ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P0DPT3 | EHGYLLDKYTGCKVWCVINNESCNGECNKRRGGYYGYCYFWKLACYCQGARKSELWNYKTNKCKS | Function: Has a toxic effect on insects and mammals. On German cockroach larvae, it provokes contraction, paralysis and lethality . Intracerebroventricular injection into mice causes severe neurotoxic symptoms . It fully competes with the binding of the iodinated Css4 (AC P60266) on rat brain synaptosomes, with moderat... |
P60275 | GKEGYPVDSRGCKVTCFFTGAGYCDKECKLKKASSGYCAWPACYCYGLPDSVPVYDNASNKCB | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). This toxin is only active against insects.
Sequence Mass (D... |
A0F0C2 | MKILTVFMIFIANFLNMMQVFSVKDRFLIINGSYELCVYAENLGEDCENLCKQQKATDGFCRQPHCFCTDMPDNYATRPDTVDPIM | Function: Binds to sodium channels (Nav) and affects the channel activation process.
Sequence Mass (Da): 9959
Sequence Length: 86
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P86408 | MNSLVMISLALLVMTGVESVRDGYIADDKNCAYFCGRNAYCDEECKKKGAESGYCQWAGQYGNACWCYKLPDKVPIKVSGKCNGR | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin inhibits inactivation of Nav1.6/SCN8A (EC(50)=3.1 uM) and drosophila DmNav1 (EC(50)=1.17 uM) . It also shows a weak inhibition o... |
Q6H611 | MAQPAFLSALRSRLRSPQPQAPALPHLQPPRRGFHVELGAREKALLEEDTALKRFKSYKNSVKQVSKVGNILTGVVLFACAYEIVALANS | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 9899
Sequence Length: 90
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q0DF13 | MIYRNWSLLSSTVVIWGGVATAGLAGIFLFGGKEKFQNYLCREGERLRQQDRAAMGKN | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 6510
Sequence Length: 58
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q9SKE0 | MIYRKWSLLSGPPVILGGAVIAAVAVGFVLQNVTKGEQKKNVSTNK | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 4884
Sequence Length: 46
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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O82663 | MWRCVSRGFRAPASKTSSLFDGVSGSRFSRFFSTGSTDTRSSYTIVDHTYDAVVVGAGGAGLRAAIGLSEHGFNTACITKLFPTRSHTVAAQGGINAALGNMSEDDWRWHMYDTVKGSDWLGDQDAIQYMCREAPKAVIELENYGLPFSRTEEGKIYQRAFGGQSLDFGKGGQAYRCACAADRTGHALLHTLYGQAMKHNTQFFVEYFALDLLMASDGSCQGVIALNMEDGTLHRFRSSQTILATGGYGRAYFSATSAHTCTGDGNAMVARAGLPLQDLEFVQFHPTGIYGAGCLITEGSRGEGGILRNSEGERFMERYA... | Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Location Topology: Pe... |
Q33862 | MLRAVRALICRIGARRTLSVSSSRLDVSTSNIAQYKVIDHAYDVVIIGAGGAGLRAAMGLGEAGFKTAVVTKMFPTRSHTTAAQGGINAALGSMNPDDWKWHFYDTAKGSDWLGDQNAMHYLTRNAVEAVTELENFGMPFSRTPEGKIYQRSFGGQSNNYGKGGVAKRTCCVADRTGHSMLHTLYGNSLRCHCTFFIEYFALDLLMDKGRCVGVIALCLEDGTIHRFRSKRTIVATGGYGRAYFSCTTAHMNTGDGTALATRAGIALEDLEFIQFHPTGIYGVGCLITEGSRGEGGFLVNSEGERFMERYAPKAKDLASR... | Cofactor: Binds 1 FAD covalently per subunit.
Function: Flavoprotein (Fp) subunit of the mitochondrial electron transport chain complex II which, together with the iron-sulfur protein (Ip) subunit forms the catalytic core of the complex . During the parasitic larvae and adult stages, which occur in an anaerobic environ... |
Q9ZPX5 | MWRCLRVASSSRRSESNGAFITSQLSRFFSAPPSAGDKSSYTIVDHTYDAVVVGAGGAGLRAAIGLSEHGFNTACITKLFPTRSHTVAAQGGINAALGNMSVDDWRWHMYDTVKGSDWLGDQDAIQYMCREAPKAVIELENYGLPFSRTEDGKIYQRAFGGQSLEFGIGGQAYRCACAADRTGHALLHTLYGQAMKHNTQFFVEYFALDLIMNSDGTCQGVIALNMEDGTLHRFHAGSTILATGGYGRAYFSATSAHTCTGDGNAMVARAGLPLQDLEFVQFHPTGIYGAGCLITEGARGEGGILRNSEGEKFMDRYAPT... | Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Location Topology: Pe... |
Q8WSR3 | MLNAARGLAIRLSTRRALSYSGPCCAAKTSNIAEYKVVDHAFDAVVVGAGGAGLRAAMGLSEGGLKTAVITKLFPTRSHTVAAQGGVNAALGNMNPDDWRWHFYDTVKGSDWLGDQDAIHYMTREAVRAVIELENYGMPFSRTADGKIYQRAFGGQSNDFGRGGQAHRTCCVADRTGHSMLHTLYGSSLQYNCQYFIEFFALDLIMDKGACVGVVAMDLEDGTIHRFRSKNTVLATGGYGRAFFSCTSAHTCTGDGTALATRAGIGNSDMEFVQFHPTGIYGAGCLITEGSRGEGGFLVNSKGERFMERYAPNAKDLASR... | Cofactor: Binds 1 FAD covalently per subunit.
Function: Flavoprotein (Fp) subunit of the mitochondrial electron transport chain complex II which, together with the iron-sulfur protein (Ip) subunit forms the catalytic core of the complex . During the free-living larvae stages, which occur in an aerobic environment, comp... |
O34607 | MFRNVKELIEITKEKQILISDVMIAQEMEVTEKTKEDIFQQMDHNLSVMEAAVQKGLEGVTSQTGLTGGDAVKLQAYIRSGKSLSGPLILDAVSKAVATNEVNAAMGTICATPTAGSAGVVPGTLFAVKEKLNPTREQMIRFLFTAGAFGFVVANNASISGAAGGCQAEVGSASGMAAAAIVEMAGGTPEQSAEAMAITLKNMLGLVCDPVAGLVEVPCVKRNAMGASNAMIAADMALAGITSRIPCDEVIDAMYKIGQTMPTALRETGQGGLAATPTGRELEKKIFGGALGSRETTSAN | Cofactor: Binds 1 [4Fe-4S] cluster.
Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 30936
Sequence Length: 300
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.3.1.17
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O34635 | MKYRSVFDIIGPVMIGPSSSHTAGAARIGRVARSLFGREPERIIVSFYGSFAETYKGHGTDVAIIGGLLDFDTFDERIKTAIQIAEAKGIDIEFRVEDAVPVHPNTAKITISDEKGELELTGISIGGGKIEITELNGFELRLSGNHPAILVVHNDKFGTIAGVANVLAKFSINVGHMEVARKDIGQLALMTIEVDQNIDDHILDELSKLPNIIQVTKIAD | Cofactor: Binds 1 [4Fe-4S] cluster.
Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 23819
Sequence Length: 220
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.3.1.17
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P80212 | MKYDSLADLVVQAEKQNVPLXXLIXKDQAE | Cofactor: Binds 1 [4Fe-4S] cluster.
Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 3394
Sequence Length: 30
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.3.1.17
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P08065 | MSQSSIIVVGGGLAGLMATIKAAESGMAVKLFSIVPVKRSHSVCAQGGINGAVNTKGEGDSPWEHFDDTVYGGDFLANQPPVKAMCEAAPSIIHLLDRMGVMFNRTPEGLLDFRRFGGTQHHRTAYAGATTGQQLLYALDEQVRRYEVAGLVTKYEGWEFLGAVLDDDRTCRGIVAQNLTNMQIESFRSDAVIMATGGPGIIFGKSTNSMINTGSAASIVYQQGAYYANGEFIQIHPTAIPGDDKLRLMSESARGEGGRVWTYKDGKPWYFLEEKYPAYGNLVPRDIATREIFDVCVNQKLGINGENMVYLDLSHKDPKE... | Catalytic Activity: a quinone + succinate = a quinol + fumarate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65152
Sequence Length: 586
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.1
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Q09508 | MLRAASNGLRNTVAARSVSLSAANHSDAKRSDIAQYKVVDHAYDAVVVGAGGAGLRAAMGLAEGGLKTAVITKLFPTRSHTVAAQGGINAALGNMNPDNWRWHFYDTVKGSDWLGDQDAIHYMTREAERAVIELENYGMPFSRTTDGKIYQRAFGGQSNDFGRGGQAHRTCCVADRTGHSLLHTLYGASLQYNCNYFVEYFALDLIMENGVCVGVIAMDLEDGTIHRFRSKNTVLATGGYGRAFFSCTSAHTCTGDGTALTARAGINNSDMEFVQFHPTGIYGAGCLITEGSRGEGGYLVNSAGERFMERYAPNAKDLAS... | Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Location Topology: Pe... |
P51054 | MSSIRVKQYDALIVGAGGAGLRAALEMAQSRQYKVAVVSKVFPTRSHTVSAQGGIAAALGNVVPDKPIWHMFDTVKGSDYLGDQDAIQYMCEQAPPSVYELEHYGLPFSRLDDGRIYQRAFGGHTRDFGKEMARRTCACADRTGHAMLHTLYQKNVEAGTHFYYEWYGIDLVRGAQGGIAGMIAMNMETSELVFFKSRATIFATGGAGRIYETTSNAYTNTGDGIGMVLRAGLPVQDMEFWQFHPTGIYGVGCLITEGARGEGGYLINKDGERFMERYSPHLKDLDCRDVVARSILQEVMAGGGVGPKKDHVLLKLDHLG... | Catalytic Activity: a quinone + succinate = a quinol + fumarate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65438
Sequence Length: 587
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1.
