Q872I5 · INO80_NEUCR
- ProteinChromatin-remodeling ATPase INO80
- Genecrf2-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1997 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | Ino80 complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent chromatin remodeler activity | |
Molecular Function | DNA binding | |
Molecular Function | histone binding | |
Biological Process | chromatin remodeling | |
Biological Process | DNA repair | |
Biological Process | DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChromatin-remodeling ATPase INO80
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Sordariaceae > Neurospora
Accessions
- Primary accessionQ872I5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000074327 | 1-1997 | Chromatin-remodeling ATPase INO80 | |||
Sequence: MDHFSTVLQRPPHFDEDGTEGRGDRGNGAGPGPAPPPPPPRGGLRDILNPVSSNSAVQSQAAAAAPPPPPAVASSSLHGIAASVPPPSSTNSMRATPHSSSSFNLRSPTREPSEYRHPLSSLATPAPFAASPPTSIANANNTNNNNALGAAGSLSSQPPPPPPTGPRSILNPPTPSQQHQQQHHHPNPFVAASAPSLPPPPSSLQAPPAITPIAGLSAPAPASGSLPLSAGGIGNSITVSSSSQPPARASQLHAPSAYYSPAESFRDRDSSVREKSSTGGSFYDPTAEASNGISGSSPRKDRDRDRDHRGTTRESQRRSVSGHSDTGSSWRNATQTSASNKTRDPYNYSPSSADYYNTRKKENYPVDNTTSSSIAAPSNFTVATRSPVAALSHPASIAAPASVGSLTGSISPRLSLRPPSMASPTIRSAVLANPTNGTTSTALPALGRNDSPPSKMSPGTSTNPSRAAGVMSFSNILSSSEPVPRPRATSPNNPDDDDDVPMKVERADSSEKVVKEKKERKPRQPKQPRISDIRHSESTPKGRRGSTKQESPLPNIRIPAKRMANGAPKQQKTFSAENEEKIRKAMDRIETRELPHEDEFEEELRLWRERREYKRQQMNQRDLRQRRQRRADYTEVEAQKLKLHADFGKRRYDDLNYDDALQEVRERELFAEKERKKDMQRKRRREKSMATTMEAKAAALARASAAQDEAERQKYMREAERANKKVQQTRLILQKGIKGPSRNTGPIEPNLEGGTMATFQAENMEPGKTKGKGRAGARPKKSKEQKQAEKDAAEAAQAALDAGLELPPKEETNKIRIKLTKTKAPKEADVDKDKENKEPQEPKEPKEPKEKVIKEKVVEEPKDPLELKFQSKGFNQIYDQIWRDLARKDVNKVFRLAIDSYSTKSSNLKKTAILASKEAKRWQLRTNKGTKDLQARAKRVMRDMMGFWKRNEREERDLRKAAEKQELENARKEEADREAARQKRKLNFLISQTELYSHFIGKKIKTNEVERSTDHPDEIAAEKDKIPENEMDIEVPTGPIGAKVTNFENLDFDAEDESTLRAAAMANAQNAIAEAQKKAREFNKEESKLDEDGEMNFQNPTMMGDVEIEQPKLLNCQLKEYQLKGLNWLVNLYEQGINGILADEMGLGKTVQSISVMAYLAEKYDIWGPFLVVAPASTLHNWQQEITKFVPQFKVLPYWGTAGDRKVLRKFWDRKHTTYKKDAPFHVMITSYQLVVSDVAYFQKMKWQYMILDEAQAIKSSQSSRWKCLLGFHCRNRLLLTGTPIQNNMQELWALLHFIMPSLFDSHDEFSEWFSKDIESHAQSNTKLNEDQLKRLHMILKPFMLRRVKKHVQKELGDKIEMDVFCDLTYRQRAMYANLRNQISIMDLIEKATLGDDDSASLMNLVMQFRKVCNHPDLFERADTASPYSFGHFAETASFIREGSQVTVGYSTRSLIQYELPRLLWRDGGRLHKAGEDNQVAGWRNQWLNEKFNIWTPEHIRESLAGTDNFSWLRFADTSYEEAYRASHKDLFARAVEMSTKKNRLAEIKIAYDEPEDLNFTPAHALFHIREREDRRPLAEITEQGILGSLMNVSRSAFSETGLGRLEQAAAPKASAPPIEVVCDSRSAVVERENIMFNAPMRKVLFGPTLAEEKALVVQKVPPSRYPPPALLPAPDKEKQKFTNITVPSMRRFVTDSGKLAKLDELLRELKENGHRVLLYFQMTRMIDLMEEYLTYRNYKYCRLDGSTKLEDRRDTVADFQTRPEIFIFLLSTRAGGLGINLTSADTVIFYDSDWNPTIDSQAMDRAHRLGQTKQVTVYRLITRGTIEERIRKRAMQKEEVQRVVITGGSSAAGGGVDFSGRRAPENRNRDIAMWLADDEQAEMIEKRERELLESGELDKMQKKSRGGNKRKRGGAGGEGKEVSLDEMYHEGEGNFDDGGNNIKGSGTATPNGAAGGEGGDGKGAVGGAAKKRKTGGSKKAKTTKQRLAIADGEIDI |
Proteomic databases
Interaction
Subunit
Component of the INO80 chromatin-remodeling complex.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-378 | Disordered | ||||
Sequence: MDHFSTVLQRPPHFDEDGTEGRGDRGNGAGPGPAPPPPPPRGGLRDILNPVSSNSAVQSQAAAAAPPPPPAVASSSLHGIAASVPPPSSTNSMRATPHSSSSFNLRSPTREPSEYRHPLSSLATPAPFAASPPTSIANANNTNNNNALGAAGSLSSQPPPPPPTGPRSILNPPTPSQQHQQQHHHPNPFVAASAPSLPPPPSSLQAPPAITPIAGLSAPAPASGSLPLSAGGIGNSITVSSSSQPPARASQLHAPSAYYSPAESFRDRDSSVREKSSTGGSFYDPTAEASNGISGSSPRKDRDRDRDHRGTTRESQRRSVSGHSDTGSSWRNATQTSASNKTRDPYNYSPSSADYYNTRKKENYPVDNTTSSSIAAPS | ||||||
Compositional bias | 9-23 | Basic and acidic residues | ||||
Sequence: QRPPHFDEDGTEGRG | ||||||
Compositional bias | 30-44 | Pro residues | ||||
Sequence: GPGPAPPPPPPRGGL | ||||||
Compositional bias | 81-109 | Polar residues | ||||
Sequence: AASVPPPSSTNSMRATPHSSSSFNLRSPT | ||||||
Compositional bias | 127-153 | Polar residues | ||||
Sequence: PFAASPPTSIANANNTNNNNALGAAGS | ||||||
Compositional bias | 155-170 | Pro residues | ||||
Sequence: SSQPPPPPPTGPRSIL | ||||||
Compositional bias | 171-187 | Polar residues | ||||
Sequence: NPPTPSQQHQQQHHHPN | ||||||
Compositional bias | 192-207 | Pro residues | ||||
Sequence: ASAPSLPPPPSSLQAP | ||||||
Compositional bias | 229-250 | Polar residues | ||||
Sequence: SAGGIGNSITVSSSSQPPARAS | ||||||
Compositional bias | 275-296 | Polar residues | ||||
Sequence: KSSTGGSFYDPTAEASNGISGS | ||||||
Compositional bias | 297-320 | Basic and acidic residues | ||||
Sequence: SPRKDRDRDRDHRGTTRESQRRSV | ||||||
Compositional bias | 321-378 | Polar residues | ||||
Sequence: SGHSDTGSSWRNATQTSASNKTRDPYNYSPSSADYYNTRKKENYPVDNTTSSSIAAPS | ||||||
Region | 397-579 | Disordered | ||||
