ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q1L6Q1 | MVSKLPQEFRRYLRNRNQLQHVLEETQQALELINLENFFPEENVVEELLSPLTLNRITHILANSPAIIILGQDSKAKAIVVNTLISNDILPVCNGLWRWIRLTYGQTNHISLTLDLEYELVENLQANEKPWSTLPIEDLTKSDNEDITYPTVLEVQLNLPILKDGVQIFIAPNNGAVKVLANEFLSILPIFLYALGEQPLTEQNLEELRDLKETYPFNPVLFISSLENISLNGIDPELTESEQHRLQNRLYTNDSTSSKTDDDSIDFDRMNSLGLSWLDQLTNLGFLGMKESVEVDQLSWLGSGQYISDFVGSCRKTDQI... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 110428
Sequence Length: 969
Subcellular Location: Cytoplasm
EC: 2.7.12.1
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Q4VSN4 | MEGDAPQRVSERVSGPGPGGGGGGMIRELCRGFGRHRRYLGQLRQNLRETQKFFRDIKCSHSHSCPSSPAGGGAAELGPAGDVAEAPLPAGQLSCIAFPPKEEKYLQQIVDCLPCILILGQDCNVKCQLLNLLLGVQVLPTTRLGSEENCKLRRLRFTYGTQTRVSLALPGQYELVHTLVAHQGNWDTIPEEDLEVQEDSEDAAHVLAELEVTMHHALLQDVDIVVAPCQGLRPAVDVLGDLVNDFLPVITYALHKDELSERDEQELQEIRKYFSFPIFFFKVPKLGSEIIASSTRRTENERSPLHHQLMDLGYLSSSHC... | Function: Acts as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. Involved in the regulation of both caspase-dependent apoptosis and caspase-independent cell death. In the skin, it plays a predominant role in suppressing caspase-dependent apoptosis in response to ... |
Q6XUX0 | MEGEGAPSWRGGPGGLIRELCRSFGHYNRHLARLQHNLRETKKFFRDVKYSQGNLFASGAAIGEGSPSGAGGGGTRDGGQNFISFPRHEEEHLQQTVSWHPCLLILGQNCNAKCQLLNILLGEKLLPTTKISSEENCKRRRIRFTHGTQTRVSLALPEQYELVHMMAAHRGHWDTIPEEDLEIRGDSEDPAHRIAELEVVLPYSLLKEVDVVVAPCRGFQSAEATLEEYMNQVLLIVIFAISEAELSSSDENELREIKEKFSLPIFFFKVPESGVELISPKKTDNEKSSLYCQLMDLEYLSTNHCSCGAPSPDAVAQSML... | Function: May act as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 105410
S... |
Q6XUX3 | MEGDGVPWGSEPVSGPGPGGGGMIRELCRGFGRYRRYLGRLRQNLRETQKFFRDIKCSHNHTCLSSLTGGGGAERGPAGDVAETGLQAGQLSCISFPPKEEKYLQQIVDCLPCILILGQDCNVKCQLLNLLLGVQVLPTTKLGSEESCKLRRLRFTYGTQTRVSLALPGQYELVHTLVAHQGNWETIPEEDLEVQENNEDAAHVLAELEVTMHHALLQEVDVVVAPCQGLRPTVDVLGDLVNDFLPVITYALHKDELSERDEQELQEIRKYFSFPVFFFKVPKLGSEIIDSSTRRMESERSPLYRQLIDLGYLSSSHWNC... | Function: Acts as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation . Involved in the regulation of both caspase-dependent apoptosis and caspase-independent cell death . In the skin, it plays a predominant role in suppressing caspase-dependent apoptosis in response t... |
A2CI35 | MSSRRLGSSRARGRDLAHEVKHFGGLTKHLKKIIFDSNNCLTELKTSDHFEEEVISTLVLPPVADEIVGKVTKNPPALVIFGQTYTSKATLVNKIFREDLFQIVDDSDNNKTWRAVHLKYGSQRNTRLTLTNSFELLNEEPGSPVMRNSWTGIPRVEMLVKEEHQKDACMLSATTEATLNHPLLQCKLQILVTPHNCPGISISQAYNVCTHNVLPVLLYCFDKDQLSEENLRDLQELQNCAGTLPILFVDCREPSEPLVAHRERRLVEDAHEDFDDDSAYDTDERIEGERERHNGLDARLRRRCRPTPNDRPSVIDQLSR... | Function: May act as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death. May play a role in the embryonic development.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-... |
A1WZE9 | MHRRIEARIVDARLGSEIPLPDYATDGSAAIDLRACLDEPLALEPGQRRLIGTGLAVNIHDPGLVGVVASRSGLSLKHGLRVAQGIGVIDSDYHGEIGVILAHDGTEPYTITPGERIAQLLFQPVVQVTLDYVSAFSATTERGEGGFGHSGTL | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 16161
Seq... |
B0R858 | MYERGAFVADHVEPVADDQIQPNGVDLTVDAVLEQTEPGRIDTDGKTIGDRSPVTPTADEDSTDTTVTIQPGTYILQYAETITIPENHVGFVYPRSSLMRNSCMLHSAVWDAGYTGRGEGLFEVHHEITIARGARVAQLVLATGDHENTYDGSYQHERTDTRPGE | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 18118
Seq... |
P16824 | MLTMLTDRIDSQLVLSRLPRSRFQRFWETPTLIMKEESASSSGSIILAEKSVNMRYCVRFASDSDFQTTFTLPQSTEEKYDKEQHPGEDEASSPLPSPLKVPYKWMPSSFIVKQCHTQLAFYNKHIIWLSRERKVPTSLGVSLYIPEGFFGITFYKCLDAQFVCMPELLESRLQVPQLDVVNLNDTFQSIFPGTIEGDIGVFPCFVPEPWQLMNLPPPNEHRFFSLRTRQTLVIGPGHTQTVYFDAAYVHAPGICALIVGVRQFSQSDLIIRPTIWLPGTAAGVTVVNTSHTTVCISPHTTVAKAVFTTHRFTYLPVGSH... | Function: Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP to avoid uracil incorporation into viral DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 43575
Sequence Length: 388
Pathw... |
Q7VJU0 | MMKHMHIKIKKLHSHAVIPSYQTPQAAGFDLHAVEDSLIKARDRGLVGTGLAFEIESGFEVQVRPRSGLALHNGVSVLNTPGTIDSDYRGEIKVILINHSNEDFHIHRGDRIAQAVVSEVTQAVFTEVQELGQSVRGERGFGSSGVARKGHYQGKPLA | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 17258
Seq... |
B0TAH2 | MKVQIKRLHPEAMIPERQTKLASGFDLHVLDAVLPENASDPYYDHFEAIRIFPGERILVRTGIAIQMGEGMEAQVRPRSGLALRHGITLLNSPGTVDADYTGDVGVILINLGDKHVDIRKKDRVAQLVFQPVFHQVELEERESLNETERGDGGFGHTGVNSQP | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 18117
Seq... |
P70583 | MPLLCALLRSRLQPSLLRSLTLTSAQSLSCGGSRGVRTWSARTGPGACADPAVSVSKRARAEDDASLRFVRLSEHATAPTRGSARAAGYDLYSAYDYTIPSMEKALVKTDIQIAVPSGCYGRVAPRSGLAVKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILYPDLEEVQTLDNTERGSGGFGSTGKN | Function: Catalyzes the cleavage of 2'-deoxyuridine 5'-triphosphate (dUTP) into 2'-deoxyuridine 5'-monophosphate (dUMP) and inorganic pyrophosphate and through its action efficiently prevents uracil misincorporation into DNA and at the same time provides dUMP, the substrate for de novo thymidylate biosynthesis (By simi... |
Q92SM6 | MHTPENRPALTPGLTLVRLPHGEGLDLPAYETAGAAGMDLRAALPADEPMTIRPGERALVPTGFIFEIPAGHEGQIRPRSGLAFKHGITCLNTPGTVDSDYRGEVKVLLVNLGAEDFAVERGMRIAQMVIAPVTRLAIREAGGATTTARGAGGFGSTGTK | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 16724
Seq... |
C0ZYU5 | MSDHLSIALKRLDPDLPVPQRAHPGDAGVDLCSTSDVTIEPGHRTLVGTGIAIALPVGTVGLIHPRSGLAAKSGLSIVNAPGTVDAGYRGELKVCLINLDPATAIDIRRGDRIAQLVVQRVELPVFEEVESLDDTTRGTGGYGSSGGHAILDTDAPGAVVGEGV | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 16815
Seq... |
P61911 | MTQKITVSIRHLPHGEGLPLPEYQTAHAAGLDLIAAVPQDAPLTLQPGRYVLVPTGLTIALPENYEAQVRPRSGLAAKHGVTVLNAPGTIDADYRGEIGVLLINHGTEPFAIRRGERIAQMVIAPVSRAQFVAVEALPESGRGAGGFGSTGR | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 16001
Seq... |
Q18212 | MEEEQLLDYEEEQEEIQDKQPEVGGGDARKTKGTYASIHSSGFRDFLLKPEILRAIGDCGFEHPSEVQHECIPQAILGMDVVCQAKSGMGKTAVFVITTLQQLEPVDGEVSVVCMCHTRELAFQISKEYERFSKYLPGVKVAVFFGGMAIKKDEERLANDCPHIVVGTPGRMLALARSGKLKLDKVKYFVLDECDKMIGDADMRRDVQEIVKMTPQQKQVMMFSATLPKELRTVCKRFMQDPMEVYVDDEAKLTLHGLQQHYVKLKEAEKNRRLLNLLDALEFNQVVIFVKAVKRCEALHQLLTEQNFPSIAIHRQMAQE... | Function: Required for spliced RNA export out of the nucleus . May play a role in spliceosome assembly.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 48493
Sequence Length: 425
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q27268 | MADNDDLLDYEDEEQTETTAVENQEAPKKDVKGTYVSIHSSGFRDFLLKPEILRAIVDCGFEHPSEVQHECIPQAVLGMDILCQAKSGMGKTAVFVLATLQQLEPSDNNTCHVLVMCHTRELAFQISKEYERFSKYMPTVKVAVFFGGMAIQKDEETLKSGTPHIVVGTPGRILALIRNKKLNLKLLKHFVLDECDKMLEQLDMRRDVQEIFRSTPHGKQVMMFSATLSKDIRPVCKKFMQDPMEVYVDDEAKLTLHGLQQHYVNLKENEKNKKLFELLDVLEFNQVVIFVKSVQRCVALSQLLTEQNFPAIGIHRGMTQ... | Function: Required for mRNA export out of the nucleus. Probable RNA helicase that may regulate entry into mitosis by down-regulating the expression of other genes whose activity may be rate-limiting for entry into mitosis during embryogenesis. Binds to salivary gland chromosomes and modifies position effect variegation... |
Q13838 | MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKLFDLLDVLEFNQVVIFVKSVQRCIALAQLLVEQNFPAIAIHRG... | Function: Involved in nuclear export of spliced and unspliced mRNA. Assembling component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-... |
Q6CPU0 | MTTVSCDKDENKVDQLGESLSQLRISTRKNNKPSQKKGSLVLSCKKFPHVSVNYVVDKTPKLLTDCKEVHNCSYIINDATLLWNEASRKPRLRPEVCTYIKDSKWENKAVKDSFIGIDLTKGYDDYVPLDRNVLNSLVILKEAYQRYEKTLNPEKTTFVSLRHHIIDIIMCPFLDEPLSLLMTVQPDKNILISVDKSKDKPNGIHETRNSFNKKICYTGFALEDLLIESPTEGHILEHELYYSIVHGSLNDEIDLLIQAEMDSINTLTDTYTEIKSSVHFKLGNTYHRRKLLRMWIQTNLLPKSDLLIGFRNSYSNELEQ... | Cofactor: Divalent metal cation.
