ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8TUQ0 | MTIRALVVDDSALIRKVLSDILNEDPKIRVVGTAVNGKDGLEKVIKLRPDVVLLDNVMPVLDGLKTLARIMKEQPTPVVIVSALGERAEEITLTAFEYGAVDVIEKPSGILSQSMPEMAEEICRKVRTAPKANLKNLECMRDSEPLNPEKRETKENRVLKKAAPRNILAIGASTGGPRALEKLICSLPAELPAAVLVVQHMPPGFTASLSKRLDSKSALRVKEAQEGDRVEDGTVLIAPGNYHMEIVRNKVNSLEEETIHLSCGPKELGSRPSVNVLFRSIASVYGSRVISLVLTGMNCDGADGAEEIKKMGGKVIAEAR... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q2FQU2 | MIRVLLVDDSPVTLMVLQSILEKEPDISVIGQAKNGKEAIILASRLAPDIITMDINMPDLDGFATTRQIMERTPVPIIIVSGIDNLEEIRASFRAVEAGALAVFRKPPAYGDPDYEEAVSEFVNAIRTYSEVKVIRRRSNHLKVPKPEASTIQIPFQIHQDIRVIVIGASTGGPQVIQEIISNLPLGFPLPLVLVQHMSPGFIEGLALWLTESTGFPVSIAREGEVLQPGKLYVAPDGIHTGVTSDLRFSFSISPPEHNLRPSVSYLFRSAAKNLGSHVLGILLSGMGSDGAEELLQIRQNGGCTIIQDRDSSFVYGMPG... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q1D225 | MGKKVSVLVVDDSLICRQLICEALSKDPDIEVVGTCADGKQAVEMTKELRPHVITMDVDMPVMDGLTATEHIMAECPTPILVLTADPRSQAPELTYRALELGALALQIKPAIDAGPDAWNLVREIRLLSSVRVIRHLRRPQRGPLLPPRVATSVLPAVSMGVVVVAASTGGPQVLFKMLSELPADFPAPIVIVQHINAAFAESLAGWLAGASKLKVRLAQDGEPLMPGHVLIAPPGQHTVIPFRGRVGIKLGVERDGHMPSGTVLLESAARTYGRRAVGLVLTGMGADGADGLLAIKQAGGLAVAQNEESCVVFGMPGAA... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q6LTM2 | MTVKVLVVDDSSFFRRRVSEIINADPRLEVIGNAVNGKEAVELVKKLQPDVITMDIEMPVMDGITAVREIMKVLPTPILMFSSLTQEGAKATLDALDAGALDFLPKKFEDIARNRDEAISLLQKRVGELARKRMFMRRPLRTTPAVAPASRYSAPVNAALTREAALTTAARTTAARVTPTSTTRQTMHSAVAAKPMARFKASGKKYQLMAIGTSTGGPVALQKILTQLPANFPYPIVLVQHMPATFTAAFAARLNNLSKISVKEAEDGDTLRAGVAYLAPGGKQMMLEGRPGSARLRILDGGDRMNYKPCVDVTFGSAAK... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q9I6V9 | MPISVLVVDDSALIRSLLKEIIQADPELRLVGCAPDAFVARDLIKQHAPDVISLDVEMPRMDGLTFLDKLMKARPTPVLMISSLTERGSEATLRALELGAVDFIAKPRLGIAEGMQAYAEEIRAKLKTVARARLRRRAADAPAPPESAAPLLSTEKIIALGASTGGTEALKEVLLGLPAHSPGVVITQHMPPGFTRSFAERLDRLTRLSVSEARDGDRILPGHALVAPGDHHMEVQRSGANYVVRLNRQAQVNGHRPAVDVMFESLARCAGRNLLAGLLTGMGKDGARGLLAIRQAGGYTLAQDEATCVVYGMPREAVEL... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q1MC14 | MAKKIRVLIIDDSASIRQTLTHVLEQDPDIEIMAVASDPFMAARKLQEEIPDVITLDVEMPRMDGITFLRKLMSQRPIPVVMCSSLTEAGSETLLQALEAGAVDVILKSKIGAADSLSDDAMRIREVVKSASHARLSNVRRAAGTIRSASVEGPAKKLTADVMLPPPTGRAMAKTTEMVVCVGASTGGTEALREFLEELPANAPGMVIVQHMPEKFTAAFAKRLNGLCEVEVKEAVDGDPVLRGHVLIAPGDKHMLLERQGARYYVSVKTGPLVSRHRPSVDVLFRSAARSAGSNAMGIIMTGMGDDGARGMLEMHQAGA... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q8TLH2 | MSDDILFVSNGNGKAIFLTSRAVLVKSFCSLSKTCSFKDSCQSCEIVDAAKSYLMGKKSDLNVKSLDGELSAGIGEYKIGKNVLLKVMGLGSCIGVILSDVSTGICGIAHVLLPGASNSGEAKYAETAIENMFEDMIRMGARKNRITAKFAGGAQVFKHMSLDILKIGDRNAISVEETLVKRNIPILAKDVGGEVGRNVIFNPVDGSMIVKYTKGEVLWL | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 23520
Sequence Length: 220
EC: 3.5.1.44
|
Q1GM98 | MDKVEVSELHVRIGQVKIGSPGQVLTAILGSCVGIGFFFPQRQIYGLAHCLLSQSSSQPVASSAAQTGRTREDGQLVGNGRHVDKAIESLLKMMDIQDEERRQLRVVLAGGANMSMPFDTPPSQLVGSVNAKFARQAIRSAGLRLLGDDLGGLNGRRISINCDSGEYDIQQIPRLGGTV | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 19173
Sequence Length: 179
EC: 3.5.1.44
|
Q8EEQ1 | MENMAFNQRTVVMIGPGEHYVTAKNEVIKTLLGSCVAVCLYDPKAQVIGMNHFLLAADRRKFTHFLDSRAGYYGVHAMEILINAMLKRGAQRKYLQSKIFGGANVLSLCADNILNHYDIGGMNIDFVRHFLQRERIPIISEDIGGHCGRVIYFDPTDYSVYRSLIEHKYEEIASLQDEEYRYFNQASEDIHSSGVPVVIWSD | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 23028
Sequence Length: 202
EC: 3.5.1.44
|
Q2LSL4 | MNSKAIKPSCEYFLLPGYIFMSPEPYLISTVVGSSVAVALWDADSKLGGMLSFLYPFRESSAESTAIYGNVAITYMVRMFREEGAKKKNLRSQIFGGAESDCCEADQIAHENVKTARSVLKKHGIKVISEDVGGRLGRKIVYNTFQNEALIYKVNTLRNSDWYPYDGQGRQA | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 19184
Sequence Length: 172
EC: 3.5.1.44
|
Q47GX8 | MSAAPSELHEVFLNPGEFHFGESNTRISTLLGSCVSITLWHPRKRIGGMCHYMLTERKRPPNAALDGRFGSEAFELFLQHVAAAGTRPGEYQAKLFGGANMLTGPTGKQMDIGPRNVALGRQLLAANHIALMVEHVGGSGRRKLHFDVWSGDVWLAFPQGADAEIRNAHG | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 18515
Sequence Length: 170
EC: 3.5.1.44
|
Q747R4 | MSRIVSVGISEFKIASAPTILMTYGLGSCVGIALHDPVALTGGLAHTLLPAPVRGMDSMVKSAKFTCWAVDLMVEELIKCGCVAERLVAKLAGGATMFEPQHRTTHSGIGERNVTAAKEALERRGIPLVASDTGDDYGRSLEFNTVTGVITVRALQRPIKRM | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 17253
Sequence Length: 162
EC: 3.5.1.44
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A5G222 | MTPVAAASPDYARRINIVQGEHRVEHDPEAVLCTILGSCVAACLWDPGASVGGMNHFLLPGDAHAQAGGGGAAMRYGAYAMELLINDLLRHGARRDRLKAKLFGGACLMKGLTDIGRLNADFAERFLAAEGIEIVGGSLRGERGRRIQFWPVSGRARQTLLAADQPALLRAEPDLRTLRAPPPSGAVELF | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 20278
Sequence Length: 190
EC: 3.5.1.44
|
Q5WFS5 | MTKGETISIGEWKVVKGEGVLRTCGLGSCIGIVLYDQERVIAGMVHVMLPDSTKARKGANPWRYADTAIASLQAELKKQGARKLCAKMAGGAQMFKHAVKREFMQIGERNAAAARETLARLGITLVAEDIGGTKGRTIQYDVKTGELAVRTVHHGQMIL | Function: Deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity).
