGDAQHKQHQRLREVKQVAPDTWIVTDGAAIWTQTAN | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29747
Sequence Length: 267
Subcellular Location: Membrane
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Q99N03 | MAGQAPTAVPGSVTGEVSRWQNLGPAQPAQKVAQPQNLVPDGHLEKALEGSDLLQKLGGFHIAIAFAHLAFGGYLISTVKNLHLVVLKCWYPLWGTVSFLVAGMAAMTTVTFPKTSLKVLCVIANVISLFCALAGFFVIAKDLFLEGPFPWPIWRPYPEPTTYIQRLELTLFCFTFLEIFLSGSTAITAYRMKRLQAEDKDDTPFVPDTPMELKGLSLGPPPSYKDVAQGHSSSDTGRALATSSGLLLASDSFHQALLHTGPRTLRK | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28972
Sequence Length: 267
Subcellular Location: Membrane
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Q9NXJ0 | MMSSKPTSHAEVNETIPNPYPPSSFMAPGFQQPLGSINLENQAQGAQRAQPYGITSPGIFASSQPGQGNIQMINPSVGTAVMNFKEEAKALGVIQIMVGLMHIGFGIVLCLISFSFREVLGFASTAVIGGYPFWGGLSFIISGSLSVSASKELSRCLVKGSLGMNIVSSILAFIGVILLLVDMCINGVAGQDYWAVLSGKGISATLMIFSLLEFFVACATAHFANQANTTTNMSVLVIPNMYESNPVTPASSSAPPRCNNYSANAPK | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28069
Sequence Length: 267
Subcellular Location: Membrane
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Q2YDM3 | MTGIFCIFMWYLLLILYMGQIKGVFGTYEPITYKTGCSLWGIFFIISGISIIRATWYPSQRQLTCAMLENILCMILAIISMILTIVELSTFKSVSYRNYGQAKLGRQISRVLLSFYPLEVSMALTYSIFGCVGLCRKKEDARTADTEEVEDAF | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17429
Sequence Length: 153
Subcellular Location: Membrane
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Q5J8X5 | MIGIFHIFMWYFLLVLYMGQIKGAFGTYEPVTYKTGCTLWGIFFIIAGVFLIRVTKYPTRSGIISTLIINIICIITTITAVTLTIIELSHFNSVSYRNYGQAKLGREVSRILLFFYGLEFSIALTHSIYSCSNLFRRQNDLTSVTEEAESTP | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17307
Sequence Length: 152
Subcellular Location: Membrane
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Q5FWC3 | MECRNPKVSSANITVLGVIQIMIGIYHVLMWYFLLLLYMGQIKGVFGTYEPVTYKMGTSLWGFAFVISGAFTVKAAKYQSRHMILCTMSLNILCIIITIVAASLTIVELSHFRSVSYRNYGQAKLGREVSRVLLCSYPLEFAIALLYSISSCAYLPLSSIVKSLVRKTWRLSSLAAWRQMIWLEAGNQEETLESVTEVVEGNS | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22802
Sequence Length: 203
Subcellular Location: Membrane
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Q96JA4 | MESTSQDRRATHVITIKPNETVLTAFPYRPHSSLLDFLKGEPRVLGATQILLALIIVGFGTIFALNYIGFSQRLPLVVLTGYPFWGALIFILTGYLTVTDKKSKLLGQGVTGMNVISSLVAITGITFTILSYRHQDKYCQMPSFEEICVFSRTLFIVLFFLPSDVTQNSEQPAPEENDQLQFVLQEEFSSDDSTTNAQSVIFGGYAFFKLTLSRSPLVSQPGNKGREFVPDEQKQSILPSPKFSEEEIEPLPPTLEKKPSENMSIQLDSTFKQMKDEDLQSAIVQPSQMQTKLLQDQAASLQVFPSHSALKLEDISPEDL... | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76580
Sequence Length: 679
Subcellular Location: Membrane
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Q8N5U1 | MSAAPASNGVFVVIPPNNASGLCPPPAILPTSMCQPPGIMQFEEPPLGAQTPRATQPPDLRPVETFLTGEPKVLGTVQILIGLIHLGFGSVLLMVRRGHVGIFFIEGGVPFWGGACFIISGSLSVAAEKNHTSCLVRSSLGTNILSVMAAFAGTAILLMDFGVTNRDVDRGYLAVLTIFTVLEFFTAVIAMHFGCQAIHAQASAPVIFLPNAFSADFNIPSPAASAPPAYDNVAYAQGVV | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25050
Sequence Length: 240
Subcellular Location: Membrane
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P57109 | MKLYTYYRSTSSYRVRIALALKGLDYQSLPVNLIRDGGEHRQPAYLALNPQGRVPALQVDEGELLIQSPAIIEYLEERYPQPALLSSDPLRRARERGVAALVGCDIHPLHNASVLNLLRQWGHDEEQVRQWIGHWVGQGLAAVEQLIGDQGWCFGDRPGLADVYLVPQLYAAERFGVALDAWPRIRRVADLAAAHPAFRQAHPANQPDTPAA | Catalytic Activity: 4-maleylacetoacetate = 4-fumarylacetoacetate
Sequence Mass (Da): 23685
Sequence Length: 212
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.
EC: 5.2.1.2
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P57113 | MQAGKPVLYSYFRSSCSWRVRIALALKGIDYEIVPINLIKDGGQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEETRPIPRLLPQDPQKRAIVRMISDLIASGIQPLQNLSVLKQVGQENQMPWAQKAITSGFNALEKILQSTAGKYCVGDEVSMADVCLAPQVANAERFKVDLSPYPTISHINKALLALEAFQVSHPCRQPDTPAELRT | Cofactor: Glutathione is required for the MAAI activity.
Function: Probable bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1, 3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with t-butyl and cumen... |
Q9X4F7 | MANETVLYDYWRSSASYRVRIALNLCGEAYRSVPVDLLAKAHRAPEHLARNPQGLVPVLDIDGERLTQSLAIIEYLAETRDGTGLLPAHPIDRQRVRALSYAVAMDIHPVCNLGVVARVMAGAGDGEAARREWMQKFIGEGLAAFERMLDHPATGAFCHGDRPTMADLCLVPQVYNARRWDVDLAACPLLVAIDRRCAGIDAFQRAHPDRAKP | Catalytic Activity: 4-maleylacetoacetate = 4-fumarylacetoacetate
Sequence Mass (Da): 23525
Sequence Length: 213
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.
EC: 5.2.1.2
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Q9KSB2 | MMSLILYGYWRSSAAYRVRIALNIKQLVYESRAVHLSREGGEQHHAEFHRLNPSELIPVLIDGELCLNQSLAIIEYLDETYPAPRLIPERGAERYQVKALALDIAADIHPINNLRILQYLTAKLGVADEEKNRWYRHWIDKGFQGLEEKLRHTAGEYCVGNRLSLVDVCLVPQVYNAERFDLDMSRYPTLQQIAARLRALPAFAQAAPENQPDAC | Catalytic Activity: 4-maleylacetoacetate = 4-fumarylacetoacetate
Sequence Mass (Da): 24628
Sequence Length: 215
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.
