ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9ULC3 | MLEEDMEVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQACVLVFSTTDRESFEAVSSWREKVVAEVGDIPTVLVQNKIDLLDDSCIKNEEAEALAKRLKLRFYRTSVKEDLNVNEVFKYLAEKYLQKLKQQIAEDPELTHSSSNKIGVFNTSGGSHSGQNSGTLNGGDVINLRPNKQRTKKNRNPFSSCSIP | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
P35288 | MLEEDMEVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQACVLVFSTTDRESFEAISSWREKVVAEVGDIPTALVQNKIDLLDDSCIKNEEAEGLAKRLKLRFYRTSVKEDLNVSEVFKYLAEKHLQKLKQQITEDPEQTHSSSNKIGVFNASVGSHLGQNSSSLNGGDVINLRPNKQRTKRTRNPFSSCSVP | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
Q55FU9 | MTKTKIDLKVVLLGYASVGKTCIVTRYTSGQFGDTHTTIGGAFSSKRVVVGETEVLLGIWDTAGTERYQAVNVSYYRRANAAIVCYDLTNRESWEKVTFWAEELTQNEPEIEIYIVGTKLDLIQQGDIKAVPEEEVKQTARRYKAHIFETSSRTGENVSLLFQTIAEDFCKRTNNGTNPVNSNPSNVVNVNTQTQKKKGGCC | Function: May be involved in autophagy-related processes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22516
Sequence Length: 202
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment
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Q969Q5 | MSGQRVDVKVVMLGKEYVGKTSLVERYVHDRFLVGPYQNTIGAAFVAKVMSVGDRTVTLGIWDTAGSERYEAMSRIYYRGAKAAIVCYDLTDSSSFERAKFWVKELRSLEEGCQIYLCGTKSDLLEEDRRRRRVDFHDVQDYADNIKAQLFETSSKTGQSVDELFQKVAEDYVSVAAFQVMTEDKGVDLGQKPNPYFYSCCHH | Function: May be involved in autophagy-related processes.
PTM: Isoprenylation is inefficient compared to other Rab family members.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23124
Sequence Length: 203
Subcellular Location: Cytoplasm
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P35290 | MSGQRVDVKVVMLGKEYVGKTSLVERYVHDRFLVGPYQNTIGAAFVAKVMCVGDRTVTLGIWDTAGSERYEAMSRIYYRGAKAAIVCYDLTDSSSFERAKFWVKELRSLEEGCQIYLCGTKSDLLEEDRRRRRVDFHDVQDYADNIKAQLFETSSKTGQSVDELFQKVAEDYVSVAAFQVMTEDKGVDLSQKANPYFYSCCHH | Function: May be involved in autophagy-related processes.
PTM: Isoprenylation is inefficient compared to other Rab family members.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23144
Sequence Length: 203
Subcellular Location: Cytoplasm
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Q58DW6 | MGNRAEEDYNFVFKVVLIGESGVGKTNLLSRFTRNEFSHDSRTTIGVEFSTRTVMLGTAAIKAQIWDTAGLERYRAITSAYYRGAVGALLVFDLTKHQTYAVVERWLKELYDHAEATIVVMLVGNKSDLSQSREVPTEEARMFAENNGLLFLETSALDSTNVELAFETVLKEIFAKVSKQRQNNARTNAVTLGSGPAGQELGPGEKRACCISL | Function: Involved in the regulation of cell survival. Promotes invasive migration of cells in which it functions to localize and maintain integrin alpha-V/beta-1 at the tips of extending pseudopodia. Involved in the regulation of epithelial morphogenesis through the control of CLDN4 expression and localization at tigh... |
P57735 | MGNGTEEDYNFVFKVVLIGESGVGKTNLLSRFTRNEFSHDSRTTIGVEFSTRTVMLGTAAVKAQIWDTAGLERYRAITSAYYRGAVGALLVFDLTKHQTYAVVERWLKELYDHAEATIVVMLVGNKSDLSQAREVPTEEARMFAENNGLLFLETSALDSTNVELAFETVLKEIFAKVSKQRQNSIRTNAITLGSAQAGQEPGPGEKRACCISL | Function: Involved in the regulation of cell survival. Promotes invasive migration of cells in which it functions to localize and maintain integrin alpha-V/beta-1 at the tips of extending pseudopodia . Involved in the regulation of epithelial morphogenesis through the control of CLDN4 expression and localization at tig... |
Q9WTL2 | MGNRTDEDYNFVFKVVLIGESGVGKTNLLSRFTRNEFSHDSRTTIGVEFSTRTVMLGTAAVKAQIWDTAGLERYRAITSAYYRGAVGALLVFDLTKHQTYAVVERWLKELYDHAEATIVVMLVGNKSDLSQAREVPTEEACMFAENNGLLFLETSALDSTNVELAFQTVLKEIFAKVSKQKQNSTRTSAITLGNAQAGQDPGPGEKRACCISL | Function: Involved in the regulation of cell survival. Promotes invasive migration of cells in which it functions to localize and maintain integrin alpha-V/beta-1 at the tips of extending pseudopodia. Involved in the regulation of epithelial morphogenesis through the control of CLDN4 expression and localization at tigh... |
Q29RR0 | MSRKKTPKSKAGSAPATSALPAANGPRPVRPGTARPGPEAPPNGPPQPGRSSVGGGGDFYDVAFKVMLVGDSGVGKTCLLVRFKDGAFLAGTFISTVGIDFRNKVVDVDGMKVKLQIWDTAGQERFRSVTHAYYRDAHALLLLYDVTNKASFDSIQAWLTEIQEHAQDDVVLMLLGNKVDSAQERAVKREDAEKLAKDYGLPFMETSAKTGLNVDLAFTAIAKELKQRHTKAPSEPRFQLHDYIKREGRGASCCRP | Function: Participates in exocrine secretion: regulates the secretion of acinar granules in the parotid gland.
Location Topology: Lipid-anchor
Sequence Mass (Da): 27802
Sequence Length: 256
Subcellular Location: Cell membrane
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Q9VP48 | MASTAVGLGGGEGDPGAGGPPAGSAHPDDASSMSDDVFEDAETTQARIEELRRRPFGDGSYNPPAAPASVSASITTTTTQQQQQHHNPSHHHQSSHHQPSHHHHHHHHSQLSLTGSHHYHDDAIMAPVQRSATGYPGYRPSREAMQMYAYGTDDYDDDYNDGWRSYRYDEVDMHPAPSNAHQQPFDDTVNHKTILLGDSGVGKTSFLVKYNTGEFRLGSFSATVGIALTNKVVVVDGTRVKLQIWDTAGQERFRSVTHAYYRDAHALLLLYDVTNKTTYDNIRAWLGEIREYAQEDVVIVLIGNKADCSGSERQVKREDG... | Function: Participates in exocrine secretion.