Subcellular Location: Cell inner membrane
EC: 1.3... |
Q9U3X4 | MLSSALKLTKKVCSTKSNGLIRSFSTQTQSRDYAVVDHTYDAIVVGAGGAGLRAALGLTEKGYKTACITKLFPTRSHTVAAQGGINAALGNADQDDWRWHAYDTVKGSDFLGDQDAIHYMCKEAVPTVLELEQYGVPFSRMDDGRIYQRAFGGQSKNFGKGGQATRCCAAADRTGHALLHTLYGQAVKHNTKFFIEYFVTDLIMENGDCRGVVAINLEDGTIHRFRSHATVIATGGYGRAYFSATSAHTCTGDGNAMVIRAGLPCQDLEFVQFHPTGIYGSGCLITEGARGEGGYLLNSSGERFMPRYAPSVADLASRDV... | Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Location Topology: Pe... |
G4V4G2 | MDIDNKPRIHWACRRGMRELDISIMPFFEHDYDTLSDDDKRNFIRLLQCDDPDLFNWLMNHGEPTDQGLKHMVSLIQTRNKNRGPVAM | Function: An FAD assembly protein, which accelerates covalent attachment of the cofactor into other proteins . Plays an essential role in the assembly of succinate dehydrogenase (SDH, respiratory complex II), an enzyme complex that is a component of both the tricarboxylic acid cycle and the electron transport chain, an... |
Q9LZA6 | MDISNEASVDPFSIGPSSIMGRTIAFRVLFCRSMSQLRRDLFRFLLHWFLRFKLTVSPFVSWFHPRNPQGILAVVTIIAFVLKRYTNVKIKAEMAYRRKFWRNMMRTALTYEEWAHAAKMLEKETPKMNESDLYDEELVKNKLQELRHRRQEGSLRDIMFCMRADLVRNLGNMCNSELHKGRLQVPRHIKEYIDEVSTQLRMVCNSDSEELSLEEKLSFMHETRHAFGRTALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELQSFFENSLHSLQFFDQLGGVFSIVKRVMTQGALHDIRQ... | Function: Involved in the release of fatty acids from the oil body in germinating seedlings . Can hydrolyze triacylglycerols and diacylglycerols but not monoacylglycerols, phospholipids, galactolipids or cholesterol esters . SDP1 lipase activity is required to limit triacylglycerol accumulation in roots, leaves and ste... |
P40479 | MNIYTSPTRTPNIAPKSGQRPSLPMLATDERSTDKESPNEDREFVPCSSLDVRRIYPKGPLLVLPEKIYLYSEPTVKELLPFDVVINVAEEANDLRMQVPAVEYHHYRWEHDSQIALDLPSLTSIIHAATTKREKILIHCQCGLSRSATLIIAYIMKYHNLSLRHSYDLLKSRADKINPSIGLIFQLMEWEVALNAKTNVQANSYRKVP | Function: Mediates dephosphorylation of MAPK substrates such as SLT2, acquiring enhanced catalytic activity under oxidative conditions.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 23886
Sequence Length: 209
EC: 3.1.3.48
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Q9SS48 | MSLASIRRLAAGAAVIAAASGGAVYLSPSVASSDKGGGPILDSLRRRLGDPTASVPSRSAQESALIAATASDPLDVLVIGGGATGSGVALDAVTRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYLEKAVFNLDYGQLKLVFHALEERKQLIENAPHLCHALPCMTPCFDWFEVIYFWMGLKMYDLVAGPRLLHLSRYYSAKESIELFPTLARKGKDKNLRGTVVYYDGQMNDSRLNVGLACTAALAGAAVLNHAEVVSLITDDATKRIIGARIRNNLTGQEFNSYAKVVVNAAGPFCDSIRKMIDEDTKPMICPSSGVH... | Function: Required for glycerol catabolism and involved in NADH/NAD(+) homeostasis . Essential for postgerminative growth and seedling establishment .
Catalytic Activity: a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 68451
... |
Q700X4 | MSPAFDIAPLDATFGAVVTGVKLADLDDAGWLDLQAAWLEYALLVFPDQHLTREQQIAFARRFGPLEFEMAAISNVRPDGSLRVESDNDDMMKILKGNMGWHADSTYMPVQAKGAVFSAEVVPSVGGQTGFADMRAAYDALDEDLKARVETLQARHSLHYSQSKLGHQTKAADGEYSGYGLHDGPVPLRPLVKIHPETGRKSLLIGRHAHAIPGLEPAESERLLQQLIDFACQPPRIYHHDWAPGDAVLWDNRCLLHQATPWDMTQKRIMWHSRIAGDPASETALAH | Function: Involved in the degradation of the phenoxypropionate herbicides. Catalyzes the enantiospecific cleavage of the ether bond in the herbicid S-dichlorprop ((S)-2-(2,4-dichlorophenoxy)propionate)(S-2,4-DP) and S-mecoprop ((S)-2-(4-chloro-2-methylphenoxy)propionate)(S-2,4-MCPP). It can also accept (RS)-2-(4-chloro... |
O34616 | MKILNSLEGYIDTYNPWKNTYALFRSLLGFSTLLVLLFNSTDILFSYSANNVTCENVYIPTAFCFAKEYSINFEIIRYLMIFILTLVVIGWRPRFTGLFHWYICYSIQTSALTIDGGEQIATVLSFLILPVTLLDSRRNHWNIKKNNNESFTKKTVLFYIMTIIKIQVFIIYLNAALERLKNKEWAEGTAIYYFFSDPVFGLPEYQLNLMNPLLESNFIVVITWLVTIFELFLAASIISNIRIKRIALVLGILFHIGIIFSIGIVSFGLIMISALIIYLHPVQQNITMNWCSPLFKYIYVKGKRNFKRIGGESVKFLTKL... | Function: Required for the maturation of SdpC to SDP . Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37450
Sequence Length: 323
Subcellular Location: Cell membrane
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O34344 | MKSKLLRLLIVSMVTILVFSLVGLSKESSTSAKENHTFSGEDYFRGLLFGQGEVGKLISNDLDPKLVKEANSTEGKKLVNDVVKFIKKDQPQYMDELKQSIDSKDPKKLIENMTKADQLIQKYAKKNENVKYSSNKVTPSCGLYAVCVAAGYLYVVGVNAVALQTAAAVTTAVWKYVAKYSSSASNNSDLEAAAAKTLKLIHQ | Function: Produces a 42-residue extracellular sporulation delaying protein (SDP) that collapses the proton motive force (probably both the membrane potential and pH gradient) across the cell membrane, which leads to autolysis; may form a proton channel . Induces the lysis of other B.subtilis cells that have not entered... |
O32241 | MKKNIISIIIVCLSFLTSIILYQYLPEEIPIQWSGNKPAAIVSKPLTIFIIPVVMLIYYLTFYMLTIKSTQKNKALLFLASNNMLILLYILQLSTLLISLGYEVNIDLIIGLGVGIFLIIGGNSMQLAEQNHLIGLRTPWTLKDETVWKLGNRFASKVLVVCGFIIAVLSFFTGEYIILIMIVLVLLALVISTLASYHYYKKLNGSR | Function: Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacteria... |
P42789 | MRNAASVGLCVGLSALGAAANDILKPEADYRDFRHYQLNNGMHAIAVHHPRSNESGFAVAANTGSLYDPQDVPGLAHFLEHMLFLGTSKYPEPESYDSFLTESGGANNAYTDEEKTVFFNKVTDSSFEEALDRFSFKSPLFSRQYEEKEVNAIDAEHQKNIPNDDERAWYSIRSLAKGPMSRFATGNSSTLSTTPKAKGIDLVDRLKDFHTQYYCGSNMVAVTISPRSLDEQEALIREKFEGVSAGHADWLGMVQCPGPMFDTVKPFDESNTGKFIHLQSFSSEPSLWVAFGLPPTLTSYKKQPISVLTYLLEYTGQGSL... | Cofactor: Binds 1 zinc ion per subunit.
Function: May be involved in the degradation of a protein which is a component of the signal transduction pathway regulating oocyst sporulation.
