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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 directly responsible for vesicle formation, movement, tethering and fusion. Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 26659
Sequence Length: 237
Subcellular Location: Cell membrane
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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 directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes (By similarity). Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 26678
Sequence Length: 237
Subcellular Location: Cell membrane
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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 tight junctions (By similarity). May selectively regulate the apical recycling pathway. Together with MYO5B regulates transcytosis (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 23537
Sequence Length: 213
Subcellular Location: Cell membrane
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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 tight junctions (By similarity). May selectively regulate the apical recycling pathway. Together with MYO5B regulates transcytosis (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 23496
Sequence Length: 213
Subcellular Location: Cell membrane
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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 tight junctions . May selectively regulate the apical recycling pathway. Together with MYO5B regulates transcytosis (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 23473
Sequence Length: 213
Subcellular Location: Cell membrane
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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 | MASTAVGLGGGEGDPGAGGPPAGSAHPDDASSMSDDVFEDAETTQARIEELRRRPFGDGSYNPPAAPASVSASITTTTTQQQQQHHNPSHHHQSSHHQPSHHHHHHHHSQLSLTGSHHYHDDAIMAPVQRSATGYPGYRPSREAMQMYAYGTDDYDDDYNDGWRSYRYDEVDMHPAPSNAHQQPFDDTVNHKTILLGDSGVGKTSFLVKYNTGEFRLGSFSATVGIALTNKVVVVDGTRVKLQIWDTAGQERFRSVTHAYYRDAHALLLLYDVTNKTTYDNIRAWLGEIREYAQEDVVIVLIGNKADCSGSERQVKREDGERLGREHNVPFMETSAKTGLNVELSFTAVARQLKSRGYEHGDDGKFNVHDFVRDNTKARSVCAQCRNM | 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 directly responsible for vesicle formation, movement, tethering and fusion. Mediates transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Plays a role in the maturation of zymogenic granules and in pepsinogen secretion in the stomach. Plays a role in the secretion of amylase from acinar granules in the parotid gland.
Location Topology: Lipid-anchor
Sequence Mass (Da): 27900
Sequence Length: 256
Subcellular Location: Golgi apparatus membrane
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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 directly responsible for vesicle formation, movement, tethering and fusion. Mediates transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Plays a role in the maturation of zymogenic granules and in pepsinogen secretion in the stomach (By similarity). Plays a role in the secretion of amylase from acinar granules in the parotid gland.
Location Topology: Lipid-anchor
Sequence Mass (Da): 28619
Sequence Length: 260
Subcellular Location: Cytoplasmic vesicle
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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 directly responsible for vesicle formation, movement, tethering and fusion. Mediates transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Plays a role in the maturation of zymogenic granules and in pepsinogen secretion in the stomach (By similarity). Plays a role in the secretion of amylase from acinar granules in the parotid gland.
Location Topology: Lipid-anchor
Sequence Mass (Da): 28203
Sequence Length: 257
Subcellular Location: Cytoplasmic vesicle
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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: 197
Subcellular Location: Cytoplasm
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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 body elongation, which involves dramatic cytoskeletal reorganization . ced-2 and ced-5 function to activate ced-10 in a GTPase signaling pathway that controls the polarized extension of cell surfaces . Plays a redundant role with mig-2 in dorsal axonal guidance in ventral cord commissural motoneurons and in P neuroblast migration. May regulate these 2 processes by activating pak-1 and/or max-2 . Plays a role, probably via mig-10, in orientating axonal growth of HSN and AVM neurons in response to guidance cues such as slt-1. Regulates mig-10 asymmetric distribution in HSN neurons . During the dorso-ventral axonal guidance and outgrowth of VD neurons, required together with mig-2 to inhibit growth cone filopodial protrusion mediated by netrin guidance cue unc-6 and its receptors unc-5 and unc-40 . Specifically, regulates growth cone filopodial protrusion polarity, and thus migration, by promoting F-actin polarization and, together with mig-2, by restricting plus-end microtubule accumulation in the growth cone . Plays a role in protecting dopaminergic neurons from oxidative stress-induced degeneration . During gonad morphogenesis, plays a role in distal tip cell (DTC)-mediated guidance of gonad elongation, probably by activating max-2 . Furthermore, plays a role in distal tip cell polarity and migration by negatively regulating the unc-6/Netrin receptor unc-5 . May be involved in signal transduction during cell migration . May be involved in the positioning of ray 1, the most anterior ray sensilium, in the male tail .
Location Topology: Lipid-anchor
Sequence Mass (Da): 21455
Sequence Length: 191
Subcellular Location: Cell membrane
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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, migration and differentiation, and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). In neurons, is involved in dendritic spine formation and synaptic plasticity (By similarity). In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs), such as ARHGEF6/ARHGEF7/PIX (By similarity). In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3 (By similarity). In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in PAK1 activation and eventually F-actin stabilization (By similarity).
PTM: The N-terminus is blocked.
Location Topology: Peripheral membrane protein
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 8810
Sequence Length: 77
Domain: The effector region mediates interaction with DEF6.
Subcellular Location: Cytoplasm
EC: 3.6.5.2
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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 of the border cell (BC) cluster through the nurse cells to the oocyte. Once activating by Pvr and Egfr, promotes the formation of forward-directed actin protrusions which stabilize the DE-cadherin (shg)-mediated adhesions. In turn, DE-mediated adhesion between the leader border cells and nurse cells further promotes Rac1 signaling creating a positive feedback loop that amplifies the output of RTK activity and leads to higher Rac activity at the front, thus promoting polarization of the border cell cluster and directionally persistent migration . Involved in axon outgrowth and myoblast fusion . Plays a role in regulating dorsal closure during embryogenesis . Involved in integrin alpha-PS3/beta-nu-mediated phagocytosis of Gram-positive S.aureus by hemocytes .
Location Topology: Lipid-anchor
Sequence Mass (Da): 21354
Sequence Length: 192
Subcellular Location: Cell membrane
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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, migration and differentiation, and growth-factor induced formation of membrane ruffles . Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity . In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts . In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In neurons, is involved in dendritic spine formation and synaptic plasticity (By similarity). In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs), such as ARHGEF6/ARHGEF7/PIX . In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3. In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in PAK1 activation and eventually F-actin stabilization (By similarity).
PTM: GTP-bound active form is ubiquitinated by HACE1, leading to its degradation by the proteasome.
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 21450
Sequence Length: 192
Domain: The effector region mediates interaction with DEF6.
Subcellular Location: Cell membrane
EC: 3.6.5.2
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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: 197
Subcellular Location: Cytoplasm
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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. Activates phytoalexin production and alters defense-related genes. Down-regulates metallothionein 2b, a reactive oxygen scavenger . May control lignin synthesis through regulation of both NADPH oxidase and CCR1 activities during defense responses. Stimulates lignin synthesis in suspension cell culture .
PTM: May be palmitoylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23717
Sequence Length: 214
Subcellular Location: Cytoplasm
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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: 201
Subcellular Location: Cytoplasm
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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 production of reactive oxygen species (ROS) by NADPH oxidase (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 21424
Sequence Length: 192
Subcellular Location: Cytoplasm
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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 base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity (By similarity).
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 31610
Sequence Length: 280
Subcellular Location: Nucleus
EC: 3.1.11.2
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Q3SWX9 | MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLASTGASNLLLEPEQSTSNLNEKINHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNVSMGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNNRLLKLFTRCLTPLVPEDLRKRRKGGEADNLDEFLKEFENPEVPREDQQQQHQQRDVIDEPILEEPSRLQESMETSRTNLDESAMPPPPPQGVKRKAGQIDPEPMIPPQQAEQMEIPPVELPPEEPPNICQLIPELELLPEKEKEKEKEKEDDEEEEDEDASGGDQDQEERRWNKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEPYSDIIATPGPRFHII | 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 repetitive regions. The cohesin complex may also play a role in spindle pole assembly during mitosis (By similarity). In interphase, cohesins may function in the control of gene expression by binding to numerous sites within the genome (By similarity). May control RUNX1 gene expression. Binds to and represses APOB gene promoter (By similarity). May play a role in embryonic gut development, possibly through the regulation of enteric neuron development (By similarity).
PTM: Cleaved by separase/ESPL1 at the onset of anaphase; this cleavage is required for sister chromatid separation and cytokinesis. Cleaved by caspase-3/CASP3 or caspase-7/CASP7 at the beginning of apoptosis.
Sequence Mass (Da): 71514
Sequence Length: 630
Domain: The C-terminal part associates with the ATPase head of SMC1A, while the N-terminal part binds to the ATPase head of SMC3.
Subcellular Location: Nucleus
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O60216 | MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLVSTTTSNLLLESEQSTSNLNEKINHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNVSMGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNNRLLKLFTRCLTPLVPEDLRKRRKGGEADNLDEFLKEFENPEVPREDQQQQHQQRDVIDEPIIEEPSRLQESVMEASRTNIDESAMPPPPPQGVKRKAGQIDPEPVMPPQQVEQMEIPPVELPPEEPPNICQLIPELELLPEKEKEKEKEKEDDEEEEDEDASGGDQDQEERRWNKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEPYSDIIATPGPRFHII | 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 repetitive regions . The cohesin complex may also play a role in spindle pole assembly during mitosis . In interphase, cohesins may function in the control of gene expression by binding to numerous sites within the genome (By similarity). May control RUNX1 gene expression (Probable). Binds to and represses APOB gene promoter . May play a role in embryonic gut development, possibly through the regulation of enteric neuron development (By similarity).