EC: 5.2.1.2
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Q3AEU2 | MRIKDVLFVKGSSGFYFDDQKAIKSGAVTDGFTYKGKPLTPGFSRVRQGGEAVSIMLFLENGEIAVGDCVAVQYSGVDGRDPVFLADNFIEVLEEEIKPRLVGYNLVRFREAARYFTNLTDKRGKRYHTALRYGLTQALLDAVAKINRTTMAEVIAEEYGLDLTLNPVPLFAQSGDDRYINADKMILKRVDVLPHGLFNHPAKTGEEGKNLTEYALWLKQRIKTLGDHDYLPVFHFDVYGTLGTVFNDNLDRIADYLARLEEKVAPHPLQIEGPVDLGSKERQIEGLKYLQEKLITLGSKVIIVADEWCNNLSDIKEFVD... | Function: Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate. It can also catalyze the amination of fumarate and ethylfumarate, and the de... |
Q05514 | MKIVDVLCTPGLTGFYFDDQRAIKKGAGHDGFTYTGSTVTEGFTQVRQKGESISVLLVLEDGQVAHGDCAAVQYSGAGGRDPLFLAKDFIPVIEKEIAPKLIGREITNFKPMAEEFDKMTVNGNRLHTAIRYGITQAILDAVAKTRKVTMAEVIRDEYNPGAEINAVPVFAQSGDDRYDNVDKMIIKEADVLPHALINNVEEKLGLKGEKLLEYVKWLRDRIIKLRVREDYAPIFHIDVYGTIGAAFDVDIKAMADYIQTLAEAAKPFHLRIEGPMDVEDRQKQMEAMRDLRAELDGRGVDAELVADEWCNTVEDVKFFT... | Function: Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate. It can also use L-erythro-beta-methylaspartate (L-erythro-(2S,3R)-3-methylas... |
Q5V465 | MRIEDVRTVPGLSGFFFDDQQAIKDGATQTGFAYDGQPVTDGFDRIREAGEALIVEIELADGSIATGDCAAVQYSGAGGRDPLFRAEKYRPVVEGAVADALRGQDATQFGANATMLEEMSPQRSGGDQLHTAVRYGVSQALLNAAAQARGVTPTDVLADTYDTEPATSPVPVFGQSGDERRINAEKMLIKGVPVLPHGLFNSVEKVGENGEGLRDYLAWLSDRATALGPEPYSPRFHVDVYGILGKVFGPPYDRTEVTDYFETLREAAAPYPLQVEGPMDAGGRQAQITEMAELREGLADAGVDVDIVADEWCNTFEDVQ... | Function: Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate (Probable).
Catalytic Activity: (2S,3S)-3-methyl-L-aspartate = mesaconate + N... |
P37515 | MLRTEKEKMAAGELYNSEDQQLLLERKHARQLIRQYNETPEDDAVRTKLLKELLGSVGDQVTILPTFRCDYGYHIHIGDHTFVNFDCVILDVCEVRIGCHCLIAPGVHIYTAGHPLDPIERKSGKEFGKPVTIGDQVWIGGRAVINPGVTIGDNAVIASGSVVTKDVPANTVVGGNPARILKQL | Function: Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars. Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides.
Catalytic Activity: acetyl-CoA + D-maltose = 1-O-acetylmalt... |
P77791 | MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLAEEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNFFANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPIDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL | Function: Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars . Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides .
Catalytic Activity: acetyl-CoA + D-maltose = 1-O-acetylma... |
P40333 | MFAVFWTNLRCLGYNTFTCGVETPTTWGKVGSLDASSSTFTTYRGYPLAMAISAGTPACDSPDDNIRRAINTLRADLSALLRGESVAYSAFLSACTKFDGFAQSCHGMLSDDTLDLLYSFSESLLALSENMALLETKKEAESNKFTAEVMAILSDKTSGLDLSDDKNEPTSPTPAYVEPCARWLKDNWYNPYPSGEVRTQIARQTRTSRKDIDAWFIDARRRIGWNEVRRKHFENKRVDIVRAASIFTGPQSIPAEVDALPDHIELEFAGILSRARSLYEEKFSPSKLAVKLDTAVKDMTPSLKEQLKNDEARRKREAST... | Function: Has a major regulatory role in sexual and asexual development. It may bind DNA itself or it may have a role in preventing DNA-binding of another protein.
Sequence Mass (Da): 75057
Sequence Length: 681
Domain: The C-terminal domain has a high percentage of Ser, Pro and Thr residues.
Subcellular Location: Nucle... |
Q0PAR0 | MIFLKNICKNIGENAILKNVSLSIEKGEFVAIIGQSGSGKTSLLNIIGTLDTPSSGTYVFDEYEVTKLNNDEKARLRREKIGFIFQRYNLLSLLSAKENVSLPAVYAGKNLQERSQNAKKLLNDLELAHKLDSKPNELSGGQQQRVSIARALINGGELILADEPTGALDSKSGIMVLEILQKLNEQGHTIVLVTHDPKIAAQAKRVIEIKDGEILSDTKKEKAQEKLILKTMPKEKKTLTLLKNQAFECFKIAYSSILAHKLRSILTMLGIIIGIASVVCVVALGLGSQAKVLESIARLGTNTIEIRPGKGFGDLRSGKT... | Function: Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70273
Sequenc... |
Q3B5J7 | MAPTTPLLELVDVHRTYPVGESTVNALRGVSLEIREGEFVAIMGSSGSGKSSLLHILGLLDNPDRGEYRILGRNVNALPEDGQAGLRNHVAGFVFQQFHLLKRMSIVDNVRLPHIYSGLKGDFRHEALESLKKVGLMHRLDHTPGQLSGGEQQRVAIARALIGNPMILFADEPTGNLDSRNSLEIMKILEELHREGRTIVMVTHEDEIAAYADRVITMRDGLVVSDQRRDRVCLPAGPSVPLTLDPHAMMDASRNLSVWQDGRFIGFVQQAFQSIFANKVRSLLSVLGILVGVASVIAMMALGEGAKVSIEEELKSMGSN... | Function: Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72260
Sequenc... |
O06924 | MQKEKVWDKLSTDTEERMNAANELFSDRKVVPSQNGVALLEAVIRAGDRINLEGNNQKQADFLAECLGSCDSEKINNLHMVQSAVPLPIHLDIFDKGIAKKLDFAYGGPMAAKVAEFLREGKLELGAIHTYLELFARYFMDLTPRVSLICAYEGDKDGNLYTGFNTEDTPVIAEATKFRQGIVIAQVNKLVDKVQRVDIPGEWVDAVIESPKPFYLEPLFTRDPANITDTQVLMGMMALKGIYGEYGVQRLNHGIGFFTAAIELLLPTYGNELGLKGKICKHFALNPHPTMIPAIEDGWVESIHSFGGELGMQKYCEARP... | Function: Alpha subunit of the biotin-independent and biotin-dependent malonate decarboxylase multienzyme complex (EC 4.1.1.88 and EC 7.2.4.4, respectively). Acts as an acyl-carrier protein (ACP) transferase component. This first step in malonate decarboxylation involves the exchange of an acetyl thioester residue boun... |