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA . The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (By simila... |
Q06349 | MSTEQDAVLGLAKDLEGINLLTVPNLERGHQSKLCKEKTTSDSSSSRKPSQQRDNYRKRRPKLICIPYTSFLHTGMHNFLTKPPRDIFHESKEVALFTNGRAYTILRKDLIPNLKESIAELYESSLLEAKKRKVPYLGHDLFANIDEFVPMTISELDSVSPCFSYIENWILDNPGKDFKIGKKFTVVTTRHHIVDLTMHLFNRRNRQTSLIVTYMGAGLLSFCRNVKKDSQMSKEGIYSNDPNMKKICYSGFEFENWVTENSKVADLTGSKCPIFSLVESKLSEEIGLLIRCEMDAFNPVSETNTELKCFAPLSMHNSNH... | Cofactor: Divalent metal cation.
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and sno... |
Q8RY73 | MDSPPKKNPMDDLFGEDSDNDSRSSRSKSSSSGNASSSSSSSSSSSSSSSAAGGDGEGDGGGADSGSASDSGSGSSGGKEEHGDDKVESYRSNDNGESGVYPYEEEEEEEEDEKDLFGSDNEEYTKTPAISTYSIPVLPAGWSNDNHGGRGGMGRGRWSNGRGGPGLLPRPGPYPGRGGNRGGFGGRYQNYQRDERFVSELKLSKSKETLARKQTNFQEPCELTCYSRVEGGEVIYDDQGLRLFKRHIGEEIGADLNQGYDTFIEKKDLGSEGFGDLLGSIRAKNISLDNIHFVTFRNNLNKILGAAYNRHEPWEMGVHK... | Cofactor: Binds 2 magnesium ions.
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA . The NAD-cap is present at the 5'-end of some RNAs and promotes mRNA dec... |
Q753P9 | MVFESELLLQRRLATTALKQPKELGYYSTNVGGELKVMDESNLSYYYLPDADIEKHIDLSAGARKFQDEQAEAEDDTGSLHGLLQTLMEYERRKSKKVNADIIAFRGQVKRLIHCAFGGHATDVDMYVMSFDGQLFIRAARKKLEFPTSPRESWAYLAYYSGYKFERMALLDRPVAETPREVLESRGKQVVRNGPQYKTVVRTGVGEHKLVLGAEVDGIFDFREPTGDNLKHYVELKVAKKVQTLKDATNFEQKLFSVWLQCFLVGINRVIIGFRDEKFVLKSVEEFSTSEIPLLLKSTGLRNACVDAIKWYGALTKWLC... | Cofactor: Divalent metal cation.
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and sno... |
C4Z5K1 | MKNVSILGSTGSIGTQTLDVIRRNADINVVALAAGTRVSDLAEQVREFKPQLVCIGKEELVPELKTLIGDMDVKIVSGDEGLIEAATIESAEIVVTAVVGMMGITPTVEAIKAHKDIALANKETLVCAGHIIMSLAKECNVNIYPVDSEHSAIFQCLNGERRGEIEKILLTASGGPFRGKKRADLENVQLEDALKHPNWAMGRKITIDSSTMVNKGLEVMEAQWLFGVPAEKVQVIVQPQSIIHSMVEFKDGAVMAQLGSPDMRLPIQYALYYPERRKLNTERLDFYELAKITFEKPDMETFKGLKLAYEAAARGGNIPT... | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 41974
Sequence Length: 380
Pathw... |
A9KMX2 | MKIISVLGSTGSIGTQTLEVVRNNKDLKVSALAASSNITLLEEQIREFHPKLVCVYDREKALELKKRVSDLEVTVEAGMDGLIACATEESADIVVSAVVGMIGIKPVMEAILRGKDIAFANKETLVTAGHLIMPLVKKHNVNLLPVDSEHSAIFQCLQGNESSTVSRIILTASGGPFRGKSLAELKNVKVEDALKHPNWSMGRKITIDSATMVNKGLEVMEAHWLFHEPLNKIEVVIQPQSIIHSAVEFEDGGIIAQLGTPDMKLPIQYALYYPEKRRYLPGKRLDFFDIAKITFEKPDISNLPGLRLAYEAMNTGHSVP... | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 42993
Sequence Length: 388
Pathw... |
Q6AEY1 | MSVRRVVILGSTGSIGMQALEVVAANPDRFQVVGLTAGSSAGQLAEQAERFGVRETALGAGDSERLVRSVDADVVLNGITGSVGLGPTLAALESGRTLALANKESLIVGGELVKRAAAPGQLIPVDSEHSALAQALRSGAAGEVSRLVLTASGGPFRGRSRESLRQVTPAEALAHPTWDMGLVVTTNSSTLVNKGLEVIEAHLLFGVPYDRIEVTVHPQSVVHSMVEFVDGSTIAQASPPDMRLPISLGLGWPDRVPGTGLPLDWTRAHTWTFEPLDGEAFPAVALAKCVGVAGGTYPAVFNAANEQAVAAFHAGAIGYL... | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 37611
Sequence Length: 361
Pathw... |
Q72U08 | MTTSVCLLGASGSVGESTLKVLRAYPEKFRLHSFSVHSNLEKAKEIQKEFSPDFICVSSDFADVGVLGNKLGRTQILYGESSLCELVREPEVEIVITAIVGSVGLRPTIAAITAGKRLGIANKETLVTSGPLIQSLIAKHNTKVVPVDSEHNALFQLLESLNPNSVEKIILTASGGAFRDLPVEQLSSVTKEQALHHPTWNMGPKITIDSNGMINKGLEVIEAHFLFNVPYDKIGVVIHPQSIAHGIVELKDGASFLYASYPDMIFPIAHSLFHPEPVPKVLRSYPAKDWGKLEFREPDFKRYPGLGLAFEAGKVGGTAP... | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 42805
Sequence Length: 389
Pathw... |
Q16CP0 | MTDMPKTPLLDLVHRPADMKGLSDRQLVQLADELRSETVSAVSVTGGHLGAGLGVVELTVALHAVFDTPRDKIIWDVGHQCYPHKILTERRDRIRTLRMKGGLSGFTKRSESPYDPFGAAHSSTSISAALGFAVARDLGGVVPEGLGDAIAVIGDGSMSAGMAYEAMNNAGHLKKRMIVILNDNEMSIAPPTGAMSSYLSRLYSGEPFQDFKAAAKGAVSLLPEPFREGAKRAKDMLKGMAVGGTLFEELGFSYIGPIDGHDLDQLLPLLRTVKARATGPIMIHALTKKGKGYAPAETARDKGHATAKFDVLTGQQTKAP... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
Q8CJP7 | MPLLTRITGPRDLDRLSLEELTQLAEEIRTFLVDAVSKTGGHLGPNLGVVELTLALHRVFESPKDKVLWDTGHQSYVHKLLTGRQDFSKLKMKGGLSGYPSQGESEHDVIENSHASTVLGWADGIAKANQVMERDDHVVAVIGDGALTGGMAWEALNNIAAAKDRPLVIVVNDNERSYAPTIGGLANHLATLRTTDGYERFLARTKEVLERTPVVGRPLYDTLHGAKKGLKDFIAPQGMFEDLGLKYVGPIDGHDLEALESALTRAKRFGGPVIVHCLTEKGRGYQPALQDEADRFHAVGKIHPDTGLPISTSGADWTSV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
C1F3C4 | MGNLLNSIHSPADIKHFSVPQLEALAQEIRDRLIQSVARTGGHIGPNLGVVELTIAMHYVFDTPQDRFVFDVSHQAYVHKLLTGRANRFDTLRQPGGLNGFMLRSESQHDSYGAGHAGTALSAALGMAVARDIAGGHEHVVALAGDAAFTNGISFEALNNIADQTRRLIVVLNDNEWSIDRNVGAIARYLHKIVTNEHVSQFHDSAARLLKRIGGPAAANMVRRAEEAAKGMLWPSVLFEEFGLTYYGPIDGHNLSLLIDTFKFLKQQDRPVLLHAITQKGRGFEPALAGQKKFHGLGPFDPETGETSSSGQPTYSEVFA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
P73067 | MHISELTHPNELKGLSIRELEEVSRQIREKHLQTVATSGGHLGPGLGVVELTVALYSTLDLDKDRVIWDVGHQAYPHKMLTGRYHDFHTLRQKDGVAGYLKRSESRFDHFGAGHASTSISAGLGMALARDAKGEDFKVVSIIGDGALTGGMALEAINHAGHLPHTRLMVILNDNEMSISPNVGAISRYLNKVRLSSPMQFLTDNLEEQIKHLPFVGDSLTPEMERVKEGMKRLVVPKVGAVIEELGFKYFGPIDGHSLQELIDTFKQAEKVPGPVFVHVSTTKGKGYDLAEKDQVGYHAQSPFNLSTGKAYPSSKPKPPS... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