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutam... |
O29224 | MGSEILVGIGEFRVAKGAVLKTIGLGSCVGIALYDPKLRLGGLAHVMLPQSGNGTKRSAKYADHAVEMMTEAMERLGSDRKRIVAKMAGGAQIFKHMTMDMLRIGDRNAEAIRTILRDYGIRIVSEDLGGDEGRTVYFFTNDGRMLVKYSRGGELWI | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 17196
Sequence Length: 157
EC: 3.5.1.44
|
P40404 | MSTTEAVVIKVGIADVKIARFPDTIRTSGLGSCVGLVLYDKEKQTAGLVHVMLPDSTLSKTAELNRAKYADTAVQTTIDMLIEAGCRKFALKAKLAGGSEMFKFKSTNDLMKIGPRNVLAIKEQLSLFNIPIISEDTGGSSGRTIEFEPKSCMLHIRTVKQGEKTI | Function: Deamidates 'Gln-593' and 'Gln-594' of the chemoreceptor McpA. In addition, deamidates other chemoreceptors, including McpB and McpC. CheD-mediated MCP (methyl-accepting chemotaxis proteins) deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kin... |
Q6MJE9 | MLPVEHHVRIGQILIAENGEVLKTVLGSCVGIALVWRRQNKWALAHCLLPYPETFKEDKEARYVSQTIPRMLERMGATMADVSELEAIVAGGGRMMDGDKNYIKFVVGDENLKAAKAVLEKHRIRIVAFEPGGEQGTKMRIAGDGDYSIEKLPKTA | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 17304
Sequence Length: 156
EC: 3.5.1.44
|
O51551 | MLNHFNFKLKRDVTIIVPGEAFVSNKRVISTILGSCVAVVLCDESNNLIGMNHYVLVKSDLDISPDQRGRYGIYAIPMLINAMLENGASKSNLKAKLFGGTNFMAKGSVKVGLENSEFAVNTLNKYRIPILAKDFDQSKSRKIFAFPENFKVIVEYPDGTKVF | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 18141
Sequence Length: 163
EC: 3.5.1.44
|
P07364 | MTSSLPCGQTSLLLQMTERLALSDAHFRRISQLIYQRAGIVLADHKRDMVYNRLVRRLRSLGLTDFGHYLNLLESNQHSGEWQAFINSLTTNLTAFFREAHHFPLLADHARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVLEKARSGIYRHEELKNLTPQQLQRYFMRGTGPHEGLVRVRQELANYVDFAPLNLLAKQYTVPGPFDAIFCRNVMIYFDQTTQQEILRRFVPLLKPDGLLFAGHSENFSHLERRFTLRGQTVYALSKD | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32849
Sequence Length: 2... |
Q9KCB8 | MADDYNWFIEQVKERTGIDLNLYKETQMKRRLIALREKRNYQDFRSYFTAMTNDDTLQNEFLERMTINVSEFFRNRKRWDVLDETIIPQLLKEKKRLKVWSAACSTGEEPYTLAMILQKHLPLKDVSILATDIDRAILQQAKVGYYTERSLKEIPVELKEGFFTKDRAGYYVSNELKQAVTFKQHNLLADRFERDCDLIVCRNVLIYFTEEAKRELYHKFSEALRPGGVLFVGSTEQIFEASKYGLETNETFFYRKV | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30546
Sequence Length: 2... |
B0R4J5 | MTDFQTLLEFIETETGFATSYYDESYLDRRVSARMRRRGVEEYAGYLTLLEEDDDDERAELLDTLSVNVTEFFRDEKVWTALRDVLLELADTVRSIDIWSAACADGREPYSLAMLALDAGLDPRNVSILATDIDEDALARARAGRYESTRTADISDQLGFLDNPQEYVDREGDRAFVVNDRVKDLVTFERHDLITGDPKSGFDLVACRNVCIYIDKQYKLPILDTVSKSLREGGHLVLGQTETLPGEVKERFEAEDPRIRIYSRVADT | Function: Catalyzes the methylation of several Htr transducer proteins (methyl-accepting chemotaxis proteins) to form gamma-glutamyl methyl ester residues.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30533
Se... |
Q9XDE8 | MIPDLEKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKKYITFGEFFKHLKKDAVLLDEFISLITINVSSFFRNRNRWDALEKQVLPRLLEDSRGKLRVWSAACSSGEEPYSLAMMMERSVGTRHYDILATDLEPAILKRAVIGEYQSRQMEELSEQERHTAFVEKGDTYQILPKYRKSIRFRRHDLLTDYYEKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGVLFIGGSEQILNPADYGLATLNNFFYIKT | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30820
Sequence Length: 2... |
Q2KCH9 | MIYSDAGIFLNETKASLVYSRLSKHIRNLGLSGFREYCELVASPAGAAARREMLSHLTTNFTRFFRENHHFEHLRDHVLPELLQRARSGGRVRIWSAASSDGQEPYSIALTVLSLMPNVADYDFKILATDIDPKILAIARAGAYDESALETVSPAMRKQWFSEVEVQGRRKFQVDDRVKRLITYNELNLMAQWPFKGKFDVIFCRNVVIYFDEPTQMKIWQRFAGLLPEGGHLYIGHSERVSGEAKHVFDNIGITTYRYTTKGLGRKA | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30638
Sequence Length: 2... |
Q9WYT5 | MQEERSEKKIGPFKFQSNFEWKEFPQEEFEWFVKEVEKRFGLNLSSYKPQRVKRRTELLLRKYNVGYREYLNMLIKDKKYLDEFMDKMTINVTEFFRNPEKWWELRDEIIPLIAKNSLRMKFWSAGCSSGEEPYSLAILVHELNLSYKTRILATDIDIGVLRRAQEGIYEERAFVSTPKEYLEKYFEKLPDGRYRIKDSVKKIVEFKRHDLLKDPFEKNFDLIVCRNVVIYFEPEAKNELYRKFAESLKPGGFLFVGNTERIFNYKELGFEIYKPFIYRKVK | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34225
Sequence Length: 2... |
P37599 | MSLQQYEILLDSGTNELEIVKFGVGENAFGINVMKVREIIQPVEVTSVPHSHQHVEGMIKLRGEILPVISLFSFFGVEPEGSKDEKYIVTEFNKRKIVFHVGSVSQIHRVSWEAIEKPTSLNQGMERHLTGIIKLEDLMIFLPDYEKIIYDIESDSGVDTYNMHTEGFDERRTDKKLIIVEDSPLLMRLLQDELKEAGYNNIASFENGKEAYEYIMNLAENETDLSKQIDMIITDIEMPKMDGHRLTKLLKENPKSSDVPVMIFSSLITDDLRHRGEVVGADEQISKPEISDLIKKVDTYVIE | Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl-accepting chemoreceptors to the central two-componen... |
P21227 | EQCGRQAGGATCPNNLCCSQYGY | Function: Defense against chitin-containing fungal pathogens.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 2424
Sequence Length: 23
EC: 3.2.1.14
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Q9D9G3 | MADFDEIYEEEEDEERALEEQLLKYSPDPVVVRGSGHVTVFGLSNKFESEFPSSLTGKVAPEEFKASINRVNSCLRKNLPVNVRWLLCGCLCCCCTLGCSMWPVICLSKRTRRSIEKLLEWENNRLYHKLCLHWRLSKRKCETNNMMEYVILIEFLPKTPIFRPD | PTM: Palmitoylation in the CHIC motif is required for membrane association.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19282
Sequence Length: 165
Subcellular Location: Membrane
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O81862 | MSSTKLISLIVSITFFLTLQCSMAQTVVKASYWFPASEFPVTDIDSSLFTHLFCAFADLNSQTNQVTVSSANQPKFSTFTQTVQRRNPSVKTLLSIGGGIADKTAYASMASNPTSRKSFIDSSIRVARSYGFHGLDLDWEYPSSATEMTNFGTLLREWRSAVVAEASSSGKPRLLLAAAVFYSNNYYSVLYPVSAVASSLDWVNLMAYDFYGPGWSRVTGPPAALFDPSNAGPSGDAGTRSWIQAGLPAKKAVLGFPYYGYAWRLTNANSHSYYAPTTGAAISPDGSIGYGQIRKFIVDNGATTVYNSTVVGDYCYAGTN... | Function: Can hydrolyze glycol chitin and chitin oligosaccharides (e.g. N-acetylglucosamine) (GlcNAc)4, (GlcNAc)5 and (GlcNAc)6 . Hydrolyzes N-acetylglucosamine oligomers producing dimers from the non-reducing end of the substrates .
