ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q58419 | MSPIKHKTIRMIKDKIFLFIVGALTLLAILPLFHIIISIVEKGLPIIMERGLTFITGTLSEGGIGPAIVGTLMLTFLATLIGLPLAFLAGAYAYEFPNSFIGRATKMLLQIMLEFPTILVGTFVMGMLVVPMGTFSALAGALALALILTPYVAVYTEEAMAEVPKIYKEGGYALGCTRAQVIFKVITKMAKKGILTGILIGMAKVAGETAPLLFTAGGLYEVYPTNPLEPVGAIPLLIYTLVQSPSIEDHQMAWGAALVMLIIFLAIFVPIRYALKDDIKL | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30249
Sequence Length: 281
Subcellular Location: Cell membrane
|
Q9YG51 | MKLMDVRVSGLNVWITDKHILKGISFKAQPGTVTAIMGPSGSGKSTLIRVINRLIDLIPGARVEGEVWINNMNVMKEDPYNIRRYTGMVFQEPNPFPHMTIYENVAIGPKLHGLAKNKKELDEIVEWALKMAHLWDEVKDRLSDYPHQLSGGQRQRLSLARALALKPRVLLLDEPTANIDPVSTVKIEQSIVEYAKEEMATVIIVTHTPQQAARISDQILFLYEGRVIEYGPTKELVLRPRHELTKKFLGGEV | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28610
Sequence Length: 253
Subcellular Location: Cell membrane
EC: 7.3.2.1
|
O28912 | MEVAFDIRNFSVYYGNKVGIRNVNLEIYRNKVTAIIGPSGCGKSTLLRSLNRLIELVDGVRIEGEVIFDGKNIYDDGVDAVELRRRIGMVFQHPNPFPKSIFDNVAYGPRVHGIKDKERLKEIVEESLKKAALWDEVKDRLSDSALGLSGGQQQRLCIARAIATNPEVILFDEPTSALDPIAAAKIEELMVELKKNYTVVVVTHNIQQAARISDYVAFFWMGELVEYGKTAKVFEKPEKELTEKYLTGRVG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28220
Sequence Length: 251
Subcellular Location: Cell membrane
EC: 7.3.2.1
|
Q5P1F3 | MRSIDRPGGQAARPTIGSVAGASNTRTRDARSLPDTPPLKAAAENFSFYYGQFQALKSITLPVYEKHVTALIGPSGCGKSTLLRACNRMHDLSPGNRYEGAIRLLPDNTNLLDPAVDPIEVRMRIGMVFQKPNPFPKSIYENVAYGLRIRGEKSRSVLDDRVEEALKGAALWAEVAHRLNEPAFALSGGQQQRLCIARCLATDPEVLLFDEPTSALDPIATASIEELIDQLRQKVTILIVTHNMQQAARVSDFTAYMYLGELIEFGQTRQLFVNPVRRETEDYITGRFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32021
Sequence Length: 289
Subcellular Location: Cell inner membrane
EC: 7.3.2.1
|
Q5NNN6 | MTNKDNTVEDLEQFIAPPAAENLNLEARNLDFYYGTHQTLFNVSLPVERNKITALIGPSGCGKSTLLRILNRIYALYPQQYAVGRVLLDGKDILTDHDTLTRLKERGDNVTLDPLGDDISQIRARIGMVFQKPTPFPMSIYDNVAYGVRLHFNKSRQELDHIVERSLHRAALWDEVKDKLKESGLSLSGGQQQRLCVARGLAVEPEVLLLDEPASALDPVSTARLEETLMELKKDLSIVIVTHNLQQAARISDYTGFMYLGNMIEFCSTDRLFARPKTRRARDYLTGRFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32751
Sequence Length: 290
Subcellular Location: Cell inner membrane
EC: 7.3.2.1
|
P0A629 | MLARAGEVGRAGPAIRWLGGIGAVIPLLALVLVLVVLVIEAMGAIRLNGLHFFTATEWNPGNTYGETVVTDGVAHPVGAYYGALPLIVGTLATSAIALIIAVPVSVGAALVIVERLPKRLAEAVGIVLELLAGIPSVVVGLWGAMTFGPFIAHHIAPVIAHNAPDVPVLNYLRGDPGNGEGMLVSGLVLAVMVVPIIATTTHDLFRQVPVLPREGAIALGMSNWECVRRVTLPWVSSGIVGAVVLGLGRALGETMAVAMVSGAVLGAMPANIYATMTTIAATIVSQLDSAMTDSTNFAVKTLAEVGLVLMVITLLTNVAARGMVRRVSRTALPVGRGI | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34793
Sequence Length: 338
Subcellular Location: Cell membrane
|
P0AGH9 | MAATKPAFNPPGKKGDIIFSVLVKLAALIVLLMLGGIIVSLIISSWPSIQKFGLAFLWTKEWDAPNDIYGALVPIYGTLVTSFIALLIAVPVSFGIALFLTELAPGWLKRPLGIAIELLAAIPSIVYGMWGLFIFAPLFAVYFQEPVGNIMSNIPIVGALFSGPAFGIGILAAGVILAIMIIPYIAAVMRDVFEQTPVMMKESAYGIGCTTWEVIWRIVLPFTKNGVIGGIMLGLGRALGETMAVTFIIGNTYQLDSASLYMPGNSITSALANEFAEAESGLHVAALMELGLILFVITFIVLAASKFMIMRLAKNEGAR | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34121
Sequence Length: 319
Subcellular Location: Cell inner membrane
|
P45191 | MLTKSRKYFNQTWIESLFKQTTALFALLVFILLAAILISLVIGSWESIKRFGGSFLLETYWDPVQEQYGAIIPILGTLITAGIALFIAVPISFGIAIFLTELAPNWLKRPISIAIEMLAAIPSIIYGMWGLFVFVPLFQEHIQPVLIDNLGNLPGLELFFSGVPFGVGLFTAGLVLAIMIIPFIASVMRDVFSIVPPMLKEGAYGLGATTWEVVRQVIVPHTRIGLVGSVMLGLGRALGETMAITFIIGNSFQLPNSLFSPSTSIASAIANEFNEAGGLQKSALMELGLLLFVITTMVLILSRLMITKMQQTKGK | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34343
Sequence Length: 315
Subcellular Location: Cell inner membrane
|
Q58420 | MKTMEIKKLLRKIDEFKIITLPAIFVVFILFVLILGFYFFNALPAIERYGIDLFITNVWKAAEEPAKEVYGLAAPIWGSIYTATIAVLIALPLSICYAIFVNDYAPKRLKYPLIVISDIMAGLPTIIYGIWGAFILVPLLRDHIMKFLYEHFSFIPLFDYPPLSGYCYLSAGILLGIMVTPFAAAIIREAYAMIPSVYKEGLVALGATRYETTKVLIKYIRPAIISGLILAFGRALGETVAVSLVIGNSFNLTYKLFAPGYTISSLIANQFGNAVLYEYMTSVLYSAGLVLFVIGLVVNIIGIYYLKRWREHVSH | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35263
Sequence Length: 315
Subcellular Location: Cell membrane
|
Q50098 | MIKPTPAAVGSYVTRRCDRLFKSAAAAAGSTVVAAILLIAIFLLLRAVPSLRANHANFFTSAKFDTTGDKNLAFGIRDLFMVTVLSSICALVLAVPVAIGIAVFLTQYVPARLSRLFSAMVDLLAAVPSIIFGLWGVFVLAPKLQPIAVFLNHNLGWLFLFKQGNVSLAGGGTIFTSGIVLAVMILPIVTSVSREVFRHTPLIQIEAAQALGATKWEVVQMTVLPFGRSGVAAAAMLGLGRALGETLAVLIILRSAARSGNWSLFDGGYTFASKIASAASEFSQPLPTGAYIAAGFALFFLTFVVNAVARAISGGRVNG | Function: Part of a binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33505
Sequence Length: 319
Subcellular Location: Cell membrane
|
O51508 | MTLSGKRISKGIGIGEVLCIRKNFDKIISREKIDFSQVDSEISKFNKAKSKAIEALRDLERKAMLQFGDDKKGIFEGQVLIVEDDELDELVIELIVKENYSAAYSIYLAFENLVKSVEDYKDPYLKERASDYKDIRNRLISIILGQVSDFSEINKDIILVTEELTPSDTMQFDLNYVKGFLTAVGGETSHAAILARTMGLPALVMTLSDIDALKDGDKIVIDAMSSIVIKNPSSDEINLYEGKILRQVELEKELFSLKDKDAETKDGTKVFLKANIGTPVDITYVNKYGVEGIGLFRTEFLYMRSLQPPTEDEQFETYKRVIETMEKKGVVTIRTLDVGGDKEIPYLNFKKEENPFLGFRALRMYKEYEELIQAQFNAIFRASHYGKIRVMVPMLTIYEEIETIEYFVNNAKINLKSRGLPFDENLEVGCMIEVPSAALISSKLANKLKFFSIGTNDLTQYVLAVDRGNQKISNLYDKYNPAVLKLIKKVLDDGVSSGIDVSVCGELGGDDAGALLLVGLGFRSLSMIPSATLRIKYLLKKYTIMELEELANKVLNSDSKQETLSYFDKFIGD | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 64595
Sequence Length: 573
Domain: The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Cytoplasm
EC: 2.7.3.9
|
Q9Z9E3 | MDTQSSIGNEEWRIAGTSVVSGMALGKVFFLGTSPLHVRELTLPQEEVEHEIHRYYKALNRSKSDIVALEQEVTGQQGLQEVSSILQAHLEIMKDPLLTEEVVNTIRKDRKNAEYVFSSVMGKIEESLTAVRGMPSVVDRVQDIHDISNRVIGHLCCQHKSSLGESDQNLIIFSEELTPSEVASANSAYIRGFVSLVGAATSHTAIVSRAKSIPYLANISEELWNIAKRYNGKLVLIDGYRGELIFNPKPATLQSCYKKELSVVAHTSQRLVRKSLHPIVSSHAGSDKDVEDLLENFPQTSIGLFRSEFLAVILGRLPTLREQVDLYEKLARFPGDSPSVLRLFDFGEDKPCPGIKNKKERSIRWLLDYSVILEDQLQAIAKASLQGSIKVLIPGVSDVSEIIEVKKKWETIQTRFPKGHKVSWGTMIEFPSAVWMIEEILPECDFLSIGTNDLVQYTLGISRESALPKHLNVTLPPAVIRMIHHVLQAAKQNQVPVSICGEAAGQLSLTPLFIGLGVQELSVAMPVINRLRNHIALLELNSCLEITEALLQAKTCSEVEELLNRNNKITS | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 63479
Sequence Length: 571
Domain: The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Cytoplasm
EC: 2.7.3.9
|
P23536 | MPFALHGIPVSRGVAIGRAHLLAPAALDVSHYLVDEDQLDAEVERLRAARAAVRAELAALKRDLPRDAPEELGAFLDVHAMILDDEALAREPEALIRGRRYNAEWALTTRLEELMRQFDEIEDEYLRERKTDIRQVVERILKALAGAPVLVPAPVPALAADGEAATGVIVVAHDIAPADMLQFRHTVFHGFVTDMGGRTSHTAIVARSLDIPAAVGVQSASELIRQDDWIIIDGDAGLVIVDPTAIILEEYRHRQSERALEKKRLQRLRHTPAVTLDGLEIDLLANIEMAEDAGAALAAGAVGVGLFRSEFLFMNRRDELPGEDEQFQAYRGAVDAMHGLPVTIRTIDIGADKPLDARGDEFETALNPALGLRAIRWSLSEPGMFLTQLRALLRASAFGPVRLLVPMLAHASEIDQTLALIAKAKRQLDERGEAYDPGMKVGAMIEIPAAVLLLPLFLRKMDFLSIGTNDLIQYTLAIDRADNAVAHLFDPLHPAVLQLVARTIREANRAGVPVAVCGEMAGDPSMTRLLLGMGLREFSMHPAQLLRVKQEILHAHCERLEPLVDQVLQAFDPEEQAAALRQLARP | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 64300
Sequence Length: 586
Domain: The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Cytoplasm
EC: 2.7.3.9
|
P08839 | MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAIRIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) . Can also use (Z)-3-fluoro-PEP (ZFPEP), (Z)-3-methyl-PEP (ZMePEP), (Z)-3-chloro-PEP (ZClPEP) and (E)-3-chloro-PEP (EClPEP) as alternative phosphoryl donors .