Sequence Mass (Da): 65280
Sequence Length: 596
EC: 3.4.24.-
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D2WKD9 | MDRWAGKVAVVTGASSGIGAAITTDLAKAGMVVVGLARRVERVEALKANLPESAKPRLHAVKCDVSKEEDITQVFKWVEKKFGGVDVLVNNAGILRQTDLLGTDNGQMLREVLDTNVMGLVLCSQKAYQSMKKRSVDGHIVHINSVVGHKVFDFPQSNIYPASKHAVTAITETMRNELRNAGSRIKVTSISPGVVRTEILPESIIEGGHALLESEDISEAVLYVLGTPPRVQVHELTIKPVGEKF | Function: Mediates oxidation of farnesol into farnesal, a precursor of juvenile hormone in the corpora allata (CA), the glands that synthesize juvenile hormone. Able to oxidize C(10) to C(15) isoprenoid and aliphatic alcohols.
Catalytic Activity: (2E,6E)-farnesol + NADP(+) = (2E,6E)-farnesal + H(+) + NADPH
Sequence Mas... |
Q9M2E2 | MAEETPRYAVVTGANRGIGFEICRQLASEGIRVVLTSRDENRGLEAVETLKKELEISDQSLLFHQLDVADPASITSLAEFVKTQFGKLDILVNNAGIGGIITDAEALRAGAGKEGFKWDEIITETYELTEECIKINYYGPKRMCEAFIPLLKLSDSPRIVNVSSSMGQLKNVLNEWAKGILSDAENLTEERIDQVINQLLNDFKEGTVKEKNWAKFMSAYVVSKASLNGYTRVLAKKHPEFRVNAVCPGFVKTDMNFKTGVLSVEEGASSPVRLALLPHQETPSGCFFSRKQVSEF | Function: Aldehyde reductase that catalyzes the reduction of the aldehyde carbonyl groups on saturated and alpha,beta-unsaturated aldehydes with more than 5 carbons . Involved in basal resistance against pathogens.
Catalytic Activity: (+)-neomenthol + NADP(+) = (1R,4S)-menthone + H(+) + NADPH
Sequence Mass (Da): 32803
... |
I3PLR3 | MHGQKNISERYQKFKEMEGTGKIVCVTGGAGYLASWLIMRLLERGYSVRTTVRSDPKFREDVSHLKALPEATEKLQIFEADLENPESFDDAINGCVGVFLVAQGMNFAEEYTLEKIIKTCVEGTLRILQSCLKSKTVKKVVYTSSADAAMMISNLKAVKEIDETIWSEVDNFISKPEQVIPGLPSYVVSKVLTERACLKFSEEHGLDVVTILPPLVVGPFITPHPPPSVSIALSIISGDVSMMLGVRLENAVHIDDVALAHIFVFECEKAKGRHICSSVDFPMHDLPKFISENYPEFNVPTDLLKDIEEQEPVHLSSDKL... | Function: Oxidoreductase that catalyzes the last step in the biosynthesis of the benzylisoquinoline alkaloid noscapine . Converts narcotine hemiacetal to noscapine .
Catalytic Activity: NAD(+) + narcotine hemiacetal = H(+) + NADH + noscapine
Sequence Mass (Da): 38815
Sequence Length: 348
Pathway: Alkaloid biosynthesis.... |
P78603 | MAPKSAAQALFEKADKKANSSGGWFSSANSKWEEAGDLYQQAANAFKLEKQFKEAGDAFAREAECREKCKESLDAGNAWWNAAKAYKRGYPDLAIQALQQTIQHLVAGGRFRQAADREKEIAQIYLQETHDLSRACESFLRAGDWYAEEDATATANQCYKDAADLYAELEQFPQAITLYERVADHSLTSNLTKYSVKEYWLKSLLCTVALGDIVTARRNAQKYIGQDNTFVGTREFKFADALMEAVDAGDVGAYTAAVVEFDRITKLDNWKTAILLKIKRGIQEEPGLT | Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32288
Sequence Length: 289
Subcellular Location: Membrane
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Q9P4D0 | MSEAEQLIAKADKKCAPVSGFASFFSGSGSYRFEEAADLYTQAANLYRIQRKSNKAGHVFEKAADAQIKADSKDEAANSLIEAYKCYKLDAPSDAARCLNKAVEFFALKGQFRRGANFKAELAELYETKMADPKHAILAYEEAGEWYRGDSAEALANKCYVKAADLSCSDEVQDFLKAAESYERIAKESLNNSLAKWSLKDYFFKAILCRLALNDYPSASALLERFVSWDPTFEKTREYEFALKLVDGLKEGDPDIIASASHEYDQISRLDNFKVKILNKIKNNIRDSDDLAEDDLT | Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33321
Sequence Length: 297
Subcellular Location: Membrane
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Q9P6A5 | MAVDPRVLQQEAEKTLASASKGWGLFGNKEDKYQNAADQYIQAANAFRLQKSNTEAGKCFEEAAKIFTEKLKEPNDAANAMLDAFKVYRKDAPDNAVRCVEVAIKQYTMAGNFRRAASHKENQAEVYENELQNKPEAIKAYTTAAEWYENDGAVALANKLWLKVADLSALAGDFFAAIEKFEKVAEASLGNNLMRYSVKEYFLKAGLCSLATKDMVTAQRNITKYAEKDPSFTGQREYQLLVDLLEAASNNNLEMFQDKLAAYDKMSRLDDWKAAVLLQIKNNFEEADNEFS | Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32805
Sequence Length: 292
Subcellular Location: Membrane
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Q9P4X4 | MIADPDQLMQKAAKKAQGTGGFALFGGGNKYDEASELFLDAANGYRLQKQGSAAGYAFEKAAEMQLKTDDKDDAASTYVEAFKSYRREKPSEAARVLQIAIELFTRRGNFRRAANYKMDLGDIFEQELQDTKAALGAYEDAGEWYSSDQADALANKAYLKAADLAGLCGEYSLAIRKFEQVARASVQNNLLKWSVKDYLLKAGLCYMANGDEIATRRALEHFLEIDPSFASTREYQLLKDLQDTIEASDANMFADKVFTYDQLSKLDSWKTTILLKIKSSIQEAEDDLT | Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32222
Sequence Length: 289
Subcellular Location: Membrane
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P32602 | MSDPVELLKRAEKKGVPSSGFMKLFSGSDSYKFEEAADLCVQAATIYRLRKELNLAGDSFLKAADYQKKAGNEDEAGNTYVEAYKCFKSGGNSVNAVDSLENAIQIFTHRGQFRRGANFKFELGEILENDLHDYAKAIDCYELAGEWYAQDQSVALSNKCFIKCADLKALDGQYIEASDIYSKLIKSSMGNRLSQWSLKDYFLKKGLCQLAATDAVAAARTLQEGQSEDPNFADSRESNFLKSLIDAVNEGDSEQLSEHCKEFDNFMRLDKWKITILNKIKESIQQQEDDLL | Function: SNARE complex protein that binds to cis-SNARE complexes on membranes and is required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus and for homotypic vacuole fusion. During the priming step of membrane fusion, is released from cis-SNARE complexes by SEC18 to establish a pool... |
Q9TTY3 | MWDMRAVAPQRPAAGHPRAGWPRKLKTAATRFWATCPSSSTVCFLFVIFAVSTVFHCHRRLALVPAPWAYAGHVVLFPRHLPRGGVFTINAKGRLGNQMGEYATLYALAKMNGRAAFIPPQMHSTLAPIFRITLPVLHDATARSVPWQNYHLNDWMEEQYRHIPGEYVRLTGYPCSWTFYHHLRAEILQEFTLHAHVREEAQNFLRGLRVNGSRPSTYVGVHVRRGDYVRVMPTMWKGVLADRGYLQQALDWFRARHHSPLFVITSDDMAWCRRNINSSHRDVVFAGSGQQGSPARDFALLTQCNHTVITVGTFGIWAAY... | Function: Catalyzes the transfer of alpha 1,2-linked fucose to ganglioside GM1 and galacto-N-biose.