PTM: Cleaved by separase/ESPL1 at the onset of anaphase; this cleavage is required for sister chromatid separation and cytokinesis . Cleaved by caspase-3/CASP3 or caspase-7/CASP7 at the beginning of apoptosis .
Sequence Mass (Da): 71690
Sequence Length: 631
Domain: The C-terminal part associates with the ATPase head of SMC1A, while the N-terminal part binds to the ATPase head of SMC3.
Subcellular Location: Nucleus
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P30776 | MFYSEAILSKKGPLAKVWLAAHWEKKLSKVQTLHTSIEQSVHAIVTEETAPMALRLSGQLMLGVVRIYSRKARYLLEDCTEALMRLKMSFQPGQVDMIEPATALQSLKGKDAVTQSANLTLPETITEFDLLVPDSTFDFQWSQLLRTPSRSSNTLELHSLPISSSPSFPSSQLSIEAGRNAQVESGFSLGESFAHVGNDMQFHLPISNSGAATPRSVHSDNQSQISIEVGRDAPAAAATDLSGIIGPQMTKSPASSVTHFSTPSMLPIGGTSLDDELLAPVDDLNLDLGLDDLLGDEQGANAPAIEADEQAETSSIHLPSDIMEDDSSRPAAAGVEEGQVVESATAPQQEKINPQKTVRRQRAIIDPVTELSSKQMKKQLADTSSITSPLCLNTSSIVFNATVNFTRNGKFNTSIFSSNLNPKVNELLQADFKQAILRKRKNESPEEVEPAKHQRTDTSTENQETAEVLDPEEIAAAELANITEAAIATLPQETVVQPEGEAPELGSPMGFPVTALESADDSLFDAPPVMLDEADLLGSERLDSSVSEALPSSQTAKDSLRNKWDPYTEGEKVSFQTLSAGCNREEAVQLFFDVLVLATKDVISVKQDVAIQNEITLTAKRGMLLSSL | 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 metaphase-anaphase transition, this protein is cleaved by cut1 and dissociates from chromatin, allowing sister chromatids to segregate. Also involved in the DNA double-strand-break (DSB) repair system.
PTM: Hyperphosphorylated during S and G2 phases.
Sequence Mass (Da): 67854
Sequence Length: 628
Subcellular Location: Nucleus
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Q6E6J3 | MTRCGWHTCTRVRPRMGETLLPRKASQHEFEPEEIRMKQEHTECPLLVSHNGIIILETFTANAKQATDFLIAIAEPVSRPAHVHEYRITPYSLYAAVSVGLTTEDILSTLDRFAKNTVPDTIVRFVRECTLSYGKTRLVFKGGRFLVEAATREVFDVLTGDAEISRLRAAGTVRDADARYVFEVRVDCIEQVRRRCIEIDYPMIEEYDFRDDVALRSLDMDLRDTVSIRTYQEVSLNKMFGNRRARSGVIVLPCGAGKTLVGITAMCTIKKPCIVLCTSGVSVEQWRQQVLAFSTVSADAVSRFTSERKEMFEADAGILITTYTMLAFSGRRSAEAQRVMEWLRGTEWGLMILDEVHVVPAAMFRKVVSAVSHHCKLGLTATLVREDDKIEDLNFLIGPKLYEADWQDLSMQGHIARVECVEVWCDMTAEFYREYLGQDPRRRRVLSIMNPAKFQTCEFLIRKHEALGEKIIVFSDNVLALRTYALKLGKPFIYGPTGQTERMRILRQFQTNPAINTLFLSKVGDTSIDLPEASCLIQISSHFGSRRQEAQRLGRILRAKRRNDPGFRVYFYTLVSKDTEEMYYSRKRQQFLVDQGYTFRTVTALEGFRDTDVRVFRGKAEQRELLATVLLASEEDLESEESEDGDEAAADRRHLRTRGGAEDTVPASRTRTERHLLFRKMHKRHRR | 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 acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/SSL2, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/SSL2 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 78771
Sequence Length: 687
Subcellular Location: Nucleus
EC: 3.6.4.12
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P62135 | MVIVKKVILNNVKTHSKREFDFEKGINLILGPNGSGKTTLVESIFLALFGGDFARVIDYFKKGEKTMAITLILEDKGKTYRIRRKWVLENNAKLVESSLELIDTIPKKLASDHNKLLQQIKHLFGLDKKIIPLIYYKQNEITKIIEMDPRKRKEWFDEILGIKDLEEFSEKLKMAIKLIKTGKISRIEDRIKLLKAELNKKSLLENKLKNYKEKLVLLSNELENLEKEYKILENQYKEYLELKAKLKSIEGQINNINVKEIESKINNIREELNNIEELTDYEKDILSKKHEIIRCNEIKNRLKELEKEIKDYDKIKKEFLEIESKYKQYEEKRLEYEKAKMLEKEKEKAKREYSYLLKEKESLEKEIAELQNKINQIKELEKMEQELLEIQERIGVIKAKLKLLENIKDRCPLCGAKLSSDTIEHLQKEREKLQKEYYYLKEKYNQLLIKIRALEKYKGLEKVLEAKTKHLETIENRLKEIKPIIELEIPKIELDESIPYKYKQLLNKVSYLEAKIKEYERYKNIECPYDIAIEELKRIEDKYNKYIKKPALERELNLLLKELERYNSLLKEKEEILSKLNPEIETKYKELTKKKENLLSEISKVKGIIKEIESQIKEIEKHESTIKQLEEKKRKWEKLVEKLNRIVKALGRDGIPKALREGAINYINDMANIYLREFTDKYKLKVNNDLSIYAIPIDNPHYEIEAKNLSGGEKVVFSLSIALAIISWLSLQNMFMVLDEPTANLDNERTLALRKTFDKLEKMVEQAIIVTHNELLDTGENHVVRL | 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 and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
Sequence Mass (Da): 93236
Sequence Length: 786
Domain: The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
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Q9UZC8 | MKIEEVKVYNFRSHEETVVRFRKGINLIIGQNGSGKSSLLDAILVGLYWSKKLRLRGLKKDEFRRIGGKGGTRIEIKFENDDSKYVLFRDFSRNVAYLKVQENGKWRHASEPSMESVSSYIERILPYNVFLNAIYIRQGQIDAILESDETRDKVVREILNLDKLESAYENLKRIKTNINLLIESKKSFIARTENIEELIKANEDELTKKLSEINEISSKLPPIRGELEKVRENVKELESIKGKISELKIQVEKLKGRKKGLEEKIVQIERSIEEKKAKISELEEIVKDIPKLQEKEKEYRKLKGFRDEYESKLRRLEKELSKWESELKAIEEVIKEGEKKKERAEEIREKLSEIEKRLEELKPYVEELEDAKQVQKQIERLKARLKGLSPGEVIEKLESLEKERTEIEEAIKEITTRIGQMEQEKNERMKAIEELRKAKGKCPVCGRELTEEHKKELMERYTLEIKKIEEELKRTTEEERKLRVNLRKLEIKLREFSVMRDIAEQIKELESKLKGFNLEELEQKEREFEGLNEEFNKLKGELLGLERDLKRIKALEGRRKLIEEKVRKAKEELENLHRQLRELGFESVEELNLRIQELEEFHDKYVEAKKSESELRELKNKLEKEKTELDQAFEMLADVENEIEEKEAKLKDLESKFNEEEYEEKRERLVKLEREVSSLTARLEELKKSVEQIKATLRKLKEEKEEREKAKLEIKKLEKALSKVEDLRKKIKDYKTLAKEQALNRISEIASEIFSEFTDGKYSNVIVRAEENKTKLFVVYEGKEVPLTFLSGGERIALGLAFRLALSMYLVGRIDLLILDEPTPFLDEERRRKLLDIMERHLRRISQVIMVSHDEELKDAADYVIRLRLEGGKSKVEVVS | 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 and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
Sequence Mass (Da): 103971
Sequence Length: 880
Domain: The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
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P58301 | MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPLRIKDIKKDEFTKVGARDTYIDLIFEKDGTKYRITRRFLKGYSSGEIHAMKRLVGNEWKHVTEPSSKAISAFMEKLIPYNIFLNAIYIRQGQIDAILESDEAREKVVREVLNLDKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLYEEIKAKKENLRQLKEKLGDKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCPVCGRELTDEHREELLSKYHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEIFAEFTEGKYSEVVVRAEENKVRLFVVWEGKERPLTFLSGGERIALGLAFRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAADHVIRISLENGSSKVEVVS | 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 and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex . The ATP-bound conformation promotes DNA end binding and end tethering, and alters Mre11 nuclease activity . ATP hydrolysis promotes both Mre11 activity as well as HerA/NurA activity . Has also reversible adenylate kinase activity .
Sequence Mass (Da): 103840
Sequence Length: 882
Domain: Binding of ATP induces a closed, compact conformation of the Rad50/Mre11 complex. ATP hydrolysis opens the complex.