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 63562
Sequence Length: 575
Domain: The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Cytoplasm
EC: 2.7.3.9
|
D4GYE2 | MTERTLSGIGVTPLSGVGTVVWYRPDADLPEPPAPVDVDAEAELARFEDARAAAEDELEAERERTAERVGEEEAAVFDAHVQFLNDPQITDGVSDAIESGLPAEHAVQETFTEFVEQFENMGGRMGERADDLRDVRDRLVRVLSDGERVDLSSLPEGSVVVAERLTPSDTAQLDPERVAGFVTVTGGRTSHAAIFARSLALPAIVGVGEELQSVEDGTEVVVDGESGDLVVDPSDERKEAAAAAADVDIRHEAVETADGVDIEVAANIGTLADLGPAVDRGADGVGLFRTEFLFLDRESPPDEDEQYEAYVEALESFDGGRVVVRTLDIGGDKPVPYLDLPDEENPFLGERGIRRSLGPDADLFETQVRALLRAAASADGANLSVMLPLVSTVEELRAGRERFESVAADLDAEGVANELPEFGIMVETPAAAFMADQFAPHVDFFSIGTNDLAQYVMAAERGNERVSELGDYRQPAVLRAIDATVSAAEGEDCWVGMCGEMAGDPDLTELLVGLGLDELSMSAVTVPQVKAAVAETDTADARDLAERVLQADTKAEVAEILTLDQ | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 60325
Sequence Length: 565
Domain: The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Cytoplasm
EC: 2.7.3.9
|
Q9ZAD8 | MTTMLKGIAASSGVAVAKAYLLVQPDLSFETKTIADTANEEARLDAALATSQSELQLIKDKAVTTLGEEAASVFDAHMMVLADPDMTAQIKAVINDKKVNAESALKEVTDMFIGIFEGMTDNAYMQERAADIKDVTKRVLAHLLGVKLPSPALIDEEVIIVAEDLTPSDTAQLDKKFVKAFVTNIGGRTSHSAIMARTLEIPAVLGTNNITELVSEGQLLAVSGLTGEVILDPSTEQQSEFHKAGDAYAAQKAEWAALKDAETVTADGRHYELAANIGTPKDVEGVNDNGAEAIGLYRTEFLYMDAQDFPTEDDQYEAYKAVLEGMNGKPVVVRTMDIGGDKTLPYFDLPKEMNPFLGWRALRISLSTAGDGMFRTQLRALLRASVHGQLRIMFPMVALVTEFRAAKKIYDEEKSKLIAEGVPVAEGIEVGIMIEIPAAAMLADQFAKEVDFFSIGTNDLIQYTMAADRMNEQVSYLYQPYNPSILRLINNVIKAAHAEGKWAGMCGEMAGDQTAVPLLMGMGLDEFSMSATSVLQTRSLMKRLDSKKMEELSSKALSECATMEEVIALVEEYTK | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 62577
Sequence Length: 575
Domain: The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Cytoplasm
EC: 2.7.3.9
|
O31149 | MAKELKGIAASDGIAIAKAYLLVEPDLSYEKTEVTDVESEVKRFESALEVSRTELSMIREKAAKDLGEDKAQIFDAHLLVLNDPELTGPIEESIKNSKTNAETALQETTDMFIGMFESMDNEYMRERAADIKDVRKRVLSHLLGVTIPNPALIDEEVVVVAADLTPSDTAQLNRNFVKGFVTDIGGRTSHSAIMARSLEIPAVVGTKEVTASVAKNDIVIIDGLEGNVIIHPTEEQIAHYEKIKSDFALQQAEWDKLKNEKTVSKDGVHVELAANIGTPNDLEGVISNGGEAVGLYRTEFLYMGRDNFPTEEEQFEAYKAVVSGMDGKSVVVRTLDIGGDKTLPYLELPEEMNPFLGFRAIRLCFANEELFRTQLRALLRASVYGNLKIMFPMIATVNEFRQARDILLDEKAKLKAAGTEVSDSIELGIMIEIPAAAVLADQFAKEVDFFSIGTNDLIQYTMAADRMNERVSYLYQPYNPSILRLVKMVIDASHKEGKWTGMCGEMAGDQTAVPLLLGLGLDEFSMSASSILKSRSLIKRLDQSEMVKLAEEALNKSTAEEVVELVEKYTAE | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 63212
Sequence Length: 572
Domain: The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Cytoplasm
EC: 2.7.3.9
|
Q9CIF0 | MADKVIALACAAGMSTSLLVSKMQKAAADNGKDYEIFAKSTADIDNMLAGTGSPKPDVLLLGPQVAFMKGEVAKKAEIAGVPMDVIKMQDYGMMRGDKVLAAAENLMN | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (By similarity). Involved in cellobiose transport with PtcA and CelB. This system can also transport lactose .
Catalytic Activity: D-cellobiose(out) + N(pros)-phospho-L-histidyl-[protein] = 6-phospho-beta-D-glucosyl-(1->4)-D-glucose(in) + L-histidyl-[protein]
Sequence Mass (Da): 11310
Sequence Length: 108
Domain: The PTS EIIB type-3 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-3 domain.
|
Q9KCQ4 | MFKKLFGLDKKAKNEAASPQEELIYAPLNGTLVDIEDVPDPTFAQKMMGDGFAIDPRDGHVVAPVAGEIVQVFPTKHAVGIKTPGGAELLIHIGLETVNMKGEGFTAHVKEGDKVNVGDALVDFDLELVKEKAESTVTPVVVTNIDQLAVFEKQAATETKAGETSLVTIKVQG | Cofactor: Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport.
Sequence Mass (Da): 18438
Sequence Length: 173
Domain: The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
Subcellular Location: Cytoplasm
|
P45618 | MWFFNKNLKVLAPCDGTIITLDEVEDEVFKERMLGDGFAINPKSNDFHAPVSGKLVTAFPTKHAFGIQTKSGVEILLHIGLDTVSLDGNGFESFVTQDQEVNAGDKLVTVDLKSVAKKVPSIKSPIIFTNNGGKTLEIVKMGEVKQGDVVAILK | Cofactor: Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport.
Sequence Mass (Da): 16703
Sequence Length: 154
Domain: The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
Subcellular Location: Cytoplasm
|
Q8CZD5 | MFKNLFKIKEREPKEITVVAPITGEIIPLEEVPDPVFAQKMMGEGVAVKPANGEVISPVDGEVKLVFQTKHAIIVEAENNAEILIHIGLDTVNLEGEGFTAHVKDGDIVKVGDKLMSFDIATIEEKATSSITPIIISNTDNVREVKNIKVTEVTAGENQILQVIN | Cofactor: Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport.
Sequence Mass (Da): 17970
Sequence Length: 165
Domain: The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
Subcellular Location: Cytoplasm
|
P0A284 | MGLFDKLKSLVSDDKKDTGTIEIVAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMVAPVDGTIGKIFETNHAFSIESDSGIELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDPVIEFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK | Cofactor: Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport.
Sequence Mass (Da): 18247
Sequence Length: 169
Domain: The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
Subcellular Location: Cytoplasm
|
P57437 | MFKNVFANLQKVGKSLMLPVSVLPIAGILLGIGSAHFNFLPDILSQIMAQTGGSVFSNMPLIFAIGVALGFTNNDGVAALAAVVSYGILIQTLTAVEPIVLHTTIEVIKNKHLSDTGILGGIIAGAISAYMFNKFYRIQLPEYLGFFAGKRFVPIISGLSAILIGVILSLIWPPIGHGIQIFSKWAAYQNPILAFALYGLVERALVPFGLHHIWNVPFQMQIGEYTNSIGQVFHGDIARYMAGDSTAGNLSGGFIFKMYGLPGAALAIWHTSKKENKTKIGSIMISAALTAFLTGITEPIEFSFIIVAPVLYVIHAILAGLSFPLCIFLDMRAGTSFSHGFIDFIVLSGNSHHILLFPIIGILYGLLYYILFYLFIINFNLDTPGRENIKNNILEKDNNEIAPYIITALGGKNNIKNLDACITRLRITVSDISKVKQKDLKNIGAAGIIISGSGIQVVFGTRSENIKTAMDECIKNI | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport.
Catalytic Activity: D-glucose(out) + N(pros)-phospho-L-histidyl-[protein] = D-glucose 6-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51727
Sequence Length: 477
Domain: The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
Subcellular Location: Cell inner membrane
|
A9NE82 | MKLIVGLGNPGKQYVQTRHNIGFIAIDKLLSYLNTELKVDSKLQAAYTKTKIEGEDVIIAKPLTYMNLSGDAVTKLMNFYKIDVEDILVILDDTALPLGKIRIRQTGSHGGQNGLKDIINKLGTKDFKRLRIGIGEHAHMDKVDYVLGKFSTNELNTILPTIEYVNDAIIEWISTNNFNNIMTKYNTPQTL | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21455
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q6F8I7 | MSKISLIVGLGNPGAEYAQTRHNAGFWFVEQLADRYNITLKKDPKFHGFSGRGQIEGHDVRLLIPTTFMNRSGQSVVPFSKFYQISPEAILIAHDELDMDPGVIRLKTGGGHGGHNGLRDIVPHIGANFHRLRIGIGHPGSKDRVSGHVLGKAPQNEQTLMEDAIHHALSNTRLLVDGQIAQAMNQINAYKPK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21211
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
A5FZ48 | MKLWVGLGNPEPGMARNRHNIGFMAIDVIADRHGFAPWRKRFSGLVSEGSVGGEKIVALKPLTYMNESGRAVQPASAFFKLPPDAVTVFHDELDLIPGKVRVKRGGGAAGHNGLRSIDRTLGTQDYWRVRLGIGHPGDKARVHGHVLGNFAKTDEDWLVDTLEAVSDAAPLLAAGKPEDFMTKVALLTKDTA | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20773
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
B7J502 | MDWLLAGLGNPGAEYARTRHNAGFWTLQTLADRVGASLRMEKRWHCLAATARASGLELGLCMPQDFMNRSGGPVQAMAAFYKVAAERILVMHDELDLPPGAARLKRGGGHGGHNGLRDLDRALGTRDYWRLRIGIGHPGHKDAVIPYVLSAPPPADKTLIDEAIERSLGVLPDFLCGRTDAAQKSLHSD | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20542
Sequence Length: 189
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
B8D8Y9 | MIVGLSNPKKEYHSTRHNVGSWYLYSLAESYLRNFKNEKKFFGFTTSLNIESNYIRLLIPNIFMNINGQSVFKMASFYNINLSEILIVHDDLELQPGISKLKYSYGHNGHNGLRDIVNTFNKNINFYRFRIGIGRPINRDQIASFVLSNPTKKEKILIQKSILHAIEKNVLSNILKF | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20576
Sequence Length: 177
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
P59490 | MKEIKLIVGLANPIKKYNDTRHNVGSWLVNSLVTQQNKKLKKNNKFLGYSTEINILSKNIHVLVPDTFMNLSGISVLAISNFYNIKLHEILVVHDELDLKPGNVKFRLRSSHNGHNGIRNVLAVLGTNIKFLRIQIGIGRPINSGYKISKFVLSKPNVSEKLLINRAILCAIRVIYDSINQRNVIMTESSLNSMLDHYMNSCVIHHN | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 23466
Sequence Length: 207
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q057V0 | MNKIKMIVGLGNSVYKYNQTRHNVGFWYINMLSSFYKTSLKFKKKFSGYVSSFFLNNNKIFLLKPDLFMNLNGYSVFALSSFYKIKLSEILVVRDELDLSPGILKVKYGIGHNGHNGVKSIINTFEKKKPFIQLCIGIGRPEFKKNVSNFVLECPSKIDTINIKKAILKFIFLTKDYIYKKEFLKNKKIILI | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 22308
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q1IHW2 | MKLIVGLGNPGMQYQFTPHNLGFLAVDRIAEKYGIRVANRNCKALTGRGVIEGVDVVLAKPETYMNLSGASVQELVSELEIDGTKDMIVIYDDLDLPYGSIRVRERGSAGGHNGVQSIIGALDTQEFLRIRIGIAPEFKLSDGASYVLSQLKKSQLPVVDQALDDAAEAVKVILREGPGPAMNRFNRKPEPPESGGEVAAK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21691