Location Topology: Lipid-anchor
Sequence Mass (Da): 43037
Sequence Length: 388
Subcellular Location: Cell membrane
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Q9ULW5 | MSRKKTPKSKGASTPAASTLPTANGARPARSGTALSGPDAPPNGPLQPGRPSLGGGVDFYDVAFKVMLVGDSGVGKTCLLVRFKDGAFLAGTFISTVGIDFRNKVLDVDGVKVKLQMWDTAGQERFRSVTHAYYRDAHALLLLYDVTNKASFDNIQAWLTEIHEYAQHDVALMLLGNKVDSAHERVVKREDGEKLAKEYGLPFMETSAKTGLNVDLAFTAIAKELKQRSMKAPSEPRFRLHDYVKREGRGASCCRP | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
Q504M8 | MSRKKTPKSKGGSEPATSTLPAAAAATNGPRLAHPRTVRPGPEAPPNGPPQSIRPSLGSTGDFYDVAFKVMLVGDSGVGKTCLLVRFKDGAFLAGTFISTVGIDFRNKVLDVDGMKVKLQIWDTAGQERFRSVTHAYYRDAHALLLLYDITNKDSFDNIQAWLTEIQEYAQQDVVLMLLGNKVDSTQDRVVKREDGEKLAKEYGLPFMETSARTGLNVDLAFTAIAKELKQRSAKAPSEPRFRLHDYVKREGRGVSCCRL | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
P51156 | MSRKKTPKSKGGSVPAASTLPAAANGPRLAHPRTARPGPEAPPNGPPQSGRPSLGGTGDFYDVAFKVMLVGDSGVGKTCLLVRFKDGAFLAGTFISTVGIDFRNKVLDVDGMKVKLQIWDTAGQERFRSVTHAYYRDAHALLLLYDITNKDSFDNIQAWLTEIQEYAQQDVVLMLLGNKVDSTQERVVKREDGEKLAKEYGLPFMETSAKSGLNVDLAFTAIAKELKQRSTKAPSEPRFRLHDYVKREGRGVSCCRL | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
Q39435 | MSASRFIKCVTVGDGAVGKTCLLISYTSNTFPTDYVPTVFDNFSANVVVNGATVNLGLWDTAGQEDYNRLRPLSYRGADVFILAFSLISKASYENVSKKWIPELKHYAPGVPIVLVGTKLDLRDDKQFFIDHPGAVPITTAQGEELRKLIGAPAYIECSSKTQQNVKAVFDAAIKVVLQPPKTKKKKSKAQKACSIL | Function: Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21516
Sequence Length: 19... |
Q03206 | MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGRPINLGLWDTAGQEDYDRLRPLSYPQTDVFLVCFALNNPASFENVRAKWYPEVSHHCPNTPIILVGTKADLREDRDTVERLRERRLQPVSQTQGYVMAKEIKAVKYLECSALTQRGLKQVFDEAIRAVLTPPQRAKKSKCTVL | Function: Required in engulfing to control the phagocytosis of apoptotic cell corpses . Required in embryonic development for the correct positioning and orientation of the mitotic spindles and division planes in blastomere cells . Involved in hypodermal cell fusion, together with pak-1 and cdc-42, leading to embryonic... |
P80236 | AKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRTVFDEAIR | Function: Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion,... |
P40792 | MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDAKPINLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVNPASFENVRAKWYPEVRHHCPSTPIILVGTKLDLRDDKNTIEKLRDKKLAPITYPQGLAMAKEIGAVKYLECSALTQKGLKTVFDEAIRSVLCPVLQPKSKRKCALL | Function: During various developmental processes, regulates changes in cell morphology in response to extracellular signals . During oogenesis, mediates signaling from the tyrosine kinase (RTK) chemoattractant receptors (Egfr and Pvr) to the guidance pathway that control the directional persistent collective migration ... |
P63000 | MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL | Function: Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion,... |
O04369 | MSASRFIKCVTVGDGAVGKTCLLISYTSNTFPTDYVPTVFDNFSANVVVDGSTVNLGLWDTAGQEDYNRLRPLSYRGADVFILAFSLISKASYENIAKKWIPELRHYAPGVPIILVGTKLDLRDDKHFLADHPGAVPITTAQGEELRKLIGAPAYIECSSKTQQNVKAVFDAAIKVVLQPPKQKKKKREAQKSCSIL | Function: Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21619
Sequence Length: 19... |
Q9SSX0 | MSSAAAATRFIKCVTVGDGAVGKTCMLICYTCNKFPTDYIPTVFDNFSANVSVDGSVVNLGLWDTAGQEDYSRLRPLSYRGADVFILSFSLISRASYENVQKKWMPELRRFAPGVPVVLVGTKLDLREDRAYLADHPASSIITTEQGEELRKLIGAVAYIECSSKTQRNIKAVFDTAIKVVLQPPRHKDVTRKKLQSSSNRPVRRYFCGSACFA | Function: Small GTPase playing a general role in disease resistance signaling pathway. Acts downstream of heterotrimeric G protein alpha subunit. Regulates cell death and reactive oxygen species production, probably through NADPH oxidase. Also involved in sphingolipid elicitor (SE)-dependent defense signaling. Activate... |
A0A286QZ36 | MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGRPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRTKWYPEVSHHCPSTPIILVGTKLDLRDDKETMNKLSERSLRPIAYPQGLQMQKEIHAVKYLECSALTQKGLKTVFDEAIRAVLCPPAKNKSKRSCQLL | Function: Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states.
Location Topology: Lipid-anchor
Sequence Mass (Da): 21476
Sequence Length: 192
Subcellular Location: Cell membrane
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O49841 | MGSSSGQSGYDLSFKILLIGDSGVGKSSLLVSFISSSVEDLAPTIGVDFKIKQLTVGGKRLKLTIWDTAGQERFRTLTSSYYRGAQGIILVYDVTRRETFTNLVDVWGKEIELYSTNQECVRMLVGNKVDRESERGVSREEGIALAKELNCMFLECSARTRQNVEQCFEELALKIMEVPSLLEEGSSAVKRNILKQKPEHQTNTQSGCCS | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23306
Sequence Length: 210
Subcellular Location: Cell membrane
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Q9SF92 | MGSSSGQSGYDLSFKILLIGDSGVGKSSLLLSFISSSVEDLAPTIGVDFKIKQMKVRGKRLKLTIWDTAGQEKFRTLTSSYFRGSQGIILVYDVTKRETFLNLADIWAKEIELYSTNHDCIKMLVGNKVDRESERKVSREEGMALAKDLNCLFHECSARTRENVNGCFEELALKIMEVPSLLEEGSSSVKRKPDYRAHQGRCCSS | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22904
Sequence Length: 205
Subcellular Location: Cell membrane
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Q38903 | MSTARFIKCVTVGDGAVGKTCMLISYTSNTFPTDYVPTVFDNFSANVVVDGSTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLISKASYENIHKKWLPELKHYAPGIPIVLVGTKLDLRDDKQFLKDHPGAASITTAQGEELRKMIGAVRYLECSSKTQQNVKAVFDTAIRVALRPPKAKKKIKPLKTKRSRICFFL | Function: Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22393
Sequence Length: 20... |
Q9TU25 | MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLRDDKDTIEKLKEKKLAPITYPQGLALAKEIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQPTRPQKRPCSIL | Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the prod... |
Q94124 | MQAIKCVVVGDGAVGKTCLLLSYTTNAFPGEYILTVFDTYSTNVMVDGRPINLSLWDTAGQDDYDQFRHLSFPQTDVFLVCFALNNPASFENVRAKWYPEVSHHCPNTPIILVGTKADLREDRDTIERLRERRLQPVSHTQGYVMAKEIKAVKYLECSALTQIGLKQVFDEAIRTGLTPPQTPQTRAKKSNCTVL | Function: During gonad morphogenesis, plays a role in distal tip cell (DTC)-mediated guidance of gonad elongation .