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Q97WH0 | MRIDKITLTNFLSHEHSEIQFMGEINVIVGQNGAGKSSIIDGIVFSLFRTHSRGNNDNLIRKGSNRGSVTLYLSNEKDKIEIIRDIRSTTEDRLIRNQFPIARSATVVSNEIEKILGIDKDIALSTIIVRQGELDKILENFQEIMGKILKLELIEKLIDSRGPIVEFRKNLENKLRELDRIEQDYNNFKKTVEEKRARVLELKKDKEKLEDEIKNLEKRIKDIKDQFDEYEKKRNQYLKLTTTLKIKEGELNELNRSIEELRKQTENMDQLEKEINELENLRNIKLKFEKYEVLAKSHTEMSANVINLEKEIEEYEKAIRRKEELEPKYLKYKELERKLEELQPKYQQYLKLKSDLDSKLNLKERLEKDASELSNDIDKVNSLEQKVEETRKKQLNLRAQLAKVESLISEKNEIINNISQVEGETCPVCGRPLDEEHKQKIIKEAKSYILQLELNKNELEEELKKITNELNKIEREYRRLSNNKASYDNVMRQLKKLNEEIENLHSEIESLKNIDEEIKKINEEVKELKLYYEEFMRLSKYTKEELDKKRVKLDEMKKKKEEIEKEMRGLESELKGLDRKALESKILDLENKRVKLDEMKKKKGILEDYIRQVKLLQEEVKNLREEVNIIQFDENRYNELKTSLDAYNLSLKEKENRKSRIEGELESLEKDIEEISNRIANYELQLKDREKIINAINKLEKIRSALGERKLQSYIIMTTKQLIENNLNDIISKFDLSIKNVEMEIMPKTGRGRSSSGDILVYTNSGDTLPIVSLSGGERIALSIALRLAIAKALMSNTNFFILDEPTIHLDDQRKAYLIEIIRAAKESVPQIIVVTHDEEVVQAADYVIRVEKRGNKSFVREET | 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 and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
Sequence Mass (Da): 101602
Sequence Length: 864
Domain: The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
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O33600 | MIIREIRLQNFLSHEDTTVKFEGSINVIIGNNGAGKSSIIDGILFGLFKRTNRDIGKNEELIKKGKKSGQVSIKFEINGDTYLIDRNVGETSRDTISLLKEGKIITLARQSTTVNNKIKEILGFDHKILMSTTIIGQGSVESVFSDFPEVMKELLKINKLEMLRESNGPIHSLIKVLTDRIRSLQSIKDILKREEAEIDRLKKEIEEIKVKLENIEREAKEKEDELNQYNTEFNRIKEIKVQYDILSGELSVVNKKIEEIALRLKDFEEKEKRYNKIETEVKELDENREKINTISSFKSILVQIDSLKSQINVVENDLKRKKEKLKRKKELEEKEKQYEEIEKRKKELEEKEKQYEEIEKRLTYVLKNIERQKNEIEKLNYVDTQDLENKIKDVSDRINQIDNELKGLLDRRGDLNGRKEQTLKIYNNLNSIEDDRCPICGRPLDSEHKAKIREEIKVQLLELNKQITALQARINSLIKEREELEATRNKLQLELQKRSKEKGIYEAKLKELQRLEEEKNKLQNEILSLLSYHQEFENIAEKEKELIDYHEEYLKNSDILEEDIQEQEQRLNELNSKLSELEKSYNDYKAKYQFLPADLKSLVSLEERIRRRISELEKLKIEYERLKEEITRMKGLKEEYEKLKEEEDALLNRISELGYSEKRYKQLEEIIDKLSKILSGIEADKGKIKGSLEEKIKNIEEKERNIEELRNKMNEESKLNLGISKLQKLREVLDNKHLQSHIMNIVRNQIENNVNEVIAKFDLSFSAVEIDFVGKSELYVYTASGQKIHINALSGGERISIALALRLAIAKALMNQFSTLILDEPTVNLDEYRRKELIDVIRSAIEIVPQIILVTHDQELIQAGDYIIRVEKKGDTSKVEVSSYDR | 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 and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
Sequence Mass (Da): 103858
Sequence Length: 886
Domain: The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
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Q96YR5 | MIIRRIDIENFLSHDRSLIEFKGTVNVIIGHNGAGKSSIIDAISFSLFRKSLRDAKKQEDLIKRGAGRATVTLYLENKGKIYVIKRNAPNQYTSEDTISELTNDTRRTIARGATTVSQKIKELLNLDEEVLKSTIIVGQGKIESVFENLPDVTKKILKIDKIEKLRDSNGPIKEVMDKINNKIIELQSLEKYKNESENQKIQKEKELENIKRELEDLNIKEEKERKKYEDIVKLNEEEEKKEKRYVELISLLNKLKDDISELREEVKDENRLREEKEKLEKDILEKDKLIEEKEKIIEAQNKIKLAQEKEKSLKTIKINLTDLEEKLKRKRELEEDYKKYIEIKGELEELEEKERKFNSLSDRLKSLKIKLSEIESKISNRKISINIEELDKELQKLNEDLNNKNQEREKLASQLGEIKGRIEELNKLLGNLNQVKGNVCPVCGRELSDDHKRKIQNEIIEKLKELDELNKKFKLEINKINGLISELNQIINKKSKEKDIAIRNLADYNNLLTQQQELRKEIEEIENEIERLSIYHEKYIRLKEEEKNLKPKYEEYLKYYDVTEEKIRELERQKIELEKEIEEIMNKVREYYNTDLTQKIRDIEKRIQEIKGKENKLRELDTLLAKIETAKQKIKQNEEEIKKLTDELQLLNFDPNRFQQIKREKEVLEKILGEINSKKGELLGKKEVLENDIKRLEEQIKDYEEKLKNKQKLITAYDKLKKLREHLAEDKLQAYLMNTVKSLVEDSLNSILSRFELSFTRVEVDFNDKNGIYAYTTSGQRLPVNLLSGGERVSIALALRLAIAKSLMNEVGFLILDEPTVNLDEYRKKELIDIIRSTVEVVPQIIVVTHDEELLQAGDYIIRLEKRGDSSKVEVINND | 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 and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
Sequence Mass (Da): 103488
Sequence Length: 879
Domain: The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
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Q9HLR8 | MIIDRIRLINFLSHEDSEIFFDTGVNIIVGHNGAGKSSIIDAIRFALFGDKRTKKIEDMIRKGAKSLEVEMEFRHGGHTYIIRRSITRRSKNPESNAMIMVDGSALSQSVKDANDYIEKNIITKSKDVFLNSVFSKQGEMDDLISGDPARRKKLLDEILEIEKLEETYDVLKDVIDSLQAGISNLDYLISENERDRDDLRRYQDDVAELSKQIDQEEAIESDLLRKKEEASAEYNAVSKELIMLDATLKNMMSLSDEANRYEEEIRKIDGKLQEISGSTERYNEITSSKVYASRERIRGYWTDKGQIIDYRKMLKNIDGQVQSYEDNMKKAAELQADHDQYEIMQRRMDEIKHELDDLRTYESKYVSLINEIEQKKKKREEYRKKQKDLGDEISRTLGRAFANASELVAIYEEIRRDIDEINTDLGNLQVKIGALRQKEEEIRRNMNMLEGHNKCPVCGTDLGDEGSRRIREHYSEDLNRLNEEIDHLEREASAIDEKKRQLISMESYLAKGKIREYETYDRQMKDLEAQITDDENSLSTIAYKHTKYEQLDEEYRSMHLEDLRQKYTDWNNAMAVISNIGDIEALRKQKDEVSKKLKDAEDRTHEIESEFPDINSYTPSYIGKIEDEVRLLEPQIKLAEDLKRQRETLREKVKDLRSRSAGMDEIQKRKNELSVKASESETRLKYVEGQIQATLSSLSGKRSKVETLRSHVSEIEQRISDRERDIERMKKIEKAINDVKRIREAFGKNGVPAMIRQSVSDYLTAKTRDYLSSFDLDFDDISVDQDFNVTVYRGGVPEGIDSLSGGEKTAVAFAIRVAVAQFLNADLSLLILDEPTAFLDEERRNSLSDIIEYTLKDSSVIPQVIIISHHRELLASANVAIEVKKIGGRSVVSNAD | 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 and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
Sequence Mass (Da): 103436
Sequence Length: 896
Domain: The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
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Q5JHN1 | MKIEKLIIKDFRSHALTKVNFSSGINLIIGQNGSGKSSILDALLVGLYWPSKPKDLKKDDFERINGSGTEITVFFEKGNVKYQIHRNIGRGLAFVKYHDGSSWKTLETGQKPVRDWMEKLVPYDVFLNAIYIRQGEIDAILESDESREKVVRQVLGLDRYENSYKNLLDVRKEIDARIKAIEDYLKSTENIDELIGNLEKELTSVLREINEISPKLPELRGELGGLEKELKELEKTAEELAKARVELKSEEGNLRELEAKKSGIQSMIRETEKRVEELKEKVKELESLEEKAKEYERLSRFYRNFTEGINRIEKLLATYSQQAENLRERIDELSKKEARVKELLKEKEGLQKELGALEEDLKAYQRAKELMANLERLKKRLTLSEEEIEKLEAEIQKARERKEEIMKELEEIGSRRGELKSIAGERNKALMELKKAKGRCPVCGRELTEEHRKELLEKYTAELKEISAEMKELEKREKKLRAELVEVEKTLKKERELFALKEVLEQIRETEEKLKEYDLEKLEEANEKAEELKKKLAGLEGEIKSLEDEIKKGELLKKKLALVEKKLRELEEERASLLGELKKLGFGDVKELEERLKELEPAYKRYIELRPARDELKREEDLLKSLKLDLTAILKEIEKTSKRVEELRKRVEELEKSYDKDRHEELKGKTRELSNELAGLEARLKSLEERRDEVKASLEKLREEKETRKEKAKELEKLKKARERVQRLREKVKAYKNLLKEGALAKVGEMASEIFEELTEEKYSGVTVKAEENKVRLGVVYNGKEYGLGFLSGGERIALGLAFRLALSLYLAGEISLLILDEPTPYLDEERRRRLVDIMQRYLRKIPQVIVVSHDEELKDAADRVIRVSLENGVSVVREAEVG | 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 and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
Sequence Mass (Da): 102727
Sequence Length: 883
Domain: The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