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-bet... |
Q9FRV0 | MRSLAVVVAVVATVAMAIGTAHGSVSSIISHAQFDRMLLHRNDGACQAKGFYTYDAFVAAANAFPGFGATGSTDARKRDVAAFLAQTSHETTGGWATAPDGAFAWGYCFKQERGAAADYCTPSAQWPCAPGKRYYGRGPIQLSHNYNYGPAGRAIGVDLLRNPDLVATDPTVSFKTALWFWMTAQAPKPSSHAVITGKWSPSGADRAAGRAPGFGVITNIINGGLECGHGQDSRVADRIGFYKRYCDILGVGYGDNLDCYNQRPFA | Function: Defense against chitin-containing fungal pathogens. Binds the hyphal tips of fungi and degrades nascent chitin.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 28302
Sequence Length: 266
EC: 3.2.1.14
|
Q6YXN5 | MKLAYWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTASIVDRHVLARGSQEKVVDNINRKDKEERPDLIVLTPTCTSSILQEDLQNFVDRASTTSNSDVILADVNHYRVNELQAADRTLEQVVRYYLEKARRQGTLDQSLTKEPSANIIGIFTLGFHNQHDCRELKRLLQDLNIKVNKVIPEGGSVKDLQSLPKAWFNLVPYREIGLMTAIYLEKNFGMPYVSITPMGIVDTAECIRQIQKHVNNLIPNKKVDYEPYIDQQTRFVSQAAWFSRSIDCQNLTGKKAVVFGDATHAASITRI... | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophy... |
P29683 | MKPLKLKRLIMENNKSHATNLSLGGPFQGNCMPINQYFSKNQPNRGSSSSEKRSSLLPLWESKNAADGFSIVSHNVLLDGATTILNLNSFFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNALGVMIFAEPRYAMAELEESDISAQLNDYKELKRLCLQIKQDRNPSVIVWIGTCTTEIIKMDLEGMAPRLETEIGIPIVVARANGLDYAFTQGEDTVLSAMALASLKKDVPFLVGNTGLTNNQLLLEKSTSSVNGTDGKELLKKSLVLFGSVPSTVTTQLTLELKKEGINVSGWLPSANYKDLPTFN... | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophy... |
Q20EX8 | MRNTVLNTLNAFPTQLGSNKSTLSSKIFHSYLGVLRPPTPLNTSMEVLGEGAHQNREAKRSSLRFEFCSALKECQKGKVPFGSSLRLEAAENLTFECETGNYHTFCPISCVRWLYQQIADSFFLVIGTKTCGYFLQNAMGVMIFAEPRYAMAELEEGDIAAQLNDYKELKRLCLQIKHDRNPSVIVWIGTCTTEIIKMDLENLAKLIEAELKVPIVVARANGLDYAFTQGEDTVLASLVNRCPSSHESSLDSMKLPSGGREKQINDVNTSKPEGYLSEVISLTSNGDDINKKSCTKPVPKKSLVLFGSVPNSVQTQLTLE... | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophy... |
C4QXE9 | MVKESKFSYNSKDEKKYSLGKTFRGDIFNVPETHDMVRSLFDPTVKKSVSDYLIVLSLFINGIVYYYSPVTWRIPVFIVLYSFWRLGYNLGIGILLYKQSKSHSMFHWLKQIQINGGWAKKFVELELSSKLNAQQLNSVPDEFKTWIVFRSLVNLILMNDFTTYMCLVFACSDGAFNQSLSLIFLRWVLGISFFIFNIIVKLNAHLIVKDYAWYWGDFFFRLHNNEELIFDGVFDLAPHPMYSIGYAGYYGCALMTKSYTVLIMSIFGHLLQFLFLNYVETPHIEKIYGDDNLSENTISVNKRDDSVFIGTGGKPLVMLT... | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glyc... |
B0D4E6 | MTSSQSFLRQRKPQANDETESELHNTPEPTKQDVVWGKTPGGEVFRVPTTHDVITTLFNPRYKKSHLDLLNLTLLGFQLVLFFILPRRASQIFFLFYFAFWRGAYDAGLGWVLTKQSKKKWIVREVQRLGWLDEKRRPAVRNWIRKQLADKMGKDYSFDDLPLEYNTWLLFRQAVDVILVNDFLSYCMFAFSCFRVPEGLSVLALLILRRWLGGFLLIAFNLWVKTEAHNVVKDYGWYWGDVFFQRGNLVFDGVFELAPHPMYSVGYAGYYGLSLIAGSYAVLFVSLAAHAAQFAFLVFFENPPVAASYKKISRHVSQPS... | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glyc... |
C5DGB6 | MIKERKPSKSRAPGKGHKQIPGVAKESQPIARTRTGNVEFTPAKTHDMVRSLFDPTLKKSFLECWISLAILSNVVLCYFMATKFGASFTKKFFLWQYVFWRLCYNVGIGVVLHFQSNYETLTNFAKMRSLFSKKNQQWLARFCRFEIESKMPNTYCLEEYPEEFNVWLLFRQFVDLILMQDFTTYILFVVLSIPKTVLSSHTVSFALGVIMILFNVWVKVDAHRVVKDYAWYWGDFFFFQDSKLVFDGVFNVSPHPMYSIGYMGYYGLSLISGDYKVLLVSIGGHLLQFLFLKYCENPHIEKIYGSDAVENDNAHIDELL... | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glyc... |
A8PRN6 | MKAESSSMAEWHASEGLRQRYALDEAKQGDASRKESVQDELTDTKDDPAAEAMGGSPSMVLGRTPDGRLFHVIDTPDMVTSIFRLDRPKAPLDILTLVLLLWQVCLFCVLPRKQAQVFFAVYFAFWRIMYNVGLGYVLTKQSRSRWIVRMLDSSGWLDACKNPRMHAWVQYHFKTKLGASSQRIAAAPIDFQAWILFRSVVDVILLNDVTAYAFFALSNIQGLGEHGVLLFVIRWLLGLLLLAFNAWVKLDAHRVVKDYAWYWGDCFFLCLQKLKFDGVYEVAPDPMYSIGYIGYYGLSLLTGSYAVLYVSLAAHASQLL... | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glyc... |
Q7SAJ6 | MSSSAADPFAARLNSDVRQRHPTASATSKNVEGTSQQKQQQQQQQSEANAAASRVKKTYGKTPDGTVFVVPTTHDMVTQLLDPREPKNLSDVAVLAIIALHFLAAYYLPWGVKRPLFAAIFMFWRLAYNVGIGYLLTIQSKYKLLVTWAKRWKLFENPATGKNPRPWLYNLLKKELETKIPQDYKFEEAPIEYNTWLTFRRVVDLILMCDFISYCLFAIVCAHKPDGEGLFMCFARWAAGITLVGFNLWVKLDAHRVVKDYAWYWGDFFYLIEQELTFDGVFELAPHPMYSIGYAGYYGISMMAASYDVLFISIIAHAAQ... | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glyc... |
B6HJA3 | MDQGLSTGAHQDTDGLRERNTRVDSTVGREALTAVGEGEIKDKDGKASKTFGRTPDGTVFTVPQTHDMVSQLLLPSEPKNFGDLVVLILLAGHIMFLWALPAGAKIPIFAVTYLFWRLAYNAGIGWLLHNQSHHKTLIRWAEKTKVFVNPATGENPHPKLYNWIKRELETKIPQDYSFDNAPIEYNTWLVFRRLVDLILMCDFTSYCLFAIACGHQPVDESILMTVLRWSAGIVLVLFNLWVKLDAHRVVKDYAWYWGDFFYLIDQELTFDGVFEMAPHPMYSVGYAGYYGISLMAASYKVLFISIIAHAAQFAFLVLVE... | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glyc... |
O74787 | MTNQIPSASSAADFGSSKSTSVDAVPNMDKSSSVRRKNIDSNGLQQTNQIEQAESSLNAEADHSEPERYGCTPSGKVFLLPKEQENRRSILETVDPRFSKTPWDWIVISSILAQVLLFFMTTGAVRRYSMMLCFFFWRISYDAGIGFLLHMQSNHRKVVTWISDFGFFDKENHPKLYDLTKKQLISKMDSSYNYDTSPLEFNSWLVFRHFVDLILMCDFCSYILMGLAWTCWPKVNIILQFLRIFGGIALIVFNYWVKMDAHRVVRDYAWYWGDFFFLLRSSLVFNGVFELAPHPMYSVGYAGYYGMSLLTGSYAVLFAS... | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glyc... |
Q9Z0E2 | MPSLPAPPAPRLLLGLLLLGSRPASGTGPEPPALPIRSEKEPLPVRGAAGCSFGGKVYALDETWHPDLGEPFGVMRCVLCACEAPQWARRGRGPGRVSCKNIKPQCPTLACRQPRQLPGHCCQTCPQERSNLDPQPAGLVFEYPRDPEHRSYSDRGEPGVGERTRADGHTDFVALLTGPRSQAVARARVSLLRSSLRFSVSYQRLDRPSRVRFTDPTGNILFEHPATPTQDGLVCGVWRAVPRLSVRLLRAEQLRVALVTSTHPSGEVWGPLIWQGALAAETFSAILTLEDPLQRGVGGIALLTLSDTEDSLHFLLLFRG... | Function: Dorsalizing factor. Key developmental protein that dorsalizes early vertebrate embryonic tissues by binding to ventralizing TGF-beta family bone morphogenetic proteins (BMPs) and sequestering them in latent complexes.