O06923 | MEQLMSLFPAISTLFTQDPVISITRIALIIFGFFLSYFGFKRTLEPLIMVPMGLGMIAINAGVLFLEAGVVGTIHLDPLVSEPSVLVNLMQVNWLQPVYNFTFSNGLIACIVFFGIGAMSDISFILIRPWASIIVALFAEMGTFATLIIGIKMGLLPNEAAAVATIGGADGPMVLFASLILAKDLFVPIAIIAYLYLSLTYAGYPYLIKLLVPKKYRGLEVEMDFPEVSQRSKFVFSVLACMLLCLLLPVASPLILSFFLGIAIKEAQIEPFQNLLETTLTYGSTLFLGLLLGALCEAKTILDPKISLIVVLGITALLIS... | Function: Beta subunit of the biotin-dependent malonate decarboxylase multienzyme complex (EC 7.2.4.4). Acts as an integral membrane-bound carboxybiotin protein decarboxylase by releasing the carboxyl group of the carboxylated biotin carrier MADF. The free energy of the decarboxylation reaction is used to pump Na(+) ou... |
Q13477 | MDFGLALLLAGLLGLLLGQSLQVKPLQVEPPEPVVAVALGASRQLTCRLACADRGASVQWRGLDTSLGAVQSDTGRSVLTVRNASLSAAGTRVCVGSCGGRTFQHTVQLLVYAFPDQLTVSPAALVPGDPEVACTAHKVTPVDPNALSFSLLVGGQELEGAQALGPEVQEEEEEPQGDEDVLFRVTERWRLPPLGTPVPPALYCQATMRLPGLELSHRQAIPVLHSPTSPEPPDTTSPESPDTTSPESPDTTSQEPPDTTSPEPPDKTSPEPAPQQGSTHTPRSPGSTRTRRPEISQAGPTQGEVIPTGSSKPAGDQLPA... | Function: Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes. Isoform 2, lac... |
Q61826 | MESILALLLALALVPYQLSRGQSFQVNPPESEVAVAMGTSLQITCSMSCDEGVARVHWRGLDTSLGSVQTLPGSSILSVRGMLSDTGTPVCVGSCGSRSFQHSVKILVYAFPDQLVVSPEFLVPGQDQVVSCTAHNIWPADPNSLSFALLLGEQRLEGAQALEPEQEEEIQEAEGTPLFRMTQRWRLPSLGTPAPPALHCQVTMQLPKLVLTHRKEIPVLQSQTSPKPPNTTSAEPYILTSSSTAEAVSTGLNITTLPSAPPYPKLSPRTLSSEGPCRPKIHQDLEAGWELLCEASCGPGVTVRWTLAPGDLATYHKREA... | Function: Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both the integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes. Both isofo... |
O06926 | MAKWTELQDKSFLEATARERAVGIVDEGTFTEFCGPFDKIYSPHLPLMGEAIEYDDGLVAGVGKIGKKPIFVISQEGRFIGGSIGEVSGAKMVKTIQLASDLYEEMVSEKPDLPEEMRPAVVISFETGGVRLHEANAGLLAHAEVMDQIQNCRGRVPIISLIGSRVGCFGGMGFVAAATDVIIMSQFGRLGLTGPEVIEQEMGKDEFDASDRALVYRTTGGKHKYIIGDCNYLAADSIRSFRETTTAVLQKPMEEIETFRRIGSMEKIKEQIELVKLSVSLKPKDSMDVWAHAGNENPESLINMTLDEFLAQAKRLKA | Function: Gamma subunit of the biotin-dependent malonate decarboxylase multienzyme complex (EC 7.2.4.4). The two subunits MADC and MADD are required for the transfer of the malonate carboxy group from the acyl-carrier protein (ACP) to the prosthetic group of the biotin carrier MADF. Required for the regeneration of ACP... |
G5EDB2 | MPILHQKIASTGGQPSTNSLALRRLPLVVIPRKRKYKNYVSRRRNTQLLASLRRCVSDPNVYKSYNHWKALLRPMTPIKSGAPTPKTVTPMPVPQIPPHQKMTPNPTPTQNPVQLPLPHAVSEKPGDKKSTGPTPSPVPSKAPISAAKLPGTVTKVAPLLSAAQPPPKTLAPAPGASETNSGSGPVSKQVSGKLTELKSKNGTVTEKTEKAVLRIPSSASTRAKAASAVAPEANPAPVPTATKPSPFAPAIAPLRDGAPAQPPAPIQASAPLRPPVAKQNSLQKPPEPKRSVGAPPKALPSELVNKIDGIEFLPQSSNQN... | Function: Probable dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Negatively regulates p38 MAPK signaling to allow for the plasma membrane of body wall muscle cells to form projections, also called muscle arms, that extend and connect the body wall muscles to target motor ne... |
Q757I6 | MSPTNNGRNKKLGPRRKVPGRVSKSKSRAKVQAGDAKRVLDANALKWEKVDVPDTLGDFGGFYGLEEIDGVDVEVVDGKVQFVARDESRLKSPADAVDGTDMVEVDEDAGMEDVTEFRNLDDVAEGELSALSDEGSASEDDGSDSSGSSDMDEDDDQELQSEIFNKDIGLDEAEAPELPSWTNTMKLSATVLQGLSRLGFSNPTEIQLQSIPKALDGHDIMGKASTGSGKTLAYGIPILEGIIRDDTDSRPIGLIFTPTRELAHQVTDHLREVGALLVKRNPYSIMCLTGGLSIQKQERLLKYKGSARVVVATPGRFLEL... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 83477
Sequence Length: 752
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
Q4WMS3 | MGQKRQRDSKNLTLHSKKRKKAENATATDSDDGWDGIVGADELNWKEVALPDRLEDAGGFYGLEEIEGVDIVRGSGNGEVKFKAVAGKPKKSILKKKALEDENPEYEEEWSGFSDDDADRPENASSTVVEKPEKSDRKADKKSEKNADKKEAKDAKKKEAKAAKKEQKEKGSAIQRDMSINAGLSFAALQDTEEDDGADVSAWDSLGLSPEILTGLSKMKFGSPTSVQEACIPQILEGHDVIGKASTGSGKTLAFGIPILEHYLEKKRDDISAQKEQMSEKDSTPIALILSPTRELAHQLSKHIGELIAQAPGVNARIAL... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 85509
Sequence Length: 777
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
Q59ZH9 | MAKQGKNKVSKPRKPPTLKQKLKKESKVVKAKDLQWKLVDIPDNLGDYEGFYGLEEIDGVDVQIVNGKAEFIVRDNGKVENKSKKEETNENGENNMDVEDNETPEVEDEKPTEQEEEEEEEEEEEEEEEEEEEEEEFAGFEDDENNQEDANTSERVSNNDKDDKLAESNDELNAVSFANLDLPLPDDNEINLPNWQEGDLGSSISAYTLYGLSQLDFKKPTPIQKETIPIALSGKDVIGKATTGSGKTLAYGIPILEKYIQSLNLIKQNNKDKKINHPTGIIFAPTRELAHQVVDHLNKLAKYSPLSTRGIVSITGGLSI... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 88059