Q9X291 | MLLDEIKRMSYDELKRLAEDIRKRITEVVLKNGGHLASNLGTIELTLALYRVFDPREDAIIWDTGHQAYTHKILTGRDDLFHTIRTFGGLSGFVTRRESPLDWFGTGHAGTSIAAGLGFEKAFELLGEKRHVVVVIGDGALTSGMALEALNQLKNLNSKMKIILNDNGMSISPNVGGLAYHLSKLRTSPIYLKGKKVLKKVLEKTEIGFEVEEEMKYLRDSLKGMIQGTNFFESLGLKYFGPFDGHNIELLEKVFKRIRDYDYSSVVHVVTKKGKGFTAAEENPTKYHSASPSGKPKMLSYSELLGHTLSRVAREDKKIV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
B9L1L6 | MYLERIDSPQDLKRLSVPELEKLAEEIREAIIEVVLGKTGGHFAPNLGTVELTLALHYVFDSPRDKIVWDVGHQAYPHKLVTGRRDRFHTIRQEGGLSGFLQREESPHDHFGAGHASTSISAALGMAVAAKLRGDRYHTIAVIGDGALTGGMAYEALNHAGALQVPLIVVLNDNEMSIAPNVGALARYLTRVRTDTRYRQAKVEIERLLRRLPQGERLVELSHRFLDGLKEVVYRTMIWEELGFTYIGPIDGHNLRELIETFQLVKTFDSPVFVHVLTVKGKGYQPAEDDPFKHHSAAVKVPGAPPTPPRYQDVFGQTLV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
O83796 | MDLSLLRSLTGPHDLKSLSPEQVRALAQEVRQEILRVVSANGGHLASNLGVVELTIALHRVFSCPHDVVVWDVGHQCYAHKLLTGRAGRFHTLRQKDGISGFPRRDESPYDAFGTGHSSTALSAASGILSALRYRGKSGKVVAVVGDGALTAGLAFEALLNVGRSCSDLIVILNDNKMSISPNTGSFSRYLSTLTVKGPYQKLKTRLRRALQTVPLVGRPACRALSRLKRSARTLLYQSNIFADFGFEYVGPLNGHHIEDLERVLNDAKKLTRPTLLHVQTVKGKGYPFAEQNPTDFHGVGPFNLAEGIVEKKDALTFTE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
Q08877 | MGNREMEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLHCKGKKFTDFDEVRHEIEAETDRVTGMNKGISSVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFITRENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLPNFRNKLQGQLLSIEHEVEAFKNFKPE... | Function: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 97914
Sequence Length: 8... |
Q8N1N2 | MVADIKGNEQIEKYSWREACDTGSSRMDRKHGKYILNVEHSENQPPITHPNDQEAHSSICWCLPSNDITSDVSPNLTGVCVNPGILAHSRCLQSESCNTQVKEYCRNDWSMWKVFLACLLACVIMTAIGVLIICLVNNKGSANSSIVIQLSTNDGECVTVKPGTPSPACPPTMTTTSTVPASTATESTTSTATAATTSTEPITVAPTDHL | Function: Plays a role in the regulation of cell proliferation. Promotes activation of the AKT1 signaling pathway. Promotes phosphorylation of AKT1 at 'Ser-473'.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22529
Sequence Length: 210
Subcellular Location: Golgi apparatus membrane
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P27619 | MDSLITIVNKLQDAFTSLGVHMQLDLPQIAVVGGQSAGKSSVLENFVGKDFLPRGSGIVTRRPLILQLINGVTEYGEFLHIKGKKFSSFDEIRKEIEDETDRVTGSNKGISNIPINLRVYSPHVLNLTLIDLPGLTKVAIGDQPVDIEQQIKQMIFQFIRKETCLILAVTPANTDLANSDALKLAKEVDPQGVRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGRKDIHQALAAERKFFLSHPSYRHMADRLGTPYLQRVLNQQLTNHIRDTLPGLRDKLQKQMLTLEKEVEEFKHFQPGDASIK... | Function: Microtubule-associated force-producing protein which is involved in the production of microtubule bundles and which is able to bind and hydrolyze GTP. Implicated in endocytic protein sorting.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 97809
Sequence Length: 877
Subcellular Loca... |
K7N5M8 | MPVDLSTTLSWKSATGEAATMLDELQPNILKAHVRDRLTVLFLGFGDAAEARTFLNGLSGLMKSARTHLQEVEAHKLTKAVGTPYLGVGLTAHGYATLGVTAPADPSFTAGAKAAVEKLADPAVTEWEGHYQQTIDAVLLLGDATAGPVRTLRRQVEALRPASVTVVGEESGLGLANANGDGIEHFGYVDGRSQPLFLTEDVDAERDTTDGVNDWDPSAPLEQVLVPDPAAPDPTVHFGSYFVFRKLEQNVRLFKEAERDLAHDLGLRGEDRERAGAMLVGRFEDGTPLTAQSAPGSHHPVGNDFSYDSDKLGQKCPFHA... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Displays both high peroxidase and manganese peroxidase activity. Is likely involved in lignin degradation. Also has a Mn-dependent oxidase mode of action that expands its substrate scope in vitro; is thus able to catalyze the O(2)- and M... |
I2DBY1 | MRLSPVFVALLSGLLAADLGLARSVAPRVADSPAAVTGTRKTSLLKNVAGLPPVPSAAQVAATSLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTHLASDIAPVVASVTQLSNVATQPLVALNIAFSNTGLLALGVTDNLGDSLFANGQAKDATSFKESTSSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLSASIRPGNEAGHEMFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATNDPITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQARADLLGARMVGRWKSG... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.
Function: Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactiv... |
A0A3T0E4B9 | MTEAFPNGKTPQHVLGPPAPAAVFLVLTVRSGAEAEAKDFLGDIAGVVRSVGFRAREDHLSCVTGIGAELWDRMFDAPRPAGLHPFIEQRGDVHTAPSTPGDLLFHIRARRMDLCFELARQLVGELGDAVSVVDEVHGFRYFDERDIMGFVDGTENPEDQEAVDSVFTPTGGDDPASSTYVIVQKYTHDMAAWEALSVEDQEAAFGRHKLSDMEFPDEDKAPNSHLILNTIEDEDGTEHKIVRDNMVFGSVESGEFGTYFIGYAADVSVTEQMLENMFIGNPRGTYDRILDFSTAQTGGLFFVPSQDFLDDPDGELAAAE... | Function: Cargo protein of a type 1 encapsulin nanocompartment. Has both general peroxidase activity and dye-decolorizing activity. Can catalyze the oxidation of both protoporphyrinogen IX and coproporphyrinogen III to their corresponding porphyrins. Also efficiently decolorizes the dyes alizarin red and Cibacron blue ... |
I2DBY2 | MRLSPSFLSLALVIFVGEVVARNVVARASNPASVTGTRKVSLLKNVAGLPAVPTAQQVAVSSLNTDDIQGDILVGMHKQQQRFYFFTINDAATFKTHLAADIAPVVASVTQLSSVSTQPLVALNIAFSQTGLNALGVTDNVGDALFTAGQASNTVGNLKETTDNWVAQFKTPGIHGVILLASDDKSLIDQQEASIQSTFGAAISKVYSLDGAIRPGAEAGHEMFGFLDGIAQPAISGLGTPLPGQLVVDEGVIIVGGTNDPIARPADGWMTGGSFLAFRQLEQLVPEFNKYLLDNAPAVDGKSLQDRADLLGARMVGRWK... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.