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Q9X1X1 | MRPERLTVRNFLGLKNVDIEFQSGITVVEGPNGAGKSSLFEAISFALFGNGIRYPNSYDYVNRNAVDGTARLVFQFERGGKRYEIIREINALQRKHNAKLSEILENGKKAAIAAKPTSVKQEVEKILGIEHRTFIRTVFLPQGEIDKLLISPPSEITEIISDVFQSKETLEKLEKLLKEKMKKLENEISSLQALYTAIWKYLEENDLEVLKSELKTVSEKKKELLKKREELQKEEEQLKRLLEKYRELVKKKERLRVLSLRRNELQKEVIYEQKVKKAKELEPLFREIYLRQREFERFSQELNSREKRYKELESEKEAISKEIPVHRERLSKLEEIGEKIKEELDLLEKVLKASRPLLEQRIRLKENLTRLEEEFRRLVGEKEKREKELLSIEKTENETKNELEKLLDELSILKKDHMKWLAYQIASSLNEGDTCPVCGGVFHGKVEAVEFNIDEFEKLDQKRSELENTLNVLKERKKSLSSLIEDLLMKIEEGKKNLKSIRNQIEKIEEELHRLGYSEDLEEKLDEKRKKLRKIEEERHSISQKITAADVQISQIENQLKEIKGEIEAKRETLKEQREEMDQLKSDFFDRLRKIGIGFEEFRILVKEEVKDAEKELGVVETEIRLLEESLKELESENVRDVSEDYEKVRNQLEALSQEISDLERKEGRLNHLIEETLRRERELKSLEKKLKEMSDEYNNLDLLRKYLFDKSNFSRYFTGRVLEAVLKRTKAYLDILTNGRFDIDFDDEKGGFIIKDWGIERPARGLSGGERALISISLAMSLAEVASGRLDAFFIDEGFSSLDTENKEKIASVLKELERLNKVIVFITHDREFSEAFDRKLRITGGVVVNE | 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 repositioning DNA ends into the Mre11 active site (By similarity).
Sequence Mass (Da): 100002
Sequence Length: 852
Domain: The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer (By similarity).
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P58302 | MIIERIRLRNFLSHSDSDIYFDTGINMIIGQNGAGKSSIVDAIRFALFSDKRTRRTEDMIKKGERYMEVELYFRSEGHSYRIRRTIERRGKSISTDAEIERDGSIITRGASDVSNYVEKNVLNINKDVFLTSIFVRQGEMDALVSKDPAERKKILDEILNIDRLEAGYLLLKEVIDDLTANVSDYDYLKNELQSKINEIDNNNKQIEELESKLRLIEPEIKALEEEINIKENKKDHLNEELHRLNAQLETIKKYEMELAESQSRKASIEMEVVKLPSIEEELKRLENNAAVVKRNEIIEYINLKKDLGSLSEIIEGLKSDLSKYDEAHRKLEDLQSFRSEFLEKKKRKEDLDKLRSSLKEDEDNYQSAVRNIENIKKWIENEEKEIERMSAFISEILKIQEITPEIINSRRAEINSSLMQIEGKIASLNASIDAMRSHKMEVEENAAMLSGRGVCPVCGTHLGTEKSEDLVKHYGEEASRLEEDINKTENEIKKLDEERKHQKKLLDRINGKDVERLIASYNLLSSKRAELKKFMDDEARLKEAHLKAEAAISQYNSIDLGDLEAKNEEWLKANAVISSIDIENIRSRFEEKNKQLNDIIKRMNEIEVNIPDVESYNENSLKRIDEELNSLRNKKNELYAKKAAMDEIQKTIEHFKEEISKKKGIEDSQAEVNAQLLQINDDLKQLSSRLDKINVDQYEWKSLHKVLLQDNEKLNIAVADIRKRLEKKETIIKAIADLKRVREAFSKDGVPAIIRKSASEFITNQTRQYIQRFELDIDDVDVDQDFNITVFRGGIAEGIDSLSGGERMAVAFALRVAIAQFLNKDVSLLVMDEPTAFLDEDRRSDLANIIEYSLKDSSGIPQVIMISHHRELLSASDLALEVKKRNGSSIVDVIR | 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 and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
Sequence Mass (Da): 103224
Sequence Length: 895
Domain: The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
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P33919 | MIFTLRPYQQEAVDATLNHFRRHKTPAVIVLPTGAGKSLVIAELARLARGRVLVLAHVKELVAQNHAKYQALGLEADIFAAGLKRKESHGKVVFGSVQSVARNLDAFQGEFSLLIVDECHRIGDDEESQYQQILTHLTKVNPHLRLLGLTATPFRLGKGWIYQFHYHGMVRGDEKALFRDCIYELPLRYMIKHGYLTPPERLDMPVVQYDFSRLQAQSNGLFSEADLNRELKKQQRITPHIISQIMEFAATRKGVMIFAATVEHAKEIVGLLPAEDAALITGDTPGAERDVLIENFKAQRFRYLVNVAVLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPGKTDCLILDYAGNPHDLYAPEVGTPKGKSDNVPVQVFCPACGFANTFWGKTTADGTLIEHFGRRCQGWFEDDDGHREQCDFRFRFKNCPQCNAENDIAARRCRECDTVLVDPDDMLKAALRLKDALVLRCSGMSLQHGHDEKGEWLKITYYDEDGADVSERFRLQTPAQRTAFEQLFIRPHTRTPGIPLRWITAADILAQQALLRHPDFVVARMKGQYWQVREKVFDYEGRFRLAHELRG | 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 is stimulated by a peptide with the last 10 residues of SSB, but not when the peptide's last Phe residue is missing. Binds ssDNA; binding is slightly better in the presence of nucleotides . May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds to DNA structures with 3 branches that resemble replication forks .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 66413
Sequence Length: 586
Domain: The C-terminal domain (residues 356-586) is required to alleviate the deleterious effects of UV or ciprofloxacin (CFX) treatment in a double radA-radD mutant; its effect on ionising irradiation (IR) survival in the single radD mutant were not reported . Crystals have 4 domains; helicase ATP-binding (residues 7-185), helicase C-terminal (residues 187-365), a zinc finger domain (residues 376-425) and the C-terminal domain (429-574) .
EC: 3.6.4.12
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C5H884 | MATSRDFGREPPRQQQDSDEAGHTLHDGCQHVSEHPQIDVTAHDSSASALPGDETTVGAATAALDPKEEERDPNIVDWDGPDDPANPQNWPPLKKWGNVAVLSIITFMVPLASSMFAPGIPQVLSDFDTNNPSLATFVVSVYILGLAAGPLVLAPMSELYGRVVIYHVGNVLFIIFTVACALSTNMNMLIAFRFLCGLVGAGPIAIGGGTIADLTTLQQRGTAMSVWSLGPLLGPSVGPVAGGFLSQAEGWRWIFWVLAITAGVITIAGLLVLRETHPGTLLERKTRRLRKETGNMNLRSKLDLQVAPRTLFLRSIVRPSKLLVLSPICLVLSVYSAFVYAMIYFMISTFTFVFQDNYGFSEGIVGLVYIALGLGMLFGVVVQQAIGNRIMKRLADKLNKGKPKPEYRIPPTLLAGFLIPTGLFIYGWTVQYHIQWAVPLLGALLAGMGICIINISTNLYLVDAFTLYAASALAASTVLRSIFGATFPLFALQMYETLGLGWGNSLLAFIAVAMFAIPPLLFYYGERLRSHPRFQVKL | 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 | MSIPKSCEVLVAGGGPAGSYAASALAREGVDVVLLEADKHPRYHIGESMLPSIRPLLRFIDLEETFEKHGFQKKLGAAFKLTAKREGYTDFVAAHGPNGYSWNVVRSESDELLFKHAAKSGALTFQGVKVDSLEFEPYDSDFPSGGKVANPGRPVAARWSAKDGRSGTISFQYLVDATGRAGITSTKYLKNRKFNEGLKNLAIWGYYKGARPWAEGTPRENQPYFEGMRDGAGWCWTIPLHNGTVSVGAVLRSDLFFAKKKSLGEDVTNAMIMAECMKLCPTIKELLEPAELVSDIKQATDYSYSASAYAGPYFRIVGDAGCFIDPFFSSGHHLAMAGALAAAVSIRASMKGDCSEYEASNWHARKVDEGYTLFLLVVMAALKQIRMQEEPVLSDIDDDGFDRAFQFLKPVIQGSGSAEIVKRFTKKEVSEAIDFAVLALDNMAGAGEHANETNGSNGTGETNGDAKTLENITVEDEKVLSGIRILAKVAPSADMKDLEGTAIDGFMPRLEHGHLGLNRV | 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 enzymes, a cytochrome P450 monooxygenase (radP) and a non-heme halogenase (radH) that introduce the epoxide and the chlorine, respectively . If this cluster includes all the genes required for radicicol biosynthesis, the remaining structural features of radicicol are presumably generated by the PKSs rads1 and rads2 . The C-2' ketone could arise if the R-PKS rads1 and NR-PKS rads2 each carry out four iterations, in contrast to the five iteration-three iteration split for the hypothemycin PKSs (By similarity). The origin of the cis 5',6' double bond is not known (By similarity). The radicicol R-PKS rads1 ER domain may catalyze either double bond isomerization or reduction in the third iteration (By similarity).