Location Topology: Lipid-anchor
Sequence Mass (Da): 21915
Sequence Length: 195
Subcellular Location: Cell membrane
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P48554 | MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDAKPINLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVNPASFENVRAKWFPEVRHHCPSVPIILVGTKLDLRDDKQTIEKLKDKKLTPITYPQGLAMAKEIAAVKYLECSALTQKGLKTVFDEAIRSVLCPVVRGPKRHKCALL | Function: Involved in integrin alpha-PS3/beta-nu-mediated phagocytosis of Gram-positive S.aureus by hemocytes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 21359
Sequence Length: 192
Subcellular Location: Cell membrane
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Q9QWZ1 | MPLLTQYNEEEYEQYCLVASLDNVRNLSTVLKAIHFREHATCFATKNGIKVTVENAKCVQANAFIQADVFQEFVIQEESVTFRINLTILLDCLSIFGSSPTPGTLTALRMCYQGYGHPLMLFLEEGGVVTVCKITTQEPEETLDFDFCSTNVMNKIILQSEGLREAFSELDMTGDVLQITVSPDKPYFRLSTFGNAGNSHLDYPKDSDLVEAFHCDKTQVNRYKLSLLKPSTKALALSCKVSIRTDNRGFLSLQYMIRNEDGQICFVEYYCCPDEEVPES | Function: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch b... |
Q3SWX9 | MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLASTGASNLLLEPEQSTSNLNEKINHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNVSMGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKR... | Function: As a member of the cohesin complex, involved in sister chromatid cohesion from the time of DNA replication in S phase to their segregation in mitosis, a function that is essential for proper chromosome segregation, post-replicative DNA repair, and the prevention of inappropriate recombination between repetiti... |
O60216 | MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLVSTTTSNLLLESEQSTSNLNEKINHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNVSMGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKR... | Function: As a member of the cohesin complex, involved in sister chromatid cohesion from the time of DNA replication in S phase to their segregation in mitosis, a function that is essential for proper chromosome segregation, post-replicative DNA repair, and the prevention of inappropriate recombination between repetiti... |
P30776 | MFYSEAILSKKGPLAKVWLAAHWEKKLSKVQTLHTSIEQSVHAIVTEETAPMALRLSGQLMLGVVRIYSRKARYLLEDCTEALMRLKMSFQPGQVDMIEPATALQSLKGKDAVTQSANLTLPETITEFDLLVPDSTFDFQWSQLLRTPSRSSNTLELHSLPISSSPSFPSSQLSIEAGRNAQVESGFSLGESFAHVGNDMQFHLPISNSGAATPRSVHSDNQSQISIEVGRDAPAAAATDLSGIIGPQMTKSPASSVTHFSTPSMLPIGGTSLDDELLAPVDDLNLDLGLDDLLGDEQGANAPAIEADEQAETSSIHLPS... | Function: Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphas... |
Q6E6J3 | MTRCGWHTCTRVRPRMGETLLPRKASQHEFEPEEIRMKQEHTECPLLVSHNGIIILETFTANAKQATDFLIAIAEPVSRPAHVHEYRITPYSLYAAVSVGLTTEDILSTLDRFAKNTVPDTIVRFVRECTLSYGKTRLVFKGGRFLVEAATREVFDVLTGDAEISRLRAAGTVRDADARYVFEVRVDCIEQVRRRCIEIDYPMIEEYDFRDDVALRSLDMDLRDTVSIRTYQEVSLNKMFGNRRARSGVIVLPCGAGKTLVGITAMCTIKKPCIVLCTSGVSVEQWRQQVLAFSTVSADAVSRFTSERKEMFEADAGILI... | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH... |
P62135 | MVIVKKVILNNVKTHSKREFDFEKGINLILGPNGSGKTTLVESIFLALFGGDFARVIDYFKKGEKTMAITLILEDKGKTYRIRRKWVLENNAKLVESSLELIDTIPKKLASDHNKLLQQIKHLFGLDKKIIPLIYYKQNEITKIIEMDPRKRKEWFDEILGIKDLEEFSEKLKMAIKLIKTGKISRIEDRIKLLKAELNKKSLLENKLKNYKEKLVLLSNELENLEKEYKILENQYKEYLELKAKLKSIEGQINNINVKEIESKINNIREELNNIEELTDYEKDILSKKHEIIRCNEIKNRLKELEKEIKDYDKIKKEFL... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging ... |
Q9UZC8 | MKIEEVKVYNFRSHEETVVRFRKGINLIIGQNGSGKSSLLDAILVGLYWSKKLRLRGLKKDEFRRIGGKGGTRIEIKFENDDSKYVLFRDFSRNVAYLKVQENGKWRHASEPSMESVSSYIERILPYNVFLNAIYIRQGQIDAILESDETRDKVVREILNLDKLESAYENLKRIKTNINLLIESKKSFIARTENIEELIKANEDELTKKLSEINEISSKLPPIRGELEKVRENVKELESIKGKISELKIQVEKLKGRKKGLEEKIVQIERSIEEKKAKISELEEIVKDIPKLQEKEKEYRKLKGFRDEYESKLRRLEKEL... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging ... |
P58301 | MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPLRIKDIKKDEFTKVGARDTYIDLIFEKDGTKYRITRRFLKGYSSGEIHAMKRLVGNEWKHVTEPSSKAISAFMEKLIPYNIFLNAIYIRQGQIDAILESDEAREKVVREVLNLDKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKNEYLDKKYKIEK... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair . The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA . Rad50 controls the balance between DNA end bridgin... |
Q97WH0 | MRIDKITLTNFLSHEHSEIQFMGEINVIVGQNGAGKSSIIDGIVFSLFRTHSRGNNDNLIRKGSNRGSVTLYLSNEKDKIEIIRDIRSTTEDRLIRNQFPIARSATVVSNEIEKILGIDKDIALSTIIVRQGELDKILENFQEIMGKILKLELIEKLIDSRGPIVEFRKNLENKLRELDRIEQDYNNFKKTVEEKRARVLELKKDKEKLEDEIKNLEKRIKDIKDQFDEYEKKRNQYLKLTTTLKIKEGELNELNRSIEELRKQTENMDQLEKEINELENLRNIKLKFEKYEVLAKSHTEMSANVINLEKEIEEYEKAIR... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging ... |
O33600 | MIIREIRLQNFLSHEDTTVKFEGSINVIIGNNGAGKSSIIDGILFGLFKRTNRDIGKNEELIKKGKKSGQVSIKFEINGDTYLIDRNVGETSRDTISLLKEGKIITLARQSTTVNNKIKEILGFDHKILMSTTIIGQGSVESVFSDFPEVMKELLKINKLEMLRESNGPIHSLIKVLTDRIRSLQSIKDILKREEAEIDRLKKEIEEIKVKLENIEREAKEKEDELNQYNTEFNRIKEIKVQYDILSGELSVVNKKIEEIALRLKDFEEKEKRYNKIETEVKELDENREKINTISSFKSILVQIDSLKSQINVVENDLKR... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging ... |