Sequence Length: 782
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
Q1E7Y4 | MAQKRSHNHKDHTAKAIKRRKFNAATAKSSDDAAHDIVSVDQLDWKTVTLPDRLDDAEGFYGLEEIEGVDILRPSGGGEIKFKASKSKIKGILKNSTDKSGQPAEDWEEWSGFGDDSEDGDGTTLEAEKKAENHGKVNDRRTKTNNSNKEKESNKLPKDRGPRIKTDNGIKTGVSFAALQDEVEEDVDVSAWDSLDLSAELQTSLGRLKFSSPTPIQSACIPAVLQGHDVIGKASTGSGKTLAFGIPIVEYFLGKYRGGRAPTASEERESTKEPMALILSPTRELAHQLNKHLTDLVNHAPNTQVRIATVTGGLSIYKQQ... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 86750
Sequence Length: 783
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
P0CQ90 | MAKIDKKTKLKLNKKSVRAPSKPTTEKKPKKYVTADTLTWKPVKTSSFSGIDGGGGMMMLEELEDVGIEWEETDGGRKIAKFVEVESKTSKGKKNAAQEEPNQEGRGDDEKASSASETEEGKKADDKEAVEEDDEEEFPDFAGFAEEDLNAADEEEHPNLDDEPAFNDDLLPEWSSISLHPSLKRSFLASSFTAPTAIQSRAIPAGITGRDVVGVAETGSGKTLAYSLPILHYLLGQRKSKAGIKRPLSALVLCPTRELALQVMDHLNALLKHALATPDGEKPQGPPRVSVGSVVGGLSAQKQKRILERGCDVIVATPGR... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 85544
Sequence Length: 772
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
Q4IBS2 | MVPPSKKRKLPAATGPATKRSKNIPKPSSSKKKSGKESRSTVEAGALSWASVGEDFGGLEVIEGVDVVKDGNRVQFLVSGDKNKSNIIDPQQEVVDGDRPFEGFGDDAVEVGDIDSGEVGSDQAGAESKKPQGKNKGKNEPKEGQEKADQETNKKQKQKQNKNKLDGKNGAGNKQDEQLVKAAQGVQKSSTRGGNTFGALADGNDYKDQEDVDMAAWVSLNLSPQIISAIAKLKFMKPTKIQKRTIPEIVAGHDVIGKAQTGSGKTLAFGIPMVERWLEMQEQGVKRTGPMSLVLSPTRELAKQLGDHLKALCDGLPSAP... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 84922
Sequence Length: 781
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
A4REU9 | MTTDTTKQKRKLDSKQNTSPKRRKVQANGKAQPKAKKPKRVVAADSLSWRSVEIPELFDDAEGFFGLEEVEGVDVIRDGGMVKFVTAAPAAEKEDEGDDFSGFDDNPESTSLVAAEEAKSEEPAKPQSQKKQQTKQPKSETKEKKEKPAKAKKNEKQTSKTDDDDLATGSFAALAEIDETDEGADVSEWEPLGLSEEIMSSIAKLKFAKPTAIQAATIPEILAGHDVVGKASTGSGKTLAFGIPIVEKWLSINASTQSKRVAEGETKTPIALVLSPTRELAHQLTDHIKNLCAGLATSPYVCSVTGGLSVHKQQRQLEKA... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 82752
Sequence Length: 760
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
O06992 | MKNLENKSFIIRCLKAAASPSGVCRYGNTFSWLQLSFLFLFLTACLMAPLAVSFVKMDRFSVSSFMPSAIQGVNDQFADQLQGFQIRNGKLTGGKSSERIEDGQNVMAVDMKHEYETSGENGRLKVTGFENAIIFQPDQLVITDQNETGFSVGYAKMDVKLEKPNVHDVEVLIDTLWLAQYKPMIMMLAYTVVSMIQLLLTFVLAGGLWITKISNMVSIASFKEAASIAICASALPAFAAAAIGMVHFDLITVLMIHSCGVTLMISFAFRYLTKTRRDNGNLHSGGNDDKSAVI | Function: Could have a role in maltodextrin utilization.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32330
Sequence Length: 294
Subcellular Location: Cell membrane
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Q45632 | MGAAFKWGAAARKTVFPLFYFLIFFAFGALFPLLSVYLQEEARLSGAAIGWIMSLPPIVTMAAQPLWGTAADYTRKPVGLLLAALVLAALFGVMYALAGSYRLFVVLTVLLSAMQSAIVPLSDSLALRHVHEQGGNYGAIRLWGSLGFAMAVLAVGWLSDHIAFAVIFYAFSLALLTAAALATRLPRYPMGAPGALTRQDVRGLLASRPFRLLLVATFLLFGPILANNSYFGLLIHELGGTLTGIGLAFLFAAGSEAPFMKAADRLIGRFGMVRLLLLAALISAARWLAYAADPPLWFVYMTTVVQGCSVGLAIPTALQY... | Function: High affinity transport of maltose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42326
Sequence Length: 394
Subcellular Location: Cell membrane
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L8B068 | MHHPGPPRFVATGDEVELAPRDPDPTATYTWRLTQAPAQSTVSLGDDPVEHFVPDAPGRYVVRLTAPDGEHDLTVRAFPGTLESSGTHTSGRSGGHSGGVSGGRSGPGRSGSGEYTQAGDGSDGGGGGQPRLTLRPDIEGDEAVVRADCSPHPEGTETAADLAVEFLLDDRDDVDADAVTRDGTALRIPLDALPERARIHAVAVGNHGYSVPDAVEFTRGGDGVETVTSGAGVAARRPYDAPAWAEDSVIYEIYVRTFAGERDESPFDAITDRLDYLDSLGVDAIWLTPVLQNDHAPHGYNITDFFEIASDLGTRADYER... | Function: Alpha-amylase that cleaves starch into oligosaccharides, the first step in starch degradation (By similarity). Endo-acting enzyme which prefers a linear polysaccharide to branched polysaccharides hydrolyzing alpha-1,4 glucosidic bonds efficiently. Has also transglycosylation activity, but does not act on alph... |
L0E155 | MAPTPKYTFTERAAAGNLSDAEILNSNNPTGSELPDESDVVVGGAGIHGLIYALHASKYKPNNLKISVIEKNTRPGYKIGESTLPIFYTWCKLHGISAAYLLRLFGLKDGLCFYFLDRENQGQYTDFCSVGAPGLVLASLQIERPMSELLFTILAQRNGVNVYHGREVDFKSTVVQGGGQGNKIAVSRGKYDSTPKTIDSALFVDATGRFRQFCSKKAPRHRFDGWNCNAFWGYFTAPKDESKIPFDLYEGDHTNHLCFPEGWVWVIRLPSWEGSLIANLMDMVTYILECADAGVPGDELPSSEELARMFGLKFQWVTSI... | Cofactor: Binds 1 FAD per subunit.