Function: Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactiv... |
I6Y4U9 | MAVPAVSPQPILAPLTPAAIFLVATIGADGEATVHDALSKISGLVRAIGFRDPTKHLSVVVSIGSDAWDRLFAGPRPTELHPFVELTGPRHTAPATPGDLLFHIRAETMDVCFELAGRILKSMGDAVTVVDEVHGFRFFDNRDLLGFVDGTENPSGPIAIKATTIGDEDRNFAGSCYVHVQKYVHDMASWESLSVTEQERVIGRTKLDDIELDDNAKPANSHVALNVITDDDGTERKIVRHNMPFGEVGKGEYGTYFIGYSRTPTVTEQMLRNMFLGDPAGNTDRVLDFSTAVTGGLFFSPTIDFLDHPPPLPQAATPTL... | Cofactor: Tetramer binds heme in a 1:1 ratio . Addition of hemin to purified protein yields a tetrameric protein (Probable).
Function: Cargo of a type 1 encapsulin nanocompartment in situ; this cargo protects against oxidative stress at low pH. When expressed in the cytoplasm (absence of the encapsulin shell gene) it i... |
Q47KB1 | MTEPDTERKGSSRRGFLAGLGAAALTGAGIGMAAGEVLRPLLPDSDPAASPEAEQRLRMAAQRADATAAPQPGISGPAPAFVHVIALDLAEEARKNPDTARDSAAAALRSWTELAARLHEESPHDIAEGAASAGLLPASLMVTVGIGGSLLSAIDAEDRRPDALADLPEFSTDDLHPRWCGGDFMLQVGAEDPMVLTAAVEELVAAAADATAVRWSLRGFRRTAAAARDPDATPRNLMGQIDGTANPAQDHPLFDRTITARPADNPAHAWMDGGSYLVVRRIRMLLTEWRKLDVAARERVIGRRLDTGAPLGSRNETDPV... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.
Function: Peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. Shows high reactivity towards anthraquinone dyes (e.g. Reactive Blue 19) and a modest activity towards standard peroxidase s... |
Q04515 | MNISLIFANELITRAFGNQGKLPWQFIKEDMQFFQKTTENSVVVMGLNTWRSLPKMKKLGRDFIVISSTITEHEVLNNNIQIFKSFESFLEAFRDTTKPINVIGGVGLLSEAIEHASTVYMSSIHMVKPVHADVYVPVELMNKLYSDFKYPENILWVGDPIDSVYSLSIDKFVRPASLVGVPNDINT | Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Mass (Da): 21220
Sequence Length: 187
Pathway: Cof... |
Q59408 | MNPESVRIYLVAAMGANRVIGNGPDIPWKIPGEQKIFRRLTESKVVVMGRKTFESIGKPLPNRHTVVLSRQAGYSAPGCAVVSTLSHVSPSTAEHGKELYVARGAEVYALALPHANGVFLSEVHQTFEGDAFFPVLNAAEFEVVSSETIQGTITYTHSVYARRNG | Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Mass (Da): 17925
Sequence Length: 165
Pathway: Cof... |
Q9FHX5 | MASSSLQSLFSLFCLALFSLPLIVSSIGINYGQVANNLPPPKNVIPLLKSVGATKVKLYDADPQALRAFAGSGFELTVALGNEYLAQMSDPIKAQGWVKENVQAYLPNTKIVAIVVGNEVLTSNQSALTAALFPAMQSIHGALVDCGLNKQIFVTTAHSLAILDVSYPPSATSFRRDLLGSLTPILDFHVKTGSPILINAYPFFAYEENPKHVSLDFVLFQPNQGFTDPGSNFHYDNMLFAQVDAVYHALDAVGISYKKVPIVVSETGWPSNGDPQEVGATCDNARKYNGNLIKMMMSKKMRTPIRPECDLTIFVFALFN... | Function: Plasmodesmal-associated membrane beta-1,3-glucanase involved in plasmodesmal callose degradation and functions in the gating of plasmodesmata.
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45358
Sequence Length... |
Q8L868 | MELTSFHRSSLLFLISLTLIILPTTTTSIGVNYGQIGDNLPSPTDVIPLIKSIGATKVKLYDANPQILKAFSNTGIEFIIGLGNEYLSKMKDPSKALTWIKQNVTPFLPATNITCITIGNEILALNDSSLTTNLLPAMQGVHSALITAGLSDQISVTTAHSLSILKSSFPPSAGEFQPDLLDSLTPILEFHRKTDSPFLINAYPFFAYKGNPKEVPLDFVLFQPNQGIVDPATGFHYDNMLFAQIDAVYSALAAAGFKSLRVEISETGWPSKGDDDEVGATPENAKRYNGNLIKMMMSGKKTKTPLKPNNDLSIYVFALF... | Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45421
Sequence Length: 426
Subcellular Location: Secreted
EC: 3.2.1.39
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Q8VYE5 | MGQRLNLVFWIFVSILAFLNFGMASKIGICYGRNADNLPSPNRVSELIQHLNIKFVRIYDANIDVLKAFANTGIELMIGVPNADLLAFAQFQSNVDTWLSNNILPYYPSTKITSISVGLEVTEAPDNATGLVLPAMRNIHTALKKSGLDKKIKISSSHSLAILSRSFPPSSASFSKKHSAFLKPMLEFLVENESPFMIDLYPYYAYRDSTEKVPLEYALFESSSQVVDPATGLLYSNMFDAQLDAIYFALTAMSFKTVKVMVTESGWPSKGSPKETAATPENALAYNTNLIRHVIGDPGTPAKPGEEIDVYLFSLFNENR... | PTM: Contains two additional disulfide bonds.
Location Topology: Lipid-anchor
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 57659
Sequence Length: 534
Subcellular Location: Secreted
EC: 3.2.1.39
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Q9ZQG9 | MATHSLSFFFRVLLLLFLTLSERIKGQGVGINYGQIANNLPSPARVAVLLRSLNITRVKLYDADPNVLFSFSNSQVDFMIGLGNEYLQNMSTDPTKAQDWLQQRLEPHISKTRITSIVVGNEIFKTNDHVLIQSLLPAMKSVYAALTNLGLEKQVTVTSAHSLDILSTSYPPSSGSFKEEFIQYLQPLLDFHSQIESPFLINAYPFFAYKDSPKEVPLEYVLFQPNQGMVDPNTNLHYDNMLFAQVDALYSAIKTLGHTDIEVRISETGWPSKGDENEIGASPENAALYNGNLLKLIQQRKGTPAKQSVPIDVYVFALFN... | Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Location Topology: Lipid-anchor
Sequence Mass (Da): 44074
Sequence Length: 392
Subcellular Location: Cell membrane
EC: 3.2.1.39
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O65399 | MAFTSMVSTVPVLFFFFTLLLISANSSSLSHNIKVQEQDKDPFVGFNIGTDVSNLLSPTELVKFLQAQKVNHVRLYDADPELLKALAKTKVRVIISVPNNQLLAIGSSNSTAASWIGRNVVAYYPETLITAISVGDEVLTTVPSSAPLLLPAIESLYNALVASNLHTQIKVSTPHAASIMLDTFPPSQAYFNQTWHSIMVPLLQFLSKTGSPLMMNLYPYYVYMQNKGVVPLDNCLFEPLTPSKEMVDPNTLLHYTNVLDAMVDAAYVSMKNLNVSDVAVLVTESGWPSKGDSKEPYATIDNADTYNSNLIKHVFDRTGT... | PTM: Contains two additional disulfide bonds.
Location Topology: Lipid-anchor
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 55630
Sequence Length: 511
Subcellular Location: Cell membrane
EC: 3.2.1.39
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Q9C7U5 | MASLLHLLLLSLSLLVLASASPSPPADEGSYIGVNIGTDLSDMPHPTQVVALLKAQEIRHIRLYNADPGLLIALANTGIKVIISIPNDQLLGIGQSNSTAANWVKRNVIAHYPATMITAVSVGSEVLTSLSNAAPVLVSAIKNVHAALLSANLDKLIKVSTPLSTSLILDPFPPSQAFFNRSLNAVIVPLLSFLQSTNSYLMVNVYPYIDYMQSNGVIPLDYALFKPIPPNKEAVDANTLVRYSNAFDAMVDATYFAMAFLNFTNIPVLVTESGWPSKGETNEPDATLDNANTYNSNLIRHVLNKTGTPKRPGIAVSTYI... | PTM: Contains two additional disulfide bonds.
Location Topology: Lipid-anchor
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 54206
Sequence Length: 505
Subcellular Location: Cell membrane
EC: 3.2.1.39
|
P52401 | MATSQIAVIVLLGLLVATNIHITEAQLGVCYGMMGNNLPSHSEVIQLYKSRNIGRLRLYDPNQGALNALRGSNIEVILGLPNVDVKHIASGMEHARWWVQKNVKDFWPDVKIKYIAVGNEISPVTGTSSLTSFQVPALVNIYKAVGEAGLGNDIKVSTSVDMTLIGNSYPPSQGSFRNDVRWFTDPIVGFLRDTRAPLLVNIYPYFSYSGNPGQISLPYALFTAPNVVVQDGSRQYRNLFDAMLDSVYAAMERTGGGSVGIVVSECGWPSAGAFGATQDNAATYLRNLIQHAKEGSPRKPGPIETYIFAMFDENNKNPEL... | Function: Is thought to be an important plant defense-related product against fungal pathogens.