Catalytic Activity: ganglioside GM1 + GDP-beta-L-fucose = ganglioside Fuc-GM1 + GDP + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 41649
Sequence Length: 368
Pathway: Protein modificat... |
Q12981 | MAAPQDVHVRICNQEIVKFDLEVKALIQDIRDCSGPLSALTELNTKVKEKFQQLRHRIQDLEQLAKEQDKESEKQLLLQEVENHKKQMLSNQASWRKANLTCKIAIDNLEKAELLQGGDLLRQRKTTKESLAQTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALALFLATVLYIVKKRLFPFL | Function: As part of a SNARE complex may be involved in endoplasmic reticulum membranes fusion and be required for the maintenance of endoplasmic reticulum organization . Also plays a role in apoptosis . It is for instance required for endoplasmic reticulum stress-induced apoptosis . As a substrate of RNF185 interactin... |
P21825 | MSAVGPGSNAGASVNGGSATAIATLLRNHKELKQRQGLFQAKQTDFFRYKRFVRALHSEEYANKSARQPEIYPTIPSNKIEDQLKSREIFIQLIKAQMVIPVKKLHSQECKEHGLKPSKDFPHLIVSNKAQLEADEYFVWNYNPRTYMDYLIVIGVVSIILALVCYPLWPRSMRRGSYYVSLGAFGILAGFFAVAILRLILYVLSLIVYKDVGGFWIFPNLFEDCGVLESFKPLYGFGEKDTYSYKKKLKRMKKKQAKRESNKKKAINEKAEQN | Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. In an initial step, the signal sequence seems to bind simultaneo... |
P82008 | AGQQFQYDDSGNTFFYQMAEVFEKEQSIXAAXE | Function: Mediates cotranslational and post-translational transport of certain precursor polypeptides across endoplasmic reticulum (ER). Proposed to play an auxiliary role in recognition of precursors with short and apolar signal peptides. May cooperate with SEC62 and HSPA5/BiP to facilitate targeting of small presecre... |
Q9UGP8 | MAGQQFQYDDSGNTFFYFLTSFVGLIVIPATYYLWPRDQNAEQIRLKNIRKVYGRCMWYRLRLLKPQPNIIPTVKKIVLLAGWALFLFLAYKVSKTDREYQEYNPYEVLNLDPGATVAEIKKQYRLLSLKYHPDKGGDEVMFMRIAKAYAALTDEESRKNWEEFGNPDGPQATSFGIALPAWIVDQKNSILVLLVYGLAFMVILPVVVGSWWYRSIRYSGDQILIRTTQIYTYFVYKTRNMDMKRLIMVLAGASEFDPQYNKDATSRPTDNILIPQLIREIGSINLKKNEPPLTCPYSLKARVLLLSHLARMKIPETLEE... | Function: Mediates cotranslational and post-translational transport of certain precursor polypeptides across endoplasmic reticulum (ER) . Proposed to play an auxiliary role in recognition of precursors with short and apolar signal peptides. May cooperate with SEC62 and HSPA5/BiP to facilitate targeting of small presecr... |
Q9HGN7 | MSSEYKYDEQGIFFPVFLLVGTSCCVLPLTYSTILGPSASKEKKNVRDPFQKYRPKDLKVQRKSIFRLRYIFLILGWLAIGFLSYKIANSRLKLNIWDPYEILGIAKGTSVDDVRRHYKRLSIKFHPDKVRNMVNTTREEVEKHYIEITNAYRALTDDKTRENYALYGTPDVPQHISVGIALPKWISESENSIYILGFYGLVFGIVLPYAVGKWWYGSRTYTRDHVHVDTVDEWFPKMETSLTLDELLSLFASSKELTSLVPNEKNPKEYILKLLFDHLNRKKTNNFNTHQILSQSDVVLNALLSVATAFGFANPVDNVL... | Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from sec... |
P14906 | MPTNYEYDEASETWPSFILTGLLMVVGPMTLLQIYQIFFGANAEDGNSGKSKEFNEEVFKNLNEEYTSDEIKQFRRKFDKNSNKKSKIWSRRNIIIIVGWILVAILLQRINSNDAIKDAATKLFDPYEILGISTSASDRDIKSAYRKLSVKFHPDKLAKGLTPDEKSVMEETYVQITKAYESLTDELVRQNYLKYGHPDGPQSTSHGIALPRFLVDGSASPLLVVCYVALLGLILPYFVSRWWARTQSYTKKGIHNVTASNFVSNLVNYKPSEIVTTDLILHWLSFAHEFKQFFPDLQPTDFEKLLQDHINRRDSGKLNN... | Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC... |
Q9UUA4 | MVSIYVPLIYITILMGSMYGVSRFVRKSKNQESKPVSEEWFGENYSRNIFFSLLQQNPPAEDTLLKAALVLRATEGLRRLMKLKVSRMALNNLLNRGGVGDELIRKFGRLEKETELELMDIAKTANSLQPGWNQFIFQTCNEIIENEKIHSIIDNIPKDIDSISQRWQTEKILYEAADEELRIQAQKELGVL | Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from sec... |
P33754 | MSEFNETKFSNNGTFFETEEPIVETKSISVYTPLIYVFILVVSLVMFASSYRKKQAKKISEQPSIFDENDAHDLYFQIKEMSENEKIHEKVLKAALLNRGAESVRRSLKLKELAPQINLLYKNGSIGEDYWKRFETEVKLIELEFKDTLQEAERLQPGWVQLFVMVCKEICFNQALSRRYQSILKRKEVCIKEWELKINNDGRLVN | Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC... |
Q0A6V9 | MFSAIAKKVFGTRNDRAVKRLAKEVERINALEPEIEALSDDQLRARTEAFREQVEQGRTLDDLLPEAFAVAREASRRVLGMRHFDVQLIGGMVLHQGKIAEMKTGEGKTLVATLAVYLHALSGRGVHVVTVNDYLARRDAAWMGRIYEFLGLSVGVVVPGQSREEKKAAYEADITYGTNNEFGFDYLRDNMAFRPEDRVQRELAYAIVDEVDSILIDEARTPLIISGPAEQSSELYQQMTRIVPRLQRQEEEDGPGDYYLDEKARQAHITEEGHENIERLLQAEGLLEEGESLYDARNISLVHHLNAALRAHTLFQKDVN... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-Sec... |
Q2INY3 | MFNYVLKKVLGTKNERELKRLRPLVARVAELEPRMKALRDEDFPRLVAEWKQQVREKGRTLDDVMPEAFALVREAGVRALGMRHFDVQLIGGAVLHSGKIAEMKTGEGKTLVATLPCVLNALSGRGVHVVTVNDYLARRDAEWMGRLYRFCGLSTGVIVHGLTDRERQQAYGSDITYGQNNEFGFDYLRDNMKFRLQDYVQGELNFAIVDEVDSILIDEARTPLIISGPSDESSELYARVNAVIPSMIRDQDFTVDEKSRTIVMTDAGVEKMEKKLSVQNLYAPEEIETLHHVEQALRAHHIYRNEVDYVVKEGEVLIVD... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving ... |
O67718 | MLGWIAKKIIGTKNEREVKRLRKFVNQINELEKELDALTNKELVELAQELHDKIRFDEELKERVIKGEITPEVIKAFALVREAAKRTLGLRHFDVQLIGGLVLHEGKIAEMKTGEGKTLVATSPAVVNGMTDEGVHIVTVNDYLARRDAQWMGPIYKFLGLEVGVINSDGKTYLVEWVDPEKVKEAIENDVRVWPKGYYEEILPSEKVNIDAKKTYFTTLKEAEHRRKAYEAHITYGTNNEFGFDYLRDNLAFSKEEIVQVKGHNYAIVDEVDSILIDEARTPLIISGPAQIDSQIYHVADAVVRKLKKDKDFTVDEKNR... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
Q2NJH2 | MFNFLKKIFNSSKKALRKARTIANKVQNLEAQIALLDDKDFATKTAELKKLFQEGKTLNQLLPEAYALAKEATKRVTGLTPYYVQILGAVILHQGNIAEMKTGEGKTLTAIMPAYLNALSGNAVHIVTVNEYLAKREFEGSIGDVFRFLGMTVGLNTKDKDQTQKQQAYLCDVLYTTNSELGFDYLRDNMEIEASNLVMKRPYSYAIVDEVDSILIDEARTPLIISQSVKETKNLYKEAQRFVRTLKNSHYLIELETKTIELTEEGITKAENFFQIDNLYNIEHASLLHHVKNALKAAFTMHKDKDYLVDYKDGQVLIID... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
A1K3V5 | MISGLLKKLFGSRNDRLIRQYSQNVRKINALEPEIAALSDEALRGKTGEFRQRLADGATLNDLLPEAFAVVREAGKRVHGMRHFDVQLIGGMVLHDGKIAEMRTGEGKTLVATLAAYLNALPGKGVHVITVNDYLASRDAEMMGRIYGFLGLTTGCNLSRMGHAEKQLAYAADITYGTNNEFGFDYLRDNMVYATGERVQRGLNFAVVDEVDSILIDEARTPLIISGQAEDHTDLYLKMNQVAPLLKRQEGGLDDKDSVIEPGDYTVDLKAHQVLLTEQGHENAEQILVRIGLLPEGAGLYEPGNILLVHHLYAALRAHA... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-Sec... |