Function: Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of malbran... |
L0E4F8 | MAPTRRSRDLLRGKNVLIIGGTSGIGFAVAQLVIEHGAMACIAGSNPTKLGKALDALKQHPDRDPIAIVQSATCDLFDVPNLEQNLDNLLKLAAGDSKIHHIVFTAADMVQPPPLASVTIEQIQRVGTIRFTAPMLVAKLLPKYMELCPENSYTLTSGSHAKQPDPGWSLVTGYCGGVEGLMRGLAVDMMPLRVNVVSPGAVLTPVLRDILGDSLEIALDAARKKSTTGRIARPEDVAEAYLYIMKDQNITGTVLETSAGMLLR | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of malbrancheamide biosynthesis invol... |
P0A4N1 | MKGVNMEKQQPSKAALLSIIPGLGQIYNKQKAKGFIFLGVTIVFVLYFLALATPELSNLITLGDKPGRDNSLFMLIRGAFHLIFVIVYVLFYFSNIKDAHTIAKRINNGIPVPRTLKDMIKGIYENGFPYLLIIPSYVAMTFAIIFPVIVTLMIAFTNYDFQHLPPNKLLDWVGLTNFTNIWSLSTFRSAFGSVLSWTIIWALAASTLQIVIGIFTAIIANQPFIKGKRIFGVIFLLPWAVPAFITILTFSNMFNDSVGAINTQVLPILAKFLPFLDGALIPWKTDPTWTKIALIMMQGWLGFPYIYVLTLGILQSIPND... | Function: Part of the binding-protein-dependent transport system for maltodextrin; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48302
Sequence Length: 435
Subcellular Location: Cell membrane
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Q7TQJ1 | MLPPPPRQPPPQARTARGSLRLQRAFLRGPLGVLRLLQLLAGAAFWITIATSKYQGPVHFALFVSVLFWLLTLGLYFITLLGKQELVPVLGSRWLVVNVAHDLLAAALYGAATGIMIDQTQRHSYCNLKNYRLPCAYHAFLAASVCGGLCLGLYLLSALYGCCRRYQGKEEVV | Function: Microtubule-associated protein that exhibits cell cycle-dependent localization and can inhibit cell proliferation and migration.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19087
Sequence Length: 173
Subcellular Location: Cell membrane
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Q8N4S9 | MSNDGRSRNRDRRYDEVPSDLPYQDTTIRTHPTLHDSERAVSADPLPPPPLPLQPPFGPDFYSSDTEEPAIAPDLKPVRRFVPDSWKNFFRGKKKDPEWDKPVSDIRYISDGVECSPPASPARPNHRSPLNSCKDPYGGSEGTFSSRKEADAVFPRDPYGSLDRHTQTVRTYSEKVEEYNLRYSYMKSWAGLLRILGVVELLLGAGVFACVTAYIHKDSEWYNLFGYSQPYGMGGVGGLGSMYGGYYYTGPKTPFVLVVAGLAWITTIIILVLGMSMYYRTILLDSNWWPLTEFGINVALFILYMAAAIVYVNDTNRGGL... | Function: Plays a role in the formation of tricellular tight junctions and of epithelial barriers (By similarity). Required for normal hearing via its role in the separation of the endolymphatic and perilymphatic spaces of the organ of Corti in the inner ear, and for normal survival of hair cells in the organ of Corti ... |
Q3UZP0 | MSSSDARSRIRDRGYSEVPRDTSCPDGTIRTFQSLHSSELAVSADPLPPPPLPLQPPFGPSFYSSDTEEPAVAPDLKPVRRFVPDSWKNFFRGKKKDPEWDNPVSDIRYISDGVECSPPASPARANHHPYKDPSRGSQGTFNSQHEADAMFAHDPYASLDRRTQTARTYSEKVEEYNLRYAYMKSWAGLLRILGVVELLLGAGVFACVTAYIHKDNEWYNLFGYTQPYGMGGLGSLGNTYGGYYYSGPKTPFVLVVAGLAWITTIIILVLGMSMYYRTILLDSNWWPLTEFGVNVALFILYMAAAIVYVNDTNRGGLCYY... | Function: Plays a role in the formation of tricellular tight junctions and of epithelial barriers . Required for normal hearing via its role in the separation of the endolymphatic and perilymphatic spaces of the organ of Corti in the inner ear, and for normal survival of hair cells in the organ of Corti .
PTM: Phosphor... |
P53051 | MTISSAHPETEPKWWKEATFYQIYPASFKDSNDDGWGDMKGIASKLEYIKELGADAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKGYDAEGKPIPPNNWKSYFGGSAWTFDEKTQEFYLRLFCSTQPDLNWENEDCRKAIYESAVGYWLDHGVDGFRIDVGSLYSKVVGLPDAPVVDKNSTWQSSDPYTLNGPRIHEFHQEMNQFIRNRVKDGREIMTVGEMQHASDETKRLYTSASRHELSELFNFSHTDVGTSPLFRYNLVP... | Function: Major isomaltase (alpha-1,6-glucosidase) required for isomaltose utilization. Preferentially hydrolyzes isomaltose, palatinose, and methyl-alpha-glucoside, with little activity towards isomaltotriose or longer oligosaccharides. Does not hydrolyze maltose.
Catalytic Activity: Hydrolysis of (1->6)-alpha-D-gluco... |
P59213 | MSSKFMKSAAVLGTATLASLLLVACGSKTADKPADSGSSEVKELTVYVDEGYKSYIEEVAKAYEKEAGVKVTLKTGDALGGLDKLSLDNQSGNVPDVMMAPYDRVGSLGSDGQLSEVKLSDGAKTDDTTKSLVTAANGKVYGAPAVIESLVMYYNKDLVKDAPKTFADLENLAKDSKYAFAGEDGKTTAFLADWTNFYYTYGLLAGNGAYVFGQNGKDAKDIGLANDGSIVGINYAKSWYEKWPKGMQDTEGAGNLIQTQFQEGKTAAIIDGPWKAQAFKDAKVNYGVATIPTLPNGKEYAAFGGGKAWVIPQAVKNLEA... | Function: Part of an ABC transporter complex involved in the uptake of maltodextrins. Binds glycogen-derived linear maltooligosaccharides increasing in size from maltotriose to maltooctaose with the highest affinity for maltotriose. Has a very weak affinity for maltose. Has also a very low affinity for maltotetraitol, ... |
P21517 | MLNAWHLPVPPFVKQSKDQLLITLWLTGEDPPQRIMLRTEHDNEEMSVPMHKQRSQPQPGVTAWRAAIDLSSGQPRRRYSFKLLWHDRQRWFTPQGFSRMPPARLEQFAVDVPDIGPQWAADQIFYQIFPDRFARSLPREAEQDHVYYHHAAGQEIILRDWDEPVTAQAGGSTFYGGDLDGISEKLPYLKKLGVTALYLNPVFKAPSVHKYDTEDYRHVDPQFGGDGALLRLRHNTQQLGMRLVLDGVFNHSGDSHAWFDRHNRGTGGACHNPESPWRDWYSFSDDGTALDWLGYASLPKLDYQSESLVNEIYRGEDSIV... | Function: May play a role in regulating the intracellular level of maltotriose. Cleaves glucose from the reducing end of maltotriose and longer maltodextrins with a chain length of up to 7 glucose units.