Sequence Mass (Da): 56453
Sequence Length: 520
Pathway: Secondary metabolite biosynthesis.
EC: 1.14.14.-
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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 + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 26781
Sequence Length: 252
EC: 1.1.1.-
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Q9PU45 | MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVRKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQSKYGDYNKEIHKLGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLRQIEEQTMKAQKELEEQTRRALELDQERKRAKEEAERLEKERRAAEEAKAALAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEASEWQHKAFAAQEDLEKTKEELKSVMSAPPPPPPPPVIPPTENEHDEHDENNAEASAELSSDGVMNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRGKYKTLRQIRQGNTKQRIDEFEAM | 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 | MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLRQIEEQTVKAQKELEEQTRKALELEQERQRAKEEAERLDRERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMSAPPPPPPPPVIPPTENEHDEQDENSAEASAELSSEGVMNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAM | 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 capable of actin and membrane-binding.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 68543
Sequence Length: 583
Domain: The N-terminal domain interacts with the C-terminal domain of LAYN. An interdomain interaction between its N-terminal and C-terminal domains inhibits its ability to bind LAYN. In the presence of acidic phospholipids, the interdomain interaction is inhibited and this enhances binding to LAYN.
Subcellular Location: Cell membrane
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C5H886 | MAEFHPTAFLLPAAVTMIAGYFLCTALYNVYFHPLAKFPGPRLYAASQIPITIKRLLGDEVATFHKLHAKYGQFVRVAPGELSTINPAASRDVYGHRNPAKSIPKDFKAYYMKNQRRDGTEGLMTADDDLHRRQRKIFSPAFSDRAIREQEPLLKKYTDLLVEKAGVASDADGKVDMVMMFNFATFDFIADCVFGDSLHLLEKMEYNPFLANISAVVKFSAMRRAIRSFPYMDETFEKLIPASMKRKRMEHVKFCDDLVDRRLEKAVTNHPDFWTLVLRANEKGEGLTLGEMHQNSFLFLTAATETTSSLMSALTYLLCQNPDKMKKLVDEIRGRFKSTEEMTTVSLPPLEYLQMCIEEGLRVYPPVPGGLPRRVTADGASLDGRELPPDTVVYYAHYASYHSAAHFARPDEFHPERWASVPPSEFANDCRDAVIPFSAGPRDCIGKNLAYHEARLLLAKFLWTYDVELCEESKDWIKQKSFIVGVKRPLYVKLHRVVREK | 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 monooxygenase (radP) and a non-heme halogenase (radH) that introduce the epoxide and the chlorine, respectively . If this cluster includes all the genes required for radicicol biosynthesis, the remaining structural features of radicicol are presumably generated by the PKSs rads1 and rads2 . The C-2' ketone could arise if the R-PKS rads1 and NR-PKS rads2 each carry out four iterations, in contrast to the five iteration-three iteration split for the hypothemycin PKSs . The origin of the cis 5',6' double bond is not known (By similarity). The radicicol R-PKS rads1 ER domain may catalyze either double bond isomerization or reduction in the third iteration (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57108
Sequence Length: 501
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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K7PEY4 | MHPCLVETESVSLLQEEITIITMASSTFPTVNKCTSIGREKHTVVADMDGTLLIGRSSFPYFALIAFEVGGVLRLLIYLLASPIAAILYYFISESAGIQVLVFASMAGMKLSSIESVARAVLPKFYSSDLHPETWRVFSSCGKRCVLTANPRIMVEPFLKEFLGADMVLGTEIASYKGRATGLICKPGILVGDKKAQVLKKTFGDEKPDIGLGDRVTDAPFMALCKEGYIVPAKPKVTTVTSDKLPKPIIFHDGRLVQKPTPLMALLIILWIPIGFPLACLRIAAGSLLPMKFVYCAFKALGVRVIVKGTPPPPVETSKTNHQSGVLFICSHRTLLDPIFLSTALGRAIPAVTYSVSRLSEIISPIKTVRLSRDRATDAAMIKKLLQEGDLAICPEGTTCREPFLLRFSALFAELTDELVPVAMVNRMSMFHGTTARGWKGMDPFYFFMNPSPVYEVTFLNKLPKELTCGSGKTSHEVANYIQRVVASTLSYECTSFTRRDKYRALAGNDGTVVEKTNKANKVMGC | 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 signals that promote colonization by arbuscular mycorrhizal fungi . This signaling function has been recruited by pathogenic oomycetes to facilitate appressoria formation and their own invasion .
Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57604
Sequence Length: 526
Pathway: Lipid metabolism; glycerolipid metabolism.
Subcellular Location: Membrane
EC: 2.3.1.15
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O88039 | MSPAAGAPGSGPGRRRLPALDVRRFSPVRKSRPVPPRAPGRALEVLVLLCSVAAAVAAVAQPLALGRTLDLLLRDGDAGWWLPLSAALLLGELLLDSATSLFTGRCNATWTASVRTRALRGLLRTAPEHARPYPPGDIGTRLTLNAADAGGAPAARAALAASLITPLGALVALALVDVWVALCVLTGLPALALLLRSFARDTGATVAAYQRTQSLIASRLLEALEGADTIGAAGTGERERARVLAPLAELAAQGRHMWALHGRALGRSGVLVPLLTLAATAVGGLRLAAGELSVGDLLAVGRYAQLTAGVGAAASLLGAIVRAREARRRTRELERMTATVYGTRRLPPNGPGELRLCGVRVLRGGREVLRADGVRVPGGSTVAVVGRSGAGKSVLAAVAGRLIDPDEGYVLLDGVRLDRLTHEALRTEVAYAFERPVLGEGTIAEAVADGARRSSRERVRQAARAAGADGFVRRLPHGYDTPLPRAPLSGGEHQRLGLARAFAHAGRLLVLDDATSSLDTATEHEVDLALRRSVRPGTRLVVAHRPSVADRADLVLWLEDGQVRAVGTHRELWHTAGYREVFGAGAGAGAGAGAGAGADAGAGADAGPGPDSGAATAVGGSGPGPVRRPEPEEARP | 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 | MTSTEAGALRRLAPPARRFLAHRKGVLVRLALWSLAESGQAFLVGHAVARSVDEGFLAGDPRRGLLWLGVALVAVLSGARVVRGVFAQLAGVTEPLRDGLVRHAVDRSMARAAPGGPGGTDRAAVSRLTNQVEIARDSFAGLVLTLRSFVFTAAGALLGLLSLHPALLVVVLPPLAAGLALFLVTLRPMAAAQRRALAADEALGEHAASARAALRDLTACGTGPGAERHGADLVADAAAAARTLAGWAAVRTAALGVAGHLPVLALLVAVEWLRGHGVSVGALLGAFTYLVQSLLPALHTLMTALGAAGSRLLVVLDRILGPEPEPEPEPEPEPEPELGSGLEPEPEPASEPESGPSTASASAAAFAVHTAAAPAVELRSVTLSYGVRAEPVLDALDLRVAPGEHLAVVGPSGIGKSTLTRLVAGTLAPSRGEVRVAGRVVTGRPAAELAALRVLVPQDAYVFSGTVGDNLAYLRTDPSPAELDAAVEAFGLAPLVERLGGLDATVRPAELSPGERQLVALVRAYLSPAPLLLLDEATCHLDPASEARAEKALAGRSGTLVVVAHRLSSAVRADRTLVLDGIRAQSGTHAELLGRSPLYRDLTGHWNS | 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: Membrane
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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: Membrane
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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 Location: Membrane
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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 specifically enhanced by RAC1.
Sequence Mass (Da): 25348
Sequence Length: 233
Domain: The 2 cysteine and histidine-rich (CHORD) domains bind each 2 zinc ions, and the plant-specific 20 amino acid cysteine and histidine-containing motif (CCCH motif), located between the two CHORDs, binds 1 zinc ion.
Subcellular Location: Cytoplasm
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Q7ZTI3 | MYESVDVVGLTPSPNPFLSMDYYHQNRGCLIPDKGLVSGAARGFRNPHWSGSNHSVETQSTSSEEIVPSPPSPPPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHREKSCIINKVTRNRCQYCRLQKCLEVGMSKESVRNDRNKRKKDDKKQECLENYVLSPDTEKMIEQVRKAHQETFPSLCQLGKYTTNNSADHRVALDVDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPDQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLLCGDRQDLEQSDKVDELQEPLLEALKIYVRNRRPHKPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGLEGGGSKGAGGGGGGGGGKGAPPGSCSPSLSPSSAHSSPSAHSP | 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) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for hindbrain development and, in lateral plate mesoderm, for specification of the pectoral fins.