Q24MT3 | MGFLNKLFDDNAREVKKYQKKIAAINDLEPEIKALSDEQLRAKTDEFKQRLENGESLDSLLPEAFAVVREASWRVNGQRHYDVQLIGGMVLHDGRIAEMRTGEGKTLVATLPSYLNALTGRGVHIVTVNDYLARRDSEMMGRIHQFLGLSVGLIVHGLNYAQRRESYAADITYGTNNEFGFDYLRDNMVTRPDGLVQRELHYAIVDEVDSILIDEARTPLIISGEADKPTELYNRIAMIIPRLKPEEDYNVNEKDRVVTLTEQGVSRVETMLSVENLFDDLHTELAHHVNQGLKAHALFKLDRDYVVKDGQVIIVDEFTG... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving ... |
Q6AJK1 | MIGKMLTKVFGSKNDRVLKQIRPLVTRINDLESTIKPLGDAALVAKTVEFKERIAKGESLKDLLPESFAVMREAASRVLGERHYDVQLVGGIILHKGRIAEMKTGEGKTLTSTLPVYLNGLSGKGVHVVTVNDYLAARDAEWMGQVYDFLGMSWDKIIHGMDDVERRAAYAADITYGTNNEFGFDYLRDNMKFELDDFCQRGFNFAIVDEVDSILIDEARTPLIISGPAEMSTELYDNINSIMYNFKVEEHYTVDEKARTVSLTDDGIGLGEELLDLENLCDPSSIEQLHHLNQALKAHVLFQRDVDYIVNDGQVVIVDE... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving ... |
A4J927 | MLNFFKNLFDDNAREVKKLQRVVEEINGLEEKIAKLTDEELQGKTAEFKQLLENGKTLNDILPEAFAVCREASKRVLGMRHYDVQLIGGMVLHQGRIAEMRTGEGKTLVATLPVYLNALSGKGVHVITVNDYLATRDSEWMGKLYRFLGLSVGLIVHGIKPEDRRLAYNADITYGTNNEFGFDYLRDNMSLHPEQLVQRELNYSIVDEVDSILIDEARTPLIISGVADKPTHLYYTMAKIVPKLVREVDYTVDEKAHNVLLTEEGVSKAEKLLGIENLYDEANMEINHHLNQSLKAHGLMHRDRDYVVRDGEVVIVDEFT... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving ... |
B8DRH3 | MFDTLFKSIFGSSNDRYIKRCRTRVEAINALEPQMQALADEDFPARIAEYREQAQNGRSLDDLLPEVFALTREAGKRALNMRHFDVQLVGGMVLHEGRIAEMKTGEGKTLVATLPVVLNAISGLGVHVVTVNDYLAKRDAAWMGRLYNFLGLSVGVIVHGLSDEERKEAYGADITYGTNNEFGFDYLRDNMKFYPHQLVQREHNFAIVDEVDSILIDEARTPLIISGPSEDSTGLYRRVDDIIPKLSPEAHFSVDEKARTATLTDEGVAKCEELLGIDNLFDPGNITFQHHVLQALKAHHVFRRDVDYIVTPEDQVVIVD... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving ... |
A4RW83 | MLKGDPSEKTKKRYQARVDAVNALGARTKALSDDELRAKTEEFRERLRRGESEDDLLVEAFAVVREAADRVLGLRPFDVQLIGGMILHEGQIAEMRTGEGKTLVSALPAYLNALSGKGVHVVTVNDYLARRDAEWIGQIHKFLGMTCGLIQAGMAEEERRVGYGSDVTYVTNSELGFDYLRDNLAQNTGELVQRDFNFCIIDEVDSILIDEARTPLIISGVADKPSERYIQAAKIADAFEKDYHYKVDEKQKSVLLSEEGYEAAEDLLQVTDLYDPRTQWALYIINAIKAKELQKRDVNYIVRGQEIIIVDEFSGRTMQG... | Function: Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
Catalytic Activity: ATP + H2O + chloroplast-proteinSide 1 = ADP + phosphate + chloroplast-proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 105089
Sequence Length: 93... |
Q41062 | MATSSLCSSFTSQTCNPHSRPHRKTLTLPGSVFLCRQFHLNSPSVSKTRRIRTRQSGPVASLGGLLGGIFKGTDTGEATRKQYAAIVNTINGLEPKISALSDSELRDMTFASRERAQKGESLDSLLPEAFAVVREASKRVLGLRPFDVQLIGGMVLHKGEIAEMRTGEGKTLVAILPAYLNALVGKGVHVVTVNDYLARRDCEWVGQVPRFLGMKVGLIQQNMTSEQKKENYLCDITYVTNSELGFDFLRDNLATSVEELVIRGFNYCVIDEVDSILIDEARTPLIISGPAEKSSDQYFKAAKIADAFERDIHYTVDEKQ... | Function: Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane . Facilitates the transport of precursor proteins from the chloroplast stroma to thylakoid lumen .
Catalytic Activity: ATP + H2O + chloroplast-proteinSide 1 = ADP + phosphate + chloroplast-proteinSid... |
Q4FNA5 | MLNPLNFITKFIKSSNQKELDRINKIVVKVNSLEASVKNLSDEDFPKKTTELKDKLKNGENLDTLLPEAFALVREASKRTRNERHHDVQILGGVVLHEGKIAEMRTGEGKTLTISLAAYLNALTEEGVHIVTVNDYLAKRDSQEMGEIYKFLGLTFGFINNDQDDLERKKNYNFDITYATNSELGFDYLRDNMKFSKEQMVQRGHVYTIVDEIDSCLIDEARTPLVISGAAEDKTEQYLAIDKLIKRLLPEHYEIDEKDRNILLTNEGINNVEKIFSDAGILKNNNFYDPENLSLVHHVNQSLRAHHLFEKGKDYIVKDG... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular mo... |
Q9X1R4 | MILFDKNKRILKKYAKMVSKINQIESDLRSKKNSELIRLSMVLKEKVNSFEDADEHLFEAFALVREAARRTLGMRPFDVQVMGGIALHEGKVAEMKTGEGKTLAATMPIYLNALIGKGVHLVTVNDYLARRDALWMGPVYLFLGLRVGVINSLGKSYEVVWKNPDLARKAIEENWSVWPDGFNGEVLKEESMNKEAVEAFQVELKEITRKEAYLCDVTYGTNNEFGFDYLRDNLVLDYNDKVQRGHFYAIVDEADSVLIDEARTPLIISGPSKESPSVYRRFAQIAKKFVKDKDFTVDEKARTIILTEEGVAKAEKIIGV... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
B9K8Q4 | MLFFDKNKRILKRYSKIVEKINQLDQSMRKKSNEEIVSLSSELKERVNSLEDADRNLVEAFALVREAARRTLGMRPFDVQVMGGIALHEGKVAEMKTGEGKTLAATMPVYLNALIGKGVHVVTVNDYLARRDALWMGPVYLLLGLRVGVINSLGKSYEVVWKDPSLVEKAIKENWSVWPQEFDGEILKEEQMNKEALNAFQVELKEISRKEAYMCDVTYGTNNEFGFDYLRDNLVLDYNDKVQRGHFYAIVDEADSVLIDEARTPLIISGPSKESPSTYRRFAQIAKKFVKDKDFTIDEKARTVILTEEGVAKAEKIIGV... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
Q5SIW3 | MLGLLRRLFDNNEREIARYYKQVVEPVNRLEAEVEKLPDLAAAYRELKEKHEKGASLDELLPMAFALTRESAKRYLGMRHFDVQLIGGAVLHEGKIAEMKTGEGKTLVATLAVALNALTGKGVHVVTVNDYLARRDAEWMGPVYRGLGLSVGVIQHASTPAERRKAYLADVTYVTNSELGFDYLRDNMAISPDQLVLRHDHPLHYAIIDEVDSILIDEARTPLIISGPAEKATDLYYKMAEIAKKLERGLPAEPGVRKEPTGDYTVEEKNRSVHLTLQGIAKAEKLLGIEGLFSPENMELAHMLIQAIRAKELYHRDRDY... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
B5YKT5 | MVKILEKIFGTKNERELKRYFTIVEDINRLESQISSLSDEKLKQKTDEFRERLAKGESLDDILKEAFAVVREVAKRTLGMRHFDVQLVGGLVLHEGKIAEMKTGEGKTLVATLAAYLNALEGKGVHIVTVNDYLARRDVQWMGAIYNFLGLSVGVIQPDASFLYDPNYRLPDRRFDRLRPCSKKEAYLADITYGTNNEFGFDYLRDNMRYSIDELCQRELNYAIVDEVDSILIDEARTPLIISGPSEESTDIYYAVNRIIKYLKPENDFKLDEKLKTVVLTEQGSQKAEKLLGIDNLYNPSNIQVVHHINQAIRAHYFFK... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving ... |
B8GMN9 | MVTSLVRKIFGSRNERIVKRLGKTVARINELEAELQSLDDEALKARTGQLRERLAGGESLEALLPEAFAVTREAGRRVMGMRHFDVQLIGGMVLDSGRIAEMRTGEGKTLVATLAAYLNALSGKGVHVVTVNDYLARRDAAWMGRLYHALGLSVGVINSSGGAGPDSASYLYDPGFHAEGGIAHLRPVTRREAYAADITYGTNNEFGFDYLRDNMAFRLEDRVQRELNFAIVDEVDSILIDEARTPLIISGPAGESAEMYERMNRIVPKLTPQEEEEGPGDYSVDEKMKQVFLTEDGQEKAEQLMRDAGLLAEGQGLYDA... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-Sec... |
Q73LG6 | MLDSIIKILFGSKHERDIKAMLPILHKINEKEAWALSLSEEEFKAKTDEFRERYQKGESLDSFIPEAFALAREAARRILGERPYDVQILGSLVLHSGKIVEMKTGEGKTLMSVAAAYLNSLTGKGVHIVTVNDYLAERDADWMRPVYSYLGVSVGVILSNMENDARRIEYNCDITYGTNNEFGFDYLRDNMQMRLKDKTQREFSFAIVDEIDSILIDEARTPLIISGAAEDDTQRFFEVDRLIGQLKEVEKNPETGEYPNELEGEEVIGDYTIDEKSKRVSFTDSGMLHIQDILQRQGLIKSGNLFDEENFEYIHYFTQS... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving ... |
