ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q2SSQ6 | MIKKIGILTSGGDAPGMNNAIAGVVKTASSKGIEVYGINDGYKGLVNGWFEKLNVEKTLDILSRGGTYLGSARLPEFKELEVRQKAVANLKKAGIEALVVIGGDGSYMGAQRLTEMGINCIGLPGTIDNDIASTDYTIGFHTALNTIVEAVDRIRDTMQSHNRADVVEIMGNGCGDLVTYTAVATGAEIFSPAEDLLTIEQMGQKAKQFRLLGKKSLIILVSEKLYGISAEEIAEKIQKISGYETKATVLGHIQRGGRPTAMDRYIAFTAGMFAVEKLAEGKGGLFIGLENNKLVARDIDSTLNMKKEDKKPFIKNLREI... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 35179
Sequence Length: 326
Pathway: Carbohydrate degra... |
O33106 | MRIGILTGGGDCPGLNAVIRAIVRTCDARYGSSVVGFQDGWRGLLENRRMQLCNDDRNDRLLAKGGTMLGTAHVHPDKLRAGLHQIKQTLDDNGIDVLIPIGGEGTLTAAHWLSQEDVPVVGVPKTIDNDIDCTDVTFGHDTALTVATEAIDRLHSTAESHQRVMLVEVMGRHAGWIALSSGLASGAHMTLIPEQPFDVEEVCCLVKRRFQRGDSHFICVVAEGAKPVPGSITLRQGGMDEFGHERFTGVAAQLGAEVEKRINKDVRVTVLGHVQRGGTPTAFDRVLATRFGVNAADASHAGEYGQMVSLRGQDIGRVPL... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 37002
Sequence Length: 343
Pathway: Carbohydrate degra... |
P75476 | MSPKTTKKIAILTSGGDAPGMNATLVYLTRYATSSEIEVFFVKNGYYGLYHDELVPAHQLDLSNSLFSAGTVIGSKRFVEFKELKVREQAAQNLKKRQIDYLVVIGGDGSYMGAKLLSELGVNCYCLPGTIDNDINSSEFTIGFLTALESIKVNVQAVYHTTKSHERVAIVEVMGRHCGDLAIFGALATNADFVVTPSNKMDLKQLESAVKKILQHQNHCVVIVSENIYGFDGYPSLTAIKQHFDANNMKCNLVSLGHTQRGFAPTSLELVQISLMAQHTINLIGQNKVNQVIGNKANVPVNYDFDQAFNMPPVDRSALI... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 35989
Sequence Length: 328
Pathway: Carbohydrate degra... |
Q98PW8 | MIKKIAILTSGGDSPGMNNAIRAIIKTARLYDIETYLVYEGFLGLYNGWIKPSEGIDEDSYINKGGTFIFSARFVEFAQEKYRQVAKENLLKLGIEALVVIGGDGSYKGAQKLHEMGIKTIALPGTIDNDITSSDFTIGYDTALNTIVEAVDKIRDTASSHKRCIMVEVMGHGASDLALYSGMATGSEIIVSNDYKLSVEEMAKIVKKQFEKPNKRSVIITVSEFVFKDLQQVAKQIEELTNITTKAVVLAHIQRGGYPSARERINATILGKHAVLRLKQGQSGIALGLIKNQVAATPILEALAMPQTRKDLLERRTKSY... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 35832
Sequence Length: 326
Pathway: Carbohydrate degra... |
Q8W4M5 | MAPALAVTRDLTAVGSPENAPAKGRASVYSEVQSSRINNTLPLPSVLKGAFKIVEGPASSAAGNPDEIAKLFPGLYGQPSVAVVPDQDAPSSAPKLKIGVVLSGGQAPGGHNVISGLFDYLQERAKGSTFYGFKGGPAGIMKCKYVELNAEYIQPYRNQGGFDMICSGRDKIETPDQFKQAEETAKKLDLDGLVVIGGDDSNTNACLLAENFRSKNLKTRVIGCPKTIDGDLKCKEVPTSFGFDTACKIYSEMIGNVMIDARSTGKYYHFVRLMGRAASHITLECALQTHPNITIIGEEVSAQKQTLKNVTDYMVDVICK... | Function: Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which re... |
F4JGR5 | MASQLDLIGGDYIAGISINPPTNSRVTSVYSEVQASRIDHTLPLPSVFKTPFKIIDGPPSSSAGHPEEIEKLFPNLFGQPSALLVPNQSNEVSSDQKLKIGVVLSGGQAPGGHNVICGIFDYLQEYARGSSLFGFRGGPAGIMKGKYIELTSEFVYPYRNQGGFDMICSGRDKIETPEQFKQAEETVTKMDLDGLVVIGGDDSNTNACLLAEHFRAKNMKTLVIGCPKTIDGDLKSKEVPTSFGFDTACKIYSEMIGNVMIDARSTGKYYHFVRLMGRAASHITLECALQTHPNITIIGEEVFEKKLTLKNVTDNIVDVI... | Function: Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which re... |
Q41141 | MATPNSGRAASVYSEVQSSRIEHVLPLPSVLNHPFKIVQGPPSSAAGNPDEIAKLFPNLFGQPSAMLVPDVADSLDSNQQLKIGLVLSGGQAPGGHNVISGIFDYLQDRAKGSILYGFRGGPAGIMKCNYVQLTADYIHPYRNQGGFDMICSGRDKIETPEQFKQAEETAGKLDLNGLVVIGGDDSNTNACLLAENFRSKNLKTRVIGCPKTIDGDLKCKEVPTSFGFDTACKIYSEMIGNVMIDARSTGKYYHFVRLMGRAASHITLECALQTHPNITIIGEEVAAKKLALKDVTDYIVDVICKRADLGYNYGVILIPE... | Function: Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which re... |
P21343 | MAAATLSLLNNGELASSVKSPGTGRYAAVYSEVQNSRLDHPLPLPSVLGSPFKVVDGPPSSAAGHPEEIAKLFPSLYGQPCVSLVPDDSGDVAMNQILKIGVVLSGGQAPGGHNVISGIFDYLQTHCKGSTMYGFRGGPAGVMKGKYVVLTPEFIYPYRNQGGFDMICSGRDKIETPEQFKQAEETAKKLDLDGLVVIGGDDSNTNACLLAENFRSKNLKTRVIGCPKTIDGDLKSKEVPTSFGFDTACKIYAEMIGNVMIDARSTGKYYHFVRLMGRAASHITLECALQTHPNVTLIGEEVFAKKLTLKNVTDYIADVV... | Function: Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which re... |
Q59126 | MRVGVLTGGGDCPGLNAVIRAVVRKGIEAHGWEIVGFRSGWRGPLTGDSRPLGLDDVEEILIRGGTILGSSRTNPYKEEGGVEKIRAVLADQGVDALIAIGGEDTLGVAKKLTDDGIGVVGVPKTIDNDLAATDYTFGFDTAVHIATEAIDRLRTTAESHYRAMVVEVMGRHAGWIALHAGLAGGANVILVPERPFSVEQVVEWVERRFEKMYAPIIVVAEGAVPEGGAEVLRTGEKDAFGHVQLGGVGTWLADEIAERTGKESRAVVLGHTQRGGTPTAYDRVLATRFGLHAVDAVADGDFGTMVALRGTDIVRVKLAE... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and glu... |
Q9KH71 | MSKMRIGVLTGGGDCPGLNPAIRGIVMRALDYGDEVIGLKYGWAGLLKADTMPLSLEMVEDILEIGGTILGSSRTNPFKKEEDVQKCVENFKKLNLDALIAIGGEDTLGVASKFSKLGLPMIGVPKTIDKDLEETDYTLGFDTAVEVVVDAIKRLRDTARSHARVIVVEIMGRHAGWLALYGGLAGGADYILIPEVEPNLEDLYNHIRKLYARGRNHAVVAIAEGVQLPGFTYQKGQEGMVDAFGHIRLGGVGNVLAEEIQKNLGIETRAVILSHLQRGGSPSIRDRIMGLLLGKKAVDLVHEGKSGLFVAVKGNELVPV... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and glu... |
E2RU81 | MSAFEVYRRKFKPALPRAIQGASYHLHTEEKTHPVADEQDIAALFPKTTHLPLLDIQPDTGAPKLLEPKRVGVIFSGGQAPGGHNVLCGLYDKLQQIAPKSVLLGFQNGPKGLMTNKYVELTEKFLEPFRNMGGFHAIGSGRDKIAKPEDFDAAAKTAKDNNLDIICIIGGDDSNTNACLLAEDFLKRGLKTAVIGVPKTIDRDLYSTKGIECSFGFDSSTKVYAELIGNICYDCLSAKKYWHFIRLMGRSASHITLECGLQTHANICLVGEEILSKKMTSRQLFEYLADCVTKRADSGKNYGVCLVPEGLIEFIPENNE... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and glu... |
Q609I3 | MAARNAFYAQSGGVTAVINASACGVLETARQYPDRIGTVYAGRNGIVGALTEDLIDTGQESAEAIAALRHTPSGAFGSCRYKLKGLEENRAQYERLIEVFRAHDIGYFFYNGGGDSADTCLKVSQLSEKLGYPLQAVHIPKTVDNDLPITDCCPGFGSVAKYIAVSVREASFDVRSMAATSTCIFVLEVMGRHAGWIAAAGGLASDERHELALVILFPEQVFDPERFLRAVDEKVRSHGYCSVVVSEGIRGADGRFVAESGSRDVFGHARLGGVAPVIADLIKERLGYKYHWAVADYLQRAARHIASRTDVEQAYAVGKA... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and glu... |
Q27705 | MLSSSHLPTTIVTPKNVPTLGVLVGGGPAPGINGVIGAVTIEAINNGYRVLGFLEGFQNLILQDDSKIVELTIDSVSRIHFEGGSILKTSRANPTKKQEDLQKVVKQLQKFNVSLLVTIGGDDTAFSSMSVAKAANNEIHVVTLPKTIDNDLPLPYGIPTFGYETAREFGANVVRNLMTDASTASRYFIVVAMGRQAGHLALGIGKSAGSHLTLIPEEFLPTTDSTEPEVTFSRICDMIEASIIKRLYTSKKDHGVIVLAEGLLEYMSTDELKQAFGSSLKYDAHDHIMLAELDFGRLVRDEMRERMNRRGLKIAFTEKN... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and glu... |