Sequence Mass (Da): 50525
Sequence Length: 458
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Subcellular Location: Nucleus
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Q90966 | MASNSSSCPTPGGGHLNGYPVTPYAFFFPHMLGGLSPPSSLPGIQHQLPVSGYSTPSPATVETQSTSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKDVPKTECSESYIVTPEVEELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLICGDRQDLEQPDKVDKLQEPLLEALKIYVRKRRPNKPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGMDTLGGQPGGPRTGGLGPPPGSCSPSLSPSSTRSSPATHSP | 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) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for hindbrain patterning and appears to be required for skin development.
Sequence Mass (Da): 50728
Sequence Length: 460
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Subcellular Location: Nucleus
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P10276 | MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGALTTLQHQLPVSGYSTPSPATIETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEVPKPECSESYTLTPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLICGDRQDLEQPDRVDMLQEPLLEALKVYVRKRRPSRPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGLDTLSGQPGGGGRDGGGLAPPPGSCSPSLSPSSNRSSPATHSP | 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) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 . In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression . On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation . Formation of a complex with histone deacetylases might lead to inhibition of RARE DNA element binding and to transcriptional repression . Transcriptional activation and RARE DNA element binding might be supported by the transcription factor KLF2 . RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis (By similarity). Has a role in the survival of early spermatocytes at the beginning prophase of meiosis (By similarity). In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes (By similarity). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). Together with RXRA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells . In association with HDAC3, HDAC5 and HDAC7 corepressors, plays a role in the repression of microRNA-10a and thereby promotes the inflammatory response .
PTM: Phosphorylated on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for transcriptional activity (By similarity). Phosphorylation by AKT1 is required for the repressor activity but has no effect on DNA binding, protein stability nor subcellular localization. Phosphorylated by PKA in vitro. This phosphorylation on Ser-219 and Ser-369 is critical for ligand binding, nuclear localization and transcriptional activity in response to FSH signaling.
Sequence Mass (Da): 50771
Sequence Length: 462
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Subcellular Location: Nucleus
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P10826 | MTTSGHACPVPAVNGHMTHYPATPYPLLFPPVIGGLSLPPLHGLHGHPPPSGCSTPSPATIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKETSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPTKVDKLQEPLLEALKIYIRKRRPSKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPSSSGNTAEHSPSISPSSVENSGVSQSPLVQ | 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) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors . The RXRA/RARB heterodimer can act as a repressor on the DR1 element and as an activator on the DR5 element . In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity).
Sequence Mass (Da): 50489
Sequence Length: 455
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Subcellular Location: Nucleus
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F4I6V0 | MMSRIEAYQSDIAVLMDPETVLLPDFISALSYAHELGRDWLLVSSSVEIPRFPFHWDETRHFWRQDNGKRVRFRELQKMISLRSLQSNSSASKMIMAWNNIDMPLHCGVLPPFLYQRGTHNQWIINEAMSCKRRFVFDATSTISSFFLGNAENIYNRSDNVSEPKTRNWEYVGNSHLGQLYGSLYSRSYTLPKLLKCNRRYIFVSASERSTDLSIPKGKSLGFRTREKISACITRTKSRSLKLDFVQKDETVPPLKFPFDLESLLPLVADKNRTVVLSVAGYSYKDMLMSWVCRLRRLKVPNFLVCALDDETYQFSILQGLPVFFDPYAPKNISFNDCHFGSKCFQRVTKVKSRTVLKILKLGYNVLLSDVDVYWFRNPLPLLQSFGPSVLAAQSDEYNTTAPINRPRRLNSGFYFARSDSPTIAAMEKVVKHAATSGLSEQPSFYDTLCGEGGAYRLGDDRCVEPETNLTVQFLDRELFPNGAYGDLWLKEDVRAECEKKHCFVLHNNWISGRLKKLERQMMKGLWEYDASMRMCV | 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.
Sequence Mass (Da): 61922
Sequence Length: 537
Domain: The conserved DXD motif is involved in enzyme activity.
EC: 2.4.2.-
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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 directly responsible for vesicle formation, movement, tethering and fusion . Involved in regulating the meiotic maturation of oocytes . Plays a role in egg shell formation, regulating exocytosis of chondroitin proteoglycans following fertilization . Controls cortical granule localization and targets them to the plasma membrane for exocytosis . Acts as a major regulator of membrane delivery during cytokinesis . Regulates the cytoskeleton by facilitating astral microtubule elongation and organization during metaphase to ensure proper spindle alignment and polarity in the first embryonic cell division . Maintains normal endoplasmic reticulum morphology during metaphase . Involved in vesicle formation and plasma membrane repair following exposure to pore forming toxins . Regulates endocytic recycling . May play a role in yolk receptor endocytosis in growing oocytes . Plays a role in the shedding of pathogen spores from intestinal cells via its involvement in spore fusion and endocytic trafficking .
Location Topology: Lipid-anchor
Sequence Mass (Da): 23429
Sequence Length: 211
Subcellular Location: Cytoplasmic vesicle
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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 directly responsible for vesicle formation, movement, tethering and fusion. The small Rab GTPase RAB11A regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes.
PTM: (Microbial infection) Glycosylated on arginine residues by S.typhimurium protein Ssek3.
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 24394
Sequence Length: 216
Subcellular Location: Cell membrane
EC: 3.6.5.2
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P0C2C2 | MNAPETIQAKPRKRYDAGVMKYKEMGYWDGDYVPKDTDVLALFRITPQDGVDPVEAAAAVAGESSTATWTVVWTDRLTACDMYRAKAYRVDPVPNNPEQFFCYVAYDLSLFEEGSIANLTASIIGNVFSFKPIKAARLEDMRFPVAYVKTFAGPSTGIIVERERLDKFGRPLLGATTKPKLGLSGRNYGRVVYEGLKGGLDFMKDDENINSQPFMHWRDRFLFVMDAVNKASAATGEVKGSYLNVTAGTMEEMYRRAEFAKSLGSVIIMVDLIVGWTCIQSMSNWCRQNDMILHLHRAGHGTYTRQKNHGVSFRVIAKWLRLAGVDHMHTGTAVGKLEGDPLTVQGYYNVCRDAYTQTDLTRGLFFDQDWASLRKVMPVASGGIHAGQMHQLIHLFGDDVVLQFGGGTIGHPQGIQAGATANRVALEAMVLARNEGRDILNEGPEILRDAARWCAPLRAALDTWGDITFNYTPTDTSDFVPTASVA | 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 site.
PTM: A disulfide bond might be able to form between Cys-278 in the large chain dimeric partners within the hexadecamer.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
Sequence Mass (Da): 53840
Sequence Length: 486
EC: 4.1.1.39
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Q0WQX7 | MARDRREGLEIKVVNPPAAATNNVAVETSPATATRRRRQQQRASFAEFRPFKLWFPWLVPAIVVANIALFAISMFINNCPKNSAYCLARFLGRFAFQPMKENPLLGPSSLTLEKMGALDVSMVVHKHEVWRLFTCIWLHAGVFHVLANMLSLIFIGIRLEQEFGFVRIGLLYMISGFGGSLLSSLFNRAGISVGASGALFGLLGAMLSELLTNWTIYANKFAALLTLIFIIAINLAVGILPHVDNFAHLGGFTSGFLLGFVFLIRPQYGYFNQRNNPRGYAAPSAKSKHKPYQYVLWITSLVLLIAGYTAGLVVLLRGTDLNKHCSWCHYLSCIPTSLWSCKSQNVYCESSQIGQQMNLTCITNGKTEMYKLSNDIPSRIQQLCSQLCR | 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 | MAVKKYSAGVKEYRQTYWMPEYTPLDSDILACFKITPQPGVDREEAAAAVAAESSTGTWTTVWTDLLTDMDYYKGRAYRIEDVPGDDAAFYAFIAYPIDLFEEGSVVNVFTSLVGNVFGFKAVRGLRLEDVRFPLAYVKTCGGPPHGIQVERDKMNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVQDATETAEAQTGERKGHYLNVTAPTPEEMYKRAEFAKEIGAPIIMHDYITGGFTANTGLAKWCQDNGVLLHIHRAMHAVIDRNPNHGIHFRVLTKILRLSGGDHLHTGTVVGKLEGDRASTLGWIDLLRESFIPEDRSRGIFFDQDWGSMPGVFAVASGGIHVWHMPALVNIFGDDSVLQFGGGTLGHPWGNAAGAAANRVALEACVEARNQGRDIEKEGKEILTAAAQHSPELKIAMETWKEIKFEFDTVDKLDTQNR | 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 site (By similarity) . There are estimated to be 270 RuBisCO heterohexadecamers per carboxysome (Ref.6).
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
Sequence Mass (Da): 52636
Sequence Length: 473
Domain: The N-terminus (minimally 1-122, fragment 1-136 does not bind any better) interacts with the shell proteins CsoS1A, CsoS1B and CsoS1C. A slightly longer fragment of the N-terminus (residues 1-136) is required for targeting to carboxysomes, and will direct foreign proteins to the carboxysome, with reduced efficiency compared to the whole protein.