Sequence: IAAPASVGSLTGSISPRLSLRPPSMASPTIRSAVLANPTNGTTSTALPALGRNDSPPSKMSPGTSTNPSRAAGVMSFSNILSSSEPVPRPRATSPNNPDDDDDVPMKVERADSSEKVVKEKKERKPRQPKQPRISDIRHSESTPKGRRGSTKQESPLPNIRIPAKRMANGAPKQQKTFSAENE | ||||||
Compositional bias | 402-486 | Polar residues | ||||
Sequence: SVGSLTGSISPRLSLRPPSMASPTIRSAVLANPTNGTTSTALPALGRNDSPPSKMSPGTSTNPSRAAGVMSFSNILSSSEPVPRP | ||||||
Compositional bias | 491-544 | Basic and acidic residues | ||||
Sequence: PNNPDDDDDVPMKVERADSSEKVVKEKKERKPRQPKQPRISDIRHSESTPKGRR | ||||||
Coiled coil | 666-735 | |||||
Sequence: ERELFAEKERKKDMQRKRRREKSMATTMEAKAAALARASAAQDEAERQKYMREAERANKKVQQTRLILQK | ||||||
Compositional bias | 674-691 | Basic and acidic residues | ||||
Sequence: ERKKDMQRKRRREKSMAT | ||||||
Region | 674-858 | Disordered | ||||
Sequence: ERKKDMQRKRRREKSMATTMEAKAAALARASAAQDEAERQKYMREAERANKKVQQTRLILQKGIKGPSRNTGPIEPNLEGGTMATFQAENMEPGKTKGKGRAGARPKKSKEQKQAEKDAAEAAQAALDAGLELPPKEETNKIRIKLTKTKAPKEADVDKDKENKEPQEPKEPKEPKEKVIKEKVV | ||||||
Compositional bias | 707-725 | Basic and acidic residues | ||||
Sequence: QDEAERQKYMREAERANKK | ||||||
Compositional bias | 767-791 | Basic and acidic residues | ||||
Sequence: GKTKGKGRAGARPKKSKEQKQAEKD | ||||||
Compositional bias | 807-858 | Basic and acidic residues | ||||
Sequence: PPKEETNKIRIKLTKTKAPKEADVDKDKENKEPQEPKEPKEPKEKVIKEKVV | ||||||
Domain | 881-1006 | DBINO | ||||
Sequence: IWRDLARKDVNKVFRLAIDSYSTKSSNLKKTAILASKEAKRWQLRTNKGTKDLQARAKRVMRDMMGFWKRNEREERDLRKAAEKQELENARKEEADREAARQKRKLNFLISQTELYSHFIGKKIKT | ||||||
Domain | 1130-1302 | Helicase ATP-binding | ||||
Sequence: VNLYEQGINGILADEMGLGKTVQSISVMAYLAEKYDIWGPFLVVAPASTLHNWQQEITKFVPQFKVLPYWGTAGDRKVLRKFWDRKHTTYKKDAPFHVMITSYQLVVSDVAYFQKMKWQYMILDEAQAIKSSQSSRWKCLLGFHCRNRLLLTGTPIQNNMQELWALLHFIMPS | ||||||
Motif | 1253-1256 | DEAQ box | ||||
Sequence: DEAQ | ||||||
Domain | 1702-1858 | Helicase C-terminal | ||||
Sequence: KLDELLRELKENGHRVLLYFQMTRMIDLMEEYLTYRNYKYCRLDGSTKLEDRRDTVADFQTRPEIFIFLLSTRAGGLGINLTSADTVIFYDSDWNPTIDSQAMDRAHRLGQTKQVTVYRLITRGTIEERIRKRAMQKEEVQRVVITGGSSAAGGGVD | ||||||
Region | 1891-1986 | Disordered | ||||
Sequence: ELLESGELDKMQKKSRGGNKRKRGGAGGEGKEVSLDEMYHEGEGNFDDGGNNIKGSGTATPNGAAGGEGGDGKGAVGGAAKKRKTGGSKKAKTTKQ | ||||||
Compositional bias | 1912-1934 | Basic and acidic residues | ||||
Sequence: KRGGAGGEGKEVSLDEMYHEGEG |
Domain
The DBINO region is involved in binding to DNA.