Q83NT4 | MSVKLLERILRAGEGRTLKRLRNIAHTVNAIEDEYKGCTDGELRTFAFDLKVRHQNGESLDSILPEAFAMVREASSRTLGLRHFDVQIMGGAALHMGYIAEMFTGEGKTLVATLPAFLNSLSGNGVHIVTVNDYLAGYHSQQMGRVYKVLGLETGVILADQDPSTRAQQYRADITYGTNNEFGFDYLRDNMAWSCAERVQRGHNFVILDEVDSILIDEARTPLIISGSSSGEVSRWFVEFAGIARALTAGEDYDVDERKHTVGVLEPGIAKVEDLLGISNLYESVNTPLISFLNNSIKAKELFKRDRDYVVLDGEVMIVD... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
C5A3H3 | MGTKKQKTKKKPSDEILETKRKRLSFLVRMEPRKMVLYPLVVFLVAALILAVHFPEKGIDLKGGVVVTVYHVSASPDELASYVKEKTGIDVRAEEFKDPITGLSGIRIYAPAKTAPSKIADEISNAIRLKYKDADVTPRVVDPTFGKIAQKQGIKAVIYAFIGMAIVVFLFFRDPVPSGTIIFSAFSDMVIALATMGILGIELTTATIAALLMLIGYTVDSNILLTTRLLRRKEDTIEDAYLSAVSTGFTMSTTTLGALFILWLVSTSEVIDSITIVLIFGLLADFMNTWIFNAGVLRWYIASPLKFSIKLRRGK | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34762
Sequence Length: 315
Subcellular Location: Cell membrane
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D1CDJ6 | MIDIVRWRYAFYLLSLLIIIPGTIYLLLFGLRLGIDFEGGTFWQIQFEKPVRIEDVRSALAQAGYNEAFVQSFGQQSNTAQGTVTRGVSMRLPEIKENSPEKAKLEQILKSRFGNYEELVFTSVGPAVGREIRNRSIVAIALASLGILGYIAFAFRKVSHPFRYGICAIIAMLHDVLVVVGIFAILGKHFGVEIDALFVTALLTVIGFSVHDTIVVFDRIRENQLRRYGESFEQIVNISLLQTLVRSVNTSMTVIFTLLALYFFGGTTIKHFVLALLIGIVSGTYSSIFNASLLLVSWENKDFLRIFRRTEPEAAAT | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35531
Sequence Length: 3... |
B5YIG8 | MIQILGKTNIDFLGKKYIALALSCIMIILGIFAIFQIHAGKANLGVDFAGGLSLQIRFSQPVTLAEVRTVLDKAGIKDADIQELPTEKKILIKLKKQQEGIQDTIEKALKENLTAKEPIIESVTEIGPKIGERTKRDALFAILAATAGILIYIAIRFKFHFSIGATVATFHDVMAVLGIFYILDKEINLIFISALLTIAGYSLTDTVVVFDRIRENLGKVAKGTMTLEALMNKSINEVLSRTIVTSLTTLMAAVALFFFGGEVLHDFALAMILGILVGTYSSIFVASPVVLLLGKNSLIKR | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32800
Sequence Length: 3... |
O83426 | MRQVVRFSLLFLPCAILSVVLIGAGVLRWALWGMSFGIDFQSGLIERLRIAPPAFSLVYTGTQSMQFFQDEQKVVFTVSSPGVLGERYEFLYTEYPTLRAFSEGAKKVEHLSVTLHAPETVYMRDTFSGAEGSTLSSASCFVHYFSEDVRAPGVEELRRVLKDVPSAVVQQVGVRAEHTFQVRVAAETAFPSSLLPEQGGTALAQSDAPDLVTPQGAVESVVYAALVRAYGADHVVRLAMDFVGSRFSHLLVRQALLLVLGALVLIFLYVALRFRWFFALGAIVALVHDACIMVSFMVWFGLEFNSASIAAILTIIGYSI... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45731
Sequence Length: 4... |
E9RGS4 | MFQILKAEKTIGFMRWSKVAFVFSIFMIAASIFTLSTKWLNWGLDFTGGTLIEVGFEKPANLEKIRTALDAKGFGDATVQNFGSAREVMVRLRPRDDVSGETLGNQIIGAIKDGTGESVEMRRIEFVGPNVGDELTEAGGLAILVSLICILLYVSMRFEWRLAAGAVMALAHDIIITLGVFSFLQIEVDLTIVAALLTVVGYSLNDTIVVFDRIRENFRKMRKGEPADIMDASITQTLSRTLITSGTTLFVVIALFMQGGAMIHGFATALLLGITVGTYSSIYVASALALKLGIQKEHLMPPQVEKEGAEFDEMP | Function: Expression of V.alginolyticus SecDF in an E.coli secDF mutant restores protein export in a Na(+)-dependent manner, strongly suggesting SecDF functions via cation-coupled protein translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34414
Sequence Length: 315
Subcellular Location: C... |
Q9YEC1 | MSVRRRRERRATPVTAAGLLSFYEEYEGKIKISPTIVVGAAILVSAVVAAAHIFLPAVP | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6351
Sequence Length: 59
Subcellular Location: Cell membrane
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O66505 | MYYALLTLFVIIAVVLIISTLLQKGRGDVGAAFGGGMGQSIFGVGGVETILTKATYWLGALFLVLALLLSVIPKEKGSVVEKSVQTEQSEGKGTTQESGK | Function: Subunit of the protein translocation channel SecYEG.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10464
Sequence Length: 100
Subcellular Location: Cell membrane
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O28498 | MAKAPKGKAKTPPLMSSAGIMRYFEEEKTQIKVSPKTILAAGIVTGVLIIILNAYYGLWP | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6507
Sequence Length: 60
Subcellular Location: Cell membrane
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O32233 | MHAVLITLLVIVSIALIIVVLLQSSKSAGLSGAISGGAEQLFGKQKARGLDLILHRITVVLAVLFFVLTIALAYIL | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7996
Sequence Length: 76
Subcellular Location: Cell membrane
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O51083 | MDLVRFFIFIIFVIVSIFIILLVLIQDEQGDGIGGVFGGGSSSIFGAKSSSVAVKITGFFIALFFIFVVLLSFLNTRRADDSFLNDIKTENKNSSTFWDDENSESDANINEIKENNLKEK | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13371
Sequence Length: 120
Subcellular Location: Cell membrane
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P57460 | MYLFFLIVFIFISFSLIFFILLQPGKGLNNTVHSHTKNNIKFFNSIGTNNFITKIIKILAFFFLLISIILCNINSKRIDSDFFWEDNQNNTITKKHVLDKKKLNLDIPN | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12803
Sequence Length: 109
Subcellular Location: Cell membrane
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Q8K9G9 | MYLFFLIFLIFISFSLIFLILLQSGKGFNNTIHLNTSNNFNFFNSVGSGGFIKNIIGFFAGFFLIFSIILCNINDKKVNSDVFLEKNTQKKTINEKKEQKILNSELPL | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12400
Sequence Length: 108
Subcellular Location: Cell membrane
|
Q9Z469 | MALTLQIILVVASLLMTVFVLLHKGKGGGLSSLFGGGVQSNLSGSTVVEKNLDRVTILVAVIWIVCIVALNLIQTYS | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8098
Sequence Length: 77
Subcellular Location: Cell membrane
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P0AGA1 | MYEALLVVFLIVAIGLVGLIMLQQGKGADMGASFGAGASATLFGSSGSGNFMTRMTALLATLFFIISLVLGNINSNKTNKGSEWENLSAPAKTEQTQPAAPAKPTSDIPN | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
PTM: The N-terminus is blocked.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11365
Sequence Length: 110
Subcellular Location: Cell inner membrane
|
O78500 | MLNIIWLITGILLLFAIMIHNPKSQGFGTQNQIFGSTRSAEQTLNKATWFLILLFFILTVVLSINNEF | Function: Involved in protein export. Participates in an early event of protein translocation across the chloroplast thylakoid membrane (Potential).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7756