Subcellular Location: Carboxysome
EC: 4.1.1.39
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P00878 | MSPQTETKTGAGFKAGVKDYRLTYYTPDYQVSETDILAAFRMTPQPGVPAEECGAAVAAESSTGTWTTVWTDGLTQLDRYKGRCYDLEPVPGESNQYIAYVAYPIDLFEEGSVTNLLTSIVGNVFGFKALRALRLEDLRIPPAYSKTFWGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQSFMRWRDRFLFCAEAIYKAQTETGEVKGHYLNATAGTCEEMYKRASFAAQIGVPIIMHDYLTGGFTANTSLAMYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKTLRMSGGDHLHSGTVVGKLEGEREVTLGFVDLMRDAYVEKDRSRGIYFTQDWCGMGGTMPVASGGIHVWHMPALTEIFGDDACLQFGGGTLGHPWGNAPGAAANRVASEACVQARNEGRDLSREGGDVIREACKWSPELAAACEVWKEIKFEFETIDKL | 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 competition at the same active site.
PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
Sequence Mass (Da): 52609
Sequence Length: 475
Subcellular Location: Plastid
EC: 4.1.1.39
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Q20EX7 | MPTTETKTGAGFKAGVKDYRLTYYTPDYQVKETDILAAFRMTPQPGVPPEECGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDLEPVPGEENQYIAYIAYPIDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQAERDRLNKYGRGLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVSEAIYKAQAETGEIKGHYLNATAPDCEEMYKRAECAKDFGVPIIMHDYLTGGFTANTSLATYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKALRLSGGDHLHSGTVVGKLEGEREVTLGFVDLMRDDYIEKDRSRGIYFTQDWCSLPGTMPVASGGIHVWHMPALVEIFGDDACLQFGGGTLGHPWGNAPGAAANRVALEACTQARNEGRDLAREGGDVIRQACQWSPELAAACEVWKEIKFEFETIDTL | 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 competition at the same active site.
PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
Sequence Mass (Da): 52647
Sequence Length: 474
Subcellular Location: Plastid
EC: 4.1.1.39
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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 competition at the same active site (By similarity).
PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
Sequence Mass (Da): 6102
Sequence Length: 55
Subcellular Location: Plastid
EC: 4.1.1.39
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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 similarity).
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
Sequence Mass (Da): 6209
Sequence Length: 58
Subcellular Location: Plastid
EC: 4.1.1.39
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P11383 | MSPQTETKAGVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEDSQWICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHSGTVVGKLEGEREMTLGFVDLLRDDFIEKDRARGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVQARNEGRDLAREGNEIIRAACKWSPELAAACEVWKAIKFEFEPVDTIDK | 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 competition at the same active site.
PTM: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
Sequence Mass (Da): 52851
Sequence Length: 477
Subcellular Location: Plastid
EC: 4.1.1.39
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Q9PT60 | MTECFLPPASSPSEHRRAEHGGGLARTPSSEEISPTKFPGLYRTGEPLPPHDILHEPPDIVSEDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKIKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEDKHKEKKSKDLTAADVVKQWKEKKKKKKPTPEPESLPVDIPRLRPVFGIPLIEAAERTMIYDGIRLPLVFRECIDFIEQHGMKCEGIYRVSGIKSKVDELKAAYDREESPNLEDYEPYTVASLLKQYLRELPENVLTKDLMPRFEEACGKTTEGERLQECQRLLKELPECNFCLTSWLVVHMDHVIEQELETKMNIQNISIVLSPTVQISNRVLYVFFTHVQELFGGVQIKRVIKPLRWSNMATMPALPETQETIKEEIRRQEFLLNCLHRELQAGVKDLSKEERLWEVQRILTALKRKLREAKRQDCETKIAQEIASLSKEDVSKEEMTENEEEVLNILLAQENEILTEQEELVAMEQYLRRQIATEKEEIDRLRAEISEIQSRQQHGRSETEEYSSESESESEDEEELQYILEDLQRQNEELEIKNTHLNQAIHEEREAIIELRVQLRLLQKQRVKSEQLQEEEELGKQNVPSQLPRDNLPETKAPKDQPKALMEQMKPSPIKKTGKKLSSETLI | 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. During mitosis, may act as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase of the cell cycle. During mitosis, also controls mitochondrial fission as an effector of ralA. Recruited to mitochondrion by ralA, acts as a scaffold to foster the mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of DNM1L (By similarity). Acts on the cytoskeleton, to regulate pigment distribution and to regulate gastrulation .
Catalytic Activity: an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76146
Sequence Length: 655
Domain: The Rho-GAP domain mediates the GTPase activator activity toward CDC42.
Subcellular Location: Cell membrane
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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
Subcellular Location: Nucleus
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Q15311 | MTECFLPPTSSPSEHRRVEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDILHEPPDVVSDDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQIDVPNLKPIFGIPLADAVERTMMYDGIRLPAVFRECIDYVEKYGMKCEGIYRVSGIKSKVDELKAAYDREESTNLEDYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTETEKVQEFQRLLKELPECNYLLISWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVFFTHVQELFGNVVLKQVMKPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIERLRAEIAEIQSRQQHGRSETEEYSSESESESEDEEELQIILEDLQRQNEELEIKNNHLNQAIHEEREAIIELRVQLRLLQMQRAKAEQQAQEDEEPEWRGGAVQPPRDGVLEPKAAKEQPKAGKEPAKPSPSRDRKETSI | 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 . During mitosis, may act as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase of the cell cycle . During mitosis, also controls mitochondrial fission as an effector of RALA . Recruited to mitochondrion by RALA, acts as a scaffold to foster the mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of DNM1L .
PTM: Tyrosine-phosphorylated upon stimulation of cells with EGF.
Location Topology: Peripheral membrane protein
Catalytic Activity: an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate
Sequence Mass (Da): 76063
Sequence Length: 655
Domain: The Rho-GAP domain mediates the GTPase activator activity toward CDC42.
Subcellular Location: Cell membrane
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Q62796 | MTECFLPPTSSPSEHRRAEHGSGLTRTPSSEEISPTKFPELYRTGEPSPPHDILHEPPDIVSDDEKDHGKKKGKFKKKEKRTEGYVAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKCKDFTAADVVKQWKEKKKKKKPTQEPEVPQTDAPSLRPIFGAPFADAVERTMMYDGIRLPAVFRECVDYMEKHGMKCEGIYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTEVEKVQEFQRLLRELPEYNHLLLSWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVLFTHVQELFGTVLLKQVTRPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDFSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEETNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQHGRSETEEYSSDSESESEDEEELQIILEDLQRQNEELEIKNNHLNQAVHEEREAIVELRVQLRLLQMLRAKSEQQLQEEEEPERRGGTGPLPCEGVLEVRAAKEQAKPSPSKDRKETPI | 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 . During mitosis, may act as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase of the cell cycle. During mitosis, also controls mitochondrial fission as an effector of RALA. Recruited to mitochondrion by RALA, acts as a scaffold to foster the mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of DNM1L (By similarity).
PTM: Tyrosine-phosphorylated upon stimulation of cells with EGF.
Location Topology: Peripheral membrane protein
Catalytic Activity: an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate
Sequence Mass (Da): 75252
Sequence Length: 647
Domain: The Rho-GAP domain mediates the GTPase activator activity toward CDC42.
Subcellular Location: Cell membrane
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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.
Subcellular Location: Cytoplasm
EC: 5.4.99.62
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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.