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 39759
Sequence Length: 363
Subcellular Location: Vacuole
EC: 3.2.1.39
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Q9ZU91 | MAALLLLFLFLFASSALSQDSLIGVNIGTEVTNMPSPTQVVALLKSQNINRVRLYDADRSMLLAFAHTGVQVIISVPNDQLLGISQSNATAANWVTRNVAAYYPATNITTIAVGSEVLTSLTNAASVLVSALKYIQAALVTANLDRQIKVSTPHSSTIILDSFPPSQAFFNKTWDPVIVPLLKFLQSTGSPLLLNVYPYFDYVQSNGVIPLDYALFQPLQANKEAVDANTLLHYTNVFDAIVDAAYFAMSYLNFTNIPIVVTESGWPSKGGPSEHDATVENANTYNSNLIQHVINKTGTPKHPGTAVTTYIYELYNEDTR... | PTM: Contains two additional disulfide bonds.
Location Topology: Lipid-anchor
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 53992
Sequence Length: 501
Subcellular Location: Cell membrane
EC: 3.2.1.39
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Q94CD8 | MLLPRWFAEALLLLLSILACSNAAFIGVNIGTDLTNMPPPSDIVTLLKSQQITHVRLYDANSHMLKAFANTSIEVMVGVTNEEILKIGRFPSAAAAWVNKNVAAYIPSTNITAIAVGSEVLTTIPHVAPILASALNNIHKALVASNLNFKVKVSSPMSMDIMPKPFPPSTSTFSPSWNTTVYQLLQFLKNTGSFFMLNAYPYYGYTTANGIFPLDYALFKQLSPVKQIVDPNTLLHYNSMFDAMVDAAYYSMEALNFSKIPVVVTETGWPSSGGSDEAAATVANAETFNTNLIKRVLNNSGPPSQPDIPINTYIYELYNE... | PTM: Contains two additional disulfide bonds.
Location Topology: Lipid-anchor
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 54416
Sequence Length: 505
Subcellular Location: Cell membrane
EC: 3.2.1.39
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Q9ZT66 | MPSSAQVLLCLAAVLAAAAATTAEAHSQCLDNPPDRSIHGRQLAEAGEVVHDLPGGLRAYVSGAASSSRAVVLASDVFGYEAPLLRQIVDKVAKAGYFVVVPDFLKGDYLDDKKNFTEWLEAHSPVKAAEDAKPLFAALKKEGKSVAVGGYCWGGKLSVEVGKTSDVKAVCLSHPYSVTADDMKEVKWPIEILGAQNDTTTPPKEVYRFVHVLRERHEVPFRRQDRRDGPRLHGQLVQQAPQLNEACTAPTRLNSINHSSAVIFCFDSWLPRLIFMATTSSTTVISLIFFVSMYFFSFLFAFL | Function: Plays a role in control of plant growth. Mediates specific degradation of cell wall (1,3)(1,4)-beta-D-glucans and is related to auxin-mediated growth and development of cereal coleoptiles.
PTM: Glycosylated.
Sequence Mass (Da): 33160
Sequence Length: 303
Subcellular Location: Secreted
EC: 3.2.1.-
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Q9M088 | MLFKGVFAVFFVITLLYASLLIEVEGIGVNWGSQARHPLPPATVVRLLRENGIQKVKLFEADSAILKALSRTGIQVMVGIPNDLLAPLAGSVAAAERWVSQNVSAHVSSNGVDIRYVAVGNEPFLKAFNGTFEGITLPALQNIQSAIIKAGLATQVKVTVPLNADVYQSASNLPSDGDFRPEIRDLMLNIVKFLSDNGAPFTINIYPFISLYNDPNFPVEFAFFDGTGTPINDNGRIYDNVLDANYDTLVWSLQKNGFGNLTIIVGEVGWPTDGDKNANLMYARRYNQGFMNRQKANKGTPMRPGAMDAYLFGLIDEDAK... | PTM: Contains two additional disulfide bonds.
Location Topology: Lipid-anchor
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 52715
Sequence Length: 484
Subcellular Location: Cell membrane
EC: 3.2.1.39
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Q93Z08 | MGWGSVLLLLAVALLCQRASSIGANWGTQASHPLPPDIVVRMLRENGIQKVKLFDAEYDTLRALGKSGIEVMVGIPNEMLATLASSLKAAEKWVAKNVSTHISTDNVNIRYVAVGNEPFLSTYNGSYLSTTFPALRNIQIAIIKAGLQNQVKVTCPLNADVYDSSTTFPSGGDFRANIRDLMITIVKFLSENGGPFTVNIYPYISLYTNPDFPVDYAFFDGNAQPLNDGGTFYYNMFDANYDTLVHALEKNGFGNMPIIIGEIGWPTDGDSNANLDYAKKFNQGFMAHISGGKGTPRRPGPIDAYLFSLIDEDAKSVQPG... | PTM: Contains two additional disulfide bonds.
Location Topology: Lipid-anchor
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 52211
Sequence Length: 477
Subcellular Location: Cell membrane
EC: 3.2.1.39
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P15134 | MIPRNFFFTILICAFNVCATFTAVATASPDCIGPFASYALFAFVTCICVCSIVCLVINFFQLVDWIFVRIAYLRHHPEYRNQNVAALLRLI | Function: Down-regulates the EGF receptor.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 10330
Sequence Length: 91
Subcellular Location: Host endoplasmic reticulum membrane
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P36705 | MVTVLLIFLCLPVIFSSSTFAAVSDLDPECLAPFAVYLIFTFVTATCVCSIITLLITSLQFFDYYYVRIVYRRHHPRYQNPQIAALLQLQP | Function: Down-regulates the EGF receptor.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 10425
Sequence Length: 91
Subcellular Location: Host endoplasmic reticulum membrane
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P17590 | MTNTTNAAAATGLTSTTNTPQVSAFVNNWDNLGMWWFSIALMFVCLIIMWLICCLKRKRARPPIYSPIIVLHPNNDGIHRLDGLKHMFFSLTV | PTM: N-glycosylated and probably also O-glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10523
Sequence Length: 93
Subcellular Location: Host nucleus membrane
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P15133 | MIPRVLILLTLVALFCACSTLAAVAHIEVDCIPPFTVYLLYGFVTLILICSLVTVVIAFIQFIDWVCVRIAYLRHHPQYRDRTIADLLRIL | Function: Prevents infected cell apoptosis induced by the host immune system. Acts by down-regulating a number of cell surface receptors in the tumor necrosis factor (TNF) receptor superfamily, namely FAS, TNFRSF10A/TRAIL receptor 1, and TNFRSF10B/TRAIL receptor 2. Down-regulation of these death receptors protects aden... |
P03250 | MKRSVIFVLLIFCALPVLCSQTSAPPKRHISCRFTQIWNIPSCYNKQSDLSEAWLYAIISVMVFCSTIFALAIYPYLDIGWNAIDAMNHPTFPVPAVIPLQQVIAPINQPRPPSPTPTEISYFNLTGGDD | Function: Prevents infected cell apoptosis induced by the host immune system. Acts by down-regulating a number of cell surface receptors in the tumor necrosis factor (TNF) receptor superfamily, namely FAS, TNFRSF10A/TRAIL receptor 1, and TNFRSF10B/TRAIL receptor 2. Down-regulation of these death receptors protects aden... |
Q9WV92 | MTTESGSDSESKPDQEAEPQEAAGPQGQAGAQPGPEPAGGNGSLNGEKQQPALEQFPEAAAHSTPVKREIGDKDRDFAAAAAKQLEYQQFEDDKLSQRSSSSKLSRSPLKIVKRPKSMQCKVTLLDGSEYGCDVDKRSRGQVLFDKVCEHLNLLEKDYFGLTYRDAENQKNWLDPAKEIKKQIRSGAWHFSFNVKFYPPDPAQLSEDITRYYLCLQLRDDIVSGRLPCSFVTLALLGSYTVQSELGDYDPDECGNDYISEFRFAPNHTKELEDKVIELHKSHRGMTPAEAEMHFLENAKKLSMYGVDLHHAKDSEGVEIM... | Function: Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N-methyltransferases, including PRMT3 and PRMT5 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 103338
Sequence Length: 929
Subcellular Location: Cytoplasm
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Q9HCM4 | MLSFFRRTLGRRSMRKHAEKERLREAQRAATHIPAAGDSKSIITCRVSLLDGTDVSVDLPKKAKGQELFDQIMYHLDLIESDYFGLRFMDSAQVAHWLDGTKSIKKQVKIGSPYCLHLRVKFYSSEPNNLREELTRYLFVLQLKQDILSGKLDCPFDTAVQLAAYNLQAELGDYDLAEHSPELVSEFRFVPIQTEEMELAIFEKWKEYRGQTPAQAETNYLNKAKWLEMYGVDMHVVKARDGNDYSLGLTPTGVLVFEGDTKIGLFFWPKITRLDFKKNKLTLVVVEDDDQGKEQEHTFVFRLDHPKACKHLWKCAVEHH... | Function: Plays a role in the formation and organization of tight junctions during the establishment of polarity in epithelial cells.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 81856
Sequence Length: 733
Subcellular Location: Cytoplasm
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Q8BGS1 | MLSFLRRTLGRRSMRKHAEKERLREAQRAATHIPAAGDAKSIITCRVSLLDGTDVSVDLPKKAKGQELFDQIMYHLDLIESDYFGLRFMDSAQVAHWLDGTKSIKKQVKIGSPYCLHLRVKFYSSEPNNLREELTRYLFVLQLKQDILSGKLECPFDTAVQLAAYNLQAELGDYDLAEHSPELVSEFRFVPIQTEEMELAIFEKWKEYRGQTPAQAETNYLNKAKWLEMYGVDMHVVKARDGNDYSLGLTPTGVLVFEGETKIGLFFWPKITRLDFKKNKLTLVVVEDDDQGKEQEHTFVFRLDHPKACKHLWKCAVEHH... | Function: Plays a role in the formation and organization of tight junctions during the establishment of polarity in epithelial cells.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 81636
Sequence Length: 731
Subcellular Location: Cytoplasm
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A0A1E3P8S6 | MFFTKVLNNQVANGLKQLPVHKRVQMAYDLHIPNKTVNPNLNIRSHEPIVFVHGIFGSKKNYRHDCQKIANVTHTPVYTIDLRNHGQSMHALPFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAKICMLTMLQNPDLVRSGVIIDNSPIEQPHIEIFLTQFIKSMLHVLNSTKIRADDKDWKSKANQAMRRYIPNGGIRDYLLANLINKVPKGYKSPVINYDDGYIHFQNPVRHMTEVAVKNVSAWPTEHVKGLKFEGQVRFLKGTKSAFIDEKGLEAIKEYFPNYSLSELNATHFILNERPQEYVKLICDFIKVNRYKS... | Function: Alcohol acetyltransferase that catalyzes the synthesis of ethyl acetate from ethanol and acetyl-CoA. Can also function as a thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as well as esterase hydrolyzing ethyl acetate.