Sequence Length: 201
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
C5CFR9 | MLVFIGLGNPGPRYVLTRHNVGFLFVDELLKKFQIGSSYRAETYEAFKLKSQSPAIAVKPLTYMNNSGIAVRDLIRDFGLSQNDRLIVIYDDVWIPLGRLRIRERGSDGGHNGVKSIISSLGTQEFSRIRIGIGPKPDDIDMVSYVLGEFTDSELKVLWKVLDLAISAAQEMFAADFKKVMSRYNSIGVE | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21293
Sequence Length: 190
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q5FMA9 | MKIIAGLGNPGQKYDKTKHNTGFMTMDHYLDKKGLTLNKDKFEGHWTKEKINGEDVIFLEPQTYMNESGRSVSQIANFFKVAPEDVLIIQDDMDMPIGKIRIRANGKSGGHNGIKSIIRDLGTEKFNRLKIGIRHPKNATVVSWVLTPFNDEQQKLMDDAFDTSVDIIDDFIAGRDSQYLMNKYN | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21055
Sequence Length: 185
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
C4Z4L5 | MYIIAGLGNPGKEYMGTRHNAGFSVIDELADKYNISVDTAKHKGLIGKGVIAGQKVILVKPMTYMNNSGECIREVMDYYKCDIDDFLVIFDDISLDVGKLRLRAKGSAGGHNGIKSIIAHLGSDKFKRIKFGVGDKPKNWDLADWVLGKFPAEEYATLREANKKACEAVECILTDGIESGMNKYNG | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20441
Sequence Length: 186
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
C1DBA8 | MSTIRLIVGLGNPGPEYAATRHNAGAWFTDQAARREHATPRLESKFFGLYARSGELHFVWPQTYMNASGKSVAAVARFYKILPEEILVVHDELDLPPGSARFKKGGGHGGHNGLRDIHSALGTPDYWRLRLGIGHPGDKSQVAHFVLKPPRSEEQTLIDIAIGHALDTLPDVLRGDFPAAMKTLHTAAK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20690
Sequence Length: 189
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q38V72 | MKMIVGLGNPGSKYAKTKHNIGFMVIDQLCEKYNVTLNKHDFEAEYGSFKYEGETVLLVKPLTFMNDSGRSVGPLMSYYQVGIDELLVIQDDMDLTMGKLRLRQKGSAGGHNGIKSIIAHTKSQTFKRLKIGIQHPQKSTVVNWVLTPFDKDGAPVINQAIDQACEAIDDWCQNDDFMKTMNKFN | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20810
Sequence Length: 185
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q2RMV4 | MKLVVGLGNPGPRYAGNRHNVGFMAVAALARRHGIGPFRRKFQAQVADGQIAGARLLLLAPETFMNASGQAVGEAARFHKIAPEDIIVLHDELDLAPGKIKVKQGGGAGGHNGIRDIEAHLGPAFWRVRLGIGHPGHKDRVLTYVLGDFAKAEEDWLAPMLDAVADHFALMLEGRPADFMSKVAAQTRPAEKAKPLATAKPKEGEARTSGGSVAEVGAPPPSPTGLAAALAEALDRKSQKGNG | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 25512
Sequence Length: 243
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q9ZCV4 | MILVIGLGNPGTEYQYTRHNIGFIAIERIASKYHLSFSIKKKFNCEIAEAVIDRQKIIFIKPTTYMNLSGKSVILVKTYYNIKYEKVFVIHDDIDLEIGRIKFKTGGGNGGHNGLKSIDVVIGNHYNRIRIGIGRPKNNHDVADYVLNNFSESEYKIAMQSIDNIANNFGLILEHKLAEFTNKIV | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21007
Sequence Length: 185
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
A7NK01 | MWLIVGLGNPGETYARTRHNIGFRVVTELAQRHHLRFTHKRAKAEIAEGEIAGQRVALALPQTYMNLSGQAVVGLRQWYKIDPATELLVVYDDVDLPFGVLRLRERGSAGTHNGMRSIVALLGSQVFPRLRIGIDRPPVAWNLADYVLARFTPEQEAQLPEVTRRAADALELVLREGIVVAMNRINAPPPKPEKKRGSETSDPSAESADHAGGG | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 23584
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q1AXL4 | MGLGNPGRRYALTRHNAGHMVLDELFRRHGGRWRRARRAEAAEVSVEGREAVLLKPATFMNESGEALSGYRAEDLIVVHDDLDLPAGTVRVKVGGGAGGHNGLRSVISRVGNGFVRVRVGIGRPPEGADVTGYVLGRMDRAAREAIPRAADAVEAVLEEGPEAAMNRFNARA | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 18459
Sequence Length: 172
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q67JD0 | MAKLIVGLGNPGPRYAATRHNAGWMLLDAFARKHGVAIEQRGFEGLYGELRWGAEAEKVILLKPLTYMNLSGRSVAQAARFYRIAPADILVLFDDLDLEPGRLRLRAKGSAGGHNGVKSVIAELGTAEFPRLRIGIGRPAPGWEVIDWVLAPFGPDDAAAVAAALPRAVEAVECFLTEGILAAMNRYNT | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20391
Sequence Length: 189
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q2LUK5 | MKLIVGLGNPGARYRFTRHNFGFFVLDQLAEDQDIMMSQTGFDALWGKGVIAGQSVLLAKPQTFMNLSGKSVRKLADFFKIVVEDVLVVHDDLDLPFGVIRLKAGGGQGGHKGLISICDSLGGPEFQRVRLGIGKPAQRSAVERYVLEPFTESELRILPRIIVTARSAILEVISSGIKTAMNSYNGMVINDLIQEV | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21447
Sequence Length: 196
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q3A314 | MKLVVGLGNPGPEYAATRHNIGFLVAQKFAQQMGVSLKRQAYQGIVGTGRADGQETMVLLPQTYMNRSGVSVVSACKSKGIAVEDVVVIHDEIDLPFGSIRIKVGGGHGGHNGLRSIVDLLGCRDFLRVRMGVGRPQGQVDVAKYVLGQFSSTEKSQLDNVLENSVKALEVLLQKGAQQAMNEFNNRVFLI | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20623
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q31RR0 | MSEDRPTLLVGLGNPGQKYAETRHNIGFMLIDRLAQDWGVKLSEDRKFQGEYGETAVPGLGKIRLLKPTTFMNQSGRSLRAVLDWYKLTPQQILVIYDDMDLPLGRLRLRQSGSAGTHNGMKSIISHLSSKDFPRLRLGISLPRSQSNDRHDATVSHVLGKFAVSEQSLLKQVLDLAQEATETALRSGVETAMNRYNARSLEAPAPVA | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 23083
Sequence Length: 208
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q2JV16 | MTQVKTQPPEEVALQLIVGLGNPGPQYANTRHNCGFMVVDQLAERWGIPLALEKRFQGSYGEGFALGGKRRLLKPETYMNRSGEAVRAVLDWYKLDPASVLVVYDDMDLPLGRLRLRGSGSAGGHNGMKSVIEHLGSEAFPRLRLGVGRPKGNQDRVGHVLGSFEPAEQAVLDRVLRAAVAAVECCLQEGLKTAMNRFNPLDFSGPDRQDQPAPLNPAKTAPGES | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 24456
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q59989 | MIPKLIVGLGNPEPKYDQTRHNIGFAVVDALAITWQCSWYDHKRFQGWFGEGLMAGQKTCLLKPRTYMNRSGQAVRAVVDWYKLDPQSVLVVYDDMDLPLGRLRLRQTGSAGGHNGMKSLISHLGTQDFPRLRLGIGKSDGSKDTIAHVLGKFSPSELPIVEKSLDLATEAIAHSLHHGIAKTMSLFNNRDVCP | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21524
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q9X1W1 | MVVVGLGNPGPRYAFTRHNVGFLFLDFLKNKDWKTEKYFAWNKINLAGNEVALVKPLTYMNLSGLAMPHVLKFFSASLDDIIVVYDDVSLKLGKIRIRKKGSDGGHNGMKSIIQALGTQEIKRIRVGIGDKPEGMDLVNFVLGEFSDEEWIILNKVFEVMKEALEVILVEGIEKAMSIYNSLEVRA | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20906
Sequence Length: 186
Subcellular Location: Cytoplasm
EC: 3.1.1.29
|
Q7VSX8 | MAGLSRILLSCTLACLLAGQAAQASVDDPTRAGGDNRVRALRADQARRDVLLTACRDDPGHRRGEPDCVNAERAQALQQWQAAAMTSVDAAFSDLAGALRNAAPRRMEAAIVRLTRQLQPLVYSMMTLLVLLTGYALLARRDRPFEWHIRHALLVAVVTSLALSPDRYLSTVVAGVQDVAGWLSGPWTAPDGAAGRGGLAQLDQFAAQAQAWVAQLAGQAANDANPGSAVNWLLCAMIVAASAGGWLCLAASLLIVPGLIVTLLLSLGPLFLVLLLFPALQRWTNAWLGALVRALVFMALGTPAVGLLSDVLAGALPAGLPQRFATDPLRSTMLAATLCATATLMLLTLVPLASSVNAGLRRRLWPNAAHPGLAQAHRQAAARQYAPRPAAAAAAAGPHQAGTYAASATPAPAPARPAPSFPAHAYRQYALGGARRPPPRVRRDDRPAPAPDRRVLPRKPNLP | Function: Component of the type IV secretion system ptl required for secretion of assembled pertussis toxin (PTX) through the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48679
Sequence Length: 463
Subcellular Location: Cell membrane
|
Q82IY7 | MSRAMDITRIPGSAIGAVVAGADFSGTIDDTQVEEIWQALDQHLVLVFRGHKDPSNDDLLMFARRFGHVPKTGLTTGASPDHNEILLISNILDENGQKIGVGNAEWMDWHTDYSFRPRVSRIGFLAAVELPPSGGGQTLFTDMYTAYESLPDDLRQRLHSYRARHSLRSGYEDVIEEEYQGEVSIEGPTAKPFVAPEDGTATVHQLIARNPRTGRRAVYANPLNTKRILELDVTSSKEVLQQLFAKPGEPELTYAHEWLPGDIVMWDQLGTVHAKRAFDPTERRLLRKVVTIFDDPAEPWHPEDAA | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the Fe(2+) and alpha-ketoglutarate-dependent oxidation of pentalenolactone D to pentalenolactone F. Also able to catalyze the oxidation of pentalenolactone D to pentalenolactone E. In presence of neopentalenolactone D, mediates production of PL308 and possibly neopentalenolactone E.
Catalytic Activity: 2 2-oxoglutarate + 2 O2 + pentalenolactone D = 2 CO2 + H2O + pentalenolactone F + 2 succinate
Sequence Mass (Da): 34236
Sequence Length: 306
Pathway: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
EC: 1.14.11.36
|
Q82IY8 | MVDIEAVRAKYREERDKRVQADGGRQYLSAQGEFAHYADDPHAKPIERAPVSDEVDVTIIGAGIGGLLLGARLREACAFDTIRLVDKAGDVGGTWYWNRFPGLRCDVESYVYMPLLEELGRLPSEKYATGAEIFEHCQAIARTYDLYDEALLQTSVTELSWDEDSSRWLVRTDRGDLVRSRFVAMAIGSLHRPKLPSIPGTEAFQGHSFHTSRWDFAYTGGDISGGLEKLGDKRVGIVGTGATAVQCIPHLAESAAHLYVFQRTPSTVSVRNNRPTDPGWAAGLEPGWQQRRMDNFHALTSGVDQDVDLVQDGWTEITSKLAAILPKSAADADPKDIGTAVELADFHKMEELRKRVDAIVHDKDTADALKPYYRLFCKRPCFHDGYLDTYNRPNVTLVDTQGRGVERLTPTSVVAGGREYPVDCLIFASGYESEFGVPYTNRTGFSIVGRDGIRLSEKWAEGARTFHGLQVNGFPNCFILSKAQSGLHVNVPYMLNEQSKHVAYILKAVQQRGRQVVEASATGEKEWVETILRLANRNLDFTESCTPGLFNNEGNPRNVAILNSSYGGGSVGFVNILKRWREADDLADLELREG | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the flavin-dependent Baeyer-Villiger oxidation of 1-deoxy-11-oxopentalenic acid to neopentalenolactone D in the biosynthesis of neopentalenolactone antibiotic.