Sequence similarities
Belongs to the SNF2/RAD54 helicase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,997
- Mass (Da)223,073
- Last updated2007-12-04 v3
- Checksum749AF1E8F98F1142
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
V5IMG6 | V5IMG6_NEUCR | crf2-1 | 2011 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-23 | Basic and acidic residues | ||||
Sequence: QRPPHFDEDGTEGRG | ||||||
Compositional bias | 30-44 | Pro residues | ||||
Sequence: GPGPAPPPPPPRGGL | ||||||
Compositional bias | 81-109 | Polar residues | ||||
Sequence: AASVPPPSSTNSMRATPHSSSSFNLRSPT | ||||||
Compositional bias | 127-153 | Polar residues | ||||
Sequence: PFAASPPTSIANANNTNNNNALGAAGS | ||||||
Compositional bias | 155-170 | Pro residues | ||||
Sequence: SSQPPPPPPTGPRSIL | ||||||
Compositional bias | 171-187 | Polar residues | ||||
Sequence: NPPTPSQQHQQQHHHPN | ||||||
Compositional bias | 192-207 | Pro residues | ||||
Sequence: ASAPSLPPPPSSLQAP | ||||||
Compositional bias | 229-250 | Polar residues | ||||
Sequence: SAGGIGNSITVSSSSQPPARAS | ||||||
Compositional bias | 275-296 | Polar residues | ||||
Sequence: KSSTGGSFYDPTAEASNGISGS | ||||||
Compositional bias | 297-320 | Basic and acidic residues | ||||
Sequence: SPRKDRDRDRDHRGTTRESQRRSV | ||||||
Compositional bias | 321-378 | Polar residues | ||||
Sequence: SGHSDTGSSWRNATQTSASNKTRDPYNYSPSSADYYNTRKKENYPVDNTTSSSIAAPS | ||||||
Compositional bias | 402-486 | Polar residues | ||||
Sequence: SVGSLTGSISPRLSLRPPSMASPTIRSAVLANPTNGTTSTALPALGRNDSPPSKMSPGTSTNPSRAAGVMSFSNILSSSEPVPRP | ||||||
Compositional bias | 491-544 | Basic and acidic residues | ||||
Sequence: PNNPDDDDDVPMKVERADSSEKVVKEKKERKPRQPKQPRISDIRHSESTPKGRR | ||||||
Compositional bias | 674-691 | Basic and acidic residues | ||||
Sequence: ERKKDMQRKRRREKSMAT | ||||||
Compositional bias | 707-725 | Basic and acidic residues | ||||
Sequence: QDEAERQKYMREAERANKK | ||||||
Compositional bias | 767-791 | Basic and acidic residues | ||||
Sequence: GKTKGKGRAGARPKKSKEQKQAEKD | ||||||
Compositional bias | 807-858 | Basic and acidic residues | ||||
Sequence: PPKEETNKIRIKLTKTKAPKEADVDKDKENKEPQEPKEPKEPKEKVIKEKVV | ||||||
Compositional bias | 1912-1934 | Basic and acidic residues | ||||
Sequence: KRGGAGGEGKEVSLDEMYHEGEG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX294010 EMBL· GenBank· DDBJ | CAD70746.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CM002240 EMBL· GenBank· DDBJ | ESA42365.1 EMBL· GenBank· DDBJ | Genomic DNA |