Q9FAF8 | MAKSALHLARMSYQPKMPASLQGAVKIIEGKATEAVSDKEEIAAIFPRTYGLPLISFAPGGERTEYPPTNVGVILSGGQAPGGHNVIAGLFDEMKLLNPDSRLFGFLMGPDGLIEHKYRELTAEVIDEYRNTGGFDMIGSGRTKLDKPEQFEAGLEILRELDIKALVIIGGDDSNTNACILAEYYASIDAGIQVIGCPKTIDGDLKNKQIETSFGFDTAAKVYSELIGNIQRDCNSARKYWHFIKLMGRSASHITLECALQTHPNICIVSEEVEANNYYLDDVVTYIAETVVRRSEAGMNFGTVLIPEGLIEFLPAMKRL... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and glu... |
P0CK23 | MLVVIMFFIAFAFCSWLSYSYLRPYISTKELNKSRMFYIT | Function: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
PTM: Unglycosylated be... |
P68604 | MDKLYAAIFGVFMGSPEDDLTDFIEIVKSVLSDEKTVTSTNNTGCWGWYWLIIIFFIVLILLLLIYLYLKVVW | Function: Late protein which probably plays a role in virus entry into the host cell.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8499
Sequence Length: 73
Subcellular Location: Virion membrane
|
P20990 | MIGILLLIGICVAVTVAILYSMYNKIKNSQNPNPSPNLNSPPPEPKNTKFVNNLEKDHISSLYNLVKSSV | Function: Essential for the encapsidation of DNA into immature virions (IV) and the subsequent maturation of IV into mature virions (MV).
PTM: Phosphorylated by a OPG054-independent mechanism.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7696
Sequence Length: 70
Subcellular Location: Virion membr... |
P0DSQ3 | MDMMLMIGNYFSGVLIAGIILLILSCIFAFIDFSKSTSPTRTWKVLSIMSFILGIIITVGMLIYSMWGKHCAPHRVSGVIHTNHSDISVN | Function: Envelope protein which is a major component of the mature virion (MV) membrane. Essential for membrane biogenesis. Is required, together with OPG144, to form bona fide crescents, which can progress to form the immature virion (IV) membrane. OPG140 and OPG144 form a lattice that is stabilized by disulfide bond... |
P0CK28 | MISNYEPLLLLVITCCVLLFNFTISSKTKIDIIFAVQTIVFIWFIFHFVHSAI | Function: Protein probably involved in counteracting host defense, since it enhances virulence in vivo.
PTM: Not phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6165
Sequence Length: 53
Subcellular Location: Virion membrane
|
Q5AHE8 | MRVFQIVYILIISNLIYATSGGGTSSHHHKNDNNIADNTNNNNNNNNNNNNNNITNATTTRTVTTSTKTKTHTGGGVAAMGGILGQNGWFYGDAGLMAAIFGAMLLL | Function: Cell surface GPI-anchored protein required for virulence. Mediates hyphal ramification which is important for the interaction with host cells.
Location Topology: Lipid-anchor
Sequence Mass (Da): 11343
Sequence Length: 107
Subcellular Location: Cell membrane
|
Q5AHA4 | MKFSTVFTAIFALGTAVSAQQVVTPASDPLALELSQRNLDKLYELQERDLFSIVEGLFSSINYTSILDSIDYESIAGWTNNLLVENNNIEYLDNILNFLGDTDLVPFAVSYLLSNNETRNIVGEVVIEALPLIKDIDPTPIFVALKNSGLAYVLVADLIKNPNTVPFVKQVVVDLLDEGSFGLGDLFGGSSEATTTAVAIDSLATINTNIDLTVAAAPTTKAQSIGSIDTASLAVLFSEARTANGNGATKVANTVAVTAQVTAQVTNVGTTAKATKAVATGEINYSGITGPAYESLPPTQFGSVPTSINYSALSQISGAL... | Function: Predicted GPI-anchored protein which may have a role during host infection.
PTM: Substrate for cleavage by KEX2 in vitro.
Location Topology: Lipid-anchor
Sequence Mass (Da): 59541
Sequence Length: 557
Subcellular Location: Cell membrane
|
Q5AEG7 | MKLESIAVFAGIVSTALAGVYHKPPPATTYWTTIYAPSTSVVTVTSCSKGGCGTQSYATGVTKTKTVHEGVTTEYTTYCPLTTSHEVVKSTCSDTLVVWSTRSFSWVWSFSKPDGCGQSTSTIKTTAQTDVPTTATATPSVSTTCTTGTKTKWWWVIKTTDCSVYTVSSTSSSLISTSQVTSSSSIASTTATAPATPSVSTTCTTGTKTKWWWVIKTTDCSVYTVSSTLSSLISTSKATSSSSVASSTGSTPATTPGSSIESTPATTPGSSTESTPATATGSSTKSTPATTPGSSVTTGKTSTDWITSFTTHTAHTTTVI... | Function: Cell wall protein which mediates cell-cell and cell-substrate adhesion. Required for biofilm formation and plays a role in virulence (By similarity).
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-inosito... |
Q5AD34 | MFSTTSIVLWFTILLPVTLPVSIDNRDLLLKRHVEPNDIQFFNQGVRSSLSYIYQKRDVSDSDNEQVLRKSKKKKKTTSTGTPGNENTTDFASAQEFEKWEGDREGWQISAGLYFDKAIASDSCDSDSEDEDEGRKKFWIFTDDAPVDNENLIVSSEDKLELNYISSGKNLEGLTKVIRKAKGNSTTYNQSKIKFNVDAQGEDQFESGFGSLIPYNSFYLYILLFCIIF | Function: Predicted GPI-anchored protein which may have a role during host infection.
Location Topology: Lipid-anchor
Sequence Mass (Da): 26090
Sequence Length: 229
Subcellular Location: Cell membrane
|
Q5ACL7 | MNFNKFLIIISCYLACVFALANQNDGGDDDSKTKKTTTWVWVTTTIGGQLATISTAYSQKFISTHSSEDAKSVASGEIGLGSLSGSVGGIKTYSQTTITNANIAPSNNNVFLGIESLYTGIVGGIVLILGLL | Function: Plays a role in cell wall stability and rigidity. Required for normal adhesion to host cells and for adherence during biofilm formation. Necessary for proper oxidative stress response.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13804
Sequence Length: 132
Subcellular Location: Cell membrane
|
C6Y4B3 | MREFRLIFVLLFFLPSFAIANTEIINVETGDSNKLLTSNSVCDIELSNNSSIPLLLKPNPTIPQAAGAPQQSKYTFSVCGLKPLQKYQIRASWPAVYPSDIILNYNITHIIVEINASFYSHNESLMKRPPLVPLRLVVEPLLLGFLPKSVLPIVGFVFVIILIALICMTNLFIKHKRD | Function: Essential component of the GPI mannosyltransferase 2 complex. Responsible for the transfer of the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19995
Sequence Length: 178
Pathway: Glycolipid... |
P53896 | MVRPQNVHWFIATIVFFIGFVHANTESILYKVPHNFPLKKPRDSSTYARDVNLISSISLSGEAMSQITIEANTTDLELHNTTYIELADLQRDETYQIKVCWSAIHPISINNLQTITIPRFTEFQGTKSDYARILVTFQVLSDSYPSEHAMVPIQVSLITTRLGIPVDIYPTLIVMVLLVAGLVVTRAPHVLNDLLLKF | Function: Essential component of the GPI mannosyltransferase 2 complex. Responsible for the transfer of the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22383
Sequence Length: 198
Pathway: Glycolipid biosynthesis; g... |
Q59V02 | MKYSTLAWLVIASYTVFAQDGTSVTGYTTTIVIPGSPPAGAGTAHGDTENTGTVHTTEHLTGTEETHTTGATPETTTIVAPTTTHENTTTHETSVENTATVHHNTTTLHHNTTTIHPNATGTETHTETGTGTLTGTGTEGPALTTTTVAEAFSLAAGASLGYLVALLFL | Function: Putative adhesin which may be involved in cell adhesion and virulence.