Q96YR5 | MIIRRIDIENFLSHDRSLIEFKGTVNVIIGHNGAGKSSIIDAISFSLFRKSLRDAKKQEDLIKRGAGRATVTLYLENKGKIYVIKRNAPNQYTSEDTISELTNDTRRTIARGATTVSQKIKELLNLDEEVLKSTIIVGQGKIESVFENLPDVTKKILKIDKIEKLRDSNGPIKEVMDKINNKIIELQSLEKYKNESENQKIQKEKELENIKRELEDLNIKEEKERKKYEDIVKLNEEEEKKEKRYVELISLLNKLKDDISELREEVKDENRLREEKEKLEKDILEKDKLIEEKEKIIEAQNKIKLAQEKEKSLKTIKINL... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging ... |
Q9HLR8 | MIIDRIRLINFLSHEDSEIFFDTGVNIIVGHNGAGKSSIIDAIRFALFGDKRTKKIEDMIRKGAKSLEVEMEFRHGGHTYIIRRSITRRSKNPESNAMIMVDGSALSQSVKDANDYIEKNIITKSKDVFLNSVFSKQGEMDDLISGDPARRKKLLDEILEIEKLEETYDVLKDVIDSLQAGISNLDYLISENERDRDDLRRYQDDVAELSKQIDQEEAIESDLLRKKEEASAEYNAVSKELIMLDATLKNMMSLSDEANRYEEEIRKIDGKLQEISGSTERYNEITSSKVYASRERIRGYWTDKGQIIDYRKMLKNIDGQ... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging ... |
Q5JHN1 | MKIEKLIIKDFRSHALTKVNFSSGINLIIGQNGSGKSSILDALLVGLYWPSKPKDLKKDDFERINGSGTEITVFFEKGNVKYQIHRNIGRGLAFVKYHDGSSWKTLETGQKPVRDWMEKLVPYDVFLNAIYIRQGEIDAILESDESREKVVRQVLGLDRYENSYKNLLDVRKEIDARIKAIEDYLKSTENIDELIGNLEKELTSVLREINEISPKLPELRGELGGLEKELKELEKTAEELAKARVELKSEEGNLRELEAKKSGIQSMIRETEKRVEELKEKVKELESLEEKAKEYERLSRFYRNFTEGINRIEKLLATYS... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging ... |
Q9X1X1 | MRPERLTVRNFLGLKNVDIEFQSGITVVEGPNGAGKSSLFEAISFALFGNGIRYPNSYDYVNRNAVDGTARLVFQFERGGKRYEIIREINALQRKHNAKLSEILENGKKAAIAAKPTSVKQEVEKILGIEHRTFIRTVFLPQGEIDKLLISPPSEITEIISDVFQSKETLEKLEKLLKEKMKKLENEISSLQALYTAIWKYLEENDLEVLKSELKTVSEKKKELLKKREELQKEEEQLKRLLEKYRELVKKKERLRVLSLRRNELQKEVIYEQKVKKAKELEPLFREIYLRQREFERFSQELNSREKRYKELESEKEAIS... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositio... |
P58302 | MIIERIRLRNFLSHSDSDIYFDTGINMIIGQNGAGKSSIVDAIRFALFSDKRTRRTEDMIKKGERYMEVELYFRSEGHSYRIRRTIERRGKSISTDAEIERDGSIITRGASDVSNYVEKNVLNINKDVFLTSIFVRQGEMDALVSKDPAERKKILDEILNIDRLEAGYLLLKEVIDDLTANVSDYDYLKNELQSKINEIDNNNKQIEELESKLRLIEPEIKALEEEINIKENKKDHLNEELHRLNAQLETIKKYEMELAESQSRKASIEMEVVKLPSIEEELKRLENNAAVVKRNEIIEYINLKKDLGSLSEIIEGLKSD... | Cofactor: Binds 1 zinc ion per homodimer.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging ... |
P33919 | MIFTLRPYQQEAVDATLNHFRRHKTPAVIVLPTGAGKSLVIAELARLARGRVLVLAHVKELVAQNHAKYQALGLEADIFAAGLKRKESHGKVVFGSVQSVARNLDAFQGEFSLLIVDECHRIGDDEESQYQQILTHLTKVNPHLRLLGLTATPFRLGKGWIYQFHYHGMVRGDEKALFRDCIYELPLRYMIKHGYLTPPERLDMPVVQYDFSRLQAQSNGLFSEADLNRELKKQQRITPHIISQIMEFAATRKGVMIFAATVEHAKEIVGLLPAEDAALITGDTPGAERDVLIENFKAQRFRYLVNVAVLTTGFDAPHVD... | Function: RadD contains helicase motifs, suggesting it may be a helicase, although that activity has not been observed (Probable). In combination with RadA is important in repair of double-strand DNA breaks (DSB) . Has DNA-independent ATPase activity that is stimulated by single-stranded DNA-binding protein SSB. ATPase... |
C5H884 | MATSRDFGREPPRQQQDSDEAGHTLHDGCQHVSEHPQIDVTAHDSSASALPGDETTVGAATAALDPKEEERDPNIVDWDGPDDPANPQNWPPLKKWGNVAVLSIITFMVPLASSMFAPGIPQVLSDFDTNNPSLATFVVSVYILGLAAGPLVLAPMSELYGRVVIYHVGNVLFIIFTVACALSTNMNMLIAFRFLCGLVGAGPIAIGGGTIADLTTLQQRGTAMSVWSLGPLLGPSVGPVAGGFLSQAEGWRWIFWVLAITAGVITIAGLLVLRETHPGTLLERKTRRLRKETGNMNLRSKLDLQVAPRTLFLRSIVRPS... | Function: Efflux pump that might be required for efficient secretion of radicicol or other secondary metabolies produced by the radicicol gene cluster .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58448
Sequence Length: 538
Subcellular Location: Cell membrane
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C5H881 | MSIPKSCEVLVAGGGPAGSYAASALAREGVDVVLLEADKHPRYHIGESMLPSIRPLLRFIDLEETFEKHGFQKKLGAAFKLTAKREGYTDFVAAHGPNGYSWNVVRSESDELLFKHAAKSGALTFQGVKVDSLEFEPYDSDFPSGGKVANPGRPVAARWSAKDGRSGTISFQYLVDATGRAGITSTKYLKNRKFNEGLKNLAIWGYYKGARPWAEGTPRENQPYFEGMRDGAGWCWTIPLHNGTVSVGAVLRSDLFFAKKKSLGEDVTNAMIMAECMKLCPTIKELLEPAELVSDIKQATDYSYSASAYAGPYFRIVGDA... | Cofactor: Binds 1 FAD per subunit.
Function: Non-heme halogenase; part of the gene cluster that mediates the biosynthesis of radicicol, a resorcylic acid lactone (RAL) that irreversibly inhibits the HSP90 molecular chaperone, an important target for cancer chemotherapy . The cluster encodes only two apparent post-PKS e... |
Q6WVP7 | MTDRLKGKVAIVTGGTLGIGLAIADKFVEEGAKVVITGRHADVGEKAAKSIGGTDVIRFVQHDASDEAGWTKLFDTTEEAFGPVTTVVNNAGIAVSKSVEDTTTEEWRKLLSVNLDGVFFGTRLGIQRMKNKGLGASIINMSSIEGFVGDPTLGAYNASKGAVRIMSKSAALDCALKDYDVRVNTVHPGYIKTPLVDDLEGAEEMMSQRTKTPMGHIGEPNDIAWICVYLASDESKFATGAEFVVDGGYTAQ | Function: NADP-dependent (R)-specific alcohol dehydrogenase (ADH) with a broad substrate specificity, able to catalyze in vitro the stereoselective reduction of several aliphatic and aromatic ketones as well as beta-keto esters to the corresponding enantiomerically pure alcohols.
Catalytic Activity: a secondary alcohol... |
Q9PU45 | MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVRKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQSKYGDYNKEIHKLGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLER... | Function: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 68555
Sequence Length: 583
Subcellular Location: Cell membrane
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P26043 | MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLER... | Function: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.
PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capab... |
C5H886 | MAEFHPTAFLLPAAVTMIAGYFLCTALYNVYFHPLAKFPGPRLYAASQIPITIKRLLGDEVATFHKLHAKYGQFVRVAPGELSTINPAASRDVYGHRNPAKSIPKDFKAYYMKNQRRDGTEGLMTADDDLHRRQRKIFSPAFSDRAIREQEPLLKKYTDLLVEKAGVASDADGKVDMVMMFNFATFDFIADCVFGDSLHLLEKMEYNPFLANISAVVKFSAMRRAIRSFPYMDETFEKLIPASMKRKRMEHVKFCDDLVDRRLEKAVTNHPDFWTLVLRANEKGEGLTLGEMHQNSFLFLTAATETTSSLMSALTYLLCQ... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of radicicol, a resorcylic acid lactone (RAL) that irreversibly inhibits the HSP90 molecular chaperone, an important target for cancer chemotherapy . The cluster encodes only two apparent post-PKS enzymes, a cytochrome P450... |
K7PEY4 | MHPCLVETESVSLLQEEITIITMASSTFPTVNKCTSIGREKHTVVADMDGTLLIGRSSFPYFALIAFEVGGVLRLLIYLLASPIAAILYYFISESAGIQVLVFASMAGMKLSSIESVARAVLPKFYSSDLHPETWRVFSSCGKRCVLTANPRIMVEPFLKEFLGADMVLGTEIASYKGRATGLICKPGILVGDKKAQVLKKTFGDEKPDIGLGDRVTDAPFMALCKEGYIVPAKPKVTTVTSDKLPKPIIFHDGRLVQKPTPLMALLIILWIPIGFPLACLRIAAGSLLPMKFVYCAFKALGVRVIVKGTPPPPVETSKT... | Function: Involved in the production of cutin monomers . Esterifies acyl-group from acyl-ACP to the sn-2 position of glycerol-3-phosphate, a step in cutin biosynthesis (Probable). Required for colonization of the root by mycorrhizal fungi, and appropriate hyphopodia and arbuscule formation . Cutin monomers act as plant... |
O88039 | MSPAAGAPGSGPGRRRLPALDVRRFSPVRKSRPVPPRAPGRALEVLVLLCSVAAAVAAVAQPLALGRTLDLLLRDGDAGWWLPLSAALLLGELLLDSATSLFTGRCNATWTASVRTRALRGLLRTAPEHARPYPPGDIGTRLTLNAADAGGAPAARAALAASLITPLGALVALALVDVWVALCVLTGLPALALLLRSFARDTGATVAAYQRTQSLIASRLLEALEGADTIGAAGTGERERARVLAPLAELAAQGRHMWALHGRALGRSGVLVPLLTLAATAVGGLRLAAGELSVGDLLAVGRYAQLTAGVGAAASLLGAI... | Function: Probably involved in exporting SapB from the cell (Probable). Expression of the ram locus (ramA, ramB and ramR) induces rapid aerial mycelium formation in S.lividans .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65481
Sequence Length: 636
Subcellular Location: Cell membrane
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Q7AKE5 | MTSTEAGALRRLAPPARRFLAHRKGVLVRLALWSLAESGQAFLVGHAVARSVDEGFLAGDPRRGLLWLGVALVAVLSGARVVRGVFAQLAGVTEPLRDGLVRHAVDRSMARAAPGGPGGTDRAAVSRLTNQVEIARDSFAGLVLTLRSFVFTAAGALLGLLSLHPALLVVVLPPLAAGLALFLVTLRPMAAAQRRALAADEALGEHAASARAALRDLTACGTGPGAERHGADLVADAAAAARTLAGWAAVRTAALGVAGHLPVLALLVAVEWLRGHGVSVGALLGAFTYLVQSLLPALHTLMTALGAAGSRLLVVLDRIL... | Function: Probably involved in exporting SapB from the cell (Probable). Expression of the ram locus (ramA, ramB and ramR) induces rapid aerial mycelium formation in S.lividans .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62531
Sequence Length: 608
Subcellular Location: Cell membrane
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O60894 | MARALCRLPRRGLWLLLAHHLFMTTACQEANYGALLRELCLTQFQVDMEAVGETLWCDWGRTIRSYRELADCTWHMAEKLGCFWPNAEVDRFFLAVHGRYFRSCPISGRAVRDPPGSILYPFIVVPITVTLLVTALVVWQSKRTEGIV | Function: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 16988
Sequence Length: 148
Subcellular Location: Membra... |
Q9WTJ5 | MAPGLRGLPRCGLWLLLAHHLFMVTACRDPDYGTLIQELCLSRFKENMETIGKTLWCDWGKTIQSYGELTYCTKHVAHTIGCFWPNPEVDRFFIAVHHRYFSKCPISGRALRDPPNSILCPFIALPITVTLLMTALVVWRSKRTEGIV | Function: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 16892
Sequence Length: 148
Subcellular Location: Membra... |
Q867C0 | MARGLRGLPRRGLWLLLVNHLFLATACQDTDHAALLRKYCLPQFQVDMEAIGKALWCDWDKTIGSYKDLSDCTRLVAQRLDCFWPNAAVDKFFLGVHQQYFRNCPVSGRALQDPPSSVLCPFIVVPILATLLMTALVVWRSKRPEGIV | Function: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 16760
Sequence Length: 148
Subcellular ... |
Q6EPW7 | MSTEAETTSAAAPAPAPAPASAPARCQRIGCDATFTDDNNPDGSCQYHPSGPMFHDGMKQWSCCKQKSHDFSLFLAIPGCKTGKHTTEKPITKAVPTKPSKAVPVQTSKQSVGADTCSRCRQGFFCSDHGSQPKAQIPTATSDTNMVPVEKPAVPPPKKKIDLNEPRVCKNKGCGKTYKEKDNHDEACDYHPGPAVFRDRIRGWKCCDIHVKEFDEFMEIPPCTKGWHNADAA | Function: Involved in basal disease resistance to virulent strain of bacterial blight (X.oryzae) and compatible race of rice blast fungus (M.grisea). May act as positive regulator of basal defense. Associates with HSP90 and is essential for the pathogen-associated molecular pattern (PAMP)-triggered immune responses spe... |
Q7ZTI3 | MYESVDVVGLTPSPNPFLSMDYYHQNRGCLIPDKGLVSGAARGFRNPHWSGSNHSVETQSTSSEEIVPSPPSPPPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHREKSCIINKVTRNRCQYCRLQKCLEVGMSKESVRNDRNKRKKDDKKQECLENYVLSPDTEKMIEQVRKAHQETFPSLCQLGKYTTNNSADHRVALDVDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPDQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAE... | Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) c... |
Q90966 | MASNSSSCPTPGGGHLNGYPVTPYAFFFPHMLGGLSPPSSLPGIQHQLPVSGYSTPSPATVETQSTSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKDVPKTECSESYIVTPEVEELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLE... | Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) c... |
P10276 | MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGALTTLQHQLPVSGYSTPSPATIETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEVPKPECSESYTLTPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLE... | Function: Receptor for retinoic acid . Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes . The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE)... |
P10826 | MTTSGHACPVPAVNGHMTHYPATPYPLLFPPVIGGLSLPPLHGLHGHPPPSGCSTPSPATIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKETSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLE... | Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) c... |
F4I6V0 | MMSRIEAYQSDIAVLMDPETVLLPDFISALSYAHELGRDWLLVSSSVEIPRFPFHWDETRHFWRQDNGKRVRFRELQKMISLRSLQSNSSASKMIMAWNNIDMPLHCGVLPPFLYQRGTHNQWIINEAMSCKRRFVFDATSTISSFFLGNAENIYNRSDNVSEPKTRNWEYVGNSHLGQLYGSLYSRSYTLPKLLKCNRRYIFVSASERSTDLSIPKGKSLGFRTREKISACITRTKSRSLKLDFVQKDETVPPLKFPFDLESLLPLVADKNRTVVLSVAGYSYKDMLMSWVCRLRRLKVPNFLVCALDDETYQFSILQG... | Function: Beta-arabinofuranosyltransferase that transfers specifically an arabinosyl residue from UDP-arabinofuranose to the monosaccharide galactose or beta-methyl-galactoside in vitro. Catalyzes the addition of a beta-arabinofuranose residue onto a beta-galactosyl residue of an Yariv-precipitable wall polymer in vivo... |