Sequence Length: 68
Subcellular Location: Plastid
|
P44713 | MYQVLLFIYVVVAIALIGFILVQQGKGANAGASFGGGASGTMFGSAGAGNFLTRTSAILATAFFVIALVLGNMNSHKGNVQKGTFDDLSQAAEQVQQQAAPAKDNKNSDIPQ | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11538
Sequence Length: 112
Subcellular Location: Cell inner membrane
|
P49978 | MGFMDFLAKMGENLPAVSKPKDKPTLTRKLLWTFIGLIVYLLMASIPLYGVTSSNSFLSNFLAQQIIFASSQGTLAQLGIGPVITSGLIMQILVGSKLINVDLTTQEGKSKFTQAEKALALIFIIVESSLFGYVFTRATSNILLPIIVVVQLIIASYIILLLDEMIQKGWGLGSGVSLFIMAGIMKVIFWNMFGIVSVQSQNLPVGFFPLLVSYITSGRNLQEIVLNTSSTTPYQPDLIGLIATVGLTILIVYLVNTNIYIPVTTQRLRGIRTTVPLNFLYVSSIPVIFVSVLGADIQLFASLANSISNSASGILTDIAN... | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... |
P77964 | MVVSRDKAPSAQETFLQMAQAAGLRGRLLITIGLLILVRVGIFIPVPDIDRQAFSQAINDNSVIGFLNIFTGGGLSTVGIFALGILPYINASIIMQLLTAAIPALEDLQKNEGEAGRRKISQYSRYIAFGWCIIQGLGLTVGLLRPYANNYGPLFIFQTVLAITAGSMFVMWISELITERGIGNGASLLIFVNIVATLPQTLGQTIEYAQSGGRQSITAVVLLMLVFLVMIVGIVFVQEGTRRIPIISARRQVGKKLYRERTSYLPLRLNQGGVMPIIFASAVLILPSSLAGFATGNEGLGGFGEIFVQISNALRPGTWV... | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... |
Q9X1I9 | MWQAFKNAFKIPELRDRIIFTFLALIVFRMGIYIPVPGLNLEAWGEIFRRIAETAGVAGILSFYDVFTGGALSRFSVFTMSVTPYITASIILQLLASVMPSLKEMLREGEEGRKKFAKYTRRLTLLIGGFQAFFVSFSLARSNPDMVAPGVNVLQFTVLSTMSMLAGTMFLLWLGERITEKGIGNGISILIFAGIVARYPSYIRQAYLGGLNLLEWIFLIAVALITIFGIILVQQAERRITIQYARRVTGRRVYGGASTYLPIKVNQGGVIPIIFASAIVSIPSAIASITNNETLKNLFRAGGFLYLLIYGLLVFFFTYF... | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... |
Q5SHQ8 | MLKAFWSALQIPELRQRVLFTLLVLAAYRLGAFIPTPGVDLDKIQEFLRTAQGGVFGIINLFSGGNFERFSIFALGIMPYITAAIIMQILVTVVPALEKLSKEGEEGRRIINQYTRIGGIALGAFQGFFLATAFLGAEGGRFLLPGWSPGPFFWFVVVVTQVAGIALLLWMAERITEYGIGNGTSLIIFAGIVVEWLPQILRTIGLIRTGEVNLVAFLFFLAFIVLAFAGMAAVQQAERRIPVQYARKVVGRRVYGGQATYIPIKLNAAGVIPIIFAAAILQIPIFLAAPFQDNPVLQGIANFFNPTRPSGLFIEVLLVI... | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... |
P49461 | MKQTDDKDSLLNRLLLSLGILLFIRMGTFLPVPGIDHGHLEFYIERHFRLRTLVSTFAGDNTVVVGLFTLNIFPYINASIIMQLLVSLLPGLSKLQKEGGAEARRSINSLTRLLTLGWSLIQSTSVAFYLKRALFEWNLVLAFEIVIWLTTGAMIVLWLSEIITEYGLGNGPSLLIYTNIVSSLPGFVKQVITESSGKVPIGSWLLSGFVLFVALYGIVLLQEGMRKVYLISSKQLNQTSLPFSGSSNLESGYYIPLRFNQAGVMPIILTTAVLVIPTFIYNLGLLRILTPLITLPVFVKSYKIIYWVSYFVLILLFSLF... | Function: The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compose... |
B7T1W7 | MNTKLQDSKSPRLKNRILLTISLLTIVRIGSFIPVPYITKEVLVNLLSAENSSNNTFAQLLNTFSGGGNSSFGLLSLGILPYINASIIIQLLTTIIPALSKMQKDEGEYGRRKLVDFTRYLTFFWAIVESISISYSLREVIFEWNLQVYFLISLSLITGSMIVLWFSELITKNGLGNGSSLLICFNIVSNLPDQIKFSLISLKNQINNFSNIFLLISIFLITTIGCIYINEAIIKIPLVSARQLLKKTKSEEKNSSNSILPLRINQAGVMPLVFTSYAILFFSSLFEIIKKQTNIFNIFFQYPILNSVISYWFLKILFWI... | Function: The central subunit of the protein translocation channel SecYE. Consists of two halves. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resid... |
P78283 | MARKPGQDFRSAQSGLSELKSRLFFVIGALLVFRAGSFVPIPGIDAAVLAELFEQQKGTIVEMFNMFSGGALERASILALGIMPYISASIVVQLLTVVHPALAELKKEGEAGRRKISQYTRYGTLVLATFQAIGIATGLPNMVNNLVVIDQTMFTLIATVSLVTGTMFLMWLGEQITERGIGNGISILIFAGIVAGLPKAIGQTIEQARQGELHVLLLLLIAVLAFAVIYFVVFMERGQRRIVVNYAKRQQGRKVFAAQSTHLPLKINMAGVIPAIFASSIILFPGTLAQWFGQNGESSTFGWLTDVSLALSPGQPLYVM... | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... |
Q9M8Y0 | MISSKNGAAMISRPVFLSDRVDEVFSRKLDLSVSSSSSSSLLQQFNKTHEGDDDARLALAHQLYKGGDFKQALEHSNMVYQRNPLRTDNLLLIGAIYYQLQEYDMCIARNEEALRIQPQFAECYGNMANAWKEKGDTDRAIRYYLIAIELRPNFADAWSNLASAYMRKGRLSEATQCCQQALSLNPLLVDAHSNLGNLMKAQGLIHEAYSCYLEAVRIQPTFAIAWSNLAGLFMESGDLNRALQYYKEAVKLKPAFPDAYLNLGNVYKALGRPTEAIMCYQHALQMRPNSAMAFGNIASIYYEQGQLDLAIRHYKQALSR... | Function: O-linked N-acetylglucosamine transferase (OGT) that mediates O-glycosylation of capsid protein (CP) of virus in case of infection by Plum pox virus . OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine . ... |
C5FHK0 | MSTMIFMYFIYIVLYASGIAANLSYHVHEKRSIPVWWQRVSRIDPHAFLPLTIALAQQNLEHAEDYLLSVSDPSSPQYAQYWTAEAVAAKFAPSEPTARKVMSWLNQSGIAPAGVRRSKSGGELYMNITAQEAEKLLHTTFYIYKHQLTNKTLAICEKYSVATFVEKYVDFITTTEQFHHGLRRRSFQDPEPRMPSGKSPGHYVELADDSFPFPYLSFGSSVGLLKNKILSDSLPSNCDKLITPDCLRALYHIPVRNTSHPDNSLGIIEFTWVGYLESDLDKFFNIFQPSMVGNRPKFESIDGGFIQTLVPSFAFNGEAD... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
Catalytic Activity: Release of an N-terminal tripeptide from a polypeptide.
Sequence Mass (Da): 73464
Sequence Length: 670
Subcellular Location: Secreted
EC: 3.4.14.10
|
Q70DX9 | MRLSHVLLGTAAAAGVLASPTPNDYVVHERRAVLPRSWTEEKRLDKASILPMRIGLTQSNLDRGHDLLMEISDPRSSRYGQHLSVEEVHSLFAPSQETVDRVRAWLESEGIAGDRISQSSNEQFLQFDASAAEVERLLGTEYYLYTHQGSGKSHIACREYHVPHSLQRHIDYITPGIKLLEVEGVKKARSIEKRSFRSPLPPILERLTLPLSELLGNTLLCDVAITPLCISALYNITRGSKATKGNELGIFEDLGDVYSQEDLNLFFSTFAQQIPQGTHPILKAVDGAQAPTSVTNAGPESDLDFQISYPIIWPQNSILF... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
PTM: N-glycosylated.
Catalytic Activity: Release of an N-terminal tripeptide from a polypeptide.
Sequence Mass (Da): 69963
Sequence Length: 644
Subcellular Location: Sec... |
Q01589 | MKLSTVLLSAGLASTTLAQFSNSTSASSTDVTSSSSISTSSGSVTITSSEAPESDNGTSTAAPTETSTEAPTTAIPTNGTSTEAPTTAIPTNGTSTEAPTDTTTEAPTTALPTNGTSTEAPTDTTTEAPTTGLPTNGTTSAFPPTTSLPPSNTTTTPPYNPSTDYTTDYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEKPTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEKSEAPESSVPVTESKGTTTKETGVTTKQTTANPSLTVSTVVPVSSSASSHSVVINSNGA... | Function: Component of the cell wall. Major cell wall protein in stationary phase cells. Required to stabilize the cell wall in the absence of multiple GPI-anchored mannoproteins.
PTM: The N-terminus is blocked.