Location Topology: Lipid-anchor
Sequence Mass (Da): 17335
Sequence Length: 169
Subcellular Location: Cell membrane
|
Q59V01 | MRVSTLVLSTSIIPIATALNISPFHNIEKKDILADAASAAGGAAAAVTSGAVGAANTVASGAAGAADTATSGAAGIANTVASGAAGAADTATSGAAGAAKTATSGAAGAADTATSGAVGAAKTATSGAAGAAKTATSGAAGAASGAETAAGAAASGAETAAAGQETSGAGSLVGGSGSSNSTSPSGGSGSSNGTSSGSGSGSGAGVGSGSGSGSGSRGSITGNSVATGASSGPAGLGISSSISQSTTRQLQTSGSSNSSSSAGMGNVVVGMNAVALAALVLI | Function: Probable cell surface protein involved in the process of adhesion and early events of invasion.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24390
Sequence Length: 282
Subcellular Location: Cell membrane
|
Q59L86 | MKVTAVSSVLLTVAALTNANEIDKRSFFGDLFSGLTGSKAAAPAAAPAAQPAAQPTTQSPADQPTVQSPVSSDQPSTAQPVAQNNLLLDSSNSTLVVPSSSKSSTTTRSTAGLLDNLLGGSGATSSEASSSEAPSSEAPSSEAPSSEAPSSEAPSSEAPSSSSSEALSSSSTTKRPTAAAKGFFGDLFGTQSSASETDDEDCVEETESPTSAPASAPTTSKVATTTGGGLPNILSDLFPGKSSAPISSAESSPTVASSTTGFPNILSDLFPGKSSVPSSSAETSTTVASNTTTSGGGFPNILSDLFPGKSSVPSSSAEED... | Function: Probable GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
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-inositol phos... |
Q5AA09 | MHFSKIIAGSALSSVALAEFQNGTVTTHVTATGYTTYCPYPTTITLTICEEENICTKRPIVVSEPTTVTVTEPCIISTSYETTEVVVTTTLPSSLSPSSVAPANVTSFEGAGSKNVASALVGVVAIAAAMM | Function: GPI-anchored protein involved in proper cell wall integrity. Does not seem to be directly involved in the synthesis of the cell wall. Required for normal virulence in a mouse model of disseminated candidiasis.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13509
Sequence Length: 131
Subcellular Location:... |
Q5A5K7 | MKFFAYFAVIALSSASLINLFKRATANGCEVESCYKAHQTLINSCNGAFDFNCLCNLPQSYFQNLYDCSKSCDTLQESDIHSPSDIRSIYCEAASNSIYTFSIDSISLDMIGYSDFETDTEATTGSDTRTKAATGATTSAGTGVTKTSETGGVSSTANSEAKSGSVTTSKSGSTSISESKTTSGSSSSGKSSSSTSSASSQQTSSHAGGASGAFVSLLGLFAALLI | Function: Putative adhesin which is involved in cell adhesion and virulence (By similarity). Plays a role in Candida-bacterial interactions and subsequent regulation of filamentation.
PTM: Predicted to be a cleavage substrate for KEX2.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23267
Sequence Length: 226
Subce... |
Q9P6S6 | MGFDVAGYLQSYSLKDWIRIIVYVGGYMLIRPYLMKLGAKIQEREHRKSLLEGEVDGTLDPEMTHGTKPKEHGEFDTDDEEEEENPDAEFRWGYSARRRIRKQREEYFKNQDKSPLDAYADDDEDIEEHLED | Function: Involved processing and trafficking glycosylated proteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15636
Sequence Length: 132
Subcellular Location: Endoplasmic reticulum membrane
|
P53903 | MSEVAETWVDTWMAKLVNYDYKHFIRLVIIVGGYLLLRNIASRELAKKQLAAQVEKDKRDKEEKRSKDLIDKPDDAATAETTSFGWGKKTRRRVKRQQELFENALEEAKRRNQGLDPDSDADIEELLEE | Function: Involved in the processing and trafficking of GAS1 and PHO8 glycosylated proteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15053
Sequence Length: 129
Subcellular Location: Endoplasmic reticulum membrane
|
Q5A5U6 | MKYFTIATVLTLASSALAAIRDVQLFAQSSNEEINNLGLISRREGAGVNYLFLASGAETLKFDDETFTIFSELQTGSTTARQSLVVSGGVVQLSVSGQPLHVEIAEDGSVKFAGSDSVAAAKNINDPYNYSKDSFAVVTNGGEGSIPFKIIAKFIGGGKSSSVTKHTEAPTTSPVYSNKTVTVFTTYCPESTTITLTICSEVCTPTVIETSGSVTVSSVLPSSSTEAPPKTSVAAPSTTAEAQTTAPVTSYEGGANEIVGGGSMAIALAAAAIGLVI | Function: Component of the cell wall involved in virulence which plays a role in the relationship between C.albicans and the host.
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-inositol phospholipid moiety is clea... |
Q5A5U9 | MKFLTAASLLTLSSSALAAIKDIQLYAQSSNNEVNDFGISSRHEGAALNYLFLAAPGVAENLKYDDETKTVYTELKAGSSTVRQPLNVGNTVLQLGGSGDGTKVDIAEDGTLSFDGSDSVGAAKNINDPYNYSKDSYAVVKGGDGAIPIKLVAKFTGDDKESASSSSSSAAPEPTASSSEAPKETPVYSNSTVTLYTTYCPLSTTITLTVCSDVCTPTVIETSGSVTVSSVQVPSKTASSEAAPPKTTVDSVSKPAPSGKKPTAAVTSFEGAANALTGGSVAIAVAAAIGLVF | Function: Component of the cell wall involved in virulence which plays a role in the relationship between C.albicans and the host (By similarity). Involved in the regulation or assembly of chitin within the cell wall.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the p... |
Q5ADQ7 | MKVSTLIIVSIPIVSGLQIKDTVGTTTENTFWYQLFGTPSRSQPAAVAATAAGTEVQGFTPISTSSSSSSSSAAPWYQGLFGVGRTTLGQVTTPSRTSTTTTTSNPIAPTTSIANSNNLFGTDTAPTTTTTTNARSRSRSTPVTVSGDNVLTLFGNPNLSTGNDQSNSVSKTTAETTTTSSAPSSSSRVQPTVINGGGSDGVLTLFGNSEALSNFDSTTVVDSDSTARITPIASASASSGSSTKDNDSDSSSARGIKSIPNSSEFLASLINGLGSGGGGNGSGSNTNSYKNHSTTSTTSKYFNSSSTATKLSSSKSIYSN... | Function: Putative adhesin which is involved in cell adhesion and virulence.
Location Topology: Lipid-anchor
Sequence Mass (Da): 43529
Sequence Length: 430
Subcellular Location: Cell membrane
|
Q5A210 | MKFTSLICSSILLIIPTVMADDASSDTTIINTITITKTLYTPEESSSLLSVQLESEASVASVASAASEAAASAASIASVASEASAASLASELSALAKVTEVKADVINNYNATINSTLSSSTIAPKISSSSSSSSSKKHESITSVITSSTKDNASAAVTTKTGSATSKAGAAAMAGPVPILTNSIFTAGLLALAAVLL | Function: Predicted GPI-anchored protein which may have a role during host infection.