Catalytic Activity: acetyl-CoA + ethanol = CoA + ethyl acetate
Sequence M... |
P53208 | MSRLAHNKALPYKIIVDLSFHRTRLPSDVSSLIKFEQRPAIINIHGLLGSHVMFHSLNKLLSRKLDADIFSVDVRNHGISPKAIPYDYTTLTNDLIYFIETHIGLERPIYLLGFSMGGKIALLTTLYKNINIRKCISIDLPPYETPELDPMILQNYDLIMRIIRRDVKILRGSPSWQKKVLELFKSLECNKRKCGGAVALYFANGFLSVKSNNVHQAQLHYEQQQHDPYINYSMPLSSMPNLLDEVKKWPDLSNQRDFFQKGTASRKVLFMKGLQSNFINNDYSLLRYNFPCADVREFNTGHNLLLENPEDSFKCILNFF... | Function: Alcohol acetyltransferase that catalyzes the synthesis of ethyl acetate from ethanol and acetyl-CoA . Can also function as a thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as well as esterase hydrolyzing ethyl acetate (By similarity).
Catalytic Activity: acetyl-CoA + ethanol = CoA + ethyl a... |
Q9NL29 | MTTFCRVLLIFGIYVAVCCAQSVEDDVFHFTNPSQGNAVWILDESSLPWTGGYQFLRSISGMPTTLLSVVDSSTGVTLGQCVAPQDATGNFSKRWERFSWELTASGLDCTFEHGAAIRVEFDRTQNPRTFSIRIQSITGPACLRDVVVQTEQATGCPPHLSRNSFTANALNCSCPFLDAANEDSEIENEDVDMLANTPQFPLFKGIDPSVLGSANPPTLPPSPCANHECHNNGTCLVSQEGAATCLCRNGFTGDRCELDVCSSVPCQNGGVCRSNNGIAYCECPPAFTGLLCESAHTDESVAPICRPECSNGQCVFKDGQ... | Function: Regulates pharyngeal pumping during feeding.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 87953
Sequence Length: 810
Subcellular Location: Membrane
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A0A1E5RIW9 | MIFNSLSIKRLSSTXTSLPFKKHAKLNFDLYSPQHSTYGKLPYHCQEPIIFLHGIYGYSKSFNSDYQQLSNLLHTPIYSVDMRCHGETENCLPFTYDALAGDLDNFVITHNIKKPSLIGFSLGAKLAMLAILKSPHLYTSGVIVDNVPLKQPRIKPNLTAFGNALRDSVFKSGVKRNDPSWISKSFNVMKDVCSDMPANFYLLHNIQPKPSYLKKYSTEESENSLFCKVPIRELSSHVVENVPDWPEEDLAGVKTDVPILVVKASTSGFVNEDGVAALXKHFSDFTIVEVAGTHLVMKERPQEYISAVGRWFYQQNCKKA... | Function: Alcohol acetyltransferase that catalyzes the synthesis of ethyl acetate from ethanol and acetyl-CoA . Can also function as a thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as well as esterase hydrolyzing ethyl acetate (By similarity).
Catalytic Activity: acetyl-CoA + ethanol = CoA + ethyl a... |
P34644 | MSSWNEAWDRGKQMVGEPLAKMTAAAASATGAAPPQQMQEEGNENPMQMHSNKVLQVMEQTWIGKCRKRWLLAILANMGFMISFGIRCNFGAAKTHMYKNYTDPYGKVHMHEFNWTIDELSVMESSYFYGYLVTQIPAGFLAAKFPPNKLFGFGIGVGAFLNILLPYGFKVKSDYLVAFIQITQGLVQGVCYPAMHGVWRYWAPPMERSKLATTAFTGSYAGAVLGLPLSAFLVSYVSWAAPFYLYGVCGVIWAILWFCVTFEKPAFHPTISQEEKIFIEDAIGHVSNTHPTIRSIPWKAIVTSKPVWAIIVANFARSWT... | Function: Required for glutamatergic synaptic transmission . In AWB and AWC sensory neurons, required for the detection of preferred food sources, probably via glutamatergic neurotransmission from sensory neurons . Negatively regulates the turning step of male mating behavior .
Location Topology: Multi-pass membrane pr... |
Q27295 | MNMLGSMFSMVKPRLDDLGTDRLNYYYSTLIIMGMSLTITARQYVGSPLQCWVPAQFTKAWEQYAEDYCFVYNTYWVKPNDKVPLTVEERVSQQLIYYQWAPFIMAIEAAFFYLPVIFWSMLSTKSGINIIKLVETAQKAEGAESEERKKQIDIICRHISNNLRKRRNEEETTKMAKIQRIFGMQHGKYITNVYLVTKLIYMTNSFLQFYSTNKFLGQNDPYWGMRILDDILKGTDWEHSGNFPRIAMCDFQVRVLGNLQRYSIQCVLTLNMFNEKIFLFLYIWFLLVFFVTLFDSIFLCYNMFSSHKLVEFLQQFLDNQ... | Function: Structural component of the gap junctions (By similarity). Required for synchronized pharyngeal muscle contractions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50326
Sequence Length: 423
Subcellular Location: Cell membrane
|
Q7XJ60 | MATNIGMMDSAYFVGRNEILTWINDRLHLNLSRVEEAASGAVQCQMLDMTFPGVVPMHKVNFDAKNEYDMIQNYKVLQDVFNKLKITKPLEINRLVKGRPLDNLEFLQWLKRFCDSINGGIMNENYNPVERRSRNGKERSVKGSNKIPKSLQTNNNHPPPNSSSVGLSKASGPKSAKAAEVQALSKELVDLKISTDLLEKERDFYFSKLRDVEILCQTPELDDLPIVVAVKKILYATDANESALEDAQEYLNQSLGVEDDEAEGNGEQLEEEKTQA | Function: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. May be involved in anchoring microtubules to their nucleation sites and/or functioning as a reservoir for distribution to the growing end. In plants, microtubule minus ends are not necessarily severed from the nu... |
Q8AZK7 | MGDRSEGPGPTRPGPPGIGPEGPLGQLLRRHRSPSPTRGGQEPRRVRRRVLVQQEEEVVSGSPSGPRGDRSEGPGPTRPGPPGIGPEGPLGQLLRRHRSPSPTRGGQEPRRVRRRVLVQQEEEVVSGSPSGPRGDRSEGPGPTRPGPPGIGPEGPLGQLLRRHRSPSPTRGGQEPRRVRRRVLVQQEEEVVSGSPSGPRGDRSEGPGPTRPGPPGIGPEGPLGQLLRRHRSPSPTRGGQEPRRVRRRVLVQQEEEVVSGSPSGPRGDRSEGPGPTRPGPPGIGPEGPLGQLLRRHRSPSPTRGGQEPRRVRRRVLVQQEE... | Function: Plays an important role in the establishment of B-cell immortalization by acting as an EBNA2 coactivator. This transcriptional activation preferentially enhances the expression of the major viral protein LMP1. The interaction between EBNA-LP and host SP100 correlates with coactivation of EBNA2 and the relocal... |
Q9VDC6 | MGSLPQLSIVKGLQQDFVPRALHRIFEEQQLRHADKVALIYQPSTTGQGMAPSQSSYRQMNERANRAARLLVAETHGRFLQPNSDGDFIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAGRFQGTPTLSTTELYAKSLQLAGSNLLSEEMLRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFKTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAQKLLYNLQIWVCSGEPLSV... | Cofactor: May also use Mn(2+).
Function: Nonribosomal peptide synthase which is required for the regulation of histamine and dopamine levels in various tissues through their condensation with beta-alanine . In epithelial glial cells, plays an essential role in the inactivation of histamine, the main neurotransmitter in... |
A0A1D8PPK1 | MTIESTNSFVVPSDTELIDVTPLGSTKLFQPIKVGNNVLPQRIAYVPTTRFRASKDHIPSDLQLNYYNARSQYPGTLIITEATFASERGGIDLHVPGIYNDAQAKSWKKINEAIHGNGSFSSVQLWYLGRVANAKDLKDSGLPLIAPSAVYWDENSEKLAKEAGNELRALTEEEIDHIVEVEYPNAAKHALEAGFDYVEIHGAHGYLLDQFLNLASNKRTDKYGCGSIENRARLLLRVVDKLIEVVGANRLALRLSPWASFQGMEIEGEEIHSYILQQLQQRADNGQQLAYISLVEPRVTGIYDVSLKDQQGRSNEFAYK... | Function: Oxidoreductase that binds mammalian estrogens with high affinity.