PTM: Cleaved by tolloid proteases; cleavage participates in dorsoventral patterning during e... |
Q91713 | MQCPPILLVWTLWIMAVDCSRPKVFLPIQPEQEPLQSKTPAGCTFGGKFYSLEDSWHPDLGEPFGVMHCVLCYCEPQRSRRGKPSGKVSCKNIKHDCPSPSCANPILLPLHCCKTCPKAPPPPIKKSDFVFDGFEYFQEKDDDLYNDRSYLSSDDVAVEESRSEYVALLTAPSHVWPPVTSGVAKARFNLQRSNLLFSITYKWIDRLSRIRFSDLDGSVLFEHPVHRMGSPRDDTICGIWRSLNRSTLRLLRMGHILVSLVTTTLSEPEISGKIVKHKALFSESFSALLTPEDSDETGGGGLAMLTLSDVDDNLHFILML... | Function: Potent dorsalizing factor. Has potent axis-forming activities including the ability to recruit neighboring cells into secondary axes. Regulates cell-cell interactions in the organizing centers of head, trunk and tail development.
PTM: Cleaved by bmp1; cleavage participates in dorsoventral patterning during ea... |
P40685 | MTIRHHVSDALLTAYAAGTLSEAFSLVVATHLSLCDECRARAGALDAVGGSLMEETAPVALSEGSLASVMAQLDRQIQRPAPARRADPRAPAPLADYVGRRLEDVRWRTLGGGVRQAILPTGGEAIARLLWIPGGQAVPDHGHRGLELTLVLQGAFRDETDRFGAGDIEIADQELEHTPVAERGLDCICLAATDAPLRFNSFLPKLVQPFFRI | Cofactor: Binds 2 Zn(2+) ion per subunit. The Zn(2+) bound by the N-terminus is required for anti-sigma function, the function of the Zn(2+) bound by the C-terminus is unknown.
Function: Anti-sigma factor that inhibits the activity of the extracytoplasmic function (ECF) sigma-E factor (RpoE), thereby indirectly regulat... |
P0AGE7 | MSEKLQVVTLLGSLRKGSFNGMVARTLPKIAPASMEVNALPSIADIPLYDADVQQEEGFPATVEALAEQIRQADGVVIVTPEYNYSVPGGLKNAIDWLSRLPDQPLAGKPVLIQTSSMGVIGGARCQYHLRQILVFLDAMVMNKPEFMGGVIQNKVDPQTGEVIDQGTLDHLTGQLTAFGEFIQRVKI | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the reduction of quinones. Acts by simultaneous two-electron transfer, avoiding formation of highly reactive semiquinone intermediates and producing quinols that promote tolerance of H(2)O(2). Quinone reduction is probably the primary biological role of ChrR. Can a... |
Q88FF8 | MSQVYSVAVVVGSLRKESYNRKVARALSELAPSSLALKIVEIGDLPLYNEDIEAEAPPETWKRFRDEIRRSDAVLFVTPEYNRSVPGCLKNAIDVGSRPYGQSAWSGKPTAVVSVSPGAIGGFGANHAVRQSLVFLDMPCMQMPEAYLGGAASLFEDSGKLNDKTRPFLQAFVDRFASWVKLNRAV | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the reduction of quinones. Acts by simultaneous two-electron transfer, avoiding formation of highly reactive semiquinone intermediates and producing quinols that promote tolerance of H(2)O(2). Quinone reduction is probably the primary biological role of ChrR . Can ... |
F4I902 | MSTSYSFLLAGRELDVFLSFSGKIALDVDFGYDLSRNGIKAFKSESWKESSFKPIDLRTLEALTESKVAVVMTSDEEVSSVGFLEELIVIIEFQEKRSLTVIPVFLTKHPLDVEKVSQIFPERAKIWRTAIAKLDNIAAQYSFSRNLAVMHGTHRIKQIADDIRLMFLSSASSDFKGLAGMDRHMKALYALLALESDEKVRTIGIWGSSGVGKTTLARYTYAEISVKFQAHVFLENVENMKEMLLPSENFEGEDLRSVNHEMNEMAEAKQKHRKVLLIADGVNNIEQGKWIAENANWFAPGSRVILITQEKSLLVQSGVN... | Function: Confers resistance to low temperatures by limiting chloroplast damage and cell death, thus maintaining growth homeostasis . Regulates steryl-esters and sterols accumulation . Limits leaf necrosis associated with virulent bacterial infection (e.g. Pseudomonas syringae pv. tomato DC3000) .
Catalytic Activity: H... |
Q7LGC8 | MEKGLTLPQDCRDFVHSLKMRSKYALFLVFVVIVFVFIEKENKIISRVSDKLKQIPQALADANSTDPALILAENASLLSLSELDSAFSQLQSRLRNLSLQLGVEPAMEAAGEEEEEQRKEEEPPRPAVAGPRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVSFEPGGANAAGSALVYRDVLKQLFLCDLYVLEHFITPLPEDHLTQFMFRRGSSRSLCEDPVCTPFVKKVFEKYHCKNRRCGPLNVTLAAEACRRKEHMALKAVRIRQLEFLQPLAEDPRLDLRVIQLVRDPRAVLASRMVAFAGKYKT... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin . Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the s... |
O88199 | MEKGLALPQDFRDLVHSLKIRGRYVLFLAFVVIVFIFIEKENKIISRVSDKLKQIPHFVADANSTDPALLLSENASLLSLSELDSTFSHLRSRLHNLSLQLGVEPAMESQEAGAEKPSQQAGAGTRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVFFQQRGASAAGSALVYRDVLKQLLLCDLYVLEPFISPPPEDHLTQFLFRRGSSRSLCEDPVCTPFVKKVFEKYHCRNRRCGPLNVTLAGEACRRKDHVALKAVRIRQLEFLQPLVEDPRLDLRVIQLVRDPRAVLASRIVAFAGKYENWKKWLS... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin . Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the s... |
Q8NCG5 | MLLPKKMKLLLFLVSQMAILALFFHMYSHNISSLSMKAQPERMHVLVLSSWRSGSSFVGQLFGQHPDVFYLMEPAWHVWMTFKQSTAWMLHMAVRDLIRAVFLCDMSVFDAYMEPGPRRQSSLFQWENSRALCSAPACDIIPQDEIIPRAHCRLLCSQQPFEVVEKACRSYSHVVLKEVRFFNLQSLYPLLKDPSLNLHIVHLVRDPRAVFRSRERTKGDLMIDSRIVMGQHEQKLKKEDQPYYVMQVICQSQLEIYKTIQSLPKALQERYLLVRYEDLARAPVAQTSRMYEFVGLEFLPHLQTWVHNITRGKGMGDHAF... | Function: Sulfotransferase involved in SELL/L-selectin ligand biosynthesis pathway. Catalyzes the transfer of the sulfate group from 3'-phospho-5'-adenylyl sulfate (PAPS) onto the hydroxyl group at C-6 position of the non-reducing N-acetylglucosamine (GlcNAc) residue within O-linked mucin-type glycans. Contributes to g... |
Q9GZS9 | MGMRARVPKVAHSTRRPPAARMWLPRFSSKTVTVLLLAQTTCLLLFIISRPGPSSPAGGEDRVHVLVLSSWRSGSSFLGQLFSQHPDVFYLMEPAWHVWTTLSQGSAATLHMAVRDLMRSIFLCDMDVFDAYMPQSRNLSAFFNWATSRALCSPPACSAFPRGTISKQDVCKTLCTRQPFSLAREACRSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREAAGPILARDNGIVLGTNGKWVEADPHLRLIREVCRSHVRIAEAATLKPPPFLRGRYRLVRFEDLAREPLAEIRALYAFTGLTLTPQ... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues and O-linked sugars of mucin-type acceptors. Acts on the non-reducing terminal GlcNAc of short carbohydrate substrates... |
Q9QUP4 | MRLPRFSSTVMLSLLMVQTGILVFLVSRQVPSSPAGLGERVHVLVLSSWRSGSSFVGQLFSQHPDVFYLMEPAWHVWDTLSQGSAPALHMAVRDLIRSVFLCDMDVFDAYLPWRRNISDLFQWAVSRALCSPPVCEAFARGNISSEEVCKPLCATRPFGLAQEACSSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREQTAKALARDNGIVLGTNGTWVEADPRLRVVNEVCRSHVRIAEAALHKPPPFLQDRYRLVRYEDLARDPLTVIRELYAFTGLGLTPQLQTWIHNITHGSGPGARREAFK... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues of keratan. Mediates sulfation of keratan in cornea. Keratan sulfate plays a central role in maintaining corneal trans... |