Location Topology: Lipid-anchor
Sequence Mass (Da): 19497
Sequence Length: 197
Subcellular Location: Cell membrane
|
Q63921 | MSRRSLSLQFPLLLLLLLLPPPPVLLTDAGVPSPVNPCCYYPCQNQGVCVRFGLDHYQCDCTRTGYSGPNCTIPEIWTWLRSSLRPSPSFTHFLLTHGYWIWEFVNATFIREVLMRLVITVRSNLIPSPPTYNTAHDYISWESFSNVSYYTRILPSVPKDCPTPMGTKGKKQLPDIHLLAQRLLLRREFIPGPQGTNVLFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDSLERQYHLRLFKDGKLKYQVLDGEVYPPSVEQASVLMRYPPGVPPEKQMAVGQEVFGLLPGLMLFSTIWLREHNRVCDLLKE... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Dual cyclooxygenase and peroxidase that plays an important role in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular ... |
P70682 | MLARALLLCAALALGQAANPCCSNPCQNRGECLSVGFDRYKCDCTRTGYYGENCTTPEFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRNAIMIYVLTSRSHLIDSPPTYNAHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDSNEVLEKVLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKSDQKRGPAFTTGLAHGVDLSHIYGETLDRQHKLRLFKDGKMKYQIIDGEMYPPTVKETQVEMMYPPYIPEHARFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDERLFQTSRL... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory resp... |
P27607 | MLLPCALLAALLAAGHAANPCCSLPCQNRGVCMTTGFDRYECDCTRTGYYGENCTTPEFFTWLKLILKPTPNTVHYILTHFKGVWNIINNISFLRDTIMRYVLTSRSHLIDSPPTYNSDYSYKSWEAYSNLSYYTRSLPPVGHDCPTPMGVKGKKELPDSKLIVEKFLLRRKFIPDPQGTNVMFTFFAQHFTHQFFKTDHKKGPGFTKAYGHGVDLNHIYGETLERQLKLRLRKDGKLKYQMIDGEMYPPTVKDTQAEMIYPPHVPEHLQFSVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDEQLFQTTRL... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory resp... |
P35354 | MLARALLLCAVLALSHTANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFLTRIKLFLKPTPNTVHYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNADYGYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKYQIIDGEMYPPTVKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRL... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory resp... |
Q05769 | MLFRAVLLCAALGLSQAANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSLIMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLNHIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQVEMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWGDEQLFQTSRL... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response . The cyclooxygenase activity oxygenates arachi... |
A0A0A7LRQ7 | MYTSRLLLSNLASCLSLATLVASFPANQQDLTFAKRNGTFEQSVFYGLTGPEVEAKLAKLKADGYRPTSLNIHGSTSDAKYAGIWTKQTGDDFETILGANKTVYDAWLDSHKAQGYVSTHVSATGGSSDALFAGVMEKVPSVANWIQVCGLDNPYAYANATIDEPMYIKGVSMYGAPNERQYCILGHENLVNYQQTVFYQTDYFKKDYAKLLQSETSKRHWRPVFIDLSEDLLPTPIFDDTSVGQWVARTDLSASELEAEIAAQKAKNLYAVHIAGAGSKGSKYAVLFAEHLSPLERKWTVTGEVTGFKTNDVVAKDMDA... | Function: Serine-type endopeptidase that cleaves Gly-Gly bonds in the polyglycine linker of host plant class IV chitinases to disrupt their chitin-binding, and thereby plays a role in lowering the defense responses of the host to the fungus . Degrades Z.mays Endochitinase A (CHIA) . Degrades Z.mays Endochitinase B (CHI... |
C7YS44 | MHSLSLRRLLTSVLSLCSCSSALPNQRRSNVTSHVETYYSVDGATHAEKSKALKADGYRIVSLSSYGSPDSANYAAIWVQEEGPSFEIIHDADEATYNSWLQTWKSRGYVSTQVSATGPAENAVFAGVMENINVANWFQSCELENPWAFSNTTGNVDVVVKGFRMFGTPEERRYCILGHENVGNEQTTIQYSTPSFTVNFASTFEAETTKRFWRPSRLFLSEDHIITPSFADTSVGKWSHAVDLTKAELKEKIETERAKGLYPIDIQGGGSGSSERFTVVFAERTSPKPRQWNVRGEITGFEDNKAAEEEVDSIMRRFME... | Function: Serine-type endopeptidase that cleaves Gly-Gly bonds in the polyglycine linker of host plant class IV chitinases to disrupt their chitin-binding, and thereby plays a role in lowering the defense responses of the host to the fungus . Degrades Z.mays Endochitinase A (CHIA) in vitro, although corn is not its hos... |
Q1QCY9 | MNFLRMSELSLTDKVVLIREDLNVPIKAGKVASDARLQASLPTIKMALEKGAAVIVCSHLGRPTEGNPEAIYSLAPVADYLSDKLSAPVTLNSDYFTQGVAIEAGEVVLLENVRFNEGEKKNDAALAQKYADLCDVFVMDAFGTAHRAQASTEGVTQAMHKAGKTACAGPLLAAELDALSLALETPAQPMLAIVGGSKVSTKLEVLHSLAELCSQIIVGGGIANTFLAAQGHSVGASLYEADLLDTAREIMGKTEILLPEYVVVADKSDIDFADFTGSLQQASATIKSVDTIGENDMILDIAPDSAIKLAEAITKAKTIL... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 41736
Sequence Length: 400
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q83GI2 | MRTLGGFTFPCDAPVFVRVDFNVPMDEVGTITDDLRIRASLPTIESLLGRGAPLILISHLGRPVKNEQQGFSLKPCAERLSEYIGVNVPLVDFLDLDTKLYGELTRHLDKSGIVLFENIRFFAEETSKAQADRRILAEQLAPFAGAYVNDAFGASHRRHASVYELAQAFSNKAAGFLIESEMQAFSHLASEAKRPYTVILGGAKLSDKLRLIENILPTVDRLLLCGGMAFTFLAAQGCETGKSLLEESFIPEANKIIDFAKQNNVELILPVDVIEARSLTSPLGVVSKAESISYMGLDIGPETQSIFRNVIQDSKTVFWN... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42689
Sequence Length: 395
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q9PQL2 | MNSLNKKSIKDLDVNGKTIVLHLDLNVVVDYENKRILNDRKLRASLPTINYLINHNAKIVILSHLGRIKTLADKQSGKYSLEIIVDELRNRVSKNVNRVVFSPLNYGETVVQMVNDLEERDILILENTRYCDISDEGEYVGLEWDGSEILGQFWGMLGDIFIDDAYGVAHRQLSSNYQTAKFAKKSALGFLIVNEINHLDIALEVPKSPYLALIGGNRVADKIAAIEVLCERADQVIIGGGLVYTFLYAQGYNVGLNLVERNMIDDCNNILEKYGKKILICFDFLCNNDFSDTRPIYRKIDEGLEGLYGLDIGKRSLKFI... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 47383
Sequence Length: 422
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q8D2P9 | MKIIKVTDLNLKDKKVLIRSDLNVPIKNGKIMCNMRIIKSLETINFVIKNEAKCVIVASHLGNPIEEKYDYNFSLTHIVNHMKKIIKYPIRLIQNYLNGFEAKEKEIIVLENVRFNPGERKNDKNLSKKYANLCDILVMDSFGSSHRSESSTTGIIKFAPISCIGLLFLKEIKYLKKALFNSKRPIVTIFGGSKISTKLGVIEKLSNISENVLVGGGIANTILFSKGHNIGKSLHDKNNISKIKKFLYKKNIIIPKDFIVTDNINKFSSYKEKSIKEIKNEDYIVDIGKKSCECFIKIIKKAKTIFWNGPLGLIEIKQFR... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 44705
Sequence Length: 394
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
P62422 | MNIPSIENCDLHNKTVLLRVDFNVPIKDGEIRDVTRILRALPTIQYLVNASAKIIIISHFGRPKARDNNLSLKNVIDTLSQLLNKKVKFIDDCFGEKVQRAVSVMDAGDIILLENLRFYKEEEQSDSNFAKQLASLADIYVNDAFSCSHRAHASISRITEFLPSYAGFCLQDELKYLEKAVSFKAKPITAIVGGAKISTKIKVLMKLTEKVNYLVLGGAIANNFLSFSKVNIGKSFFQNGVDDLLHNILETANKNNCKIVVPEDVLVAVNSDYSTSISRRTESILDGDIILDIGPQTLSTISSIIASSKTLLWNGPIGVF... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 43305
Sequence Length: 398
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
B3CM25 | MINVPSIESCDFHNKNVLLRVDFNVPIKNGRICDATRILRALPTIQYLANAGAKVIVISHFGRPKAKDSNLSLKNVVETLSRLLSKEVKFIDDCIGERVQRAINAMDGGDIILLENLRFYKEEEQNDSNFAKQLASLADIYINDAFSCSHRAHASISRITEFLPSYAGFCLQDELKYLEQAISFDAKPITAIVGGAKISTKIKMLIKLAEKVDYLILGGAIANNFLLFNKVNIGKSFFQNGVDDLLHDIVETANKNNCKIVVPEDVLVAVNSDYSTGVLRKIESILDGDIILDIGPQTLSTISGIIASSKTLLWNGPIGV... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 43059
Sequence Length: 396
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q54UQ2 | MTDKINNLINQWLKWDKNEITRKEIEQLKENNNEKELLVRLEERIQFGTAGLRGAMRAGFSCMNDLTVTQASQGLCEYVIETIEQSKSKGIVIGYDGRHNSYIFAKITAATFKSKGFKVYLFSHIVPTPYVSFAVPNLKAAIGVMITASHNPKNDNGYKVYWETGCQINTPHDKGISKKIDENLEPWSNVDATSDIKYGNGDDGESMIDPLSVITELYNKNIKEYSVGSKIELANEPIVYTAMHGVGGVYAKKAFETFQLKPFIPVAQQIEPDAEFPTVTYPNPEEGKGALKLSIETAEANNSRLILANDPDADRLAVAE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: This enzyme participates in both the breakdown and synthesis of glucose.