Catalytic Activity: Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alph... |
P21145 | MAPAAATGGSTLPSGFSVFTTLPDLLFIFEFIFGGLVWILVASSLVPWPLVQGWVMFVSVFCFVATTTLIILYIIGAHGGETSWVTLDAAYHCTAALFYLSASVLEALATITMQDGFTYRHYHENIAAVVFSYIATLLYVVHAVFSLIRWKSS | Function: Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Could be involved in myelin biogenesis and/or myelin function.
PTM: Lipoprotein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16714
Sequence Length: 153
Subcellular ... |
P40065 | MREKRTISNKDTNYLKFPNKLQRYSRFLSRKISNTSPEKQPKKNIKEHCLSSYHKEHSVKPKQNSGNVAAKEDKDTQHLQNNVANEEATECLTRSNLKKLQEKIFDRELNDIACDHCLCSTENRRDIKYSRLWFLFELEMSENWNENLRLSCYNKYVYSAIDESWKMENILLKEQEKHYEYFPIGQLLIPNNIDYTNKQKRKENIEDLTIEIDSIIETNHQKKRFLPQSVLIKREDEIAFDDFHLDARKVLNDLSATSENPFSSSPNTKKIKSKGKTLEVVPKKKNKKIIGALERKLHIDEN | Function: Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis.
PTM: Phosphorylated by CDC5. This phosphorylation is required for the location to the kinetochores during late pachytene.
Sequence Mass (Da): 35753
Sequence Length: 302
Subce... |
Q54KN4 | MKNFYYFILILLFFNEVCYSLKDGEIKLHLIPHSHCDSGWTSTMNEYYMGQVKSIISSMVQSLNVESNPPRKFVWSEIGFLEQWWDDMPIEIKNDFIKHVKNDRIEFVNGGWVMNDEACASLESVIRQLSNGHKFIREKFGKQPESGWQIDPFGHSSLTPTLQAQFGYKHVVLNRIHYELKKKFKEEKNLQFKWRGSPEGVGPKSDILAHVFDDFYTSPPHMSFDGYNFLAYGLPRLTMEMIELARNRSVFYKSPHVLIPMGGDFAFKNAYKSFEQMDQLVASINGQHANGESNVICQYSTLADFFSDTINWHNENKVSF... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Sequence Mass (Da): 114357
Sequence Length: 994
Subcellular Location: Secreted
EC: 3.2.1.24
|
P55145 | MRRMWATQGLAVALALSVLPGSRALRPGDCEVCISYLGRFYQDLKDRDVTFSPATIENELIKFCREARGKENRLCYYIGATDDAATKIINEVSKPLAHHIPVEKICEKLKKKDSQICELKYDKQIDLSTVDLKKLRVKELKKILDDWGETCKGCAEKSDYIRKINELMPKYAPKAASARTDL | Function: Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain . Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra (By similarity). Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons (By similarity)... |
Q84DC4 | MRHPVDMPEKVGTDAKRLFAQPEHLWELTLTEASALVRHRRITSRQLVEAWLSRIADFSELNAFISVDAAAALKQADSYDHYLEAGGDPLPLGGVPIAVKDNIQVVGFANTAGTPALSKFFPTCNARVIEPLLKAGAIVVGKTNMHELAFGTSGYNTAYHIPGVIGVRNAFDHSCIAGGSSSGSGTAVGALLIPAALGTDTGGSVRQPGAVNGCVGFRPTVGRYPVDGITPISPTRDTPGPIARSVEDIVLLDSIITGALPAEVPAAESIRLGVVDQLWADLSEPVRKLTEDALRKLEQQGVQIVRVSMSEIFEMSHAVS... | Function: Hydrolyzes both the R- and the S-enantiomers of mandelamide, and phenylacetamide. Has lower activity on 3-phenylpropionaide and lactamide. Does not hydrolyze benzamide. Hydrolyzes esters and amides with little steric bulk. Preferentially hydrolyzes aromatic substrates.
Catalytic Activity: (R)-mandelamide + H2... |
F2JVT6 | MSYPAFDSKTFLEAHIEKTMAFYFPTCIDPEGGFFQFFKDDGSVYDPNTRHLVSSTRFIFNFAQAYLHTNIAEYKHAAVHGIQYLRQRHQSQSGGYVWLLDGGTNLDETNHCYGLAFVILAYSNALQIGLSEAEVWIEVTYDLLETHFWENKHGLYLDEISSDWKTVSPYRGQNANMHMCEALMSAFDATQNPKYLDRAKLLAKNICQKQASLSNSNEVWEHYTNDWQIDWDYNKNDPKHLFRPWGFQPGHQTEWAKLLLMLDKRSPENWYLPKAKYLFDLAYKKAWDTKKGGLHYGYAPDGTVCDPDKYFWVQAESFAA... | Function: Catalyzes the reversible isomerization of D-mannose to D-fructose. Can also isomerize D-lyxose, with lower efficiency. In longer reaction with a higher concentration of enzyme, it can isomerize 4-OH D-mannose derivatives (D-talose and 4-O-monosaccharyl-D-mannose). Cannot use D-glucose.
Catalytic Activity: D-m... |
A0A0P9JFY5 | MDNNNHTFSSWLRSPAHHQWLALEGKRLLGFAKAAKLENGFGGLDDYGRLMVGATAGTMNTARMTHCFAMAHVQGIPGCAALIDHGIAALSGPLHDAEHGGWFSAALEDHGKTDKQAYLHAFVALAASSAVVAGRPAAQALLSDVIQVIQSRFWSDEEGAMRESFSQDWSDEEPYRGANSNMHSTEAFLALADVTGDAQWLDRALSIVERVIHQHAGANNFQVIEHFTSGWQPLPDYNRENPADGFRPFGTTPGHAFEWARLVLHLEAARRRAGRSNPDWLLDDARQLFANACRYGWDVDGAPGIVYTLDWQNKPVVRHR... | Function: Catalyzes the reversible isomerization of D-mannose to D-fructose . Shows high specific activity towards mannose and fructose, and has no detectable activity towards other monosaccharides and disaccharides .
Catalytic Activity: D-mannose = D-fructose
Sequence Mass (Da): 46083
Sequence Length: 414
EC: 5.3.1.7
|
A0A077LPS9 | MTLWTARAAHRAWLDAEARRLVDFAAAADHPEHGFAWLDGSGAPLPEQGVHTWITCRVTHVAALAHLEGIPGASALADHGLRALAGPLRDPEHDGWFTALDSRGTVADSRKEAYQHAFVLLAAASATVAGRPGARELLDAAAAVIEQRFWEEETGRCRESWDAAWHADEPYRGANSNMHLVEAFLAAFDATGDRVWAERALRIAHFFVHEVAAPRDWRLPEHFTPDWQVVADYNTDDRAHPFRPYGVTVGHVLEWARLLVHVEAALPDPPSWLLADAEAMFAAAVARGWSVDGTEGFVYTLDYDDTPVVRSRMHWVVAEA... | Function: Catalyzes the reversible isomerization of D-mannose to D-fructose. Shows weaker activity on D-lyxose, but cannot use N-acetyl D-glucosamine.