Q9GZX3 | MWLPRVSSTAVTALLLAQTFLLLFLVSRPGPSSPAGGEARVHVLVLSSWRSGSSFVGQLFNQHPDVFYLMEPAWHVWTTLSQGSAATLHMAVRDLVRSVFLCDMDVFDAYLPWRRNLSDLFQWAVSRALCSPPACSAFPRGAISSEAVCKPLCARQSFTLAREACRSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREQTAKALARDNGIVLGTNGTWVEADPGLRVVREVCRSHVRIAEAATLKPPPFLRGRYRLVRFEDLAREPLAEIRALYAFTGLSLTPQLEAWIHNITHGSGPGARREAFK... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues of keratan . Cooperates with B4GALT4 galactosyltransferase and B3GNT7 N-acetylglucosaminyltransferase to construct and... |
Q9NS84 | MKGRRRRRREYCKFALLLVLYTLVLLLVPSVLDGGRDGDKGAEHCPGLQRSLGVWSLEAAAAGEREQGAEARAAEEGGANQSPRFPSNLSGAVGEAVSREKQHIYVHATWRTGSSFLGELFNQHPDVFYLYEPMWHLWQALYPGDAESLQGALRDMLRSLFRCDFSVLRLYAPPGDPAARAPDTANLTTAALFRWRTNKVICSPPLCPGAPRARAEVGLVEDTACERSCPPVAIRALEAECRKYPVVVIKDVRLLDLGVLVPLLRDPGLNLKVVQLFRDPRAVHNSRLKSRQGLLRESIQVLRTRQRGDRFHRVLLAHGV... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N-ac... |
Q9H2A9 | MTLRPGTMRLACMFSSILLFGAAGLLLFISLQDPTELAPQQVPGIKFNIRPRQPHHDLPPGGSQDGDLKEPTERVTRDLSSGAPRGRNLPAPDQPQPPLQRGTRLRLRQRRRRLLIKKMPAAATIPANSSDAPFIRPGPGTLDGRWVSLHRSQQERKRVMQEACAKYRASSSRRAVTPRHVSRIFVEDRHRVLYCEVPKAGCSNWKRVLMVLAGLASSTADIQHNTVHYGSALKRLDTFDRQGILHRLSTYTKMLFVREPFERLVSAFRDKFEHPNSYYHPVFGKAILARYRANASREALRTGSGVRFPEFVQYLLDVHR... | Function: Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Required for biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Only active against terminal GalNAcbeta... |
Q7L1S5 | MQPSEMVMNPKQVFLSVLIFGVAGLLLFMYLQVWIEEQHTGRVEKRREQKVTSGWGPVKYLRPVPRIMSTEKIQEHITNQNPKFHMPEDVREKKENLLLNSERSTRLLTKTSHSQGGDQALSKSTGSPTEKLIEKRQGAKTVFNKFSNMNWPVDIHPLNKSLVKDNKWKKTEETQEKRRSFLQEFCKKYGGVSHHQSHLFHTVSRIYVEDKHKILYCEVPKAGCSNWKRILMVLNGLASSAYNISHNAVHYGKHLKKLDSFDLKGIYTRLNTYTKAVFVRDPMERLVSAFRDKFEHPNSYYHPVFGKAIIKKYRPNACEE... | Function: Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Participates in biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Has a higher activity toward carboni... |
O43529 | MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDVYSAKQEFLFLTTMPEVRKLPEEKHIPEELKPTGKELPDSQLVQPLVYMERLELIRNVCRDDALKNLSHTPVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSDAEIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRRNRTETRGIQFEDFVRYLGDPNHRWLDLQFGDHIIHWVTYVELCAPCEIMYSVIGHHETLEDDAPYILKEAGIDHLVSYPTIPPGITVYNRTKV... | Function: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-(1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-l... |
Q6PGK7 | MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDGYSAKQEFVFLTTMPEAEKLRGEKHFPEVPKPTGKMLSDSRPDQPPVYLERLELIRNTCKEEALRNLSHTEVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSKIGIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRKNRTETRGIQFEDFVRYLGDPNRRWLDLQFGDHIIHWVTYVELCAPCEIKYSVVGHHETLEADAPYILKEAGIDHLVSYPTIPPGITMYNRTKV... | Function: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-(1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-l... |
A0A1U8QH20 | MERFPRSAADAQQLLQLAELFKQSAEIIAEEWNKEDFSRIKAETNSIKSNLGSLDTARILPSPRLHEATRTVLAITGAATELVAEPYSRIQEVACQYFESRALFVAAERRIPDLLAGAGEYGLSVGEIAEATGIEERKLSRILRCLCSIHIFRQIGTDRFANNRISAALKNNEPLRAYVQLFNLDIYTASDQLPKYLLSSQGASYKVHETAWQKAVGTTKARWDWLAERVSLDEVRPKEAPYPGLPDVRHLQPGPDGKYARPELDNFGLAMVGGGKVSGAAHAYDFPWASLGDALVVDVGGGVGGFVLQLLPAYPQLRYI... | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans . The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units . Pk... |
C8V0D4 | MAILVRLFFALFVVSVYFFRVRLRLSHIPGPFLASLTNINRRQWVTTGRAHTIHTELHRQYGKVVRAGPNTVFVSDPAAIPAIYRFNEPYQKSEFYDALMPYVRGKSIPDVFATRDEHIHRTMKQPIAAIYSMSNLVSFEPYVKSTIEYFFSRLDSLFVETGKVCNFGLWLHLFASDVMGEITFSRRLGFLETGGDMENVMANNWKFFVQAAPATQMPWLDYFWKRNPLLPGSVKPNKVIEFGVARIQERLHLSEKHPDHVNSRDFLSRFIAAKEKNSQIGPDAIMTWANSNIQAGSDTTAILLSALFYHLLKNPTSLAA... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans . The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA ... |
P35522 | MSHEKNEASGNPEAQSWKAQEAMLGVKTEVSRWRAVKNCLYRHLVKVLGEDWIFLLLLGALMALVSWAMDFIGSRGLRFYKYLFAMVEGNLGLQYLVWVCYPLILILFSSLFCQIVSPQAVGSGIPELKTIIRGAVLHEYLTLRTFVAKTVGLTVALSAGFPLGKEGPFVHIASICATLLNQLLCFISGRREEPYYLRADILTVGCALGISCCFGTPLAGVLFSIEVTCSHFGVRSYWRGFLGGAFSAFIFRVLSVWVKDTVTLTALFKTNFRGDIPFDLQELPAFAIIGIASGFFGALFVYLNRQIIVFMRKKNFVTKI... | Function: Voltage-gated chloride channel. This channel is thought to ensure the high conductance of the non-innervated membrane of the electrocyte necessary for efficient current generation caused by sodium influx through the acetylcholine receptor at the innervated membrane.
Location Topology: Multi-pass membrane prot... |
Q8N5K1 | MVLESVARIVKVQLPAYLKRLPVPESITGFARLTVSEWLRLLPFLGVLALLGYLAVRPFLPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Con... |
Q9CQB5 | MVLDSVARIVKVQLPAYLKQLPVPDSITGFARLTVSDWLRLLPFLGVLALLGYLAVRPFFPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Con... |
B3RML8 | MEAIAKLIKVQLPNYLQKLPVPSSLSGFAELSPSDAIAVVFPFAVVSWLIGYSTYKFFQPKAVELPPSPKAKDTNCVNKCIDKTCKKVVHTVDIEDVGEKLVFCRCWRSKKFPYCDGSHNNHNEQEQDNVGPLIVKGKAN | Cofactor: Binds 1 [2Fe-2S] cluster.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15597
Sequence Length: 140
Subcellular Location: Endoplasmic reticulum membrane
|
P0C7P0 | MRGAGAILRPAARGARDLNPRRDISSWLAQWFPRTPARSVVALKTPIKVELVAGKTYRWCVCGRSKKQPFCDGSHFFQRTGLSPLKFKAQETRMVALCTCKATQRPPYCDGTHRSERVQKAEVGSPL | Cofactor: Binds 2 [2Fe-2S] clusters per subunit.
Function: Can transfer its iron-sulfur clusters to the apoferrodoxins FDX1 and FDX2. Contributes to mitochondrial iron homeostasis and in maintaining normal levels of free iron and reactive oxygen species, and thereby contributes to normal mitochondrial function.
Sequenc... |
B1AR13 | MGFRRLSFPTDFIFLFPNHICLPALSKPYQRREISSWLARWFPKDPAKPVVAQKTPIRLELVAGKTYRWCVCGRSKNQPFCDGSHFFQRTGLSPLKFKAQETRTVALCTCKATQRPPYCDGTHKSEQVQKAEVGSPL | Cofactor: Binds 2 [2Fe-2S] clusters per subunit.
Function: Can transfer its iron-sulfur clusters to the apoferrodoxins FDX1 and FDX2. Contributes to mitochondrial iron homeostasis and in maintaining normal levels of free iron and reactive oxygen species, and thereby contributes to normal mitochondrial function.