Catalytic Activity: alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
Sequence Mass (Da): 67535
Sequence Length: 603
Subcellular Location: Cytoplasm
EC: 5.4.2.2
|
Q96G03 | MAAPEGSGLGEDARLDQETAQWLRWDKNSLTLEAVKRLIAEGNKEELRKCFGARMEFGTAGLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFSDLKQKGIVISFDARAHPSSGGSSRRFARLAATTFISQGIPVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDKGISQAIEENLEPWPQAWDDSLIDSSPLLHNPSASINNDYFEDLKKYCFHRSVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKYPNPEEGKGVLTLSFALADKTKARIVLA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. Catalyzes the interconversion of glucose-1-phosphate into glucose-6-phosphate but with a lower catalytic efficiency . I... |
Q7TSV4 | MAAATPTETPAPEGSGLGMDARLDQETAQWLRWDQNPLTSESVKQLIAGGNKEELRKCFGARMEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLEKQFSDLKQRGVVISFDARAHPASGGSSRRFARLAATAFITQGVPVYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLVDSSPLLHNPSASIGNDYFEDLKKYCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVKYPNPEEGKGVLTLSFALADK... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. Catalyzes the interconversion of glucose-1-phosphate into glucose-6-phosphate but with a lower catalytic efficiency. In... |
P37012 | MSFQIETVPTKPYEDQKPGTSGLRKKTKVFKDEPNYTENFIQSIMEAIPEGSKGATLVVGGDGRYYNDVILHKIAAIGAANGIKKLVIGQHGLLSTPAASHIMRTYEEKCTGGIILTASHNPGGPENDMGIKYNLSNGGPAPESVTNAIWEISKKLTSYKIIKDFPELDLGTIGKNKKYGPLLVDIIDITKDYVNFLKEIFDFDLIKKFIDNQRSTKNWKLLFDSMNGVTGPYGKAIFVDEFGLPADEVLQNWHPSPDFGGMHPDPNLTYASSLVKRVDREKIEFGAASDGDGDRNMIYGYGPSFVSPGDSVAIIAEYAA... | Cofactor: Binds 1 magnesium ion per subunit. Can also use Zn(2+) as cofactor.
Function: Major phosphoglucomutase isozyme that catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate . Constitutes about 80-90% of the phosphoglucomutase activity in the cell . Key enzyme in hexose metabolis... |
O74478 | MDPILQELVDEWFKLDQDETTRNEVSQLIKAEDYATLKQIMHPRIGFGTSGLRAEIGAGFARMNCLTVIQASQGFAEYLLQTVPSAAKLGVVIGHDHRHKSNTFARLTAAVFLQKGFKTYFFDHLVHTPLVPFAVKTLGTAAGVMITASHNPAAYNGYKVYWGNGCAIIPPHDKGIAACIEKNLTPITWDKNLVENHKLADRDFAVGLLKNYWSQLHEFHSENNFSLEMKSLKFVYTPIHGVGLPFVTSALHLFGEQGDMISVPLQDSPNPDFPTVKFPNPEEEGALDLAYEQADANGISYVLATDPDADRFAFAEKING... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Converts ribose 1-phosphate to ribose 5-phosphate. Involved in ribose salvage via the pentose phosphate pathway.
Catalytic Activity: alpha-D-ribose 1-phosphate = D-ribose 5-phosphate
Sequence Mass (Da): 65494
Sequence Length: 587
Subcellular Location: Cytoplasm
EC: 5.... |
Q03262 | MLQGILETVPSDLKDPISLWFKQDRNPKTIEEVTALCKKSDWNELHKRFDSRIQFGTAGLRSQMQAGFSRMNTLVVIQASQGLATYVRQQFPDNLVAVVGHDHRFHSKEFARATAAAFLLKGFKVHYLNPDHEFVHTPLVPFAVDKLKASVGVMITASHNPKMDNGYKVYYSNGCQIIPPHDHAISDSIDANLEPWANVWDFDDVLNKALKQGKLMYSREEMLKLYLEEVSKNLVEINPLKLEVKAKPWFVYTPMHGVGFDIFSTIVKKTLCLVEGKDYLCVPEQQNPDPSFPTVGFPNPEEKGALDIGINLAEKHDIDL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Major phosphoribomutase that converts ribose 1-phosphate to ribose 5-phosphate. Involved in ribose salvage via the pentose phosphate pathway.
Catalytic Activity: alpha-D-ribose 1-phosphate = D-ribose 5-phosphate
Sequence Mass (Da): 71069
Sequence Length: 622
Subcellul... |
Q9LSC4 | MAVSVSAPVLSLCYNQSGELSRSLGYRLPKKVGFSSGRRSVSYIGFGAEKVGRFRVRVPICRAVPPLLFKDLDADDFRHPFDKQNTLLLRAIPGLNEFGKALLGSMTEQIMLLENIGTSVLVSKNQLSDLHGLLVEAAEILNIEAPDLYVRQSPVPNAYTLAISGKKPFIVVHTSLIELLTSAELQAVLAHELGHLKCDHGVWLTFANILTLGAYTVPAFGQMIARTLEEQLLRWLRSAELTCDRAALLVAQDPKVVVSVLMKLAGGCPSIADQLNVDAFLEQARSYDKASSSPLGWYIRNAQTSQLSHPLPVLRAREID... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloendopeptidase with a Zn-dependent proteolytic activity and substrate cleavage upstream of hydrophobic residues . Positive regulator of senescence, probably by degrading CCD4, thus participating in the controlled removal of carotenoids from the thylakoid membrane ... |
A0A0C3RR82 | MSSASSDSNTGSLTIAGSGIASVRHMTLETLAHVQEADIVFYVVADPVTEAYIKKNARGPCKDLEVLFDKDKVRYDTYVQMAETMLNAVREGQKVLGIFYGHPGVFVSPSRRALSIARKEGYQAKMLPGISSEDYMFADLEFDPAVHGCCAYEATQLLLREVSLDTAMSNIIWQVGGVGVSKIDFENSKVKLLVDRLEKDFGPDHHVVHYIGAVLPQSATVQDVLKISDLRKEEIVAQFNSCSTLYVPPLTHANKFSGNMVKQLFGQDVTEVSSALCPTPKWAAGSHLGDVVEYGPREKAAVDALVEHTVPADYRVLGGS... | Function: Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities . Type II borosins derive from the C-terminus of the fusion protein, and it is ... |
Q0CJD1 | MLTKRRMKFQYISCLAWLAHYDIFHLVPRDKNISYADLARAAGVPEQRLKSILRMAMTSSLFREHPNGTDVGHSAVSALLASDDDAYSYATYMCSKTAPMAMSMTEAHKRWGASTRTNETAYNVAFNTDLPFFDYLAQNKARMDEFARYMRSVRSSETVALKHLISGVDWESIPAGGMLVDVGGSTGGAAIALAQAYPHIRFTVQDLPENVETGEKAAAASLPADIASRLTFQAHDFTLPQPVRAADAYLLRMILHDWPDEQAVKILRNIVTAMDETKSRLFIMDTVLPKPGSVPISVERIARARDLTMIQSFNSKEREL... | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of pleosporalin A, ascomycone A, as well as a third cryptic naphthoquinone derived pigment, all responsible for the coloration of conidia . Specifically methylates position C-6 of the pgmA product 3-acetonyl-1,6,8-trihydroxy-2-naphth... |
O06995 | MKAVIFDLDGVITDTAEYHFLAWKHIAEQIDIPFDRDMNERLKGISREESLESILIFGGAETKYTNAEKQELMHRKNRDYQMLISKLTPEDLLPGIGRLLCQLKNENIKIGLASSSRNAPKILRRLAIIDDFHAIVDPTTLAKGKPDPDIFLTAAAMLDVSPADCAAIEDAEAGISAIKSAGMFAVGVGQGQPMLGADLVVRQTSDLTLELLHEEWEQYRIRESIP | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. It plays a key r... |
P77366 | MKLQGVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGGKEGDFNSQERAQLAYRKNLLYVHSLRELTVNAVLPGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGAQLLLPSTESLTWPRLSAFWQNV | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the conversion of beta D-glucose 1-phosphate (G1P) to D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate (Probable). Phosphatase activity with the reaction intermediate beta-G16P has been measured . In ... |
P71447 | MFKAVLFDLDGVITDTAEYHFRAWKALAEEIGINGVDRQFNEQLKGVSREDSLQKILDLADKKVSAEEFKELAKRKNDNYVKMIQDVSPADVYPGILQLLKDLRSNKIKIALASASKNGPFLLEKMNLTGYFDAIADPAEVAASKPAPDIFIAAAHAVGVAPSESIGLEDSQAGIQAIKDSGALPIGVGRPEDLGDDIVIVPDTSYYTLEFLKEVWLQKQK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose a... |
O49299 | MVFKVSTVSTSPIDGQKPGTSGLRKKVKVFKQPNYLENFVQATFNALTAEKVKGATLVVSGDGRYYSKDAVQIIIKMAAANGVRRVWVGKNTLLSTPAVSAVIRERSGADGSKATGAFILTASHNPGGPTEDFGIKYNMENGGPAPESITDKIYENTKTIKEYPIAQDLPNVDISAVGVTSFEGPEGKFDVEVFDPADDYVKLMKSIFDFEAIRKLLSSPKFTFCYDALHGVAGAYAHRIFVEELGAQESALLNCTPKEDFGGGHPDPNLTYAKELVARMGLGKSDTGGEPPEFGAAADGDADRNMILGKRFFVTPSDSV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: This enzyme participates in both the breakdown and synthesis of glucose.