O01803 | MGSRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSISVEGKTVKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHVTYENVERWLKELRDHADQNIVIMLVGNKSDLRHLRAVPTDEAKIYAERNQLSFIETSALDSTNVEAAFTNILTEIYKSVSNKHVGTDRQGYGGGSGTIIPSPASDPPKKQCCIP | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes . Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors direct... |
P62491 | MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNGLSFIETSALDSTNVEAAFQTILTEIYRIVSQKQMSDRRENDMSPSNNVVPIHVPPTTENKPKVQCCQNI | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
P0C2C2 | MNAPETIQAKPRKRYDAGVMKYKEMGYWDGDYVPKDTDVLALFRITPQDGVDPVEAAAAVAGESSTATWTVVWTDRLTACDMYRAKAYRVDPVPNNPEQFFCYVAYDLSLFEEGSIANLTASIIGNVFSFKPIKAARLEDMRFPVAYVKTFAGPSTGIIVERERLDKFGRPLLGATTKPKLGLSGRNYGRVVYEGLKGGLDFMKDDENINSQPFMHWRDRFLFVMDAVNKASAATGEVKGSYLNVTAGTMEEMYRRAEFAKSLGSVIIMVDLIVGWTCIQSMSNWCRQNDMILHLHRAGHGTYTRQKNHGVSFRVIAKWL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active ... |
Q0WQX7 | MARDRREGLEIKVVNPPAAATNNVAVETSPATATRRRRQQQRASFAEFRPFKLWFPWLVPAIVVANIALFAISMFINNCPKNSAYCLARFLGRFAFQPMKENPLLGPSSLTLEKMGALDVSMVVHKHEVWRLFTCIWLHAGVFHVLANMLSLIFIGIRLEQEFGFVRIGLLYMISGFGGSLLSSLFNRAGISVGASGALFGLLGAMLSELLTNWTIYANKFAALLTLIFIIAINLAVGILPHVDNFAHLGGFTSGFLLGFVFLIRPQYGYFNQRNNPRGYAAPSAKSKHKPYQYVLWITSLVLLIAGYTAGLVVLLRGTD... | Function: Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis. Unable to cleave the Drosophila protein Spitz.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43360
Sequence Length: 389
Subcellular Location: Golgi apparatus membrane
EC: 3.4.21.-
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O85040 | MAVKKYSAGVKEYRQTYWMPEYTPLDSDILACFKITPQPGVDREEAAAAVAAESSTGTWTTVWTDLLTDMDYYKGRAYRIEDVPGDDAAFYAFIAYPIDLFEEGSVVNVFTSLVGNVFGFKAVRGLRLEDVRFPLAYVKTCGGPPHGIQVERDKMNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVQDATETAEAQTGERKGHYLNVTAPTPEEMYKRAEFAKEIGAPIIMHDYITGGFTANTGLAKWCQDNGVLLHIHRAMHAVIDRNPNHGIHFRVLTKILRLSGGDHLH... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active ... |
P00878 | MSPQTETKTGAGFKAGVKDYRLTYYTPDYQVSETDILAAFRMTPQPGVPAEECGAAVAAESSTGTWTTVWTDGLTQLDRYKGRCYDLEPVPGESNQYIAYVAYPIDLFEEGSVTNLLTSIVGNVFGFKALRALRLEDLRIPPAYSKTFWGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQSFMRWRDRFLFCAEAIYKAQTETGEVKGHYLNATAGTCEEMYKRASFAAQIGVPIIMHDYLTGGFTANTSLAMYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKTLRM... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in... |
Q20EX7 | MPTTETKTGAGFKAGVKDYRLTYYTPDYQVKETDILAAFRMTPQPGVPPEECGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDLEPVPGEENQYIAYIAYPIDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQAERDRLNKYGRGLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVSEAIYKAQAETGEIKGHYLNATAPDCEEMYKRAECAKDFGVPIIMHDYLTGGFTANTSLATYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKALRLS... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in... |
P85085 | LTYYTPEYETKGLLLHXHRMSGGDHIHAGXVVGKEITLGFVDLLRVALEACVQAR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in... |
P31203 | MSPQTETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVSPQPGVPPEEAGAAVA | Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By s... |
P11383 | MSPQTETKAGVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEDSQWICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRM... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process . Both reactions occur simultaneously and i... |
Q9PT60 | MTECFLPPASSPSEHRRAEHGGGLARTPSSEEISPTKFPGLYRTGEPLPPHDILHEPPDIVSEDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKIKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEDKHKEKKSKDLTAADVVKQWKEKKKKKKPTPEPESLPVDIPRLRPVFGIPLIEAAERTMIYDGIRLPLVFRECIDFIEQHGMKCEGIYRVSGIKSKVDELKAAYDREESPNLEDYEPYTVASLLKQYLRELPENVLTKDLMPRFEEACGKTTEGERLQECQRLLKELPECNFCLTSWLVVHM... | Function: Multifunctional protein that functions as a downstream effector of ralA and ralB . As a GTPase-activating protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase activity. As part of the Ral signaling pathway, may also regulate ligand-dependent EGF and insulin receptors-mediated endocytosis. Dur... |
Q02427 | MPRYREWDLACKVYVGNLGSSASKHEIEGAFAKYGPLRNVWVARNPPGFAFVEFEDRRDAEDATRALDGTRCCGTRIRVEMSSGRSRDRRRGEGGSSGRSGSGRYRITPSARTTSTATSSFYNINNLQQQPSSQPQPATFNLQL | Function: Contributes to the activation of female-specific DSX splicing in vivo by recognizing the RBP1 target sequences within the purine-rich polypyrimidine tract of the female-specific 3' splice site.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 16013
Sequence Length: 144
... |
Q15311 | MTECFLPPTSSPSEHRRVEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDILHEPPDVVSDDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQIDVPNLKPIFGIPLADAVERTMMYDGIRLPAVFRECIDYVEKYGMKCEGIYRVSGIKSKVDELKAAYDREESTNLEDYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTETEKVQEFQRLLKELPECNYLLISW... | Function: Multifunctional protein that functions as a downstream effector of RALA and RALB . As a GTPase-activating protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase activity . As part of the Ral signaling pathway, may also regulate ligand-dependent EGF and insulin receptors-mediated endocytosis . D... |
Q62796 | MTECFLPPTSSPSEHRRAEHGSGLTRTPSSEEISPTKFPELYRTGEPSPPHDILHEPPDIVSDDEKDHGKKKGKFKKKEKRTEGYVAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKCKDFTAADVVKQWKEKKKKKKPTQEPEVPQTDAPSLRPIFGAPFADAVERTMMYDGIRLPAVFRECVDYMEKHGMKCEGIYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTEVEKVQEFQRLLRELPEYNHLLLSW... | Function: Multifunctional protein that functions as a downstream effector of RALA and RALB. As a GTPase-activating protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase activity . As part of the Ral signaling pathway, may also regulate ligand-dependent EGF and insulin receptors-mediated endocytosis . Du... |
Q8ENB2 | MKKKGMLNSEISKVLSDLGHTDQIVIADAGLPVPEGVTKIDVALTPGTPSFLDVLKAVKADMVIEGVTLAREIKVDNTENHKQIQEVINDIPITYVTHEQFKALSKQAKAIIRTGEITPYANCILQSGVFF | Function: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Catalytic Activity: beta-D-ribopyranose = beta-D-ribofuranose
Sequence Mass (Da): 14273
Sequence Length: 131