Sequenc... |
Q2HJ53 | MVLCVQGLCPLLAVEQIGQRPLWAQSLELPQQVMQPLSAGAFLEEAVEESPAQPEREPKVVDPEEDLLCIAKTFSYLRESGWYWGSITASEARQHLQKMPEGTFLVRDSTHPSYLFTLSVKTTRGPTNVRIEYADSSFRLDSNCLSRPRILAFPDVVSLVQHYVASCAADTRSDSPDLATTPALPTPKEDAPGDPALPATAVHLKLVQPFVRRSSTRSLQHLCRLVINRLVVDVDCLPLPRRMADYLRQYPFQL | Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. CIS is involved in the negative regulation of cytokines that signal through the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin 3 (IL3) receptor. Inhibits STAT5 trans-activat... |
Q9NSE2 | MVLCVQGPRPLLAVERTGQRPLWAPSLELPKPVMQPLPAGAFLEEVAEGTPAQTESEPKVLDPEEDLLCIAKTFSYLRESGWYWGSITASEARQHLQKMPEGTFLVRDSTHPSYLFTLSVKTTRGPTNVRIEYADSSFRLDSNCLSRPRILAFPDVVSLVQHYVASCTADTRSDSPDPAPTPALPMPKEDAPSDPALPAPPPATAVHLKLVQPFVRRSSARSLQHLCRLVINRLVADVDCLPLPRRMADYLRQYPFQL | Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. CIS is involved in the negative regulation of cytokines that signal through the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin 3 (IL3) receptor. Inhibits STAT5 trans-activat... |
A0A0S3QTD0 | MKLKERLAELIPQWRAEVAEIRKKYGNRKTMDCTIGHAYGGMRGLKALVCDTSEVFPDEGVKFRGYTIPELREGPHKLPTAEGGFEPLPEGLWYLLLTGELPTEEDVKEISAEFTKRMQNVPQYVFDVLRAMPVDTHPMTMFAAGILAMQRESVFAKRYEEGMRREEHWEAMLEDSLNMLAALPVIAAYIYRRKYKGDTHIAPDPNLDWSANLAHMMGFDDFEVYELFRLYMFLHSDHEGGNVSAHTNLLVNSAYSDIYRSFSAAMNGLAGPLHGLANQEVLRWIQMLYKKFGGVPTKEQLERFAWDTLNSGQVIPGYGH... | Function: Catalyzes both citrate generation and citrate cleavage. Part of a reversible tricarboxylic acid (TCA) cycle that can fix carbon dioxide autotrophically and may represent an ancestral mode of the conventional reductive TCA (rTCA) cycle. The direction is controlled by the available carbon source(s).
Catalytic A... |
Q28DK1 | MSLITAGRLCARILGAKNSPCALIAARQASSSANLKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAPGGEEPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEGVNKTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSSIGAIDSNLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKD... | Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 51834
Sequence Length: 468
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
Subcellular Location: Mitochondrion matrix
EC: 2.3.3.1
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P07661 | MTQQPSRAGTFGAILRVTSGNFLEQFDFFLFGFYATYIAKTFFPAESEFAALMLTFAVFGSGFLMRPIGAVVLGAYIDRIGRRKGLMITLAIMGCGTLLIALVPGYQTIGLLAPVLVLVGRLLQGFSAGVELGGVSVYLSEIATPGNKGFYTSWQSASQQVAIVVAALIGYGLNVTLGHDEISEWGWRIPFFIGCMIIPLIFVLRRSLQETEAFLQRKHRPDTREIFTTIAKNWRIITAGTLLVAMTTTTFYFITVYTPTYGRTVLNLSARDSLVVTMLVGISNFIWLPIGGAISDRIGRRPVLMGITLLALVTTLPVMN... | Function: Uptake of citrate across the boundary membrane with the concomitant transport of protons into the cell (symport system).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46980
Sequence Length: 431
Subcellular Location: Cell inner membrane
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P52687 | MSIYPMYTRKITHWFARRSFQNRIFLLILFTSTIVMLAMSWYLTDITEERLHYQVGQRALIQAMQISAMPELVEAVQKRDLARIKALIDPMRSFSDATYITVGDASGQRLYHVNPDEIGKSMEGGDSDEALINAKSYVSVRKGSLGSSLRGKSPIQDATGKVIGIVSVGYTIEQLENWLSLQISSLLIPMAIMLLLLLFCARRFSLHIKKQMLNMEPQQLSQLLIQQSVLFESVFEGLIAIDSDYKITAINQTARRLLNLSQPEPTLIGKRISSVISQEVFFYDAPQTNKKDEIVTFNQIKVIASRMAVILNNEPQGWVI... | Function: Member of the two-component regulatory system CitA/CitB. Probably activates CitB by phosphorylation. The periplasmic domain binds H-citrate(2-), which is essential for induction of the citrate-fermentation genes.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP +... |
Q1ERH9 | MKGQTGLRSLALLYISPLYILERLPLKLSAPDTLVVRGSFIVPTEPLYPSITMVQTNLEVVDDTLHLPRILCLHGGGSNAAIFQAQCRRLIAQLRSEFRFVFAQAPFLSDAEPNVMSVYSQWGPFRRWLRWCPDHPEIRPEDAIRAIDDCLEDVKRQDDAKGATGAWVGLLGFSQGAKMCASLLYRQQIRQELRGRSFAGSDYRFGVLLAGRAPLVSLDPDLDLNSSLPDVSQITDAKYHGPSQDVLRIPTVHVHGMRDPHVDLHRQLFEEFCAPESRRLVEWDGDHRVPLKYNDVSLVAYQIRELATQTGAP | Function: Esterase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III . The pathway begins with the synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT) from successive condensations of... |
P52688 | MDSITTLIVEDEPMLAEILVDNIKQFPQFDVIGIADKLESARKQLRLYQPQLILLDNFLPDGKGIDLIRHAVSTHYKGRIIFITADNHMETISEALRLGVFDYLIKPVHYQRLQHTLERFARYRSSLRSSEQASQLHVDALFNIQAREQTEPASAPLRGIDESTFQRVLQLFADPTVVHTADSLARILGSSKTTARRYLEQGVKNDFLEAEISYGKVGRPERIYHGKQTYPEQR | Function: Member of the two-component regulatory system CitA/CitB essential for expression of citrate-specific fermentation genes. Phosphorylated CitB binds to two sites in the citS-citC intergenic region where it probably activates transcription of both genes.
PTM: Phosphorylated by CitA.
Sequence Mass (Da): 26821
Seq... |
Q1ERI0 | MPISTKSSFYLPAVDISPYLQDPNSDAARKVIDDVRAACTSTGFFQLLGHGISPALQQSVFAAAAKFFALPSDVKSRCRNVGFRGYDPMASQSYELGVLPDLKEGFIAGKDIPLDDPRVASQRFFMGQNAWPPSELLPEANFRRPIEEYYQAMLKLCWVVLDLVAATLPYGPHVFDEFKENDPACPLRLLHYPPAPAPDVAKGRQLGSSAHTDFGAITLLLQDDHSGLEVQDCETGEWIGVPPNKDAYVVNLGDMMSRITRGHYKSSIHRVINQNLTDRYSVVFFFDGNLDYRLRPLDRVGQNWDEEDTLTVEEHMLERT... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III . The pathway begins with the synthesis of a keto-aldehyde int... |
P77390 | MFGNDIFTRVKRSENKKMAEIAQFLHENDLSVDTTVEVFITVTRDEKLIACGGIAGNIIKCVAISESVRGEGLALTLATELINLAYERHSTHLFIYTKTEYEALFRQCGFSTLTSVPGVMVLMENSATRLKRYAESLKKFRHPGNKIGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFIKEQSVINHCYTEIDLKIFRQYLAPALGVTHRFVGTEPFCRVTAQYNQDMRYWLETPTISAPPIELVEIERLRYQEMPISASRVRQLLAKNDLTA... | Function: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
Catalytic Activity: acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate lyase ACP] + AMP + diphosphate
Sequence Mass (Da): 40077
Sequence Length: 352
EC: 6.2.1.22
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P44462 | MQFERISTEQKKLSLIQTFLHQNALKLDEQIEYFVVGYNDNEQIVVCGGLAGNIIKCVAIDESLRGSGVALQLITELVDLAYTLKRPHLFIYTKPEYATLFKSCGFYIISDANPYVVLLENSATRLQKQCSLWEKMRVDGNRIGSIVMNANPFTLGHRYLIEQALQQCDHLHLFIVGEDASQFSYTERFEMIQQGIFDLSNITLHSGSDYIISRATFPNYFLKDQLITDESYFEIDLKLFRLHIAQALGITHRFVGTELNCPVTAEYNRQMHYWLMDAEMNAPKINVIEIPRKTASNHIISASTVRKHLAEKNWAQLAEF... | Function: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
Catalytic Activity: acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate lyase ACP] + AMP + diphosphate
Sequence Mass (Da): 38495
Sequence Length: 335
EC: 6.2.1.22
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P58161 | MSMPATLTKTTKLATSLIDEYALLGWRAMLTEVNLSPKPGLVDRINCGAHKDMALEDFHRSALAIQGWLPRFIEFGACSAEMAPEAVLHGLRPIGMACEGDMFRATAGVNTHKGSIFSLGLLCAAIGRLLQLNQLLTPTTVCSTAASFCRGLTDRELRTNNSQLTAGQRLYQQLGLTGARGEAEAGYPLVINHALPHYLTLLDQGLDPELALLDTLLLLMAINGDTNVASRGGEGGLRWLQREAQTLLQKGGIRTPADLDYLRQFDRECIERNLSPGGSADLLILTWFLAQI | Function: Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP and dephospho-CoA.
