ID F4J277_ARATH Unreviewed; 1540 AA.
AC F4J277;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000256|ARBA:ARBA00019805, ECO:0000256|RuleBase:RU368001};
DE EC=3.6.4.- {ECO:0000256|RuleBase:RU368001};
GN Name=INO80 {ECO:0000313|EMBL:AEE79638.1, ECO:0000313|TAIR:AT3G57300};
GN Synonyms=ATINO80 {ECO:0000313|EMBL:AEE79638.1}, INO80 ORTHOLOG
GN {ECO:0000313|EMBL:AEE79638.1}, INO80 ortholog
GN {ECO:0000313|EMBL:AEE79638.1};
GN OrderedLocusNames=At3g57300 {ECO:0000313|Araport:AT3G57300,
GN ECO:0000313|EMBL:AEE79638.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:AEE79638.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:AEE79638.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130713; DOI=10.1038/35048706;
RG European Union Chromosome 3 Arabidopsis Sequencing Consortium;
RG Institute for Genomic Research;
RG Kazusa DNA Research Institute;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Blocker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M.,
RA Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N.,
RA Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L.,
RA Weissenbach J., Saurin W., Quetier F., Schafer M., Muller-Auer S.,
RA Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N.,
RA Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P.,
RA Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S.,
RA Simionati B., Conrad A., Hornischer K., Kauer G., Lohnert T.H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schon O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwalder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.W., Mayer K.F., Kaul S.,
RA Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: ATPase component of the INO80 complex which remodels
CC chromatin by shifting nucleosomes and is involved in DNA repair.
CC {ECO:0000256|RuleBase:RU368001}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU368001};
CC -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex.
CC {ECO:0000256|RuleBase:RU368001}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368001}.
CC -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC {ECO:0000256|RuleBase:RU368001}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025, ECO:0000256|RuleBase:RU368001}.
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DR EMBL; CP002686; AEE79638.1; -; Genomic_DNA.
DR RefSeq; NP_001190117.1; NM_001203188.1.
DR SMR; F4J277; -.
DR ProteomicsDB; 218303; -.
DR EnsemblPlants; AT3G57300.2; AT3G57300.2; AT3G57300.
DR GeneID; 824897; -.
DR Gramene; AT3G57300.2; AT3G57300.2; AT3G57300.
DR Araport; AT3G57300; -.
DR TAIR; AT3G57300; INO80.
DR OMA; FWKKNER; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J277; baseline and differential.
DR GO; GO:0031011; C:Ino80 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:TAIR.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:TAIR.
DR GO; GO:0016444; P:somatic cell DNA recombination; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF2; CHROMATIN-REMODELING ATPASE INO80; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF13892; DBINO; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51413; DBINO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368001};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU368001};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU368001};
KW DNA-binding {ECO:0000256|RuleBase:RU368001};
KW Helicase {ECO:0000313|EMBL:AEE79638.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368001};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F4J277,
KW ECO:0007829|ProteomicsDB:F4J277};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT DOMAIN 350..475
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 598..802
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1243..1393
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 30..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1448..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1540 AA; 175960 MW; A0F710B63FDF71C9 CRC64;
MDPSRRPPKD SPYANLFDLE PLMKFRIPKP EDEVDYYGSS SQDESRSTQG GVVANYSNGS
KSRMNASSKK RKRWTEAEDA EDDDDLYNQH VTEEHYRSML GEHVQKFKNR SKETQGNPPH
LMGFPVLKSN VGSYRGRKPG NDYHGRFYDM DNSPNFAADV TPHRRGSYHD RDITPKIAYE
PSYLDIGDGV IYKIPPSYDK LVASLNLPSF SDIHVEEFYL KGTLDLRSLA ELMASDKRSG
VRSRNGMGEP RPQYESLQAR MKALSPSNST PNFSLKVSEA AMNSAIPEGS AGSTARTILS
EGGVLQVHYV KILEKGDTYE IVKRSLPKKL KAKNDPAVIE KTERDKIRKA WINIVRRDIA
KHHRIFTTFH RKLSIDAKRF ADGCQREVRM KVGRSYKIPR TAPIRTRKIS RDMLLFWKRY
DKQMAEERKK QEKEAAEAFK REQEQRESKR QQQRLNFLIK QTELYSHFMQ NKTDSNPSEA
LPIGDENPID EVLPETSAAE PSEVEDPEEA ELKEKVLRAA QDAVSKQKQI TDAFDTEYMK
LRQTSEMEGP LNDISVSGSS NIDLHNPSTM PVTSTVQTPE LFKGTLKEYQ MKGLQWLVNC
YEQGLNGILA DEMGLGKTIQ AMAFLAHLAE EKNIWGPFLV VAPASVLNNW ADEISRFCPD
LKTLPYWGGL QERTILRKNI NPKRVMFFST WIISFDPWAV RQICICKRAC NVVRFQTLSD
MDAGFHILIT SYQLLVTDEK YFRRVKWQYM VLDEAQAIKS SSSIRWKTLL SFNCRNRLLL
TGTPIQNNMA ELWALLHFIM PMLFDNHDQF NEWFSKGIEN HAEHGGTLNE HQLNRLHAIL
KPFMLRRVKK DVVSELTTKT EVTVHCKLSS RQQAFYQAIK NKISLAELFD SNRGQFTDKK
VLNLMNIVIQ LRKVCNHPEL FERNEGSSYL YFGVTSNSLL PHPFGELEDV HYSGGQNPII
YKIPKLLHQE VLQNSETFCS SVGRGISRES FLKHFNIYSP EYILKSIFPS DSGVDQVVSG
SGAFGFSRLM DLSPSEVGYL ALCSVAERLL FSILRWERQF LDELVNSLME SKDGDLSDNN
IERVKTKAVT RMLLMPSKVE TNFQKRRLST GPTRPSFEAL VISHQDRFLS SIKLLHSAYT
YIPKARAPPV SIHCSDRNSA YRVTEELHQP WLKRLLIGFA RTSEANGPRK PNSFPHPLIQ
EIDSELPVVQ PALQLTHRIF GSCPPMQSFD PAKLLTDSGK LQTLDILLKR LRAGNHRVLL
FAQMTKMLNI LEDYMNYRKY KYLRLDGSST IMDRRDMVRD FQHRSDIFVF LLSTRAGGLG
INLTAADTVI FYESDWNPTL DLQAMDRAHR LGQTKDVTVY RLICKETVEE KILHRASQKN
TVQQLVMTGG HVQGDDFLGA ADVVSLLMDD AEAAQLEQKF RELPLQVKDR QKKKTKRIRI
DAEGDATLEE LEDVDRQDNG QEPLEEPEKP KSSNKKRRAA SNPKARAPQK AKEEANGEDT
PQRTKRVKRQ TKSINESLEP VFSASVTESN KGFDPSSSAN
//