Catalytic Activity: alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
Sequence Mass (Da): 63171
Sequence Length: 583
Subcellular Location: Cytoplasm
EC: 5.4.2.2
|
A8HQD7 | MLALRQGALLLSARGGQTTHDNLQLCAGPSRRPRARWISSAPRPSTLVERHIRPQASTASDATTSTSQRILSIHDVDNGQILGFGADLAEDHPGFHDPAYKQRRAWLAEMAKTHRIGTPIPDVEYSPAEVATWDAVLEELSGLLPQHACREYLRCLTLFDFRKGRVPQLEEMNTVLRSTTGWTVRPVAGLMHPRHFLAGLAFKHFHSTQYMRHPSKPSYTPEPDVVHELIGHVPLLADPAYARLIQTIGLASLAADDKQIWHLTKVYWHTVEFGVVREGDQVKAFGAGILSSYGELAHMASGAAALERLDPFRPQPRMAY... | Function: Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine (Probable). Can functionally complement an Escherichia coli tyrosine auxotroph .
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine
Sequence ... |
P30967 | MNDRADFVVPDITTRKNVGLSHDANDFTLPQPLDRYSAEDHATWATLYQRQCKLLPGRACDEFMEGLERLEVDADRVPDFNKLNQKLMAATGWKIVAVPGLIPDDVFFEHLANRRFPVTWWLREPHQLDYLQEPDVFHDLFGHVPLLINPVFADYLEAYGKGGVKAKALGALPMLARLYWYTVEFGLINTPAGMRIYGAGILSSKSESIYCLDSASPNRVGFDLMRIMNTRYRIDTFQKTYFVIDSFKQLFDATAPDFAPLYLQLADAQPWGAGDVAPDDLVLNAGDRQGWADTEDV | Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine
Sequence Mass (Da): 33616
Sequence Length: 297
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step... |
Q54XS1 | MESNTNSQGQGIIPQSYHSSIFFSISKGSDKIGGLLEYLEIIKKHNINITRIESRPSKTEKKDYDFFLDLEYPTENNKEVEKVIKDLEEKGVKATTLQESSNQTYAPWFPRKISDLDLFANKVLEMGSDLTSDHPGASDPVYRERRREIAKIASTYKHGDEIPRIDYTEEEIKTWGVVYNRLKELFPTNACHQHAYIFPLLEQNCGYSPDNIPQLQDISNFLQECTGWRIRPVQGLLSARDFLNGLAFRVFHATQYIRHPSVPLYTPEPDCCHELLGHVPLLADPDFADFSQEIGLASIGASDEDIQLLSTCYWFTVEFG... | Cofactor: Binds 1 Fe(2+) ion.
Function: Catalyzes the hydroxylation of L-phenylalanine . Hydroxylates L-tryptophan to 5-hydroxy-L-tryptophan but does not hydroxylate L-tyrosine to L-DOPA . It uses D-threo-tetrahydrodictyopterin (DH4), also known as dictyoperin, as a cofactor.
Catalytic Activity: (6R)-L-erythro-5,6,7,8-... |
P00439 | MSTAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEK... | Function: Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine.
PTM: Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine.
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahy... |
P16331 | MAAVVLENGVLSRKLSDFGQETSYIEDNSNQNGAVSLIFSLKEEVGALAKVLRLFEENEINLTHIESRPSRLNKDEYEFFTYLDKRSKPVLGSIIKSLRNDIGATVHELSRDKEKNTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEERKTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEK... | Function: Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine.
PTM: Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine.
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahy... |
E5KBU4 | MAMEVGYLRHSTTITNGLCCNCDPKPRGARRVQTRLPGTLCLVKDTFTSSKAKLKKPSQREIFLTSRKRLNQIQAVSTAEKEREADKTSTPPIPSSIHDISNGDHILGFGADLTEDHPGYHDLEYKRRRSRIADLAKIHKIGEPIPCVDYTSEEIRVWGHVLDTLVDLYPTHACKEYLNCYELFNFKPNYIPQLQELSEVLERSTGWHIRPVAGLLHPRDFLNGLAFRTFHSTQYVRHGSNPMYTPEPDICHEVLGHVPILADPEFADLAWAIGQASLGASEKDIWHLTKLYWYTVEFGTVKEGNEIKAFGAGLLSSFGE... | Function: Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine . Does not seem to be tetrahydropterin-dependent and shows preference for 10-formyltetrahydrofolate as cosubstrate and electron donor .
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-ery... |
P43334 | MKTTQYVARQPDDNGFIHYPETEHQVWNTLITRQLKVIEGRACQEYLDGIEQLGLPHERIPQLDEINRVLQATTGWRVARVPALIPFQTFFELLASQQFPVATFIRTPEELDYLQEPDIFHEIFGHCPLLTNPWFAEFTHTYGKLGLKASKEERVFLARLYWMTIEFGLVETDQGKRIYGGGILSSPKETVYSLSDEPLHQAFNPLEAMRTPYRIDILQPLYFVLPDLKRLFQLAQEDIMALVHEAMRLGLHAPLFPPKQAA | Cofactor: Binds 1 Fe(2+) ion.
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine
Sequence Mass (Da): 30322
Sequence Length: 262
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumar... |
P04176 | MAAVVLENGVLSRKLSDFGQETSYIEDNSNQNGAISLIFSLKEEVGALAKVLRLFEENDINLTHIESRPSRLNKDEYEFFTYLDKRTKPVLGSIIKSLRNDIGATVHELSRDKEKNTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEK... | Function: Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine.
PTM: Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine.
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahy... |
Q98D72 | MSVAEYARDCAAQGLRGDYSVCRADFTVAQDYDYSDEEQAVWRTLCDRQTKLTRKLAHHSYLDGVEKLGLLDRIPDFEDVSTKLRKLTGWEIIAVPGLIPAAPFFDHLANRRFPVTNWLRTRQELDYIVEPDMFHDFFGHVPVLSQPVFADFMQMYGKKAGDIIALGGDEMITRLYWYTAEYGLVQEAGQPLKAFGAGLMSSFTELQFAVEGKDAHHVPFDLETVMRTGYEIDKFQRAYFVLPSFDALRDAFQTADFEAIVARRKDQKALDPATV | Cofactor: Binds 1 Fe(2+) ion.
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine
Sequence Mass (Da): 31348
Sequence Length: 275
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumar... |
Q9KLB8 | MSKIPLAVRIGLGRLNVTNLLRSRAMTQYHSKPVSEHGHIDWDQDEHAVWHELITRQQEVVKTRACQAYLDGLNMLNLPTDRLPQLPEINRVLQRETGWQVEPVPALISFDRFFALLADKKFPVATFLRRREEFDYLQEPDFFHEVYGHCAMLTHPDFAAFTHVYGQLGAKATPKERSYLARLYWFTVEFGLVQEQGQTKIYGGGILSSPGETLYASESTIPKREPFDIMQVLRTPYRIDIMQPIYYVLPDLSQLYQLSQRDVMALVWQAMQDGLLPPLFQPKEQQHAG | Cofactor: Binds 1 Fe(2+) ion.
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine
Sequence Mass (Da): 33445
Sequence Length: 289
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumar... |
P52090 | MLAKQIKKANSRSTLLRKSLLFAAPIILAVSSSSVYALTQVSNFGTNPGNLQMFKHVPSGMPANAPLVVALHGCTQTAAAYEASGWSALGNTHKFYVVYPQQQSGNNSNKCFNWFEPGDITRGQGEALSIKQMVDNMKANHSIDPSRVYVTGLSAGAFMTTVMAATYPDVFAGAAPIAGGPYKCATSMTSAFTCMSPGVDKTPAAWGDLARGGYSGYNGPKPKISIWHGSSDYTVAPANQNETVEQFTNYHGIDQTPDVSDTVGGFPHKVYKSANGTPLVETYTITGMGHGTPVDPGTGANQCGTAGAYILDVNVCSSYY... | Function: Specific for poly(hydroxyalkanoic acid) consisting of monomers of four or five carbon atoms and for P-nitrophenylbutyrate as substrates.
Sequence Mass (Da): 43496
Sequence Length: 414
Subcellular Location: Secreted
EC: 3.1.1.-
|
O14361 | MSASKIAFLGPRGTFSHQAALLARPDSLLCSLPSFAAVLEALSSRQVDYAVLPIENSTNGAVIPAYDLLKGRDDIQAVGEVLVPAHHCIIGKSLENVQKILSHPQAFGQCSKWISANVPNAEFVSVSSTSQAAALASKDITGTIVAISSELCAVENQFNLLVKNIEDDSNNRTRFLLLRSGGFQDDLSPLKEKSLLQFYLSHPKKLSAVFEVFAAHKVVITNLVVRPSCKFPWTYIYFVECLGMEKHLIDRVGKYCDTFTFMGSYTNQISYF | Function: Putative prephenate dehydratase required for the syntheis of L-phenylalanine.