Catalytic Activity: A + H(+) + NADPH = AH2 + NADP(+)
Sequence Mass (Da): 46089
Sequence Length: 407
EC: 1.6.99.1
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Q2FNX9 | MHIIETQDLCHTYKGNIDALKNISFIAPRNTRIAIIGPNGAGKSTLFKHFNGVLKPTSGKVLIRGEPITKENIREVRRTVGLVFQNPDDQIFSPTVEQDVAFGPINMGLDEEAVKHRVSEALRTVGLSEYRTRVPHHLSGGEKKRVAIAGIIAMEPQVLVLDEPTAGLDPQGVREIIRFIRDFSVRYGMTVIFSTHNISLVAELAEYIYVMNNGSFVAEGTVAEIFSQPDLLSSVRLDLPILPKLISSLRSKGIAIDMGYTYQEAEIAFLKAFGKIA | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30586
Sequence Length... |
P47425 | MLPTKQAACSFINVAFSYNELPLIRELSFSVYEGEYVCIVGHNGSGKSTISKLLTGLLKPQAGEIKIFGKTVDFDNVSYLRNNIGIIFQNPDNQFIGITVEDDIAFGLENKCFSRQKIKAIIDEVTLQTQTDGFIKQEPHNLSGGQKQRVAIASVLALNPAIIIFDESTAMLDPKAKKTIKQFMVKLAKQGKCVISITHDMEEVTKADKVLVMNEGKLIKQGKPVEVFTSEQELQKIRLDIPFSLSLSTKIRGITSTIDYQTLIKSIAKLWKKR | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30545
Sequence Length... |
Q6MSQ1 | MDNSAIFEEFNSKKISQDDLEATITSLNNYFVKLNDLNNQYINLIRQDNIDKIEKQNIRQQQKQVKVEIKKISATTKLFKQNLKLAESLYKKIKLTNNQDDINKAKHEVEIAKSMLLQLKEVINGQGKSIKLKKLSDIAIEINHLSFKYGPEFPNAIDDVSFTINQGEYVTIIGHNGSGKSTISKILIGVLNAQHGEIKIFGNIVNDHNIEQARKFLGIVFQNPDNQFIGSTVEADIAFGLENKRIDPKKMPDIILDSAKKVGMEWALKKEPLNLSGGQKQRVAIASTLALDPDIMIFDEATSMLDPKGKREIKEIMVQL... | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 46209
Sequence Length... |
Q4A5A5 | MIKLNNVTFRYRPSDENPAINNVSLEIKKGQYVAILGHNGSGKSTLSKILVALLKPQKGELFIDGIQYSKENLKEIRKKIGIIFQNPDNQFIGSTVEDDIAFGLENKNISRDEMRTKVVEYAKVVDMEKHLSREPEYLSGGQKQRVAIASVLALDPEVIIFDEVTSMLDPKGKSKVIQIIKQIQADKDKTLISITHDMDEAILADTVLVFAKGKLVAAGSPKDILNEEKIIEIAKIASPFIYKISKHINGIEPTYVEEELISQICK | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29721
Sequence Length... |
Q6XYZ4 | MAKKTKKINVKLEKLNYISLKLTDVEFRYRENHPNAVDGVSFEINHGEYVTIIGHNGSGKSTISKIIIGVLRPQKGKIEVFGNEVHSSTITGIRKFLGIVFQNPDNQFIGSTVRDDIAFGLENRQIPQKKMQAIIEKAAAKVGMNNFLDHEPLMLSGGQKQRVAIASALALSPDIIIFDEATSMLDPKGRKEIKQIMVDLKESREKTIISITHDMDEILNSDKAIVMNKGQMVKCGKPHEVLYDEEFLKSIHLDVPFVSKVVDSLRLNGLKVKNTLNLRELVDEICQK | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32320
Sequence Length... |
O27739 | MIELRDLSYSYPDGTPALRGINMKVERGERVAVIGPNGAGKSTLFLHLNGILKPAAGEVIIDGERVDYSKDELIKIRQKVGIVFQNPDDQLFSPTVREDVAFGPMNLGLPEDEVEERVAESLEKVGMSGYENRAPHHLSGGEKKRVAIAGILAMKPEIMVLDEPTTGLDPETADGIIRILLELSREGITVMISSHDVEIISQFAERVFVLNSGELIAEGTPLEIFRDAELIRRASLRLPRTADLLNRLRMAGFEVDVKLTVEETYHELLHLLGGDAYHRLLHFLGEEKQHRLIHLLGEKKYHELLHALKEQ | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34786
Sequence Length... |
Q2RFS8 | MIAIQGATYIYPGSTVPALEKIDLAIEPGEFLAITGPNGSGKSTLARLLNGLLRPRQGRVLVDGMDTGDDTALITIRRRVGMVFQDPDNQLVAATVAEDVAFGLENLGLPPAEIEKRVDLALRSVGLEDLAARPPHLLSGGQKQRLALAGVLAMEPRYLVLDEATAMLDPVAREEILEQVLRLRQEQGIAIILITHLMEEAVRADRMLIMKSGRIFWQGSPRELSYQERILAAAGLRLPAVIALAKSLRQGGIKLATNPVCVEELARALWKLASRE | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30004
Sequence Length... |
Q0AUL1 | MISIRDLTYFYPEEDLPALKNISLDIRENEFLVILGRNGSGKSTLARLLNGLLLPSQGKVEVDGWNTADANQIQLIRQRVGLLFSNPDNQLISNQVEEDVAFGPENLGLNTAEIRRRVNDSLRLVSMESYKNSAPAFLSGGQKQKIAIAGVMAMKPRYLVLDEALSMIDPRGKREIMESIRSLHKTEGVVVIMITHDLEEAREADRVVVLEEGEVKTISTPEELFPSRASLLALGLAPLEISHIIAEINRQGILLSTDILDIDKLVEEICHFV | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30381
Sequence Length... |
D2NWE2 | MIEKLILGRFVPGESLIHGLDARTKLLAGFYYIGILFLANNWWTYALMVLFTLMVVQMTGIKLKVFIKGVKPLIWLILFTVVMQILFASGGTIYFDWGPFTISSFGLLNGVFVFLRFVLIIIMSTVITLTTTPMNLTDAIAYILRPFAVLKVPVNDIALMISVALRFIPTLMGETDKIMKAQRARGVDFGEGNLFEQMKVVVPIFIPLFVSSFNRAEELADAMEARGYQGGEGRTRFRILHWHFGDLIAACVMILLTAGLVILRTS | Function: Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29826
Sequence Length: 26... |
D2RNY0 | MLTDITLGQYYPGNSCIHRLDPRTKILAVLFYMVMVFLANSPLSYGILIGFIVLGAALAKLPAGLLLRSIKPLWIIILLTMVIHFVTDPGEALWHWKFITVTREGIVLGVKMSLRLVLLLLVSSLMTFTTSPIVLTDGIESLLRPFKKIGVPAHELAMMMTIALRFIPTLLEETDRIMKAQMSRGADFSSGNIMKRAKNMLPILIPLFISSFRRADELALAMEARCYRGGEGRTRMHELVYGKADALTGLVMLALFVLLAFLRWGIPA | Function: Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29890
Sequence Length: 26... |
D6XVS2 | MFDSIIIGQYVPGDSVVHRLDPRVKLTAVFIFLVFMFMTRDPLLLTVAVLLSFGGLLASRVPLSFYAKGMRFISIIIVLTFVLHLFMTGGGEVIVELPFATIYSGGLIEGFMLAMKLAMIITIASLLTLTTTPIDLTDGMERMLAPFKRVKLPTHELALMMSIALRFIPTLIEETRTIVLAQLARGTNFSEGSLWKRLKALIPILVPLFTQSFKRAEELATAMEARGYAGGEGRTKYRQLHWGLKDSVVLAVFLLFAAAVMAERFMGG | Function: Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29683
Sequence Length: 26... |
P70972 | MMDSMIIGKYVPGTSLVHRLDPRTKLITIFLFVCIVFLANNVQTYALLGLFTIGVVSLTRVPFSFLMKGLKPIIWIVLFTFLLHILMTHEGPIIFQIGFFKVYEGGLVQGIFISLRFVYLILITTLLTLTTTPIEITDGMEQLLNPLKKLKLPVHELALMMSISLRFIPTLMEETDKIMKAQMARGVDFTSGPVKERVKAIVPLLVPLFVSAFKRAEELAVAMEARGYQGGEGRTKYRKLVWTGKDTSVIVSLIVLAALLFFLRA | Function: Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates (By similarity). Involved in riboflavin transport.