Catalytic Activity: 3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + ad... |
Q9H0W9 | MACAEFSFHVPSLEELAGVMQKGLKDNFADVQVSVVDCPDLTKEPFTFPVKGICGKTRIAEVGGVPYLLPLVNQKKVYDLNKIAKEIKLPGAFILGAGAGPFQTLGFNSEFMPVIQTESEHKPPVNGSYFAHVNPADGGCLLEKYSEKCHDFQCALLANLFASEGQPGKVIEVKAKRRTGPLNFVTCMRETLEKHYGNKPIGMGGTFIIQKGKVKSHIMPAEFSSCPLNSDEEVNKWLHFYEMKAPLVCLPVFVSRDPGFDLRLEHTHFFSRHGEGGHYHYDTTPDIVEYLGYFLPAEFLYRIDQPKETHSIGRD | Function: Exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate.
Sequence Mass (Da): 35117
Sequence Length: 315
Subcellular Location: Nucleus
EC: 3.1.-.-
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A2XVN3 | MELKAMYLYAAVLAVLLCSSVNFIQSPTDVLGPVALLEPTPSSARDFGAVVSDAPFAVMRPESPDDIALLLGALSSTAPSPRATVAAVGAGHSLHGQAQARDGIVVETRALPRDVHVVSARAHGGDDDATVRAYADVGAGALWVEVLEECLKLGLAPPSWTDYLYLTVGGTLSNGGISGQTFKHGPQISNVLQLEVVTGKGEVVTCSPTEIPELFFAVLGGLGQFGIITRARIPLQLAPPKVRWVRAFYDSFETFTGDQELLVSMPEQVDYVEGFMVLNEQSLHSSSVAFPAQLNFSPDFGSKGRKKVYYCIEFAVHDFQ... | Function: Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group.
Catalytic Activity: A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal + adenine + AH2
Sequence Mass (Da): 57619
Sequence Length: 532
Subcellula... |
Q75K78 | MRPSLLQYLKLLLLLALGGVTTMHVPKQDVPSSLEELTLDGHFSFHDVSAAAQDFGNLSSFPPVAVLHPGSVADIATTIRHVFLMGEHSTLTVAARGHGHSLYGQSQAAEGIIISMESLQSNTMRVNPGVSPYVDASGGELWINVLHETLKYGLAPKSWTDYLHLTVGGTLSNAGVSGQTFRHGPQISNVNELEIVTGRGDVITCSPEQNSDLFHAALGGLGQFGVITRARIPLEPAPKMVRWLRVLYLDFTSFTEDQEMLISAEKTFDYIEGFVIINRTGILNNWRSSFNPQDPVRSSQFESDGKVLFCLEMTKNFNPD... | Function: Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group (Probable). Possesses cytokinin oxidase activity toward trans-zeatin (tZ) and N6-(2-isopentenyl)adenine (2iP) in vitro . Functions as a primary strigol... |
P58763 | FLPKSLFTLVTDKSL | Function: Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group. Substrate preference is 2-(2-hydroxyethylamino)-9-methyl-N(6)-isopentenyladenine >> isopentenyladenine > cis-zeatin = isopentenyladenosine = zeatin >>... |
Q9LEX1 | MGLISGILFGIIFGVALMAGWSRMMTHRSSKRVAKAVDMKLLGSLSRDDLKKICGDNFPQWISFPAFEQVKWLNKLLSKMWPYIAEAATMVIRDSVEPLLEDYRPPGITSLKFSKLTLGNVAPKIEGIRVQSFKEGQVTMDVDLRWGGDPNIVLGVTALVASIPIQLKDLQVFTVARVIFQLADEIPCISAVVVALLAEPKPRIDYTLKAVGGSLTAIPGLSDMIDDTVDTIVKDMLQWPHRIVVPIGGIPVDLSDLELKPQGKLIVTVVKATNLKNKELIGKSDPYATIYIRPVFKYKTKAIENNLNPVWDQTFELIAE... | Function: May be involved in membrane trafficking (By similarity). Acts as a repressor of abiotic stress (e.g. drought and salt) responses by binding specifically to the promoter of THAS1 to regulate its transcription . Binds to membrane lipid ceramides .
Location Topology: Single-pass membrane protein
Sequence Mass (D... |
Q8IUN9 | MTRTYENFQYLENKVKVQGFKNGPLPLQSLLQRLCSGPCHLLLSLGLGLLLLVIICVVGFQNSKFQRDLVTLRTDFSNFTSNTVAEIQALTSQGSSLEETIASLKAEVEGFKQERQAGVSELQEHTTQKAHLGHCPHCPSVCVPVHSEMLLRVQQLVQDLKKLTCQVATLNNNASTEGTCCPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQNFVQKYLGSAYTWMGLSDPEGAWKWVDGTDYATGFQNWKPGQPDDWQGHGLGGGEDCAHFHPDGRWNDDVCQRPYHWVCEAGLGQTSQESH | Function: Probable role in regulating adaptive and innate immune responses. Binds in a calcium-dependent manner to terminal galactose and N-acetylgalactosamine units, linked to serine or threonine. These sugar moieties are known as Tn-Ag and are expressed in a variety of carcinoma cells.
Location Topology: Single-pass ... |
Q9Y240 | MQAAWLLGALVVPQLLGFGHGARGAEREWEGGWGGAQEEEREREALMLKHLQEALGLPAGRGDENPAGTVEGKEDWEMEEDQGEEEEEEATPTPSSGPSPSPTPEDIVTYILGRLAGLDAGLHQLHVRLHALDTRVVELTQGLRQLRNAAGDTRDAVQALQEAQGRAEREHGRLEGCLKGLRLGHKCFLLSRDFEAQAAAQARCTARGGSLAQPADRQQMEALTRYLRAALAPYNWPVWLGVHDRRAEGLYLFENGQRVSFFAWHRSPRPELGAQPSASPHPLSPDQPNGGTLENCVAQASDDGSWWDHDCQRRLYYVCE... | Function: Promotes osteogenesis by stimulating the differentiation of mesenchymal progenitors into mature osteoblasts . Important for repair and maintenance of adult bone (By similarity).
PTM: O-glycosylated. Probably sulfated on the O-glycans.
Sequence Mass (Da): 35695
Sequence Length: 323
Subcellular Location: Cytopl... |
Q9P126 | MQDEDGYITLNIKTRKPALISVGSASSSWWRVMALILLILCVGMVVGLVALGIWSVMQRNYLQGENENRTGTLQQLAKRFCQYVVKQSELKGTFKGHKCSPCDTNWRYYGDSCYGFFRHNLTWEESKQYCTDMNATLLKIDNRNIVEYIKARTHLIRWVGLSRQKSNEVWKWEDGSVISENMFEFLEDGKGNMNCAYFHNGKMHPTFCENKHYLMCERKAGMTKVDQLP | Function: C-type lectin-like receptor that functions as a platelet receptor for the lymphatic endothelial marker, PDPN . After ligand activation, signals via sequential activation of SRC and SYK tyrosine kinases leading to activation of PLCG2 .
PTM: Glycosylated.