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Mass (Da): 29871
Sequence Length: 272
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Subcellula... |
P32452 | MASKTLRVLFLGPKGTYSHQAALQQFQSTSDVEYLPAASIPQCFNQLENDTSIDYSVVPLENSTNGQVVFSYDLLRDRMIKKALSLPAPADTNRITPDIEVIAEQYVPITHCLISPIQLPNGIASLGNFEEVIIHSHPQVWGQVECYLRSMAEKFPQVTFIRLDCSSTSESVNQCIRSSTADCDNILHLAIASETAAQLHKAYIIEHSINDKLGNTTRFLVLKRRENAGDNEVEDTGLLRVNLLTFTTRQDDPGSLVDVLNILKIHSLNMCSINSRPFHLDEHDRNWRYLFFIEYYTEKNTPKNKEKFYEDISDKSKQWC... | Function: Catayzes the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Mass (Da): 38225
Sequence Length: 334
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Subcellular Lo... |
Q8K2W6 | MDSDSCAAAFHPEEYSPTCKRRRTVEDFNKFCTFVLAYAGYIPYPKEELPLRSSPSPANSTAGTIDSDGWDTGFSDITPSVPDRCFSHLQPSLLQRAKPSNYLLDRKTTDKLKKKKRRKRRDSDIPVKEGFRESLLKLEAADPYVETPSSPTMQDIPQASADPCSGWDSDTPSSGSCATVSPDQVTEIKTEGKRTIVRQGKQVVFRDEDSTGNDEDIMVDSDDDSWDLVTCFCMKPFAGRPMIECNECHTWIHLSCAKIRKSNVPEVFVCQKCRDSKFDIRRSNRSRMGSRKLFLD | Function: Modulates chromatin structure. Required for normal chromosome condensation during the early stages of mitosis. Required for normal chromosome separation during mitosis (By similarity).
PTM: Subject to proteasomal degradation. Stable when bound to chromatin. The soluble form is rapidly degraded (By similarity)... |
A0A286Y9D1 | MDRGSKRRQVKPLADSLLDALDYDSSDDSDFKVGESSGSEGTGNGSDEEGSKESAAGSESDSDAAAASADEEGIDDLETKDLNQEDDEEEKVKESFSEETSSKETGGSSRSRKKGEKSSDMEPNGSATTEENSAEPKKWNLRRNRPMLDFTTMEELNEMDDYDSEDDNDWRPTQGKKKGKASSGKEKEGSGEEDDDDDDGGSDEEDNEDDNDDDDDDDDEGNDDESSSSDSEEEGKKPKKKAGKNTGAFDEEETNDSHSTSHGKGNEDSLLERPQTWSSQRMEHILICCVCLGDNSEDADEIIQCDNCGVTVHEGCYGVD... | Function: Histone-binding protein . Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) . Represses PDGFRA expression, thus playing a rol... |
Q9D4H9 | MDRSSKRRQVKPLAASLLEALDYDSSDDSDFKVGDASDSEGSGNGSEDPSKDSGEGSCSDSEENILEEELNEDIQVKEEQLKNSTEEIMPSDKQLIKMEKKEEEENGERPRKKKEKEKEKEKEREKDKEKATVSDSAAASAAGTTPATSPPAVTSPSVPTTTTTTTEEQVSEPKKWNLRRNRPLLDFVSMEELNAMDDYDSEDDNDWRPTVVKRKGRSASQKEGSDGDNEDDDDEGSGSEEDENDEGNDEDHSSPASEAGGKKKRSKVLSRNSADDEELTNDSLTLSQSKSNEDSLILEKSQNWSSQKMDHILICCVCLG... | Function: Histone-binding protein (By similarity). Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity). Represses PDGFRA ... |
Q5T6S3 | MENRALDPGTRDSYGATSHLPNKGALAKVKNNFKDLMSKLTEGQYVLCRWTDGLYYLGKIKRVSSSKQSCLVTFEDNSKYWVLWKDIQHAGVPGEEPKCNICLGKTSGPLNEILICGKCGLGYHQQCHIPIAGSADQPLLTPWFCRRCIFALAVRKGGALKKGAIARTLQAVKMVLSYQPEELEWDSPHRTNQQQCYCYCGGPGEWYLRMLQCYRCRQWFHEACTQCLNEPMMFGDRFYLFFCSVCNQGPEYIERLPLRWVDVVHLALYNLGVQSKKKYFDFEEILAFVNHHWELLQLGKLTSTPVTDRGPHLLNALNSY... | Function: Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity . Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K3... |
Q9CXG9 | METQALEPGTLEAFGATSPNKGGLSKTKKNFKDLMSKVTEGQFVLCRWTDGLYYLGKIKRVSSPKQSCLVTFEDNSKYWVLWKDIQHAGVPGEEPKCDVCMGKTSGPMNEILICGKCGLGYHQQCHIPIAVDANWPLLTHWFCRRCIFALAVRKGGALKKGAIAKTLQAVKMVLSYQPEELDWDSPHRTNQQQCYCYCGGPGEWYLRMLQCYRCRQWFHEACTQCLSEPMVFGDRFYLFFCSVCNQGPEYIERLPLRWVDIVHLALYNLGVQSKKRYFDFEEILAFVNHHWELLQLGKLTSTPMTERGPHLLNALNSYKS... | Function: Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity . Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K3... |
Q8GYE0 | MEIEEASRESGHVVCGSWIRRPKKVNWVLIAKASKRRGSSVSSPALLNIFSFDPITASLSSSPLATHTLKDSDGDPVAVSVHPGGDYFVCSTSKGGCKLFELVGGATGITILAKELLPLQNAGLQKCMAFSFDGSKLAVGGVDGCLRIMEWPNLSVILDEPKAHKSIRDMDFSLDSEFLATTSTDGSARIWKAEDGFPLSTLERSGDENIELCRFSKDGTKPFLFCAAQRGDTPMVNVYDISTWKKLGFKKLSRKTASTMAVSLDGKYIALGGKDGDVSVAEVKTMEIYHYSKRLHLGQSIASLEFCPSERVMLTTSSEW... | Function: Involved in Pi uptake by facilitating the trafficking of PHT1-1/PHT1;1 from the endoplasmic reticulum to the plasma membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 43767
Sequence Length: 398
Subcellular Location: Endoplasmic reticulum membrane
|
P29166 | MKTIIINGVQFNTDEDTTILKFARDNNIDISALCFLNNCNNDINKCEICTVEVEGTGLVTACDTLIEDGMIINTNSDAVNEKIKSRISQLLDIHEFKCGPCNRRENCEFLKLVIKYKARASKPFLPKDKTEYVDERSKSLTVDRTKCLLCGRCVNACGKNTETYAMKFLNKNGKTIIGAEDEKCFDDTNCLLCGQCIIACPVAALSEKSHMDRVKNALNAPEKHVIVAMAPSVRASIGELFNMGFGVDVTGKIYTALRQLGFDKIFDINFGADMTIMEEATELVQRIENNGPFPMFTSCCPGWVRQAENYYPELLNNLSS... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Catalytic Activity: H2 + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 63828
Sequence Length: 574
EC: 1.12.7.2
|
O43189 | MAQPPRLSRSGASSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGTSWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSRLLSALNSHKDRFISGR... | Function: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it i... |
Q9Z1B8 | MAQLPRLSRLGAPSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGASWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSQLLSALNSHKDRFISGR... | Function: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it i... |
Q9BVI0 | MTKHPPNRRGISFEVGAQLEARDRLKNWYPAHIEDIDYEEGKVLIHFKRWNHRYDEWFCWDSPYLRPLEKIQLRKEGLHEEDGSSEFQINEQVLACWSDCRFYPAKVTAVNKDGTYTVKFYDGVVQTVKHIHVKAFSKDQNIVGNARPKETDHKSLSSSPDKREKFKEQRKATVNVKKDKEDKPLKTEKRPKQPDKEGKLICSEKGKVSEKSLPKNEKEDKENISENDREYSGDAQVDKKPENDIVKSPQENLREPKRKRGRPPSIAPTAVDSNSQTLQPITLELRRRKISKGCEVPLKRPRLDKNSSQEKSKNYSENTD... | Function: Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes (By simil... |
A5D962 | MLEAMAEPSPEDPPPTLKPETQPPEKRRRTIEDFNKFCSFVLAYAGYIPPSKEESDWPASGSSSPLRGESAADSDGWDSAPSDLRTIQTFVKKAKSSKRRAAQAGPTQPGPPRSTFPRLQAPDSATLLEKMKLKDSLFDIDGPKMASPLSPTSLTHASRPPAALTPVPLSQGDLSQPPRKKDRKNRKLGPGGATGFGVLRRPRPAPGDGEKRSRIKKSKKRKLKKAERGDRLPPPGPPRAPPSDTDSEEEEEEEEEEEEMAAMVGGEAPAPVLPTPEAPRPPATVHPEGAPPTDGESKEVGSTETSQDGDASSSEGEMRV... | Function: Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria.
Sequence Mass (Da): 43440
Sequence Length: 400
Domain: The PHD-type zinc-finger domain is required for interact... |
Q9BUL5 | MLEAMAEPSPEDPPPTLKPETQPPEKRRRTIEDFNKFCSFVLAYAGYIPPSKEESDWPASGSSSPLRGESAADSDGWDSAPSDLRTIQTFVKKAKSSKRRAAQAGPTQPGPPRSTFSRLQAPDSATLLEKMKLKDSLFDLDGPKVASPLSPTSLTHTSRPPAALTPVPLSQGDLSHPPRKKDRKNRKLGPGAGAGFGVLRRPRPTPGDGEKRSRIKKSKKRKLKKAERGDRLPPPGPPQAPPSDTDSEEEEEEEEEEEEEEMATVVGGEAPVPVLPTPPEAPRPPATVHPEGVPPADSESKEVGSTETSQDGDASSSEGE... | Function: Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria.