Catalytic Activity: 1-deoxy-11-oxopentalenate + H(+) + NADPH + O2 = H2O + NADP(+) + neopentalenolactone D
Sequence Mass (Da): 65925
Sequence Length: 594
Pathway: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
EC: 1.14.13.171
|
Q82IY9 | MHLQPSTAVVTGAASGIGFALSARLAQAGARVVMTDIAGDGLAGAVEELAAHGADVTAVVADLTDPAAVQELADTAFGRLGDIDVVCNNAGVVGPVGMPLWSVPLDEMHAVFDVNYWAHVHVARAFVPRLLDSGRPSHLVQTASMSAFVVGAGTASYAASKHADLAAARSLRADLDGTPVRVSVLCPGRVDTPMTRGLVAPRNATGNTTISADEAADAVWNALGSDRFYIFTNADAQTRLGDQFNDVWRHLAREKYWTESSSPSVNSSRP | Function: Catalyzes the oxidation of 1-deoxy-11-beta-hydroxypentalenic acid to 1-deoxy-11-oxopentalenic acid in the biosynthesis of neopentalenolactone antibiotic.
Catalytic Activity: 1-deoxy-11beta-hydroxypentalenate + NAD(+) = 1-deoxy-11-oxopentalenate + H(+) + NADH
Sequence Mass (Da): 28161
Sequence Length: 270
Pathway: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
EC: 1.1.1.340
|
Q7VSX4 | MLNRPSSPDGGEAHAWPPDPEIPVFANAEHAHRRPLRWMFALVAVALSCLLATGIWRSRAAPPHAATQTVAPAGQALPPGRIFTVHPREPEPAPLPDMPAAPDPILPQPRPAPPVPPPPIRAPYDYDEPAPRRDSAALKSGPAMMVATAARLGQTERAGMADDGVSADAATLIGRNVSRATRSGGRDYRLLPGTFIDCILQTRIVTNVPGLTTCIVSRDVYSASGKRVLVPRGTTVVGEYRADLAQGSQRIYVAWSRLFMPSGLTIELASPAVDGTGAAGLPGVVDDKFAQRFGGALLLSVLGDATSYMLARATDARHGVNVNLTAAGTMNSLAASALNNTINIPPTLYKNHGDQIGILVARPLDFSILRGTNE | Function: Component of the type IV secretion system ptl required for secretion of assembled pertussis toxin (PTX) through the outer membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 39471
Sequence Length: 374
Subcellular Location: Cell membrane
|
Q82IZ1 | MTNVTGDYTDCTPLLGDRAALDSFYEEHGYLFLRNVLDRDLVKTVAEQMREGLVALGAADPHATLEELTIDSFESVDEVAMHDYVKYDAFWNNPSTIKVFEQVFGEPVFVFLSTTIRYYPSQAGSEEPSFHYLTPFHQDGFYIGPNQDFRTFWIPLIRTTRESGGVALADGSHRRGKRDHVLNESFRRFGHPVRGIPPTEVSEDEHLLHSPMEPGDILLFHAHMCHKSIPNLSKDPRLMRMSMDTRVQPAKSHRGFNAMTPWTESAKDASKGIMAKITGTPTDVE | Function: Catalyzes the conversion of 1-deoxypentalenic acid to 11-beta-hydroxy-1-deoxypentalenic acid in the biosynthesis of neopentalenolactone antibiotic.
Catalytic Activity: 1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11beta-hydroxypentalenate + CO2 + succinate
Sequence Mass (Da): 32264
Sequence Length: 285
Pathway: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
EC: 1.14.11.35
|
O10274 | MLTSRRWAVIYTRTSERNCGGAWCTNGVRRRRQVHLPSVRARAMFPDRWHEYTACGAVIEGTRLLCFKVPLNAELFEYVTSDEDRWTAASVLARHSALGAVIDLTNTARYYDGAQMVKMGLLYKKIRVPGRAVPDDDIVAEFIETVDEFFRRCPTMLVAVHWTHGLNRSGYLVCRYMVERLGVSPTDAIARFETARGHKIERTNYLQDLLARKHVRGQPN | Function: Could be inactive as the active site cysteine is modified to tryptophan.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 25234
Sequence Length: 220
EC: 3.1.3.48
|
P25044 | MAAAPWYIRQRDTDLLGKFKFIQNQEDGRLREATNGTVNSRWSLGVSIEPRNDARNRYVNIMPYERNRVHLKTLSGNDYINASYVKVNVPGQSIEPGYYIATQGPTRKTWDQFWQMCYHNCPLDNIVIVMVTPLVEYNREKCYQYWPRGGVDDTVRIASKWESPGGANDMTQFPSDLKIEFVNVHKVKDYYTVTDIKLTPTDPLVGPVKTVHHFYFDLWKDMNKPEEVVPIMELCAHSHSLNSRGNPIIVHCSAGVGRTGTFIALDHLMHDTLDFKNITERSRHSDRATEEYTRDLIEQIVLQLRSQRMKMVQTKDQFLFIYHAAKYLNSLSVNQ | Function: Is not required for vegetative growth.
PTM: Activated by phosphorylation at Ser-83.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 38868
Sequence Length: 335
Subcellular Location: Cytoplasm
EC: 3.1.3.48
|
G5EC24 | MPRLALRQYNFYYRVNGEKAEELLKEYGEDGDFLLRYSESNPQNFSISVRVAEDKILHIKVTKYESDMLSIFEDERTTPNQFGSITELAEFYMEFPEKLREKNGLFLELKKPVYVPYHLEACAEEQRRTQLYRWWHGNLPASSANKLLQTEKNGTYLLRASQHIPGALVISAKTEGQVVHLTIYQDPSTGRFNIDGDRTKFQSAWLLIDSYSKNPIVEKGEASRVLYLEEPLFNTFIEADLFVDRFEIIRRPINPRESMEKTGISEEFDRLSQEALPAEQYLSKREGRRPVNAEKNRYKNIVPFDHTRVILTDRPNTPGSDYINASYVRFENSQRTKNVTFACEKSFIATQGCLETTISDFWSMVWQENSRVIVMPTMENERKEKCARYWPAEVNKPEVHGDISLTCTIERKVQRAVSDEVKAELEQEKTNRIAKGLVPEAELNGDGISYILRTLVMKKGKDTREIRQLQYLTWPDHGCPLHPYAVLNFLEDVDREYDYFNAQPIAASLPQGPIVVHCSAGIGRTGTVLVLDALLNQVKKVGLLCPMDVYKMVKYVRTYRSGLVQTEQQYQFLYKALAFYLKNNNPYPVKSFIDGDTDAFDFPRRLRPTPNASRPSSARQVTSSRPSSSASSRTSHSRPRTGPQAEPIFERSTSSTSSSSTLLKSTKK | Function: Involved in embryonic and larval development . Plays a role in oogenesis by regulating mpk-1 phosphorylation and oocyte maturation in response to major sperm protein (MSP) . During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles probably downstream of receptor egl-15 . Plays a role in fluid homeostasis probably downstream of receptor egl-15 and adapter soc-1 . Promotes vulva induction and negatively regulates fertility probably downstream of receptor let-23 . Negatively regulates daf-2-mediated repression of dauer formation .
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 76743
Sequence Length: 668
Subcellular Location: Cytoplasm
EC: 3.1.3.48
|
P29461 | MDRIAQQYRNGKRDNNGNRMASSAISEKGHIQVNQTRTPGQMPVYRGETINLSNLPQNQIKPCKDLDDVNIRRNNSNRHSKILLLDLCAGPNTNSFLGNTNAKDITVLSLPLPSTLVKRSNYPFENLLKNYLGSDEKYIEFTKIIKDYDIFIFSDSFSRISSCLKTTFCLIEKFKKFICHFFPSPYLKFFLLEGSLNDSKAPSLGKNKKNCILPKLDLNLNVNLTSRSTLNLRINIPPPNDSNKIFLQSLKKDLIHYSPNSLQKFFQFNMPADLAPNDTILPNWLKFCSVKENEKVILKKLFNNFETLENFEMQRLEKCLKFKKKPLHQKQLSQKQRGPQSTDDSKLYSLTSLQRQYKSSLKSNIQKNQKLKLIIPKNNTSSSPSPLSSDDTIMSPINDYELTEGIQSFTKNRYSNILPYEHSRVKLPHSPKPPAVSEASTTETKTDKSYPMCPVDAKNHSCKPNDYINANYLKLTQINPDFKYIATQAPLPSTMDDFWKVITLNKVKVIISLNSDDELNLRKWDIYWNNLSYSNHTIKLQNTWENICNINGCVLRVFQVKKTAPQNDNISQDCDLPHNGDLTSITMAVSEPFIVYQLQYKNWLDSCGVDMNDIIKLHKVKNSLLFNPQSFITSLEKDVCKPDLIDDNNSELHLDTANSSPLLVHCSAGCGRTGVFVTLDFLLSILSPTTNHSNKIDVWNMTQDLIFIIVNELRKQRISMVQNLTQYIACYEALLNYFALQKQIKNALPC | Function: Major phosphatase responsible with PTP3 for tyrosine dephosphorylation of MAP kinase HOG1 to inactivate its activity. May also be involved in the regulation of MAP kinase FUS3. May be implicated in the ubiquitin-mediated protein degradation.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 85868
Sequence Length: 750
Subcellular Location: Cytoplasm
EC: 3.1.3.48
|
Q5HMA8 | MKIIFVCSGNTCRSPLAESIAKSLLPHDSIASRGLFAVEGQAISKESLELIHKYDLPEPSRAQAFHIDDLDADIILTMTQAHKDLIFSMYGRQSNVFTLNEYVGDTQEIDDPFGGSFDVYEQTYTKIYDLVDKIKFKHE | Function: Dephosphorylates the phosphotyrosine-containing proteins.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 15709
Sequence Length: 139
EC: 3.1.3.48
|
Q4L7Z6 | MRITFVCTGNTCRSPIAESIAKKMLVDDTINSRGLFAIDGQSVSPESLEVIMEHNLPEPTVAKQFSEKDLNSDLILTMTDMHKQQLVSHYGDNGRIYQLSEYVGEIGDIVDPFGGSIDTYRQTFEQLLYLIGKLRTNS | Function: Dephosphorylates the phosphotyrosine-containing proteins.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 15463
Sequence Length: 138
EC: 3.1.3.48
|
Q49Z62 | MKIIFVCTGNTCRSPMAESIAQSKLPNHTIVSRGMYAIDGQPISDHTKEILLERHLNVPYQAQSFTASDINADLILTMGSSHKRIIKELYDNTDHVFTLNEYVDKIGEVSDPFGGSKSAYLEIYNELNLLIDSLKNKILN | Function: Dephosphorylates the phosphotyrosine-containing proteins.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 15703
Sequence Length: 140
EC: 3.1.3.48
|
P42910 | MHEITLLQGLSLAALVFVLGIDFWLEALFLFRPIIVCTLTGAILGDIQTGLITGGLTELAFAGLTPAGGVQPPNPIMAGLMTTVIAWSTGVDAKTAIGLGLPFSLLMQYVILFFYSAFSLFMTKADKCAKEADTAAFSRLNWTTMLIVASAYAVIAFLCTYLAQGAMQALVKAMPAWLTHGFEVAGGILPAVGFGLLLRVMFKAQYIPYLIAGFLFVCYIQVSNLLPVAVLGAGFAVYEFFNAKSRQQAQPQPVASKNEEEDYSNGI | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This system is involved in N-acetylgalactosamine transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28645
Sequence Length: 267
Domain: The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell inner membrane
|
P42905 | MEISLLQAFALGIIAFIAGLDMFNGLTHMHRPVVLGPLVGLVLGDLHTGILTGGTLELVWMGLAPLAGAQPPNVIIGTIVGTAFAITTGVKPDVAVGVAVPFAVAVQMGITFLFSVMSGVMSRCDLATNPRRI | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This system is involved in N-acetylgalactosamine transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13721
Sequence Length: 133
Domain: The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell inner membrane
|
P42911 | MGSEISKKDITRLGFRSSLLQASFNYERMQAGGFTWAMLPILKKIYKDDKPGLSAAMKDNLEFINTHPNLVGFLMGLLISMEEKGENRDTIKGLKVALFGPIAGIGDAIFWFTLLPIMAGICSSFASQGNLLGPILFFAVYLLIFFLRVGWTHVGYSVGVKAIDKVRENSQMIARSATILGITVIGGLIASYVHINVVTSFAIDNTHSVALQQDFFDKVFPNILPMAYTLLMYYFLRVKKAHPVLLIGVTFVLSIVCSAFGIL | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This system is involved in N-acetylgalactosamine transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29001
Sequence Length: 263
Domain: The EIID domain, with its homologous EIIC domain, forms the PTS system translocation channel and contains part of its specific substrate-binding site.