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
Subcellula... |
A9BJQ0 | MKKQGIFNSQISYFVASMGHKDMLSIVDMGYPIPKDATFVDLVFDKGIPNFIDTIKMVLYELEVEKVIIAGEMEVNNLKNYQKVIDIFSNIEIEKKSHEEFKDIAKNSKFFIRTGECTPFSNIILVSGVIF | Function: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Catalytic Activity: beta-D-ribopyranose = beta-D-ribofuranose
Sequence Mass (Da): 14981
Sequence Length: 131
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
Subcellula... |
P51763 | MPEYQNIFTTVQVRAPAYPGVPLPKGSLPRIGKPIFSYWAGKIGDAQIGPIYLGFTGTLSIIFGFMAIFIIGFNMLASVDWNIIQFVKHFFWLGLEPPAPQYGLTIPPLSEGGWWLMAGFFLTMSILLWWVRTYKRAEALGMSQHLSWAFAAAIFFYLSLGFIRPVMMGSWAEAVPFGIFPHLDWTAAFSIRYGNLYYNPFHMLSIAFLYGSALLFAMHGATILAVSRFGGDREIDQITDRGTAAERAAIFWRWTMGFNASMESIHRWAWWCAVLTVITAGIGILLTGTVVENWYLWAIKHGVAPAYPEVVTAVDPYATA... | Function: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36339
Sequence Length: 325
Subcellular Location: Cellular chromatophore membrane
|
P06010 | MADYQTIYTQIQARGPHITVSGEWGDNDRVGKPFYSYWLGKIGDAQIGPIYLGASGIAAFAFGSTAILIILFNMAAEVHFDPLQFFRQFFWLGLYPPKAQYGMGIPPLHDGGWWLMAGLFMTLSLGSWWIRVYSRARALGLGTHIAWNFAAAIFFVLCIGCIHPTLVGSWSEGVPFGIWPHIDWLTAFSIRYGNFYYCPWHGFSIGFAYGCGLLFAAHGATILAVARFGGDREIEQITDRGTAVERAALFWRWTIGFNATIESVHRWGWFFSLMVMVSASVGILLTGTFVDNWYLWCVKHGAAPDYPAYLPATPDPASLP... | Function: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36036
Sequence Length: 324
Subcellular Location: Cellular chromatophore membrane
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P09438 | MATINMTPGDLELGRDRGRIGKPIEIPLLENFGFDSQLGPFYLGFWNAVAYITGGIFTFIWLMVMFAQVNYNPVAFAKYFVVLQIDPPSSRYGLSFPPLNEGGWWLIATFFLTVSIFAWYMHIYTRAKALGIKPYLAYGFTGAIALYLVIYIIRPVWMGDWSEAPAHGIKALLDWTNNVSVRYGNFYYNPFHMLSIFFLLGSTLLLAMHAGTIWALEKYAAHEEWNEIQAPGTGTERAQLFWRWCMGFNANAYSIHLWAFWFAWLCGITGALGVFFSMPDFVNNWFQWGIEAGINYPQGPTPPVSLP | Function: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34967
Sequence Length: 307
Subcellular Location: Cell membrane
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P51751 | MADYQNILTPCRFAPKPHHGVELPRGNWAEKARPIFVWLLGKIGDASSDHPPGVAGTVSAVLFAFAFLIIGANFLASVDWNPIEFIRLLPWLALEPPRPNWAWVLAPMNEGGWWQITGFFLTMSLLVWWWHVYNRARALGLGTHMAWAFASALFLYLTLGFIRPLLLGNWGEAVPFGLFAHLDWTAAFSLRYGNLYYNPFHMLSIAFLYGSAVLFAMHGATILAVSHLGGDREVEQITDRGTAAERAALFWRWTMG | Function: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28788
Sequence Length: 256
Subcellular Location: Cellular chromatophore membrane
|
P11847 | MAEYQNFFNQVQVAGAPEMGLKEDVDTFERTPAGMFNILGWMGNAQIGPIYLGIAGTVSLAFGAAWFFTIGVWYWYQAGFDPFIFMRDLFFFSLEPPPAEYGLAIAPLKQGGVWQIASLFMAISVIAWWVRVYTRADQLGMGKHMAWAFLSAIWLWSVLGFWRPILMGSWSVAPPYGIFSHLDWTNQFSLDHGNLFYNPFHGLSIAALYGSALLFAMHGATILAVTRFGGERELEQIVDRGTASERAALFWRWTMGFNATMEGIHRWAIWMAVMVTLTGGIGILLSGTVVDNWYVWAQVHGYAPVTP | Function: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34442
Sequence Length: 307
Subcellular Location: Cellular chromatophore membrane
|
P26279 | MYPEYQNIFTQVQVRGTPEMGMDDAGNNMMEERVGKPFFSTLAGLFGNGQIGPYYFGWTSIVAFGTGIAWFVIVGFNMLAQVGWSIPQFIRQLFWLALEPPSPEYGLSMPPLNDGGWYIIASFFLLVSVMTWLLRAYLLAEQHKMGKHIFWGFAAAVWLFLVLGLFRPILMGSWSEAVPYGIFPHLDWTTAFSIRYGNLYYNPFHCLSIVFLYGSVLLFCMHGGTILAVTRYGGDRELEQIYDRGTATERAALFWRWTMGFNATMEGIHRWAWWFAVLTPITGGIGILLTGTVVDNWFIWAQEHHFAPMYDGSYGYEDYG... | Function: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37671
Sequence Length: 330
Subcellular Location: Cellular chromatophore membrane
|
B6QHL8 | MADQADVLADPDFEEETSIQKFKRRLKEEPLIPLGCAATCYALYRAYRSGKAKDSVEMNRMFRARIYAQFFTLLAVVAGGMYYKTERKQRREFEKKVEERKAQEKRDAWLRELEARDKEDKGWKERHAAVSVTAKKETEGAVDKNVNQAPTEEVVEKRGTGILDAVKALVQGKKD | Function: Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20137
Sequence Length: 175
Subcellular Location: Mitochondrion membrane
|
Q756G1 | MSYLPTSSEADKDLDEMTFSEKMVFHCKREPLVPAGVLMTTGAILLAIKNVRSGNRRNAQKWFRWRVGLQTGTLVALIAGSFFYGSAKHEQLSKEEQLRQKAKMREQLWIQELERRDLEVRRRKQRAEEARKKAAEMQSELSGLEQELRELEESRRK | Function: Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18367
Sequence Length: 157
Subcellular Location: Mitochondrion membrane
|
P76425 | MTEFTTLLQQGNAWFFIPSAILLGALHGLEPGHSKTMMAAFIIAIKGTIKQAVMLGLAATISHTAVVWLIAFGGMVISKRFTAQSAEPWLQLISAVIIISTAFWMFWRTWRGERNWLENMHGHDYEHHHHDHEHHHDHGHHHHHEHGEYQDAHARAHANDIKRRFDGREVTNWQILLFGLTGGLIPCPAAITVLLICIQLKALTLGATLVVSFSIGLALTLVTVGVGAAISVQQVAKRWSGFNTLAKRAPYFSSLLIGLVGVYMGVHGFMGIMR | Function: Efflux system for nickel and cobalt.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30419
Sequence Length: 274
Subcellular Location: Cell inner membrane
|
A9MRK2 | MGEFSILLQQGNGWFFIPSAILLGILHGLEPGHSKTMMAAFIIAIKGTIKQAFMLGLAATLSHTAVVWLIALGGMYLSRAYAAESVEPWLQLISAIIILGTACWMFWRTWRGEQQWLTGSHHDHDHDHDHDHDHDHDHDHDHDHHGHTYPEGAMSKAYQDAHERAHAADIQRRFHGQKVTNEQILLFGLTGGLIPCPAAITLLLICIQLQALTLGATMVLCFSLGLALTLVAVGVGAAISVQQAVKRWNGFTTLARRAPYFSSILIGLVGLYMGIHGYTGIMQ | Function: Efflux system for nickel and cobalt.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31134
Sequence Length: 283
Subcellular Location: Cell inner membrane
|
Q5PEQ4 | MGEFPTLLQQGNGWFFIPSAILLGILHGLEPGHSKTMMAAFIIAIKGTVKQAVMLGLAATLSHTAIVWLIALGGMYLSRAFTAQSVEPWLQLISAIIILSTACWMFWRTWRGEQQWLAGNHHHDHDHDHDHDHDHHGHIHPEGATSKAYQDAHERAHAADIQRRFDGQTVTNGQILLFGLTGGLIPCPAAITVLLICIQLKAFTLGATMVLSFSLSLALTLVTVGVGAAISVQQAAKRWSGFSTLARRAPYFSSILIGLVGVYMGIHGYTGIMQ | Function: Efflux system for nickel and cobalt.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29816
Sequence Length: 274
Subcellular Location: Cell inner membrane
|
A9N3J5 | MGEFSTLLQQGNGWFFIPSAILLGILHGLEPGHSKTMMAAFIIAIKGTVKQAVMLGLAATLSHTAIVWLIALGGMYLSRAFTAQSVEPWLQLISAIIILSTACWMFWRTWRGEQQWLAGNHHHDHDHGHDHDHDHDHDHDHDHDHDHDHHGHIHPEGATSKAYQDAHERAHAADIQRRFDGQTVTNGQILLFGLTGGLIPCPAAITVLLICIQLKAFTLGATMVLSFSLGLALTLVTVGVGAAISVQQAAKRWSGFSTLARRAPYFSSILIGLVGVYMGIHGYTGIMQ | Function: Efflux system for nickel and cobalt.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31483
Sequence Length: 288
Subcellular Location: Cell inner membrane
|
D0NQC3 | MRACNTLLPTAIVLTSCDALSAHRAQIMNVATSDLISPIESTVQDDNYDRQLRGFYATENTDPVNNQDTAHEDGEERVNVATVLGKGDEAWDDALMRLAYQHWFDGGKTSDGMRLIMDLPAKGEALRHPNWGKYIKYLEFVKEKKKEAADAAAVAALKRRRTYRGWYVDGKTEKDVRKIFGLPATGKAKNHPNWADFQEYLNVVREYSKVVFK | Function: Effector that enhances P.infestans colonization of Nicotiana benthamiana leaves.