Sequence Mass (Da): 43818
Sequence Length: 403
Domain: The PHD-type zinc-finger domain is required for interact... |
Q8BSN5 | MLEAMAEPSPEDPPPTLKPETQPPEKRRRTIEDFNKFCSFVLAYAGYIPPSKEESDWPASGSSSPLRGESAADSDGWDSAPSDLRTIQTFVKKAKSSKRRAVQSGPTQPGPPRSTFSRLQAPDSATLLEKMKLKDSLFDLDGPKVASPLSPTSLTHTSRPPAALAPVPLSQGDLSQPRKKDRKNRKLGPGGGAGFGVLRRPRPAPGDGEKRSRIKKSKKRKLKKADRGDRLPPPGPPRAPPSDTDSEEEEEEEEEEDDEEEMTVGGGVPAPVLPTPPEAPRPPVTVHSEGAPPTDSEGKDVGSTETSQDGDASSSEGEMR... | Function: Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria.
Sequence Mass (Da): 43547
Sequence Length: 401
Domain: The PHD-type zinc-finger domain is required for interact... |
Q5U5E5 | MLETTMGEASPEDPPLNLKSLSQPPQKRSRTVEDFNRFCSFVLAYAGYIPTPAKEERAWTPPSSVSPHRTEESDGWDSPDPPQLPAPPEPPQPPATSDISTIETFVMKAKSQGAGGGSSKMPGGQEDGAEEEEVQAKKGSRRKRRQRHRGGVRMSDTDTDEEEREERPAAPGSLPAPQLPPSAESSRDGGGSSSDADTQVMDEDIMVESGDDSWDLVTCYCEKPFAGRPMIECNVCCTWVHLSCAKIRKSNVPDVYYCQKCRAGRLPGATTPKADSAP | Function: Acts as a negative regulator of autophagy.
Sequence Mass (Da): 30183
Sequence Length: 278
Domain: The PHD-type zinc-finger domain is required for negative regulation of autophagy.
Subcellular Location: Nucleus
|
Q7CKG8 | MARLIYLMGPSGAGKDCLLSALRNATPQNRVVAHRYITRPADAGAENHVALSKQEFIQRAEQGLFALHWQAHQHCYAIGIEINLWLQHGLDVLVNGSRAYLPEAQRRYRHQLLPLCLTVSPAILAQRLRQRGRENSEQIDARLQRAQHYQQQLPSHCLQLCNDGELQHTLNQLQQLLTLDTPLSDPVEDKPCN | Function: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP).
Catalytic Activity: alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + ADP
Sequence Mass (Da): 21918
Sequence Length: 193
Pathway: Metabolic intermediate biosynthesis; 5-ph... |
Q8ZKE6 | MILMRRREDVMPVCELRHATTEDTDSVYALICELLKNELDYQAFRDGFAANLLDPNVHYRLALRNGEVVGMISLHMQFHLHHANWIGEIQELVVLPPMRGQKIGSQLLAWAEEEARQAGAELTELSTNIKRRDAHRFYLREGYKQSHFRFTKAL | Cofactor: Requires a divalent metal ion for activity. In vitro, exhibits a preference for Ni(2+) followed by Mn(2+) and very poor activity with Mg(2+). However, it is unclear what the physiologically relevant metal ion is.
Function: Aminoalkylphosphonate N-acetyltransferase which is able to acetylate a range of aminoal... |
C8WJZ5 | MIEDLHVHSTMSDGSDTFEQVLEQAAQRGVERLAFTNHDTTAGLTAARELGERLGVQVVGGIEVSAYDFERGRKVHILGLGVEEGAPALAALCGSTLERRHANSLWQLDRLVEAGYEVDVERALELGRASTCLYKQHLMAALTSEPYPSAAYRTLYRSLFKNGGICDRDIDYVDARDAVRVVVEDGGLAVLAHPGQLDSYDLLPDLVECGLGGIERFHPDHTLADHARCAELAVRYRLVCTGGSDYHGKFGRVPHVGFRVPA | Function: Involved in degradation of methylphosphonate. Catalyzes the hydrolysis of the phosphate ester at carbon-1 of 5-phospho-D-ribose 1,2-cyclic phosphate to form ribose 2,5-bisphosphate. This intermediate is then hydrolyzed to ribose-5-phosphate and inorganic phosphate.
Catalytic Activity: alpha-D-ribose 1,2-cycli... |
P16692 | MSLTLTLTGTGGAQGVPAWGCECAACARARRSPQYRRQPCSGVVKFNDAITLIDAGLHDLADRWSPGSFQQFLLTHYHMDHVQGLFPLRWGVGDPIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKTLKFLRNNQPQVMVMDCSHPPRADAPRNHCDLNTVLALNQVIRSPRVILTHISHQFDAWLMENALPSGFEVGFDGMEIGVA | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the hydrolysis of the cyclic ribose-phosphate to form alpha-D-ribose 1,5-bisphosphate.
Catalytic Activity: alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + H2O = alpha-D-ribose 1,5-bisphosphate + H(+)
Sequence Mass (Da): 27848
Sequence Length: 252
EC: 3... |
P13062 | ALTGRRPSVVYLHAAQCTGCSEALLRTTKPFR | Cofactor: Binds 1 [3Fe-4S] cluster.
Catalytic Activity: 2 Fe(III)-[cytochrome c3] + H2 = 2 Fe(II)-[cytochrome c3] + 2 H(+)
Sequence Mass (Da): 3504
Sequence Length: 32
Subcellular Location: Periplasm
EC: 1.12.2.1
|
P18187 | MNFSVGLGRDDAEKRLVQNGVSRRDFMKFCATVAAAMGMGPAFAPKVAEALTAKHRPSVVWLHNAECTGCTEAAIRTIKPYIDALILDTISLDYQETIMAAAGEAAEAALHQALEGKDGYYLVVEGGLPTIDGGQWGMVAGHPMIETTKKAAAKAKGIICIGTCSAYGGVQKAKPNPSQAKGVSEALGVKTINIPGCPPNPINFVGAVVHVLTKGIPDLDENGRPKLFYGELVHDNCPRLPHFEASEFAPSFDSEEAKKGFCLYELGCKGPVTYNNCPKVLFNQVNWPVQAGHPCLGCSEPDFWDTMTPFYEQG | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Involved in hydrogen uptake for the anaerobic reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is the physiological electron acceptor.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide clea... |
Q52990 | MLPKIAVVEDEEALSVLLRYNLEAEGFEVDTILRGDEAEIRLQERLPDLLILDWMLPGVSGIELCRRLRQRPETERLPIIMLTARGEESERVRGLATGADDYVVKPFSTPELMARVKAMLRRAKPEVLSTLLRCGDIELDRETHRVHRRSREVRLGPTEFRLLEFLMSSPGRVFSRSQLLDGVWGHDIYVDERTVDVHVGRLRKALNFSNMPDVIRTVRGAGYSLES | Function: This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited (By similarity).
PTM: Phosphorylated by PhoR.
Sequence Mass (Da): 26018
Sequence Length: 227
Subcellular Location: Cytoplasm
|
P45607 | MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISPMAVEEVIKMQGLSLNPTSHRVMAGEEPLEMGPTEFKLLHFFMTHPERVYSREQLLNHVWGTNVYVEDRTVDVHIRRLRKALEPGGHDRMVQTVRGTGYRFSTRF | Function: This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited.
PTM: Phosphorylated by PhoR.
Sequence Mass (Da): 26431
Sequence Length: 229
Subcellular Location: Cytoplasm
|
P34349 | MTAATENRTVRRNGPGTKRADWNNWSPLAFEEMDSALNIQQYIQQTIKANPADVATILTPPLDQDEGVWKYEHLRQFCIELNGLALLLQRECIPETCQQMTATEQWIFLCAAHKNPNECPAIDYTRHTLDGAATLLNSNKYFPSRVNIKEISISKLGSVARRVYRIFSHAFFHHRKLFDEFENETHLCKRFTTYVSKYNLMQQEHLIVPILPNQQQQQQTTVQ | Function: May play a role in membrane trafficking, specifically in membrane budding reactions.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25895
Sequence Length: 223
Subcellular Location: Cytoplasm
|
Q5F495 | MVMAEGTAVLRRNRPGTKAQDFYNWPDESFEEMDSTLAVQQYIQQNIRADCSNIDKILEPPEGQDEGVWKYEHLRQFCLELNGLAVKLQSECHPDTCTQMTATEQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVAKLGSVCRRIYRIFSHAYFHHRQIFDEYENETFLCHRFTKFVMKYNLMSKDNLIVPILEEEVQNSVSGGE | Function: May play a role in membrane trafficking, specifically in membrane budding reactions.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25816
Sequence Length: 223
Subcellular Location: Cytoplasm
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.