Subcellular Location: Cell inner membrane
|
P17334 | MSNVIASLEKVLLPFAVKIGKQPHVNAIKNGFIRLMPLTLAGAMFVLINNVFLSFGEGSFFYSLGIRLDASTIETLNGLKGIGGNVYNGTLGIMSLMAPFFIGMALAEERKVDALAAGLLSVAAFMTVTPYSVGEAYAVGANWLGGANIISGIIIGLVVAEMFTFIVRRNWVIKLPDSVPASVSRSFSALIPGFIILSVMGIIAWALNTWGTNFHQIIMDTISTPLASLGSVVGWAYVIFVPLLWFFGIHGALALTALDNGIMTPWALENIATYQQYGSVEAALAAGKTFHIWAKPMLDSFIFLGGSGATLGLILAIFIASRRADYRQVAKLALPSGIFQINEPILFGLPIIMNPVMFIPFVLVQPILAAITLAAYYMGIIPPVTNIAPWTMPTGLGAFFNTNGSVAALLVALFNLGIATLIYLPFVVVANKAQNAIDKEESEEDIANALKF | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ChbABC PTS system is involved in the transport of the chitin disaccharide N,N'-diacetylchitobiose (GlcNAc2) . Also able to use N,N',N''-triacetyl chitotriose (GlcNAc3) .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48332
Sequence Length: 452
Domain: The EIIC type-3 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell inner membrane
|
Q8VYE4 | MEVEMHGDVSKWEGYADWRNKAALRGRHGGMLAASFVLAVEILENLAFLANASNLVLYLKNFMHMSLARSSSEVTTFMATAFLLALLGGFLADAFFSTFVIFLISASIEFLGLILLTIQARRPSLMPPPCKSSAALRCEVVGGSKAAFLFVGLYLVSLGIGGIKGSLPSHGAEQFDEGTPKGRKQRSTFFNYYVFCLSCGALVAVTFVVWIEDNKGWEWGFGVSTISIFLSILVFLLGSRFYKNKIPRGSPLTTIFKVLLAASIVSCSSKTSSNHFTSREVQSEHEEKTPSQSLTNSLTCLNKAIEGKTHHIWLECTVQQVEDVKIVLKMLPIFGCTIMLNCCLAQLSTYSVHQAATMNRKIVNFNVPSASLPVFPVVFMLILAPTYDHLIIPFARKVTKSEIGITHLQRIGVGLVLSIVAMAVAALVELKRKQVAREAGLLDSEETLPITFLWIALQYLFLGSADLFTLAGLLEFFFTEAPSSMRSLATSLSWASLALGYYLSSVMVPIVNRVTKSAGQSPWLGEKLNRNRLDLFYWLMCVLSVVNFLHYLFWAKRYKYISTGSIS | Function: Involved in abscisic acid transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62653
Sequence Length: 567
Subcellular Location: Membrane
|
Q9LFX9 | MGVVENRKILPEKKLGGWRAITFILGNETLEKLGSIGVSANFMLYLRNVFHMEPVEAFNVYYLWMGLTNFAPLLGALISDAYIGRFKTIAYASLFSILGLMTVTLTACLPQLHPPPCNNPHPDECDDPNKLQLGILFLGLGFLSIGSGGIRPCSIPFGVDQFDQRTEQGLKGVASFFNWYYLTLTMVLIFSHTVVVYLQTVSWVIGFSIPTSLMACAVVLFFVGMRFYVYVKPEGSVFSGIARVIVAARKKRDLKISLVDDGTEEYYEPPVKPGVLSKLPLTDQFKFLDKAAVILDGDLTSEGVPANKWRLCSIQEVEEVKCLIRVVPVWSAGIISIVAMTTQATFMVFQATKMDRHMGPHFEIPAASITVISYITIGIWVPIYEHLLVPFLWRMRKFRVTLLQRMGIGIVFAILSMFTAGFVEGVRRTRATEMTQMSVFWLALPLILMGLCESFNFIGLIEFFNSQFPEHMRSIANSLFPLSFAAANYLSSLLVTTVHKVSGTKDHPDWLNKDLDRGKLDYFYYLIAVLGVVNLVYFWYCAHRYQYKAGSQIEDFNEEKSLLDIEPNQRHDQSPS | Function: Low-affinity proton-dependent nitrate transporter. Not involved in dipeptides transport. Involved in delivering nitrate for seed development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64930
Sequence Length: 576
Subcellular Location: Cell membrane
|
Q9LQL2 | MSCLEIYNKDTMKKKEGEEETRDGTVDYYGRPSIRSNSGQWVAGIVILLNQGLATLAFFGVGVNLVLFLTRVLQQNNADAANNVSKWTGTVYIFSLVGAFLSDSYWGRYKTCAIFQVIFVIGLSSLSLSSYMFLIRPRGCGDEVTPCGSHSMMEITMFYFSIYLIALGYGGYQPNIATLGADQFDEEHPKEGYSKIAFFSYFYLALNLGSLFSNTILGYFEDEGMWALGFWASTGSAIIGLILFLVGTPRYRYFKPTGNPLSRFCQVLVAATKKSSVEAPLRGREEMYDGDSEGKNASVNTGRRIVHTDEFKFLDKAAYITARDLDDKKQDSVNPWRLCPVTQVEEVKCILRLMPIWLCTIIYSVVFTQMASLFVEQGAAMNTSVSDFKIPPASMSSFDILSVALFIFLYRRVLEPVANRFKKNGSKGITELHRMGIGLVIAVIAMIAAGIVECYRLKYADKSCTHCDGSSSLSIFWQAPQYSLIGASEVFMYVGQLEFFNAQTPDGLKSFGSALCMMSMSMGNFVSSLLVTMVVKISTEDHMPGWIPRNLNKGHLDRFYFLLAALTSIDLVVYIACAKWYKPIQLEGKDEMQDMSDDDYDTESEEEREKDSKV | Function: Low-affinity proton-dependent bidirectional nitrate transporter. Involved in nitrate loading into xylem and not in nitrate uptake. Not involved in histidine or dipeptides transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68699
Sequence Length: 614
Subcellular Location: Cell membrane
|
Q9SX20 | MEEQSKNKISEEEKQLHGRPNRPKGGLITMPFIFANEICEKLAVVGFHANMISYLTTQLHLPLTKAANTLTNFAGTSSLTPLLGAFIADSFAGRFWTITFASIIYQIGMTLLTISAIIPTLRPPPCKGEEVCVVADTAQLSILYVALLLGALGSGGIRPCVVAFGADQFDESDPNQTTKTWNYFNWYYFCMGAAVLLAVTVLVWIQDNVGWGLGLGIPTVAMFLSVIAFVGGFQLYRHLVPAGSPFTRLIQVGVAAFRKRKLRMVSDPSLLYFNDEIDAPISLGGKLTHTKHMSFLDKAAIVTEEDNLKPGQIPNHWRLSTVHRVEELKSVIRMGPIGASGILLITAYAQQGTFSLQQAKTMNRHLTNSFQIPAGSMSVFTTVAMLTTIIFYDRVFVKVARKFTGLERGITFLHRMGIGFVISIIATLVAGFVEVKRKSVAIEHGLLDKPHTIVPISFLWLIPQYGLHGVAEAFMSIGHLEFFYDQAPESMRSTATALFWMAISIGNYVSTLLVTLVHKFSAKPDGSNWLPDNNLNRGRLEYFYWLITVLQAVNLVYYLWCAKIYTYKPVQVHHSKEDSSPVKEELQLSNRSLVDE | Function: May act as an efflux-type nitrite transporter. Not regulated by the PII protein involved in the regulation of nitrite uptake into higher plant chloroplasts.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66213
Sequence Length: 596
Subcellular Location: Membrane
|
Q9XWL9 | MKSISQCLGNVSLWIEQQTHDMFYWVGLKIADYPKWTLFITTIWALLMAGGVVRFKEVNNVRDHFSATNSPSRYEYRVAREFFQELGSPFHVVVAMQAADGGSLLRPKYIDKALEIEDFLQYKLKGSFGNQSYSYSDFCGTQCETSDAVSIFLSMFRDQQIKKTAHVKLTYPSMDVFGHRVYLANNIFQVKINNRSSIIEESKLVAINFHAIYNNETMYEIMKEWEQKLFAYTLSTENDPLIRVYVTSEGLVSEEVRRTGILAMPLMGVTFLIILAFTILTTLKRDPVKSKPFEAFLGVICPILSLCASFGHLFWMGFEYLPIVTVVPFLILSIGVDDVFIFIHAWHRTPYKHSVRDRMAETLADAGPSISITSLTNLLSFAIGIFTPTPAIYTFCVFISTAVIYDYIYQIFFFSAVLVLSGEREEQRKNAYLWWKDVPLPEEPTGKQKKETIVSRVLGKVLDFWVDFIMAKWSKFLIGAIMITYWIFMARGVMEIAVGLSSEKLFLDDSPLLPLVRLQTNVIFKEGGQVAVFVNNPGNMSEPDAVPEIMRILRRFEVANNSVGAASTHMWLLPYLPYVGEQEHGSIEFKYRYLPEFFKLTEFRRWSHFVNLGNHQDCLSEKPSCLQKFVFSTGFHDAVSWSDRLALLENWREMASEYQHLNLTIYEDFSMYSDQLLTIVPVTQSTVFCALICMIMILTLFTPSPVTIVTSTAAVLSINLGVFGCLVYMNIDLDPISMTTLLMAIGFSVDFVAHITWHYYKGDFHSKRARIRHALAGIAWPMFQAGTSTMLAITVLALVHAYMVQVFVKVVVLVIFLGMFHGLVVLPIVFSALPFTKTSGPQKKKVAPLQMHEAGPIPKKEEPKVIKVNGEEDEEDEKTTKEEPVEKSVRSAERA | Function: Transporter, which promotes the endocytosis-mediated degradation of hedgehog-related proteins such as grl-7 in order to establish the capacity of progenitor cells to maintain quiescence in arrested L1 stage larvae.