Location Topology: Single-pass type II membrane protein
... |
Q9SKU1 | MATFDDGDFPAQTHSPSEHEDFGGYDNFSEAQQPPTQHQSGGFSSFNGDPASPNGYGFGASSPNHDFSSPFESSVNDANGNGGGSGGDAIFASDGPILPDPNEMREEGFQRREWRRLNTIHLEEKEKKEKEMRNQIITEAEDFKKAFYEKRDKTIETNKTDNREKEKLYWANQEKFHKEVDKHYWKAIAELIPREVPNIEKKRGKKDPDKKPSVNVIQGPKPGKPTDLGRMRQIFLKLKTNPPPHMMPPPPPAKDAKDGKDAKDGKDAKTGKDGKDAKGGKDAKDLKDGKPADPKVTEEKRPSPAKDASVETAKPDAAAS... | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37225
Sequence Length: 338
Subcellular Location: Cytoplasmic vesicle membrane
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Q7XKE9 | MASFFADDGADELPRTASHPFDADDDAAPDASGGAAADDTGYGGYASFVDGGVEDVEEEEEEIAVESEGVPIGHVSGGFSPSPFSPDPELDGGDGPILPPPAQMGAEEGILLREWRRQNAIVLEEKERKEKELRAQILAEAEEFKKAFYEKRIQNCETNKVHNREREKIFVAGQEKFHAEADKQYWKSISELIPHEIATIEKRGKKDKDKKPSITVIQGPKPGKPTDLSRMRQILVKLKHAPPPHMMQPPPASAAKDGAKDGAKDGTPAPANGTKKPAESKEKPANGSPAEAEKEQPAASE | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32536
Sequence Length: 301
Subcellular Location: Cytoplasmic vesicle membrane
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Q9USP6 | MSQFPALEDFDDGLVTAPVDDSKNNTDFLEREKLALGEDAGQFETPEDKDALLNFENDSEAEQTRFEQNFPPIDAEMQASGTFSAPKAPYMGQAEVHPPEDESGDPEPVRKWKEDQMKRIQERDESSKKLRESNIEKARKAIDDFYENFNDKRDKVIAKSRKEQEKLLEENESKSTGTTSWERILKLIDLSDKPEAHGRSTERFRELLISLAKDSNAPGAAGTTVSSSS | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25863
Sequence Length: 229
Subcellular Location: Cytoplasmic vesicle membrane
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P17891 | MSEKFPPLEDQNIDFTPNDKKDDDTDFLKREAEILGDEFKTEQDDILETEASPAKDDDEIRDFEEQFPDINSANGAVSSDQNGSATVSSGNDNGEADDDFSTFEGANQSTESVKEDRSEVVDQWKQRRAVEIHEKDLKDEELKKELQDEAIKHIDDFYDSYNKKKEQQLEDAAKEAEAFLKKRDEFFGQDNTTWDRALQLINQDDADIIGGRDRSKLKEILLRLKGNAKAPGA | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi. The yeast light chain is important for cell growth. The light chain may help to properly orient the asse... |
Q6UVW9 | MINPELRDGRADGFIHRIVPKLIQNWKIGLMCFLSIIITTVCIIMIATWSKHAKPVACSGDWLGVRDKCFYFSDDTRNWTASKIFCSLQKAELAQIDTQEDMEFLKRYAGTDMHWIGLSRKQGDSWKWTNGTTFNGWFEIIGNGSFAFLSADGVHSSRGFIDIKWICSKPKYFL | Function: Plays a role in modulating the extent of T-cell expansion. Enhances the expansion of TCR-stimulated T-cells by increasing their survival through enhanced expression of anti-apoptotic proteins. May modulate the capacity of T-cells to home to lymph nodes through SELL. Facilitates dedicated immune recognition of... |
P51791 | MESEQLFHRGYYRNSYNSITSASSDEELLDGAGAIMDFQTSEDDNLLDGDTAAGTHYTMTNGGSINSSTHLLDLLDEPIPGVGTYDDFHTIDWVREKCKDRERHRRINSKKKESAWEMTKSLYDAWSGWLVVTLTGLASGALAGLIDIAADWMTDLKEGICLSALWYNHEQCCWGSNETTFEERDKCPQWKTWAELIIGQAEGPGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFPKYSTNEAKKREVLSAASAA... | Function: May influence large dense-core vesicle exocytosis in adrenal chromaffin cells.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90812
Sequence Length: 818
Subcellular Location: Cytoplasmic vesicle
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P51793 | MVNAGAMSGSGNLMDFLDEPFPDVGTYEDFHTIDWLREKSRDTDRHRKITSKSKESIWEFIKSLLDAWSGWVVMLLIGLLAGTLAGVIDLAVDWMTDLKEGVCLSAFWYSHEQCCWTSNETTFEDRDKCPLWQKWSELLVNQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLVLFY... | Function: Strongly outwardly rectifying, electrogenic H(+)/Cl(-)exchanger which mediates the exchange of chloride ions against protons . The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons . The presence of conserved gating glu... |
P51795 | MAMWQGAMDNRGFQQGSFSSFQNSSSDEDLMDIPATAMDFSMRDDVPPLDREVGEDKSYNGGGIGSSNRIMDFLEEPIPGVGTYDDFNTIDWVREKSRDRDRHREITNKSKESTWALIHSVSDAFSGWLLMLLIGLLSGSLAGLIDISAHWMTDLKEGICTGGFWFNHEHCCWNSEHVTFEERDKCPEWNSWSQLIISTDEGAFAYIVNYFMYVLWALLFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILCHCFNKYRKNEAKRREVLSAAAAAG... | Function: Proton-coupled chloride transporter. Functions as antiport system and exchanges chloride ions against protons . Important for normal acidification of the endosome lumen. May play an important role in renal tubular function. The CLC channel family contains both chloride channels and proton-coupled anion transp... |
P51797 | MAGCRGSLCCCCRWCCCCGERETRTPEELTILGETQEEEDEILPRKDYESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFFVRLFTQLKFGVVQTSVEECSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPEVKCYLNGVKVPGIVRLRTLLCKVLGVLFSVAGGLFVEKEGPMIHSGSVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCS... | Function: Voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the late endosome lumen. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for proto... |
Q9TT16 | MAGCRGSLCCCCRWCCCCGERETRTPEELTILGETQEEEDEILPRKDYESLDYDRCINDPYLEVLETMDHKKGRWYEVVKWTVVFAIGVCTGLVGLFVDFFVQLFTQLKFGVVEASVEECSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPEIKCYLNGVKVPGIVRLRTLLCKVFGVLFSVAGGLFVGKEGPMIHSGAVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGIAAAFGAPIGATLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCS... | Function: Voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the late endosome lumen. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for proto... |
Q9UBY8 | MNPASDGGTSESIFDLDYASWGIRSTLMVAGFVFYLGVFVVCHQLSSSLNATYRSLVAREKVFWDLAATRAVFGVQSTAAGLWALLGDPVLHADKARGQQNWCWFHITTATGFFCFENVAVHLSNLIFRTFDLFLVIHHLFAFLGFLGCLVNLQAGHYLAMTTLLLEMSTPFTCVSWMLLKAGWSESLFWKLNQWLMIHMFHCRMVLTYHMWWVCFWHWDGLVSSLYLPHLTLFLVGLALLTLIINPYWTHKKTQQLLNPVDWNFAQPEAKSRPEGNGQLLRKKRP | Function: Could play a role in cell proliferation during neuronal differentiation and in protection against cell death.
PTM: Does not seem to be N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32787
Sequence Length: 286
Subcellular Location: Endoplasmic reticulum membrane
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Q7Z7G1 | MNRQGNRKTTKEGSNDLKFQNFSLPKNRSWPRINSATGQYQRMNKPLLDWERNFAAVLDGAKGHSDDDYDDPELRMEETWQSIKILPARPIKESEYADTHYFKVAMDTPLPLDTRTSISIGQPTWNTQTRLERVDKPISKDVRSQNIKGDASVRKNKIPLPPPRPLITLPKKYQPLPPEPESSRPPLSQRHTFPEVQRMPSQISLRDLSEVLEAEKVPHNQRKPESTHLLENQNTQEIPLAISSSSFTTSNHSVQNRDHRGGMQPCSPQRCQPPASCSPHENILPYKYTSWRPPFPKRSDRKDVQHNEWYIGEYSRQAVE... | Function: An adapter protein which plays a role in the regulation of immunoreceptor signaling, including PLC-gamma-mediated B-cell antigen receptor (BCR) signaling and FC-epsilon R1-mediated mast cell degranulation (By similarity). Together with FGR, it acts as a negative regulator of natural killer cell-activating rec... |
Q9QZE2 | MTSQGNKRTTKEGFGDLRFQNVSLLKNRSWPSLSSAKGRCRAVLEPLPDHRRNLAGVPGGEKCNSNNDYEDPEFQLLKAWPSMKILPARPIQESEYADTRYFQDTMEAPLLLPPKASVSTERQTRDVRMTHLEEVDKPTFKDVRSQRFKGFKYTKINKTPLPPPRPAITLPKKYQPLPPAPPEESSAYFAPKPTFPEVQRGPRQRSAKDFSRVLGAEEESHHQTKPESSCPSSNQNTQKSPPAIASSSYMPGKHSIQARDHTGSMQHCPAQRCQAAASHSPRMLPYENTNSEKPDPTKPDEKDVWQNEWYIGEYSRQAVE... | Function: An adapter protein which plays a role in the regulation of immunoreceptor signaling, including PLC-gamma-mediated B-cell antigen receptor (BCR) signaling and FC-epsilon R1-mediated mast cell degranulation . Together with FGR, it acts as a negative regulator of natural killer cell-activating receptors and inhi... |
M1WEN7 | MSLQWLQQTRHELSWTWILLTTCIALISPLVLKGIYNVYFHPLRNIPGPKLAALTDFYAFYWNWIRDEGYSKQFSRLHEQYNSPIIRIGPNNVHTTQVEFYDVIFKSGSKWLKDKSFYKYFNGLDAMIEPYQYRTYRTHLAPLYAQRAIDGLAPKLRSDLTNSASGMMRQTKNGQTVNMAKVLRTLSTSMILHNLFSLDISLNDGDEYHPFLEAFEQLMTQSWLFVTYPMVPMVLSLIPGTSFARFNSSYTTFSNYCTAWNDEDMRKQRESEEQSTRDSHTKRYLSLKDDDARKKTAIPYPLDDVFNFVAGGSDTTAYTT... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid . DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan . The second step is catalyzed by th... |
Q8QGQ6 | MFFTISTHKMSSIADRNDGSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGNIIYVSESVTPLLEHLPSDLVDQSVFNFIPEGEHSEIYKILSSHLLESDSLTPEYLKSKNQLEFCCHMLRGTIDPKEQPTYEYVKFIGNFKCLNNVPNSAHNGFEGTIQRSHRPSYEDKVCFIATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLDN... | Function: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism a... |
O08785 | MVFTVSCSKMSSIVDRDDSSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKETTAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGSIIYVSESVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPEYLKSKNQLEFCCHMLRGTIDPKEPSTYEYVRFIGNFKSLTSVSTSTHNGFEGTIQRTHRPSYEDRVCFVATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLEN... | Function: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism a... |
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