Catalytic Activity: D-mannose = D-fructose
Sequence Mass (Da): 44917
Sequence Length: 407
EC: 5.3.1.7
|
P11444 | MSEVLITGLRTRAVNVPLAYPVHTAVGTVGTAPLVLIDLATSAGVVGHSYLFAYTPVALKSLKQLLDDMAAMIVNEPLAPVSLEAMLAKRFCLAGYTGLIRMAAAGIDMAAWDALGKVHETPLVKLLGANARPVQAYDSHSLDGVKLATERAVTAAELGFRAVKTKIGYPALDQDLAVVRSIRQAVGDDFGIMVDYNQSLDVPAAIKRSQALQQEGVTWIEEPTLQHDYEGHQRIQSKLNVPVQMGENWLGPEEMFKALSIGACRLAMPDAMKIGGVTGWIRASALAQQFGIPMSSHLFQEISAHLLAATPTAHWLERLD... | Cofactor: Divalent metal ions. Magnesium seems to be the preferred ion.
Catalytic Activity: (S)-mandelate = (R)-mandelate
Sequence Mass (Da): 38565
Sequence Length: 359
Pathway: Aromatic compound metabolism; (R)-mandelate degradation; benzoate from (R)-mandelate: step 1/4.
EC: 5.1.2.2
|
Q01662 | MSTATTTVTTSDQASHPTKIYCSGLQCGRETSSQMKCPVCLKQGIVSIFCDTSCYENNYKAHKALHNAKDGLEGAYDPFPKFKYSGKVKASYPLTPRRYVPEDIPKPDWAANGLPVSEQRNDRLNNIPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPDKTVLKEGDIVNLDVSLYYQGYHADLNETYYVGENISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKP... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the acti... |
Q9FV49 | MAIGNPEVATMGKENTEAESSNGNESQLSSDLTKSLDLAEVKEDEKDNNQEEEDGLKAEASTKKKKKKSKSKKKKSSLQQTDPPSIPVLELFPSGDFPQGEIQQYNDDNLWRTTSEEKREMERLQKPIYNSLRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLISENGLQAGIAFPTGCSLNNVAAHWTPNSGDKTVLQYDDVMKLDFGTHIDGHIVDSAFTVAFNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVEINGKVYQVKSIRNLNGHSIGRYQIHAEKSVPNVRGGEQTKMEE... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
Q4WAY7 | MTVDAPELLEKLRITDAGANGADMSSSTSAAANGTGKEVDDGSDDDGTENPPAVAAEHSTAKKKKNKKRKPKKKQPKVQTDPPSIPLSQLFPNNSYPKGEEVEYKDENRYRTTSEEKRHLDNLNSDFLSDYRQAAEAHRQVRQWAQRNIKPGQTLLEIANGIEESARCLVGHDGLTEGDSLIAGMGFPTGLNIDNIVAHYSPNAGCKTVLAQNNVLKVDIGIHVGGRIVDSAFTMAFDPMYDNLLAAVKDATNTGVREAGIDVRVGELGGYIQEAMESYECEIRGKTYPIKAIRNLCGHTILPYSIHGTKNVPFVKSNDM... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
Q5B4X6 | MAAQASEKLEKLDLNGQNGESAAGPAKAGQADAGEVEDESDDDADDAGAAADGAANGAAKKKKKRKSKKKKKGGAKVQSSPPRVPVSSLFANGQYPEGEIVEYKNENSYRTTNEEKRYLDRMNNDFLQEYRQGAEVHRQVRQYAQKNIKPGQTLTEIAEGIEDSVRALTGHQGLEEGDNIKGGMGFPCGLSINHCAAHYTPNAGNKMVLQQGDVMKVDFGAHINGRIVDSAFTMSFDPVYDPLLEAVKDATNTGIRSLQEAGIDVRMSDIGAAIQETMESYEIELNGTTYPIKPIRNLNGHNIDQHVIHGGKSVPIVKGS... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
Q9UEW3 | MRNKKILKEDELLSETQQAAFHQIAMEPFEINVPKPKRRNGVNFSLAVVVIYLILLTAGAGLLVVQVLNLQARLRVLEMYFLNDTLAAEDSPSFSLLQSAHPGEHLAQGASRLQVLQAQLTWVRVSHEHLLQRVDNFTQNPGMFRIKGEQGAPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGA... | Function: Pattern recognition receptor (PRR) which binds Gram-positive and Gram-negative bacteria . Also plays a role in binding of unopsonized particles by alveolar macrophages (By similarity). Binds to the secretoglobin SCGB3A2 .
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Ma... |
Q9WUB9 | MGNKKALKEEAFLGSAEEGADFDQAMFPVMETFEINDPMPKKRNWGSFCTAVMAIHLILLTAGTTLLTLKVLSLQKWILEKYLDNETLAAEDRSFFSLQLASPETHLVPRTPGLQALQVQLTQVRTSQEQLLQQVDNLTRNPELFRIKGERGSPGIPGLQGPPGIKGEAGLQGPMGAPREPGATGAPGPQGEKGSKGDKGLIGPKGEHGTKGDKGDLGLPGSKGDMGMKGVTGVMGPPGAQGNKGDPGKPGLPGLAGSPGVKGDQGQPGLQGVPGTPGAAGPSGAKGEPGHPGPPGPTGPQGISGSPGAAGLKGSKGDTG... | Function: Pattern recognition receptor (PRR) which binds Gram-positive and Gram-negative bacteria . Also plays a role in binding of unopsonized particles by alveolar macrophages . Binds to the secretoglobin SCGB3A2 (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Ma... |
P12624 | MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPAAAGSGAASPAAAEKDEPAAAAPDAGASPVEKEAPVEGEAAEPGSPTAAEGEAASAASSTSSPKAEDGATPSPSNETPKKKKKRFSFKKSFKLSGFSFKKNKKEAGEGGEAEGAAGASAEGGKDEASGGAAAAAGEAGAAPGEPTAAPGEEAAAGEEGAAGGDPQEAKPEEAAVAPEKPPASEEAKAVEEPSKAEEKAEEAGVSAAGCEAPSAAGPGVPPEQEAAPAEEAAAAPASSACAAPSQEAQP... | Function: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.
Location Topol... |
P29966 | MGAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAESGAKEELQANGSAPAADKEEPAAAGSGAASPSAAEKGEPAAAAAPEAGASPVEKEAPAEGEAAEPGSPTAAEGEAASAASSTSSPKAEDGATPSPSNETPKKKKKRFSFKKSFKLSGFSFKKNKKEAGEGGEAEAPAAEGGKDEAAGGAAAAAAEAGAASGEQAAAPGEEAAAGEEGAAGGDPQEAKPQEAAVAPEKPPASDETKAAEEPSKVEEKKAEEAGASAAACEAPSAAGPGAPPEQEAAPAEEPAAAAASSACAAPSQEAQPE... | Function: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.
Location Topol... |
P30009 | MGAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGGAATPAAADKDEAAAAPEPGAATADKEAAEAEPAEPGSPSAETEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKEAGEGAEAEGATADGAKDEAAAAAGGDAAAAPGEQAGGAGAEGAEGGESREAEAAEPEQPEQPEQPAAEEPRAEEPSEAVGEKAEEPAPGATADDAPSAAGPEQEAPAATDEPAASAAPSASPEPQPECSPEAPPAPVAE | Function: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.