PTM: Degraded in a lysosome-dependent manner before hatching.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101874
Sequence Length: 895
Subcellular Location: Apical cell membrane
|
Q8H157 | MEVEEEVSRWEGYADWRNRAAVKGRHGGMLAASFVLVVEILENLAYLANASNLVLYLREYMHMSPSKSANDVTNFMGTAFLLALLGGFLSDAFFSTFQIFLISASIEFLGLIILTIQARTPSLMPPSCDSPTCEEVSGSKAAMLFVGLYLVALGVGGIKGSLASHGAEQFDESTPKGRKQRSTFFNYFVFCLACGALVAVTFVVWLEDNKGWEWGFGVSTIAIFVSILIFLSGSRFYRNKIPCGSPLTTILKVLLAASVKCCSSGSSSNAVASMSVSPSNHCVSKGKKEVESQGELEKPRQEEALPPRAQLTNSLKVLNGAADEKPVHRLLECTVQQVEDVKIVLKMLPIFACTIMLNCCLAQLSTFSVQQAASMNTKIGSLKIPPASLPIFPVVFIMILAPIYDHLIIPFARKATKTETGVTHLQRIGVGLVLSILAMAVAALVEIKRKGVAKDSGLLDSKETLPVTFLWIALQYLFLGSADLFTLAGLLEYFFTEAPSSMRSLATSLSWASLAMGYYLSSVIVSIVNSITGSSGNTPWLRGKSINRYKLDYFYWLMCVLSAANFLHYLFWAMRYKYRSTGSRS | Function: Low-affinity proton-dependent nitrate transporter. Involved in constitutive nitrate uptake. Not involved in histidine or dipeptides transport. Involved in (+)-abscisic acid (ABA) transport, but not in gibberellin, indole-3-acetic acid or jasmonic acid import. Mediates cellular ABA uptake. Nitrate does not compete with abscisic acid as a substrate of NPF4.6 .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63982
Sequence Length: 585
Subcellular Location: Cell membrane
|
Q9M390 | MEEKDVYTQDGTVDIHKNPANKEKTGNWKACRFILGNECCERLAYYGMGTNLVNYLESRLNQGNATAANNVTNWSGTCYITPLIGAFIADAYLGRYWTIATFVFIYVSGMTLLTLSASVPGLKPGNCNADTCHPNSSQTAVFFVALYMIALGTGGIKPCVSSFGADQFDENDENEKIKKSSFFNWFYFSINVGALIAATVLVWIQMNVGWGWGFGVPTVAMVIAVCFFFFGSRFYRLQRPGGSPLTRIFQVIVAAFRKISVKVPEDKSLLFETADDESNIKGSRKLVHTDNLKFFDKAAVESQSDSIKDGEVNPWRLCSVTQVEELKSIITLLPVWATGIVFATVYSQMSTMFVLQGNTMDQHMGKNFEIPSASLSLFDTVSVLFWTPVYDQFIIPLARKFTRNERGFTQLQRMGIGLVVSIFAMITAGVLEVVRLDYVKTHNAYDQKQIHMSIFWQIPQYLLIGCAEVFTFIGQLEFFYDQAPDAMRSLCSALSLTTVALGNYLSTVLVTVVMKITKKNGKPGWIPDNLNRGHLDYFFYLLATLSFLNFLVYLWISKRYKYKKAVGRAH | Function: Peptide transporter. Mediates the transport of di- and tripeptides. High affinity transporter with low selectivity. No transport of amino acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64034
Sequence Length: 570
Subcellular Location: Cell membrane
|
Q01782 | MTAPTVPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNARRPNSAITVQADLSNVATAPVSGADGSAPVTLFTRCAELVAACYTHWGRCDVLVNNASSFYPTPLLRNDEDGHEPCVGDREAMETATADLFGSNAIAPYFLIKAFAHRFAGTPAKHRGTNYSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGVGPGLSVLVDDMPPAVWEGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYITGTCVKVDGGYSLTRA | Function: Exhibits a NADPH-dependent biopterin reductase activity. Has good activity with folate and significant activity with dihydrofolate and dihydrobiopterin, but not with quinonoid dihydrobiopterin. Confers resistance to methotrexate (MTX).
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = 2 H(+) + L-erythro-biopterin + 2 NADPH
Sequence Mass (Da): 30457
Sequence Length: 288
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from biopterin: step 1/1.
EC: 1.5.1.33
|
Q803C9 | MATTFRSQTLSKDDVNYRMHFRMINEQQVEDITIQFFYKPHTISLLTVTVLSLMYFAFTRDDGDPDSNLRVGLILLVSFFLVISVLAFPNGPFTRPHPAIWRIVFGLSVLYFLFLVFIIFLNWDQVKALMFWLDPNLRYAKREADVMEYAVNCHVITWERILSHFDIFAFSHFWGWGMKALLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMTVCRFLEMRTYHWASIKDIHSTTGKIKRAVLQFTPASWTYVRWLDPKSSLQRVMGVYLFMIIWQLTELNTFFLKHIFVFPACHALSWCRILFIGIITAPTVRQYYAYLTDTQCKRVGTQCWVFGAIAFLEALACIKFGQDLFSKTQILYVILWLVCLAFITFLCLYVMVWYAENYGPRQKSFSECEDSIYSEAGDSVTECKGEFEIDSTTSCSTRKRRDSGDSRTINGMEK | Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine (By similarity). Catalyzes mainly the conversion of phosphatidylcholine but also converts, in vitro and to a lesser extent, phosphatidylethanolamine (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54418
Sequence Length: 465
Pathway: Phospholipid metabolism; phosphatidylserine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.29
|
P48651 | MASCVGSRTLSKDDVNYKMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTRDDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLFLNFEQVKSLMYWLDPNLRYATREADVMEYAVNCHVITWERIISHFDIFAFGHFWGWAMKALLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFLEMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLTELNTFFLKHIFVFQASHPLSWGRILFIGGITAPTVRQYYAYLTDTQCKRVGTQCWVFGVIGFLEAIVCIKFGQDLFSKTQILYVVLWLLCVAFTTFLCLYGMIWYAEHYGHREKTYSECEDGTYSPEISWHHRKGTKGSEDSPPKHAGNNESHSSRRRNRHSKSKVTNGVGKK | Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine . Catalyzes mainly the conversion of phosphatidylcholine . Also converts, in vitro and to a lesser extent, phosphatidylethanolamine .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55528
Sequence Length: 473
Pathway: Phospholipid metabolism; phosphatidylserine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.29
|
O08888 | MRRAERRVAGGSGSGSPLLEGRRSTESEVYDDGTNTFFWRAHTLTVLFILTCSLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPRLGVPLPERDYGGNCLIYDADNKTDPFHNIWDKLDGFVPAHFIGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLICNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSWVRFEWKPASSLHRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGVAMREIYDFMDELKPHRKLGQQAWLVAAITVTELLIVVKYDPHTLTLSLPFYISQCWTLGSILVLTWTVWRFFLRDITMRYKETRRQKQQSHQGRAINNGDGHPGPDDDLLGTGTAEEEGSTNDSVPAEKEGASAAS | Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine . Catalyzes the conversion of phosphatatidylethanolamine and does not act on phosphatidylcholine . Shows a substrate specificity for phosphatatidylethanolamine and does not act on phosphatidylcholine (By similarity). Can utilize both phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate and the latter is six times better utilized, indicating the importance of an ester linkage at the sn-1 position (By similarity). Although it shows no sn-1 fatty acyl preference, exhibits significant preference towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at the sn-2 position (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55005
Sequence Length: 474
Pathway: Phospholipid metabolism; phosphatidylserine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.29
|
E7EY42 | MAKGEWKRSGADDLPLPGRSECEVFDDGTNTFFWRAHTVTVLFILTCALVYVTLLEETPHDTAYNTKRGIVASILVFLCFGVTQAKDGPFTRPHPAYWRFWLCVSVVYELFLIFILFQTVHDGRQFMKYIDPKLGVPLPERGYGGNCLIYDPGHPTDPFHNIWDKMDGFVPAHFLGWYIKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLVCNGLGIYCGMKTLGWLSMKPYQWQGLWNIPTYKGKIKRIAFQFTPYSWVKFEWRPASNLRRWLAVLGIIFMFLLAELNTFYLKFVMWMPPEHYLVLFRLVFFVNVGGVAMREIYDFMDDPKFHKKLGQQAWIVAAITVTEFLIVVKYDPNTIMLPIPFFITQCWILGIALILVWTLWRFFIRDITLRYKETRRRRQEVSSERDGSSSAPSGRSKLNGSMDSVRHRKS | Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine (By similarity). Catalyzes the conversion of phosphatatidylethanolamine and does not act on phosphatidylcholine (By similarity). Can utilize both phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate and the latter is six times better utilized, indicating the importance of an ester linkage at the sn-1 position (By similarity). Although it shows no sn-1 fatty acyl preference, exhibits significant preference towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at the sn-2 position (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53229
Sequence Length: 452
Pathway: Phospholipid metabolism; phosphatidylserine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.29
|
Q9Z1X2 | MRRGERRVAGGSGSESPLLKGRRSTESEVYDDGTNTFFWRAHTLTVLFILTCALGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPRLGVPLPERDYGGNCLIYDADNKTDPFHNIWDKLDGFVPAHFIGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLVCNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSWVRFEWKPASSLHRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGVAMREIYDFMDELKPHRKLGQQAWLVAAITVTELLIVVKYDPHTLTLSLPFYISQCWTLGSILVLTWTVWRFFLRDITMRYKETRRQKQQSHQARAVNNRDGHPGPDDDLLGTGTAEEEGTTNDGVTAEEGTSAAS | Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine . Catalyzes the conversion of phosphatatidylethanolamine and does not act on phosphatidylcholine . Can utilize both phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate and the latter is six times better utilized, indicating the importance of an ester linkage at the sn-1 position . Although it shows no sn-1 fatty acyl preference, exhibits significant preference towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at the sn-2 position .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55021
Sequence Length: 473
Pathway: Phospholipid metabolism; phosphatidylserine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.29
|
Q08D11 | MLRSDVRRVAAGRKASLDGLYCEELEVRGNRNLGNKFSHRGELRSSTESEVFDDGTNTFFWRAHTLTVLFILTCSLGYVTLLEETPQDTAYNAKRGIIASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVHDGRQFMKFIDPKLGVPLPERDYGGNCLIYDPGNKTDPYHNLWDKMDGFVPAHFLGWYIKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLVCNGFGIYCGMKTLEWLSMKPYKWQGLWNIPTYRGKMKRIAFQFTPYSWVKFEWKPASSLRRWLAVCGIIFVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGVAMREIYDFMDDLKFHKKLGQQAWMVAAITVTEFLIVVKYDPYTITLPLPFYVTQCWILGIVLVLTWTVWRFFIRDITLRYKEIRQQKQHRNEEEKSHRNGDVNSEKDTNKHKKH | Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine (By similarity). Catalyzes the conversion of phosphatatidylethanolamine and does not act on phosphatidylcholine (By similarity). Can utilize both phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate and the latter is six times better utilized, indicating the importance of an ester linkage at the sn-1 position (By similarity). Although it shows no sn-1 fatty acyl preference, exhibits significant preference towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at the sn-2 position (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56214
Sequence Length: 474
Pathway: Phospholipid metabolism; phosphatidylserine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.29
|
Q9VPD3 | MKKRTNSRGTPTSSGDALLDTSFSSAGDAERDHPAYKSGAASAPATPTKRRDGSDGSVSSAGARRKRKDEIAQTFVIVNERPVDDISLDFFYKPHTITLLAVSVLAVMYFAFVRNEANVDENLWAGLLCIVFFFLIVSVIAFPNGPFTRPHPAVWRILFGCSVLYLLTLQFLMFQNYPTIRSIFYWIDPKLKNFHIDMEKEYGVNCSDISWDRVKGHLDVFAWGHFLGWAFKAILIRHMGILWAISVMWEITEITFAHLLPNFIECWWDALILDVIICNGLGIWMGLKICQILEMREYKWASIKDISTTTGKIKRAMLQFTPESWSAIRWLDPKSTAMRFAAVIQLVIFWQVTELNTFFLKHIFEMPPDHFIVIGRLIFIGLFVAPSVRQYYVYVTDTRCKRVGTQCWVYGAIMVSEAILCIKNGKELFERTQAINIVLWLTVQVIISVAFVYLAVYWQQRQLKKVSSTPAKTKETIPASSSSPSKGKLSPQKEKKLK | Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56835
Sequence Length: 498
Pathway: Phospholipid metabolism; phosphatidylserine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.29
|
Q9LFY0 | MVSINSGPISSFVSRYSMIDSDTLLHLSSFGSTFNPNYKAKACIRFARKVCGSTVLGFLEVKPRKKSCCSRCNGVSRMCNKRNLGWDSEGSKDLETEILEFMKNSEKPGMFPSKKDLIRSGRFDLVERIVNQGGWLSMGWDLDEQEEKVRVNENVTPQDLHIEKQLPNCNSPEMDKTLNHGDLDLSSNLSSSTEQVESRNDSGIEGILTRLEKERNLSLGISVRENGKSNGAMHDISPNGSVPWSSRIVTASEIQEVDGSRGSGEYAQSRYQGAKSVSGKPGLSDSPTSETWRTWSMRRAGFTDEDFEAAEISSSGLTGVKKDDTKKDSGDSMNGKDRIASSSEDVNKTHIKHRLQQLQSELSSVLHSLRSPPDKVVTSKDSETTAGNLENLSDDWEYKENEIIHAQNKLRSTRAKLAVLEGKMAMAIIDAQRIVREKQRRIDHASRALRLLRTASIVWPNSASEVLLTGSFDGWSTQRKMKKAENGVFSLSLKLYPGKYEIKFIVDGQWKVDPLRPIVTSGGYENNLLIIS | Function: Involved in starch granule initiation in leaf chloroplasts. Binds and delivers suitable maltooligosaccharide substrates to starch synthase 4 (SS4).