Sequence Mass (Da): 24129
Sequence Length: 213
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
|
D0N118 | MRCHYFVLLAVAAFLAGANVAVATTDAQLSDARAVRASFNTKRALRSHTKATDHGEERAYKPSLSVVESLNNWMQRASKNILPDDVILVMASKAMTKKTSSSDAVFAMLQLDQGLKGILSNPNLKQFAYYLVLTEKAPSQALITKLISQYGDDVVAKYLFDIKHKAINVSEKLKAEARFWQGAQYVKWFDEGVTPALVRQKYNVHPETWYKNPYEGVYWEYTGVYAKLASKSNKPLPVEV | Function: Effector that enhances P.infestans colonization of Nicotiana benthamiana leaves.
Sequence Mass (Da): 26930
Sequence Length: 240
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
|
P43297 | MGFLKPTMAILFLAMVAVSSAVDMSIISYDEKHGVSTTGGRSEAEVMSIYEAWLVKHGKAQSQNSLVEKDRRFEIFKDNLRFVDEHNEKNLSYRLGLTRFADLTNDEYRSKYLGAKMEKKGERRTSLRYEARVGDELPESIDWRKKGAVAEVKDQGGCGSCWAFSTIGAVEGINQIVTGDLITLSEQELVDCDTSYNEGCNGGLMDYAFEFIIKNGGIDTDKDYPYKGVDGTCDQIRKNAKVVTIDSYEDVPTYSEESLKKAVAHQPISIAIEAGGRAFQLYDSGIFDGSCGTQLDHGVVAVGYGTENGKDYWIVRNSWG... | Function: Cysteine protease that plays a role in immunity, senescence, and biotic and abiotic stresses (Probable). Involved in immunity against the necrotrophic fungal pathogen Botrytis cinerea . Involved in elicitor-stimulated programmed cell death (PCD). During infection by the necrotrophic fungal pathogen Botrytis c... |
D0MRS3 | MRLSYILVVVIAVTLQACVCATPVIKEANQAMLANGPLPSIVNTEGGRLLRGVKKRTAEREVQEERMSGAKLSEKGKQFLKWFFRGSDTRVKGRSWR | Function: Effector that is involved in host plant infection. Contributes to virulence during the early infection stage, by inhibiting plant defense responses induced by both PAMP-triggered immunity (PTI) and effector-triggered immunity (ETI).
Sequence Mass (Da): 10863
Sequence Length: 97
Domain: The RxLR-dEER motif act... |
P54725 | MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQE... | Function: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquiti... |
P54727 | MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILNDDTALKEYKIDEKNFVVVMVTKPKAVSTPAPATTQQSAPASTTAVTSSTTTTVAQAPTPVPALAPTSTPASITPASATASSEPAPASAAKQEKPAEKPAETPVATSPTATDSTSGDSSRSNLFEDATSALVTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPQAASTGAPQSSAVAAAAATTTATTTTTSSGGHPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQISQH... | Function: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticu... |
P21651 | MVARGRTDEISTDVSEANSEHSLMITETSSPFRSIFSHSGKVANAGALEESDKQILEWAGKLELESMELRENSDKLIKVLNENSKTLCKSLNKFNQLLEQDAATNGNVKTLIKDLASQIENQLDKVSTAMLSKGDEKKTKSDSSYRQVLVEEISRYNSKITRHVTNKQHETEKSMRCTQEMLFNVGSQLEDVHKVLLSLSKDMHSLQTRQTALEMAFREKADHAYDRPDVSLNGTTLLHDMDEAHDKQRKKSVPPPRMMVTRSMKRRRSSSPTLSTSQNHNSEDNDDASHRLKRAARTIIPWEELRPDTLESEL | Function: Essential for meiotic chromosome segregation. MER1 and MER2 proteins must interact directly or indirectly. MER1 might be responsible for regulating the MER2 gene and/or gene product. MER2 is not required for mitosis and mitotic DNA repair mechanisms. Component of the MER2-MEI4-REC114 complex which seems to be... |
Q18DC9 | MLRSWEFVLLISCFLCFSSDALQRISLKKMPSIRETLQEMGMKVADVLPSLKHRISYLDEGLHNKTASTILTNFRDTQYYGEISIGTPAQIFKVVFDTGSSNLWVPSRQCSPLYSACVSHNRYDSSESSTYKPKGTKITLTYAQGYIKGFFSQDIVRVADIPIIQFFTEAIALPSIPFIFARFDGVLGMGYPKQAIGGVIPVFDNIMSEKVLSENVFSVYYSRHSESNTGGEIILGGSDPSHYTGDFHYVSTSREGYWHVDLKGVSIENKIVLCHDGCTATIDTGTSFISGPASSISVLMETIGATLSDGDYVIDCKKIN... | Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney (Probable). This protein is also found in snake venom ... |
Q8KHV6 | MSVFDLPRLHFAGTATTRLPTGPRNGLVDLSTHSVVMDGERFPASRPAAEYHAYLDRVGGKGTAFAGNGYFAIDAGITAVERAAGEVDTGDLLVGRAVDVWGHYNEYLATTFNRARIFDVDPSSSWTSTVMIGQFGFGRLGRSHDVGYVFTGGVHGMQPPRWHEDGRVLHQFTVPAGEDMTWFGSAADSPAAARLRELVESGEADGLVVQLALSDAGPAPMPHAQQWRLRGTIAPWHAGEPRTCPAGRLLTPHNLTADLRGDHVSLNLISFRPPTGISGLELRTADTDRFIARVPADDPHGVVTVPAAEGGDEALCVVGT... | Function: Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyzes the hydrogen peroxide-dependent dimerization of two L-tryptophan-derived molecules (imine form of indole 3-pyruvate (IPA)), to form dichlorochromopyrrolic acid (CPA), the precursor for the six-ring bisindolopyrrolocarb... |
Q8KI76 | MTIEFDRPGAHVTAADHRALMSLFPTGVAVITAIDEAGTPHGMTCTSLTSVTLDPPTLLVCLNRASGTLHAVRGGRFGVNLLHARGRRAAEVFSTAVQDRFGEVRWEHSDVTGMPWLAEDAHAFAGCVVRKSTVVGDHEIVLGEVHEVVREHDLPLLYGMREFAVWTPEG | Function: Catalyzes the NADH-dependent reduction of FAD to provide FADH2 for the halogenase RebH.
Catalytic Activity: NADP(+) + reduced riboflavin = 2 H(+) + NADPH + riboflavin
Sequence Mass (Da): 18435
Sequence Length: 170
EC: 1.5.1.30
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Q8KHE4 | MGARVLVATTPGDGHVNPMVPVAQEMVSRGHEVRWYTGKAFRSTVERTGARHEPMRDAHDFGGMPREEAFPQHAGLTGITGMIAGFRDIFIEPAADQMTDLLALLEDFPADVLVTDETFFGAGFVSERTGIPVAWIATSIYVFSSRDTAPLGLGLPPSSSRLGRLRNTVLKQLTDRVVMRDLRRHADVVRDRVGLPRIRKGAFENIMRTPDLYLLGTVPSFEYPRGDMPPEVRFVGPFVSPAPPDFTPPAWWGELDSGRPVVHVTQGTVANDAERLLLPAIRALAAEDVLVVATTGAPLELEPMPANVRVERFIPHHALL... | Function: Catalyzes the penultimate step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid that inhibits topoisomerase 1. Has a wide substrate range, including staurosporine aglycone, EJG-III-108A, J-104303, 6-N-methyl-arcyriaflavin and indolo-[2,3-a]-carbazole.
Catalytic Activity: 4'-demethylrebeccamyci... |
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