Location Topol... |
Q13YU3 | MTQMNPRGGLQVAANLDQFVETEALPGTGLDSAAFWSGFDALVHELAPKNRALLAERDRLQTELDNWHRANPGPVRDLRAYRAFLEGIGYIVPVPASVKATTDHVDTEIAEQAGPQLVVPLSNQRYALNAANARWGSLYDALYGTDAIPEANGAEKQKAFNPVRGAAVIAYARRFLDQAAPLANGSHADATRYGVEGGKLVVTLKNGTSELKTPAQFIGYQGEESAPSAVLLKHNGLHFEIQIDANDSIGKTDSAHVKDVVVEAAVSTIIDCEDSVAAVDADDKVQLYRNWLGLMNGDLTEEVTKNGKTFTRRLNADRVY... | Function: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Catalytic Activity: acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+)
Sequence Mass (Da): 79450
Sequence Length: 724
Pathway: Carbohydrate ... |
Q9I636 | MTERVQVGGLQVAKVLFDFVNNEAIPGTGVSADTFWTGAEAVINDLAPKNKALLAKRDELQAKIDGWHQARAGQAHDAVAYKAFLEEIGYLLPEAEDFQAGTQNVDDEIARMAGPQLVVPVMNARFALNASNARWGSLYDALYGTDVISEEGGAEKGKGYNKVRGDKVIAFARAFLDEAAPLESGSHVDATSYSVKNGALVVALKNGSETGLKNAGQFLAFQGDAAKPQAVLLKHNGLHFEIQIDPSSPVGQTDAAGVKDVLMEAALTTIMDCEDSVAAVDADDKVVIYRNWLGLMKGDLAEEVSKGGSTFTRTMNPDRV... | Function: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Catalytic Activity: acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+)
Sequence Mass (Da): 78660
Sequence Length: 725
Pathway: Carbohydrate ... |
P0C794 | MNSKHSYVELKDKVIVPGWPTLMLEIDFVGGTSRNQFLNIPFLSVKEPLQLPREKKLTDYFTIDVEPAGHSLVNIYFQIDDFLLLTLNSLSVYKDPIRKYMFLRLNKEQSKHAINAAFNVFSYRLRNIGVGPLGPDIRSSGP | Function: Plays a crucial role in virion assembly and budding.
PTM: Not glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16258
Sequence Length: 142
Subcellular Location: Virion
|
Q9E785 | MLTLFKKGKPKGGSVDDRNSSYRESDPMLVWGTAPPAYLDVYHDERDKNELQFNTKSYLIQANLEVISSKPIERTTEMLKVLDVMVDEYDGSYLSKALIITSYLTIGTHLRRMMSSVKNNHKYNNGFTEVIEFTGTAEIHPRDQEIKYNKYLMTSHMGEPVSISYQFSGKKSKRRGKNILDAYNLELGNGSKPPDLKDLLESYEINLCYNLKGEHGFTNLVKS | Function: Plays a major role in assembly and budding of virion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25494
Sequence Length: 223... |
P24615 | METYVNKLHEGSIYTAAVQYNVIEKDDDPASLTIWVPMFQSSISADMLIKELINVNILVRQISTPKGPSLKIMINSRSAVLAQMPSKFTISANVSLDERSKLAYDITTPCEIKACSLTCLKVKNMLTTVKDLTMKTFNPTHEIIALCEFENIMTSKRVVIPTFLRSINVKAKDLDSLENIATTEFKNAITNAKIIPYAGLVLVITVTDNKGAFKYIKPQSQFIVDLGAYLEKESIYYVTTNWKHTATKFSIKPIED | Function: Plays a crucial role in virus assembly into filaments and budding. Early in infection, localizes in the nucleus where it may inhibit host cell transcription. Later in infection, traffics to the cytoplasm through the action of host CRM1 to associate with inclusion bodies, the site of viral transcription and re... |
P38300 | MSVLRSTCLFFPPRSLLISFNKRRLFSTSRLILNKESETTKKKDKSKQQDFNPRHLGVAAEIFIPSAYKNLPNVFAHPLIVANALIRRLYTFGLNSVQVALFRFQSGIKPSFLLWKNKAIETYINVNTSFAHKNLSDIKGLVSLWVQEALEARSRQLPGNATLDWQLIKFNAVPKLVSVQPIMIPGMPLEHLQLVYKFDTKQRLIKVNQQTKKTETLDRDVVDYIAFLCDATTNDMILMGSLFESKPNDKLPKSYEDDAKVAIHRMKVNGDIYRLPPS | Function: Mitochondrial inner membrane-associated mitoribosome receptor that spatially aligns the mitoribosome exit tunnel with the membrane insertion machinery and allows cotranslational protein membrane insertion.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31811
Sequence Length: 278
Subcellula... |
Q9KU26 | MKLNHRILLLIAPVILLSAAASSYIIYTSQKNALLKRTDSYLQLNIEKLASHYRQAQSLVSSYAFTLAKSDIIRHYFSLEKNPYRELELVDNLRETLQILQPNEKQLVSLSILNGHEELLYYAENSSDPFAELDPKVMAYIKQRFASTQKNSDISYTVNSAGEDILVRYDMLDTQTLSTPLSYNRQDVFFVVVYVVLEQFSQLRKKIEFDNQSPIFFTHSPPSYRTGLLQSVELQPGFYAILDPAPKLINAQLHSIQRELLLSFGVSALVTVLMLLLLLYRHVINPILHLDKQLEEVENNQRKNIEKLNTDDEIGRLSSR... | Function: Plays an essential role in the maintenance and the formation of the three-dimensional structure of the biofilms at the later stages of their development. Absence of mbaA promotes the accumulation of larger amount of biomass on the surfaces at later stage of development, results in the overproduction of an ext... |
Q9FS88 | MHKLFAVRSLSSAIVKSFKSLQNQQAAFSTSLLLDDTQKQFKESVAKFAQENIAPYAEKIDRTNSFPKEINLWKLMGDFNLHGITAPEEYGGLNLGYLYHCIALEEISRASGAVAVSYGVQSNVCINQLVRNGTPDQKQKYLPKLISGDHIGALAMSEPNAGSDVVSMKCRADRVDGGYVLNGNKMWCTNGPVANTLIVYAKTDTTAGSKGITAFIIEKEMPGFSTAQKLDKLGMRGSDTCELVFENCFVPNENVLGQEGKGVYVLMSGLDLERLVLAAGPVGIMQACMDIVIPYVRQREQFGRPIGEFQLIQGKLADMY... | Function: Short/branched-chain acyl-CoA dehydrogenase (SBCAD). Uses 2-methylbutanoyl-CoA as substrate. Minor activity with the straight-chain substrates, butanoyl-CoA, valeryl-CoA, hexanoyl-CoA, and octanoyl-CoA but no activity with isovaleryl-CoA.
Catalytic Activity: 2-methylbutanoyl-CoA + H(+) + oxidized [electron-tr... |
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