Sequence Mass (Da): 59199
Sequence Length: 532
Domain: Contains a C-terminal (456-532) carbohydrate-binding domain (CBM).
Subcellular Location: Plastid
|
F4KFB3 | MATISQIPFSISFPCFEFRKPSFYYHQPQLFVSYLNSTKKHSFICFACSTKQTRVRKRVKSNEELRSEIMQFVALAGLPEGHVPSMKELSAHGRVDLANIVRRRGYKFIKELVANSGMEEDCNELVADSEDNNTNIETGGSRACLEDSSTDLSKEAEKQGSLSKDESSLAGVLSLENSFSNLGDSNHSGEITEKIFKIESVELNEIADIENSSSEASVFANHSQDLYDTSSCPDIEAGNVSMTEDEEVNDVDKDFSLTFDHYTSPTSNHYTSPDLNSIKHVDIATGSSYDLTSENTMTNVENFQNQQIDDIAANRSGSADDSLVESEDNDWMSGLSSCTSSIEEKTTRFIQNGYLDTVGADENDIPNESCPEESSETTKGGEYIGDSLGGPRIMSTPLNGSALALKEIIHATEVNSSDRNSDQRDGSVGLDTDPHHETRKRENQVEIDRLRFMLDQKELELSRLKEQIEKEKLSLSVLQRQAETEIQKAQMLISEKEVELQEAEESLSGLQEVVIEYCGDGNAVEVTGSFNGWQHRVGMELQASKSIGKQKCWSTLLWLYPGTYEIKFIVDGQWITDPQKDSVTRGHISNNILKVDSQ | Function: Involved in starch granule initiation in leaf chloroplasts.
Sequence Mass (Da): 66571
Sequence Length: 598
Domain: Contains a C-terminal (513-598) carbohydrate-binding domain (CBM).
Subcellular Location: Plastid
|
Q94AX2 | MGCVPRIEFGCSSQSLTLSWNLRAWNLCRLNTISHFQKLPYPLVASTRKHYKNSLLLKRFLVGVGTEESSLSEDLLDESLSRPLTSDELKSLLIDTERSKLVKKLSEANQQNRFLKRQLKTQEHEITNIKTELALMELEVQALVKLAEEIANLGIPQGSRKISGKYIQSHLLSRLDAVQKKMKEQIKGVEAAQSKEVHVFWIGMAESVQVMGSFDGWSQREDLSPEYSALFTKFSTTLFLRPGRYEMKFLVDGEWQISPEFPTSGEGLMENNVLVVE | Function: Involved in targeting GBSS1 to the starch granule . Was originally thought to be a carbohydrate-binding scaffold protein, but it has been shown that it is mainly found as a soluble protein and that interaction with GBSS1 is a pre-requisite for subsequent starch granule binding . Dissociation from starch as a function of pH, Mg(2+) concentration or redox state is not observed . Interacts primarily with amylopectin and is required for amylose synthesis .
Sequence Mass (Da): 31524
Sequence Length: 277
Domain: Contains a C-terminal (199-277) carbohydrate-binding domain (CBM).
Subcellular Location: Plastid
|
P39794 | MGELNKSARQIVEAVGGAENIAAATHCVTRLRFALIDESKVDQEMLDQIDVVKGSFSTNGQFQVVIGQGTVNKVYAELVKETGIGESTKDEVKKASEKNMNPLQRAVKTLADIFIPILPAIVTAGLLMGINNILTAEGIFFSTKSIVQVYPQWADLANMINLIAGTAFTFLPALIGWSAVKRFGGNPLLGIVLGVMLVHPDLLNAWGYGAAEQSGEIPVWNLFGLEVQKVGYQGQVLPILLASYMLAKIEVFLTKRTPEGIQLLVVAPITLLLTGFASFIIIGPITFAIGNVLTSGLISVFGSFAALGGLLYGGFYSALVITGMHHTFLAVDLQLIGSKLGGTFLWPMLALSNIAQGSAALAMMFIVKDEKQKGLSLTSGISAYLGITEPAIFGVNLRYRFPFIIAMVSSGLAGMYISSQGVLASSVGVGGVPGIFSIMSQYWGAFAIGMAIVLIVPFAGTYAYARFKHK | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in trehalose transport.
Catalytic Activity: alpha,alpha-trehalose(out) + N(pros)-phospho-L-histidyl-[protein] = alpha,alpha-trehalose 6-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50000
Sequence Length: 470
Domain: The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA-Glc (EIII-Glc) on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-1 domain.
Subcellular Location: Cell membrane
|
P36672 | MMSKINQTDIDRLIELVGGRGNIATVSHCITRLRFVLNQPANARPKEIEQLPMVKGCFTNAGQFQVVIGTNVGDYYQALIASTGQAQVDKEQVKKAARHNMKWHEQLISHFAVIFFPLLPALISGGLILGFRNVIGDLPMSNGQTLAQMYPSLQTIYDFLWLIGEAIFFYLPVGICWSAVKKMGGTPILGIVLGVTLVSPQLMNAYLLGQQLPEVWDFGMFSIAKVGYQAQVIPALLAGLALGVIETRLKRIVPDYLYLVVVPVCSLILAVFLAHALIGPFGRMIGDGVAFAVRHLMTGSFAPIGAALFGFLYAPLVITGVHQTTLAIDLQMIQSMGGTPVWPLIALSNIAQGSAVIGIIISSRKHNEREISVPAAISAWLGVTEPAMYGINLKYRFPMLCAMIGSGLAGLLCGLNGVMANGIGVGGLPGILSIQPSYWQVFALAMAIAIIIPIVLTSFIYQRKYRLGTLDIV | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in trehalose transport at low osmolarity.
Catalytic Activity: alpha,alpha-trehalose(out) + N(pros)-phospho-L-histidyl-[protein] = alpha,alpha-trehalose 6-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51081
Sequence Length: 473
Domain: The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA-Glc (EIII-Glc) on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-1 domain.
Subcellular Location: Cell inner membrane
|
Q3SZY3 | MSTLIYVDKENGEPGIHVAPKDGLKLGSVPSVKALDGRSQVSTPHVGKMFDAPPALPKTARKALGTVNRATEKSVKTNGPLKQKQTTFSTKKITEKTVKAKSSVPASDDTYPEIEKFFPFNPLDFENFDLPEEHQIARLPLSGVPLMILDEERELEQLLHVGPPSPLKMPPLLWESNLLQSPSSILSTLDVELPPVCCDLDI | Function: Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of TP53. The negative regulation of TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation (By similarity).
PTM: Phosphorylated at Ser-165 by CDK1 during mitosis.
Sequence Mass (Da): 22132
Sequence Length: 202
Domain: The N-terminal destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway.
Subcellular Location: Cytoplasm
|
Q9C8B8 | MTNINRLSMSTMFNALHEILNEEPLAIPPPPSRGGYSYFHIRTTEMDLQRMFNFMTGSEDLKDDISVLDTGMLMWMASFLTSDSDYFMVITRNKNGSKSLQKLMRMSDDMDVFFFVAIMRLFIHVMIDKYASYVAIQGMRIFKQDKRELMYDHILRYALFLARDQYGCIALNEIIKELDDPYYRDELMDIVSNNALLLSNDAYGNFVVQHVLKLHDSRCTGNIADKLCGYCVELSFKKYGSYIVERLLEVRDIPMATIVLDLLACKTEMLIRLARSENGNFVVCKLLELTNDILTADLFYSLVNKLRPYRFLLHRFPESKIVAILGSMRVPN | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 38511
Sequence Length: 332
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
|
Q9ZW07 | MIPELGRRPMHRGNEDSSFGDDYEKEIGVLLGEQQRRQVEADELERELNLFRSGSAPPTVDGSVSAAGGLFSGGGGAPFLEFGGVNKGNGFGGDDEEFRKDPAYLSYYYANMKLNPRLPPPLMSREDLRVAQRLKGSNNVLGGVGDRRKVNDNRSLFSMPPGFEGEKTGASASEWDANGLIGLPGLGLGGKQKSFADIFQADMGHGHPVAQQPSRPASRNTFDENVDSNNNLSPSASQGIGAPSPYSYAAVLGSSLSRNGTPDPQAIARVPSPCLTPIGSGRMSSNDKRNTSNQSPFNGVTSGLNESSDLVNALSGLNLSCSVGLDDRSQAEQDVEKVRNYMFGLQGGHNEVNQHEFPNKSDQAHKATGSLRNSQLRGPHGSAYNGGVGLANPYQQLDSPNYCLNNYALNPAVASMMANQLGNNNFAPMYDNVSALGFSGMDSRHHGRGFVSSGQNLSESRNLGRFSNRMMGGGAGLQSHMVDPMYNQYADSLDLLNDPSMDRNFMGGSSYMDMLELQRAYLGAQKSQYGVPYKSGSPNSHSYYGSPTFGSNMSYPGSPLAHHGMPNSLMSPYSPMRRDEVNMRFPSATRNYSGGLMGSWHMDASFDEGFGSSMLEEFKSNKTRGFELSEIAGHVVEFSSDQYGSRFIQQKLETATTDEKNMVYEEIMPQALVLMTDVFGNYVIQKFFEHGLPPQRRELAEKLFDHVLPLSLQMYGCRVIQKAIEVVDLDQKIKMVKELDGHVMRCVRDQNGNHVVQKCIECVPEENIEFIISTFFGHVVTLSTHPYGCRVIQRVLEHCHDPDTQSKVMEEILSTVSMLAQDQYGNYVVQHVLEHGKPDERTVIIKELAGKIVQMSQQKFASNVVEKCLTFGGPEERELLVNEMLGTTDENEPLQAMMKDQFANYVVQKVLETCDDQQRELILTRIKVHLTALKKYTYGKHVVARIEKLVAAGERRMALQSLTQPQMA | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs. Binds the APUM-binding elements (APBEs) in the 3'-UTR mRNA sequence of CLV1, PNH, WUS and FAS2.