Location Topology: Lipid-anchor
Sequence Mass (Da): 34431
Sequence Length: 338
Domain: The number of the int... |
Q70J59 | MFSSLLNRGALLAVVSLLSSSVAAEVFEKLSAVPQGWKYSHTPSDRDPIRLQIALKQHDVEGFETALLEMSDPYHPNYGKHFQTHEEMKRMLLPTQEAVESVRGWLESAGISDIEEDADWIKFRTTVGVANDLLDADFKWYVNEVGHVERLRTLAYSLPQSVASHVNMVQPTTRFGQIKPNRATMRGRPVQVDADILSAAVQAGDTSTCDQVITPQCLKDLYNIGDYKADPNGGSKVAFASFLEEYARYDDLAKFEEKLAPYAIGQNFSVIQYNGGLNDQNSASDSGEANLDLQYIVGVSSPIPVTEFSTGGRGLLIPDL... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
PTM: N-glycosylated.
Catalytic Activity: Release of an N-terminal tripeptide from a polypeptide.
Sequence Mass (Da): 65839
Sequence Length: 602
Subcellular Location: Sec... |
D4AK75 | MLLRWHSVIPLFLAMTVAFPNTYRTVVEDLPAIPEGWVQGNPPSPETSVRMNLAVGQQNTRTFEQIVLDISTPGHRNYGKHLSRRDLKGLLRPRRETSNLILSWLEKSGVPKRSIVDDGDWIHFVISISQAERMLQTRFYHFHDVQDPGISMIRTLKYSVPSRLARHVYMIQPTTKFGKPKKHANSIANLQAIYLSTNATENCNATITPRCLRELYKMGDYVAKPDCRNVIGVSGYLDQYARYSDFYKFLELYAPEMKGANFSVAHIGNGQNLQNSTRNSIEASLDIEYALGLSNASAVFYTTSGRGPLVPDLDQPEQEH... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
Catalytic Activity: Release of an N-terminal tripeptide from a polypeptide.
Sequence Mass (Da): 65507
Sequence Length: 593
Subcellular Location: Secreted
EC: 3.4.14.10
|
B5EBG1 | MTDKVRLTTMVQAAGUAAKLGPAGLEEAIHDITRSDDPNLIVGVEGAEDAGIYRIGENLALVETTDIITPLVDDPFTFGRIAAANALSDVYAMGGRPVTAMNLAFFPACSLPTSVLAAILAGGSAALKEAGTCLVGGHTVEDDELKFGLAVTGLIDPARVVRNCTARPGDLIVITKPLGTGIISTAIKAEMIEPEVEAEATRWMTTLNAKAADLMVACRATAATDVTGFGFIGHACEMALGAKVSFKIELARVPVIPGVPALIDDGMVPAGCYRNRQHYEQHVSGNSGDPLLPLFDPQTSGGLLITFAPDDARTFLSRAG... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Synthesizes selenophosphate from selenide and ATP.
Catalytic Activity: ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate
Sequence Mass (Da): 35609
Sequence Length: 343
EC: 2.7.9.3
|
Q182I1 | MKKEQKKLTEMTTAGGUAAKIGPEVLASVLSQLPKNDNIENLLVGLDTADDAAVYKLNDDMALIQTLDFFTPMVDDPYVFGQIAASNSLSDVYAMGGKPLVAMNIVCFPSCHDMDVLAEILKGGFDKVKESGALLVGGHTVDDKEPKYGLSVSGIVSPNKVLSNATAKPGDKLIITKPIGVGVLNTAMKEGMVEQHIADKVIEIMIHLNKYAAMSFEKFDVNSVTDITGFGLLGHTLEMAKASEVSIEIESKHVPIIEGAIEMAQMGIIPAGMYKNMHYVSKDVEVVGNIEVAVQDILYDPQTSGGLLISVKEELAEELV... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Synthesizes selenophosphate from selenide and ATP.
Catalytic Activity: ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate
Sequence Mass (Da): 37331
Sequence Length: 348
EC: 2.7.9.3
|
Q47H71 | MPEEKIRLTQLSHGGGCGCKIAPAVLQKILAGTTGSIIPPQLLVGTETSDDAAVYQINAQQAIVATTDFFMPIVDNPRDFGRIAATNAISDVYAMGGTPLFALALVGMPVNVLPLETIGQILQGGEDVCRAAGIPIAGGHTIDSVEPIYGLVAIGLVNPEHLKRNSGAKSGDKLILGKQLGVGIYSAALKKDQLQAKDYEAMVETTTQLNTPGPVLACLDGVHAVTDVTGFGLAGHLLEVCKGSGLRATVNYQDLPVLPKAREFMQAGLMTGASGRNWASYGEGVRIADGLEGIAQTLLTDPQTSGGLLVSCSPETVTEV... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Synthesizes selenophosphate from selenide and ATP.
Catalytic Activity: ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate
Sequence Mass (Da): 36162
Sequence Length: 348
EC: 2.7.9.3
|
Q72CF1 | MTVDRLTSRSRAAGUAAKIAPGDLERILATLPRDPREGERVVVGTRDNEDAAIVRVPGGKAIVQTLDFFTPIVDDPYLFGQIAAANALSDVYAMGGEPWCALNIVCFPVKELPEDILADILRGGADKVREAGAVLVGGHSIEDESIKYGLSVTGIIDPDCYATNTGLRPGDVLLLTKPLGSGVLATAVKAGWDGFEAHEQELGRWGAMLNRAGGRVIRELGLAAATDVTGFGLGGHLLEMANASNMSVHVDVSTLPLMPAVLDLVATGLLPAGSHANRHFCSGNVSVHPEVDSLLVDIVFDAQTSGGLILAVPPHLVDDA... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Synthesizes selenophosphate from selenide and ATP.
Catalytic Activity: ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate
Sequence Mass (Da): 36973
Sequence Length: 351
EC: 2.7.9.3
|
Q94497 | MSISIKDKKEELLCRLTDFTKLKGUGCKVPQAELLSLLDGIGEGIGYDCSISQTKFPDIVMIQTTDFFFPLVDDPYFQGKIACANVLSDLYSFGIEDCDNMLMLLACSTDMTAEQRQWSSKLMIQGFNDQAICAGSKVSGGQTVKNPWPIVGGVATSILKTNEFIKPVNAVPGDVLVLTKPLGTQVCVNFHQWLSKPERWEKINTITNAEECEQVFNYATLSMARLNRVGARLMKKYNAHAATDVTGFGILGHSTNLAQNQLLPIRFEIHTLPIIKHMKKLEDHLNHPFKLLKGTSAETSGGLLISMSRENAEAFCKEIY... | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Synthesizes selenophosphate from selenide and ATP.
Catalytic Activity: ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate
Sequence Mass (Da): 40552
Sequence Length: 364
EC: 2.7.9.3
|
C6C1K6 | MDAEIISVMPFDNSYARLDKKFYQRINPTPVKHPRIILVNRELAGEMEFPLPETDAELAELFSGNKPPQGSEPLAQVYAGHQFGNFVPQLGDGRAVLLGEFVSSSGKRYDIQLKGAGQTMYSRNGDGRSPLGPVIREYIVSEAMFRLGIPTTRALAMVCSGEEVFREQALPGAVFTRVASSHIRIGTFEYFASRNDYEGVKTLADYAIDRHYPHLKEAGNPYAAFLGKVCSVQARLIAKWMRIGFIHGVMNTDNTTISGETIDYGPCAFMDGYDPATVFSSIDHYGRYAYARQPSIAQWNLAGLAGCLLPLIHKDTGQAK... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 55692
Sequence Length: 492
EC: 2.7.7.108
|
Q60B95 | MSTAMPGAFSPPRGLADLPLCPVYSRLGRPFHQPVAATSLPEPRMVHFNAALAGELGFGPEAGPQLLEILAGNRPWPGYASSASVYAGHQFGAWVPQLGDGRALLIAEVRTPARERVELQLKGAGPTPYSRGLDGRAVLRSSIREYLASEAMHALGVPTTRCLSLVASPQPVARETVESAAVVCRAAASFVRFGQFEYFAGRGQTEPMARLADHVIAEHFPHLQGHPERHAAWLGEVIERTARLIAQWQLLGFCHGVMNTDNFSVLGLTLDYGPFGFMDRFRWYHVCNHSDYEGRYAYRAQPEVGRWNCERLLQAVSPLL... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 56060
Sequence Length: 504
EC: 2.7.7.108
|
Q9RA11 | MRQKTATITRRDKSFTGHYVPVKPTPIKDPEYVAHSKNLFSELGFADSMAESADFVRMFSGDMSGVPVPMRQVGWASGYALSIYGTEYTQQCPFQTGNGYGDGRAISVLETLIKGQRWEMQLKGGGRTPYCRGADGRAVLRSSIREFLAQDHMHALGVPTSRSLSLYVSKTETVKRPWYSQGSRSENPDMLISEAVAISTRVAPSFIRVGQLELFARRSRSNEHPKAMEELEKIVLHLIDREYADVIDTQLATPEKIVLLAREFRGRLTSMVANWIRVGFCQGNFNSDNCAAGGFTLDYGPFGFCDVFNPYYQPWTGGGN... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 63003
Sequence Length: 557
EC: 2.7.7.108
|
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