Subcellular Location: Cytoplasm
EC: 5.4.99.62
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P51763 | MPEYQNIFTTVQVRAPAYPGVPLPKGSLPRIGKPIFSYWAGKIGDAQIGPIYLGFTGTLSIIFGFMAIFIIGFNMLASVDWNIIQFVKHFFWLGLEPPAPQYGLTIPPLSEGGWWLMAGFFLTMSILLWWVRTYKRAEALGMSQHLSWAFAAAIFFYLSLGFIRPVMMGSWAEAVPFGIFPHLDWTAAFSIRYGNLYYNPFHMLSIAFLYGSALLFAMHGATILAVSRFGGDREIDQITDRGTAAERAAIFWRWTMGFNASMESIHRWAWWCAVLTVITAGIGILLTGTVVENWYLWAIKHGVAPAYPEVVTAVDPYATATGVTQ | 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
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P06010 | MADYQTIYTQIQARGPHITVSGEWGDNDRVGKPFYSYWLGKIGDAQIGPIYLGASGIAAFAFGSTAILIILFNMAAEVHFDPLQFFRQFFWLGLYPPKAQYGMGIPPLHDGGWWLMAGLFMTLSLGSWWIRVYSRARALGLGTHIAWNFAAAIFFVLCIGCIHPTLVGSWSEGVPFGIWPHIDWLTAFSIRYGNFYYCPWHGFSIGFAYGCGLLFAAHGATILAVARFGGDREIEQITDRGTAVERAALFWRWTIGFNATIESVHRWGWFFSLMVMVSASVGILLTGTFVDNWYLWCVKHGAAPDYPAYLPATPDPASLPGAPK | 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
|
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 | MYPEYQNIFTQVQVRGTPEMGMDDAGNNMMEERVGKPFFSTLAGLFGNGQIGPYYFGWTSIVAFGTGIAWFVIVGFNMLAQVGWSIPQFIRQLFWLALEPPSPEYGLSMPPLNDGGWYIIASFFLLVSVMTWLLRAYLLAEQHKMGKHIFWGFAAAVWLFLVLGLFRPILMGSWSEAVPYGIFPHLDWTTAFSIRYGNLYYNPFHCLSIVFLYGSVLLFCMHGGTILAVTRYGGDRELEQIYDRGTATERAALFWRWTMGFNATMEGIHRWAWWFAVLTPITGGIGILLTGTVVDNWFIWAQEHHFAPMYDGSYGYEDYGSYEAFIGKEN | 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
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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
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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
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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
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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
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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
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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
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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
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P43297 | MGFLKPTMAILFLAMVAVSSAVDMSIISYDEKHGVSTTGGRSEAEVMSIYEAWLVKHGKAQSQNSLVEKDRRFEIFKDNLRFVDEHNEKNLSYRLGLTRFADLTNDEYRSKYLGAKMEKKGERRTSLRYEARVGDELPESIDWRKKGAVAEVKDQGGCGSCWAFSTIGAVEGINQIVTGDLITLSEQELVDCDTSYNEGCNGGLMDYAFEFIIKNGGIDTDKDYPYKGVDGTCDQIRKNAKVVTIDSYEDVPTYSEESLKKAVAHQPISIAIEAGGRAFQLYDSGIFDGSCGTQLDHGVVAVGYGTENGKDYWIVRNSWGKSWGESGYLRMARNIASSSGKCGIAIEPSYPIKNGENPPNPGPSPPSPIKPPTQCDSYYTCPESNTCCCLFEYGKYCFAWGCCPLEAATCCDDNYSCCPHEYPVCDLDQGTCLLSKNSPFSVKALKRKPATPFWSQGRKNIA | 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 cinerea, functions as PCD-promoting protease that is released from the ER body or vacuole to the cytoplasm . Accumulates in endoplasmic reticulum-derived bodies in epidermal cells and may participate in cell death in stressed or injured cells . Involved in water stress-induced cell death through its protease activity that is released to the cytoplasm after vacuolar collapse . Possesses protease activity in vitro and is involved in cell death in the transmitting tract and septum epidermis during flower development . Possesses peptide ligase activity. Can ligate peptides to unmodified N-termini of acceptor proteins. Probably ligates through a thioester intermediate .
Sequence Mass (Da): 50966
Sequence Length: 462
Subcellular Location: Vacuole
EC: 3.4.22.-
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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 acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
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P54725 | MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE | 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 polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.
Sequence Mass (Da): 39609
Sequence Length: 363
Domain: The ubiquitin-like domain mediates interaction with ATXN3.
Subcellular Location: Nucleus
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P54727 | MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILNDDTALKEYKIDEKNFVVVMVTKPKAVSTPAPATTQQSAPASTTAVTSSTTTTVAQAPTPVPALAPTSTPASITPASATASSEPAPASAAKQEKPAEKPAETPVATSPTATDSTSGDSSRSNLFEDATSALVTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPQAASTGAPQSSAVAAAAATTTATTTTTSSGGHPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGGQGGGGGGGSGGIAEAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQNFDED | 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 reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.
Sequence Mass (Da): 43171
Sequence Length: 409
Domain: The ubiquitin-like domain mediates interaction with ATXN3.
Subcellular Location: Nucleus
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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 required for meiotic double-strand break (DSB) formation.
PTM: Phosphorylated during meiotic prophase. Dephosphorylation seems to be dependent on DSB formation.
Sequence Mass (Da): 35683
Sequence Length: 314
Subcellular Location: Nucleus
|
Q18DC9 | MLRSWEFVLLISCFLCFSSDALQRISLKKMPSIRETLQEMGMKVADVLPSLKHRISYLDEGLHNKTASTILTNFRDTQYYGEISIGTPAQIFKVVFDTGSSNLWVPSRQCSPLYSACVSHNRYDSSESSTYKPKGTKITLTYAQGYIKGFFSQDIVRVADIPIIQFFTEAIALPSIPFIFARFDGVLGMGYPKQAIGGVIPVFDNIMSEKVLSENVFSVYYSRHSESNTGGEIILGGSDPSHYTGDFHYVSTSREGYWHVDLKGVSIENKIVLCHDGCTATIDTGTSFISGPASSISVLMETIGATLSDGDYVIDCKKINLLPDITFHLGDMTYSLSSSTYVLKFSDETECTVAFMAVDIPPPLGPLWLLGATFIKQYYIEFDRQNNRIGFATSF | 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 and shown to specifically cleave human and porcine angiotensinogen into angiotensin I. It does not have general protease activity, no cleavage of alpha or beta casein. May be directly responsible for elevation of blood pressure in the victims of envenomation .
PTM: N-glycosylated.
Catalytic Activity: Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.
Sequence Mass (Da): 43872
Sequence Length: 395
Subcellular Location: Secreted
EC: 3.4.23.15
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Q8KHV6 | MSVFDLPRLHFAGTATTRLPTGPRNGLVDLSTHSVVMDGERFPASRPAAEYHAYLDRVGGKGTAFAGNGYFAIDAGITAVERAAGEVDTGDLLVGRAVDVWGHYNEYLATTFNRARIFDVDPSSSWTSTVMIGQFGFGRLGRSHDVGYVFTGGVHGMQPPRWHEDGRVLHQFTVPAGEDMTWFGSAADSPAAARLRELVESGEADGLVVQLALSDAGPAPMPHAQQWRLRGTIAPWHAGEPRTCPAGRLLTPHNLTADLRGDHVSLNLISFRPPTGISGLELRTADTDRFIARVPADDPHGVVTVPAAEGGDEALCVVGTTAAGERIVVSREREVTVHVDDASVFLEHPRGPGDSDQDAEIAVRTYVRGEPAAATIHIGQYFNPRAFPLDEHATAASATPEDLDVVALCVDGTRWSRHCVISTDENGDGRFLLRGARPGATRLLLSAEGATPFDGLTAAAAYDNDDSLGLWSGLASVAVRVLPDHWWMDDIPRDKVTFDLLYREVFAFYELLYSFMGEEVFSLADRFRVETHPRLIWQMCDPRNRAKTYYMPPTRDLTGPQARLLLAYLRAQNSDVVVPVIEPSHTRSGTPISTRTDLVRALRHGVAIELAVMLQYLYAAFSIPTHGAGQELVSRGDWTPEQLRLMCGDGGETTDGGVRGSLLGVAREEMIHFLVVNNVLMAVGEPFHVPDLDFGTINDTLMVPLDFSLEALGLGSVQRFIQIEQPEGLTGAVRLGDLPVPVREAEDFHYASLSELYGDIREGLQRVPGLFLVERGRGGGEHHLFLRESVNAVHPDYQLEVDDLSSALFAIDFVTEQGEGHVLTDEDTGEESHYDTFVRVADLLMKERLTAADTRRAQWSPAYPVARNPTVHGGGQSKELVTSPVARELMVLFNKSYFMMLQLMVQHFGGSPDASLRRSKLMNAAIDVMTGVMRPLAELLVTVPSGRHGRTAGPSFELDEKPAFIPRADVARRAISLRFRHLAESARTCALVPDKVVRNLDFLADQFATEGPR | 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 bisindolopyrrolocarbazole scaffold of the rebeccamycin. The hydrogen peroxide is provided together with iminoindolpropanoate by RebO. Due to the instability of indole 3-pyruvate (IPA), which is hydrolyzed in solution and exits in equilibrium with the predominant ketone form of IPA, the concerted functioning of the RebO/RebD system appears to prevent the buildup of significant amounts of IPA and its imine in solution, effectively shepherding the imine further down the biosynthetic chain.
Catalytic Activity: 2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 = dichlorochromopyrrolate + H(+) + 2 H2O + NH4(+)
Sequence Mass (Da): 110746
Sequence Length: 1013
EC: 1.21.98.2
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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 | MGARVLVATTPGDGHVNPMVPVAQEMVSRGHEVRWYTGKAFRSTVERTGARHEPMRDAHDFGGMPREEAFPQHAGLTGITGMIAGFRDIFIEPAADQMTDLLALLEDFPADVLVTDETFFGAGFVSERTGIPVAWIATSIYVFSSRDTAPLGLGLPPSSSRLGRLRNTVLKQLTDRVVMRDLRRHADVVRDRVGLPRIRKGAFENIMRTPDLYLLGTVPSFEYPRGDMPPEVRFVGPFVSPAPPDFTPPAWWGELDSGRPVVHVTQGTVANDAERLLLPAIRALAAEDVLVVATTGAPLELEPMPANVRVERFIPHHALLPHVDAMVTNGGYGGVNTALAHGVPLVVAAATEEKHEVAARVSWSGAGVHLKKRRLSERDIRRAVRAVLDEPRFRVHAARLRDEYAARDAVVDAVDLIEGLV | 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'-demethylrebeccamycin + H2O = beta-D-glucose + dichloroarcyriaflavin A
Sequence Mass (Da): 46021
Sequence Length: 421
Pathway: Alkaloid biosynthesis.
EC: 4.3.3.5
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