Sequence Mass (Da): 106563
Sequence Length: 968
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
|
Q9XI17 | MAHQLRFAAAREPISEEYPAVALPHPRCISVAFPPPRFTPSPSPLTNYSFLAALTPQELEMRLQIAMDVQMISKLDQRKLQTMASLLTSDPDYFLMIARNMNGSKRIQKLLGKTDDVDALFAAAILRRFLHIITDKYASYVVRRGMTVFDKKKKKAMYEHILHYASHIARDKHGNLALNDIITDAYRNKLFDVIAHKALVLSNDAYGNFVIQRVLKLNDLRSKNNIVVSLRGHFVDLSFQKYGSYVVDVLLETKESMVVVVEELMECEGDMLMRLARNEYGNFLVCKALRVTQKEMVRTDLFWGLVHKLKPFHNLLRWSRGKNIASILNSIR | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 38112
Sequence Length: 332
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
|
Q9LXC5 | MADDNGKNPMPNDRGYDTLLTAFNNLKLYANYNHQEPGESGNTNINSNNNHPNPPLLTAFKSLKLYANKNNQEPGESGNTTINRNKNHPNPPLVTAFNNLELYANYNHQEPGESGTTNINNNNPNPPLLTAFDNLRLYANYNHQEPGESSNNNYPNLNVYNVGHISAASFNAPPFTPSSLTQPDDSSSRYSGKPFPPPPLSFVSPGVDKDRNWLSSLLDMMTCAQRFTEFQKYLQDLDTYPTAERESHLFKIGSALTTTKRIFLHLATNQYGSQALRILFRRSPSLDHLLFCAVDTNFFLLMSDKYGRGLIIPAIRAVDKTKKESLYKLTYEYTLHLARLETGCLALNNVLQEIRGIYRDLIFECVANNADWLSFDPYGTHVVQNILILQNPVATTAIAERLRGSFFRLAMERQGSYVVEKCLKSDFARDQVLEEFRGNAKEWVRMTTDKFGNFVVQSALRVMKEKEMRPLLREFVEKLRPHFGKMEIGRGRNTLRVIQEEIVGWINQLPDKSGYVN | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 58776
Sequence Length: 517
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
|
Q9LNI2 | MTHERGYDLASQVLNICNVHHKKLFCHITYRHLLVLSSDDNGCVILKKVITIADDFLKDEFLDLIAQHAHSLSMHDLGISLIQHVLELDFTKKTTQDDKRLHELMAEFDEVLSTSVTADVDKLHKLASKLMLDSDLFFEFVITRRGSLMIQIILGKSEEVDQVILAGVKQRFIDVTTNFYGYRIMIQTIKVFKKRGDLKVYDQILRLIGVHALYLTKDPDMGNKTFQHAINLHHQDCTTFIACGLQSHYIELSFLKHGSKIVEMLIDDRISMVPLVLLMMEIVKCDEDTLVRLATDEYGNNILKKFLALAKEHKEDFFGDLVDKLNPLLDSLRGTLGENIVAIIDSETEMVKDRIVSQGNN | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 41255
Sequence Length: 361
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
|
Q9C552 | MVSVGSKSLPSRRHRTIEEDSLMGERGKSSNNHSERNKGMRRKDHKGNRGFDVDSSKKNQSGGAPNVKPASKKHSEFEHQNQFVRKEIDPETSKYFSEIANLFDSNEVELEERSVICGNALEETRGREYEIATDYIISHVLQTLLEGCELDQLCSFIRNSASVFPAIAMDRSGSHVAESALKSLATHLENPDAYSVIEEALHSICKVIVDNPLDMMCNCYGSHVLRRLLCLCKGVSLDSPELYGAKSSKALAKRLNLKMSQLDDNNLEIPHQGFPGMLTYLLSGLLSCSREDMKYLQVDQYSSLVLQTALRLMLKQDEQLLEIIPLILRCNSTNKKVEGFHIETNVAKEILESMKDNSFSHLVEVILEVAPESLYNEMFNKVFKNSLFELSVDRCANFVIQALISHARDQEQMGIMWEELAPRFKDLLEQGKSGVVASLIAVSQRLQSHENKCCEALVGAVCSTNESRISILPRLLFLDYYFGCRDKSTWEWAPGAKMHVMGCLILQGIFKFSSDHIQPYITSLTSMKAEYITETAKDSSGARVIEAFLASDAATKQKRRLIIKLRGHFGELSLHTSGSFTVEKCFDACNLTLREAIASELLDVKVDLSKTKQGPYLLRKLDIDGYASRPDQWKSRQEAKQSTYNEFCSAFGSNKSNFPKNTFVSDASEDAAQEIEVKNTRKEIDHHPTSGFKRHREKHAKDKDEPFAGEKRSKQKKNKTSEATDKPKLAGSKRPFLSGEMTGKNRHSNKMRI | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 84828
Sequence Length: 753
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Nucleus
|
Q9LRZ3 | MSSKGLKPQKSTKRKDTDSSAKFDSLKSKKPKLVSGEQQQHVKPKFGKPKSAGDKEQSTNLSKKERRVQAKELTEARKKKRKPHYNLEQELVSLWEKMRRRNIGKEDRSKLISEAIRKMKGKVPEIAVSHVSSRVLQTCVKFCSQAEKDVLFTELQPQFLNLASNKYAVHFIQKMLDGASKQQLAACISSLRGHVAPLLRHVFGSLVVEHAYHLGSAAQKQELLAELYSTELQLFKGLTTSNEKTVVDIIAKLGLQKGAVNRHMTAIIQPILEKGIVDHTITHKLLIEYLTIADKTSAADVLQLLTGSLLLRMVHTRDGSRLAMLSIKHGSAKERKKIIKAMKEHVKKMAFDQFGSMVLACIFSIVDDTKLVTKIIVRELEATLKDLVMDKNGRRPLLQLLHPNSSRYLSHDDLAALDLSVPSLCSMDKSETSSKTKDTDGNEIGEETKDEQEDTVAEHSDHEENVTAMGGKKDPLVRRQELLVNSGLAERLIDVCVENAEEFLQSKFGNEVMYEVAIGGSDGILCPSLSEKLCELYEAISSVAAEPKPQESEKDSEHILENFHSSRTIRRLVLNRPGFASILFKKALSGKCRSWAQGHCSKILSAFVETEDVQVREMAKTELQVLVNEGTLKISATKKPE | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 71604
Sequence Length: 641
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Nucleus
|
Q9LK18 | MVQLLFKFLIQVGATFVELSRNEIGNKNLLLLIHHAGSLLLSMFGSFSNYPVQKFLDMLDERCLTLIASEFDSYFENLVKDRVGNYVVQRLIWGFKRTGIDLPHSLTSVLVTRSIHLCKHRYGYQVIEAFDRSTRLA | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 15798
Sequence Length: 137
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
|
Q9FGE7 | MLNLDFTHKTTQATPRLHAVATEFLRVSNDVAELHKLSSKLTSDPYLFVEFVKTIRGFLSVQTALGLSGEIDTVFLQVIKGWFPDLITETFSFLIVVRIINLFNKRANSKVYPDILRRIGNNALYLTRNPLRGICLVEKAINVRDPDCTVFIALKLHSHYVELSFEELGSNIVEKLLSVGESGICGV | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 21009
Sequence Length: 187
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
|
Q9ZW06 | MIPELGRRPMHRGNEDSSFGDDYEKEIGVLLGEQQRRQVEADELERELNLYRSGSAPPTVDGSVSAAGGLFSGGGGAPFLEFGGGNKGNGFGGDDEEFRKDPAYLSYYYANMKLNPRLPPPLMSREDLRVAQRLKGSSNVLGGVGDRRKVNDSQSLFSMPPGFDQRKQHEFEVEKTSASSSEWDANGLIGLPGLGIGGKQKSFADIFQADMGHGHPVTKQPSRPASRNTFDENVDSKNNLSPSASQGIGAPSPYSYAAVLGSSLSRNGTPDPQAIARVPSPCLTPIGSGRVSSNDKRNTSNQSPFNGGLNESSDLVNALSGMNLSGSGGLDERGQAEQDVEKVRNYMFGLQGGHNEVNQHGFPNKSDQAQKATGLLRNSQLRGAQGSTYNDGGGVATQYQHLDSPNYCLNNYGLNPAVASMMANQLGTNNYSPVYENASAASAMGFSGMDSRLHGGGYVSSGQNLSESRNLGRFSNRMMGGGTGLQSHMADPMYHQYADSLDLLNDPSMDVNFMGNSYMNMLELQRAYLGAQKSQYGVPYKSGSPNSHTDYGSPTFGSYPGSPLAHHLLPNSLVSPCSPMRRGEVNMRYPSATRNYAGGVMGSWHMDASLDEGFGSSMLEEFKSNKTRGFELAEIAGHVVEFSSDQYGSRFIQQKLETATSDEKNMVYEEIMPHALALMTDVFGNYVIQKFFEHGLPPQRRELADKLFDNVLPLSLQMYGCRVIQKAIEVVDLDQKIKMVKELDGHVMRCVRDQNGNHVVQKCIECVPEENIEFIISTFFGNVVTLSTHPYGCRVIQRVLEHCHDPDTQSKVMDEIMSTISMLAQDQYGNYVIQHVLEHGKPDERTVIIKELAGKIVQMSQQKFASNVVEKCLTFGGPEEREFLVNEMLGTTDENEPLQAMMKDQFANYVVQKVLETCDDQQRELILGRIKVHLNALKKYTYGKHIVARVEKLVAAGERRMALQSLTQPQMA | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs. Binds the APUM-binding elements (APBEs) in the 3'-UTR mRNA sequence of CLV1, PNH, WUS and FAS2.
Sequence Mass (Da): 106655
Sequence Length: 972
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
|
B8FP03 | MGYSYRQAGVDIDAGNQAVELMKPAVKRTVRPEVMGGLGGFGGLFALDLKKYPEPVLVSGTDGVGTKLKLAFQMNRHDTIGQDAVAMCVNDILVQGAEPLFFLDYLAVGKLVPERVAQVVGGIAKGCELAGCALIGGETAEMPGFYDEGEYDIAGFAVGAVNRPDLIDGSQIQAGDVLIGLPSSGFHSNGYSLVRKIFTPDLWEKNYPELGETLGEALIRPTRIYVKTVLPLIESRKVLGMAHITGGGLTENIPRILPEGLGIKIARSAWQVPALFTLLQRLGEVEEAEMLRTFNMGIGFVLIVHPEDVDFIQTQLQAAGEKCFVLGEVSGQSEGVSYL | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 36329
Sequence Length: 339
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
|
A8LNB8 | MTTDTPPPKPGLTYAEAGVDIDAGNTLVDRIKPAAKATSRPGVMSGLGGFGALFDLRAAGYADPVLVAATDGVGTKLRIAIDTGHVDTIGIDLVAMCVNDLVCQGAEPLLFLDYFATGKLDVAEAATIVEGIARGCATSGCALIGGETAEMPGMYAKGDFDLAGFAVGAMERGGALPANVAAGDMILGLASDGVHSNGYSLVRRIVERSGLGWGDPAPFEGRTLGAALLTPTRLYVQPALAAIRAGGVHGLAHVTGGGLTENLPRVLPEGLGIEINLGAWELPPVFRWLAAEGGLDEAELLKTFNAGIGMALIVAPDRAEALADLLAGAGERVAVIGHVTEGAGAVHYRGTLL | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 35828
Sequence Length: 353
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
|
Q8EDI8 | MSTPTPLSYKDAGVDIDAGNALVNNIKAAVKRTRRPEVMGNLGGFGALCELPTKYKQPVLVSGTDGVGTKLRLAIDYKKHDTVGIDLVAMCVNDLIVQGAEPLFFLDYYATGKLDVETATAVVNGIGEGCFQSGCALIGGETAEMPGMYEGEDYDLAGFCVGVVEKADIIDGSKVAAGDALIALASSGPHSNGYSLVRKVLEVSQADPQQDLNGKPLIQHLLEPTKIYVKSLLKLIEASDVHAMAHITGGGFWENIPRVLPENCKAVIQGDSWQWPAVFSWLMENGNIAEYEMYRTFNCGVGMIVALPADKVDAALALLAAEGEQAWLIGAIAAREGNEEQVEIL | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 36761
Sequence Length: 345
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
|
Q5E4Q3 | MSLSDQVLAVNDDLPIRTDKPVHSGKVRSVYWLTEEDSRRLIKEKGYNVAPDAPLAIMVISDRISAFDCIWHGEGDLKGIPGKGAALNAISNHWFQLFKDNGLADSHILDIPHPFVWIVQKAKPVMIEAICRQYITGSMWRAYTQGEREFCGITLPERLEKDEQLAELLLTPSTKGILKGIDGVPEVDDVNITRKNIEDNYDKFNFSCIEDIATYEKLLKEGFAVIAKALNKIDQIFVDTKFEFGYVEDAQGNEKLIYMDEVGTPDSSRIWDTKAYRSGHIIENSKEGFRQFLLNHFPEPDILLNKNRMEERFALAEENALPLEAMMDLSKTYLDIAAKITGAPITLSDNPKAEIIKVLKEEYQLVD | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 41599
Sequence Length: 367
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
|
O67881 | MKKVRKLYEGKAKIVYETDEKDKLILEFKDVATAFDGVKKEEIKGKGSLNNEISSLIFEILEDHGIKTHYIKKLSDREMLVWRAERFPVEVVVRNYAAGSFVKRYGVKEGTKLEQPLVEFFMKSDELHDPMVCINHIKVLKLAPAELVPEMEKIALKVNEILKKIFEEKGILLVDFKLEFGRLPSGELAIVDEISPDSMRLWDKSTGENWIKTDSV | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 24872
Sequence Length: 216
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.