Location Topology: Multi-pass membrane pro... |
C0ZIL1 | MLQNIAIGQYVPGQSFLHRADPRSKLLFIILFATLIFLANNTVTYAILIGFTLYAALLSRLSLSYILKSLKPVWILILFTVVLHIFITKGGTVYFQWGWFTVEEQGVRQAIFISLRLGLLILISSLLTLTTSPIDLTEGLERLLGPLGKIGIPVHDIALMMSIALRFIPTLMEETDKIIKAQTARGANFTSGSLVRRAKNLIPIAIPLFVSAFRRAEELALAMEARGYRGGVGRTRLNKLTFTWRDGIVAVVSVILVIVIGWWRT | Function: Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29554
Sequence Length: 26... |
A5N4S9 | MIKDITIGQYVPGDSFIHKLDPRVKILISLIYIVDLFIVNSFKGYIFIVVFTLISILVSKVQFTYIYKGLKPIFILVLITAVLNIFMTGGANPPLFKWKFLVVYREGLIMAAFMALRLVFLIIGTSLLTLTTSPIELTDGIEKLLKPVSKIGVPSHELAMMMTIALRFIPTLMDETDKIMKAQIARGADLESGNLIQKAKNLVPILVPLFISSFRRADELAMAMEARCYRGGDGRTRMKELKLSNRDFIASLCALVLVCISILSRIWWGK | Function: Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30352
Sequence Length: 27... |
B0TC89 | MLKDITLGQYVPLDSPVHRLDPRTKVIATLLFSIALFLLPTLRSVTLAGLPIIIAIVATRLPIHYILRGIKPLWIFIVFTLLVHLLSTPGETAVRLGPFAITWEGLRQGAMVSQRLIWLYAATSLLTLTTSPIALTDGLELLLSPGKRIGLPVHEFAMMTSIALRFIPTLIEETEKIMKAQSSRGADFDSGSLVARVKSLVPLMVPLLLSAFRRADELAMAMEARCYRGGEGRTRMRPLVMSGKDYAVTVAVSGVFILICLWKKAL | Function: Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29288
Sequence Length: 26... |
A8YXN4 | MMGLRKMCRGSLMSKIIIGRYIPGDSLVYKMDPRGKLLITILFIWAIFLANNPITYAIITFFCFLAIIATGLKARVFWNGVKPLIGLIFFTSLLQLFFMTGGHVFWHWWIFSISSYGVENAIYIFIRFTLIILISTVMTVTTMPLEIADAMEWLLKPLKIFKVPVDEIALVISIALRFVPTLFDETLKIMNAQRSRGADFNDGGLIKRAKAIAPILVPLFIHSLETAIDLSTAMESRGYRGSAGRTKYRVLNWSKYDLISLAYFILLVGLLLIFRTH | Function: Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31504
Sequence Length: 27... |
P38248 | MQFKNALTATAILSASALAANSTTSIPSSCSIGTSATATAQADLDKISGCSTIVGNLTITGDLGSAALASIQEIDGSLTIFNSSSLSSFSADSIKKITGDLNMQELIILTSASFGSLQEVDSINMVTLPAISTFSTDLQNANNIIVSDTTLESVEGFSTLKKVNVFNINNNRYLNSFQSSLESVSDSLQFSSNGDNTTLAFDNLVWANNITLRDVNSISFGSLQTVNASLGFINNTLPSLNLTQLSKVGQSLSIVSNDELSKAAFSNLTTVGGGFIIANNTQLKVIDGFNKVQTVGGAIEVTGNFSTLDLSSLKSVRGGA... | Function: Required for proper cell wall integrity and for the correct assembly of the mannoprotein outer layer of the cell wall. Important for apical bud growth.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inosi... |
P38728 | MEGRKSEDEKNEAALACDVFESSNAKLPKNVFRSSFTWYCYEVINRSAFHIWLLLCLTLIVGWKVFSGIGGRRPSDSNMDGPQTKHKRNPGFLRRHSTIVILVISLAVSFSWEAFKMYRERTFGKQITQFAKEIIKSAPSTDMESWDRVAADFNSYMYENKLWNTEYFFC | Function: May be involved in cell wall organization and biogenesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19812
Sequence Length: 170
Subcellular Location: Membrane
|
Q05902 | MLLCNRKVPKTLNTCFILHIFTLLTLGVLVSGMPSKMVSFASQETLQRINNLLRGSANRDVDIIAEYLKKDDDDDGGDKDHHNIDIDPLPRRPSLTPDRQLLKVGLHGAISSDLEVCSNLTINEVLLKFPGSNAADAAVTQALCKGMVNFFNSGIGGGGYVVFSGKDDEDHLSIDFREKAPMDSHKFMFENCSLCSKIGGLAVGVPGELMGLYRLFKERGSGQVDWRDLIEPVAKLGSVGWQIGEALGATLELYEDVFLTLKEDWSFVLNSTHDGVLKEGDWIKRPALSNMLMELAKNGSVAPFYDPDHWIAKSMIDTVA... | Function: Catalyzes the transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH. Plays a role in the turnover of the vacuolar GSH, serving as an alternative nitrogen s... |
Q99252 | MTHITLGQAIWASVRPIIKIYLIIGVGFGLCKMNILTVQATRSISDIVLTILLPCLSFNKIVANIEDNDIKDVGIICLTSVILFATGLGFAFIVRSVLPVPKRWRGGILAGGMFPNISDLPIAYLQSMDQGFIFTEAEGEKGVANVIIFLAMFLICVFNLGGFRLIENDFHYKGDDDEENTLTNDDSAQQPTQPIEGNSSSSSNQDILKEPNESTVPNSSQASYISEKNKKEKTELSVPKPTHTAPPAIDDRSSNSSAVVSIDSITHSLRTNHVDAQSVSELNDPTYRTRSQPIAYTTESRTSHVHNNRRNSITGSLRSI... | Function: May be involved in cell wall organization and biogenesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68015
Sequence Length: 613
Subcellular Location: Endoplasmic reticulum membrane
|
Q06200 | MVMSRIRDTIARPFQNLTALEKVVQWLRLGTTLLIISFGLALTVGPLSSPRTLYMSRLDTYSADITTGLFTVLRESMEQSTSTEENNGVGLTTSELYILTAYTESQIKNVPQYITVSLYGRCDSTYTMVEVFDSEGNMHSVKNSTTKSTCSSIGTDYLFDYREVLESLGLDIILDYAYNKIGSQQAESSAYTTYMRSLKHKKANVLHLLYAVISFQVCMLFFMIWYYYIKGRFMNALKERALVHINSLLSLVVFIGGLISSISLAWVNYTIQSRINTELEAFGFSYHLGVTWFALLWCFAGLISVSCLAWSGLEWCISDN... | Function: May be involved in cell wall organization and biogenesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50328
Sequence Length: 448
Subcellular Location: Membrane
|
Q3IZ90 | MTQKDSPWLFRTYAGHSTAKASNALYRTNLAKGQTGLSVAFDLPTQTGYDSDDALARGEVGKVGVPICHLGDMRMLFDQIPLEQMNTSMTINATAPWLLALYIAVAEEQGADISKLQGTVQNDLMKEYLSRGTYICPPRPSLRMITDVAAYTRVHLPKWNPMNVCSYHLQEAGATPEQELAFALATGIAVLDDLRTKVPAEHFPAMVGRISFFVNAGIRFVTEMCKMRAFVDLWDEICRDRYGIEEEKYRRFRYGVQVNSLGLTEQQPENNVYRILIEMLAVTLSKKARARAVQLPAWNEALGLPRPWDQQWSLRMQQIL... | Function: Radical enzyme that catalyzes the transformation of (2R)-ethylmalonyl-CoA to (2S)-methylsuccinyl-CoA. Is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for R.sphaeroides growth on acetate as sole carbon source. Is highly specific for its substrate, ethylmalonyl-CoA, and accepts ... |
Q49115 | MSAQASVAEVKRDKPWIIRTYAGHSTAAESNKLYRGNLAKGQTGLSVAFDLPTQTGYDPDHELARGEVGKVGVSIAHLGDMRALFDQIPLAQMNTSMTINATAPWLLSLYLAVAEEQGAPLAALQGTTQNDIIKEYLSRGTYVFPPAPSLRLTKDVILFTTKNVPKWNPMNVCSYHLQEAGATPVQELSYALAIAIAVLDTVRDDPDFDEASFSDVFSRISFFVNAGMRFVTEICKMRAFAELWDEIAQERYGITDAKKRIFRYGVQVNSLGLTEQQPENNVHRILIEMLAVTLSKRARARAVQLPAWNEALGLPRPWDQ... | Function: Radical enzyme that catalyzes the transformation of (2R)-ethylmalonyl-CoA to (2S)-methylsuccinyl-CoA . Is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for M.extorquens growth on one- and two-carbon compounds such as ethylamine, methanol or ethanol as sole carbon source . This ... |
P56551 | MMKRLLGLVMLLLFTCTLLTGCNTARGFGEDIKHLGNSISHAAS | Function: Acts as antidote to the effect of entericidin B.
Location Topology: Lipid-anchor
Sequence Mass (Da): 4736
Sequence Length: 44
Subcellular Location: Cell membrane
|
P0ADB6 | MMKRLIVLVLLASTLLTGCNTARGFGEDIKHLGNSISRAAS | Function: Acts as antidote to the effect of entericidin B.
Location Topology: Lipid-anchor
Sequence Mass (Da): 4359
Sequence Length: 41
Subcellular Location: Cell membrane
|
P56550 | MVKKTIAAIFSVLVLSSVLTACNTTRGVGQDISEGGSAISGAGTKAQQ | Function: Plays a role in the bacteriolysis. Is activated under conditions of high osmolarity by the factor sigma S. Entericidin A functions as an antidote.
Location Topology: Lipid-anchor
Sequence Mass (Da): 4767
Sequence Length: 48
Subcellular Location: Cell membrane
|
P0ADB9 | MVKKTIAAIFSVLVLSTVLTACNTTRGVGEDISDGGNAISGAATKAQQ | Function: Plays a role in the bacteriolysis. Is activated under conditions of high osmolarity by the factor sigma S. Entericidin A functions as an antidote (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 4810
Sequence Length: 48
Subcellular Location: Cell membrane
|
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