ID G5BM08_HETGA Unreviewed; 1553 AA.
AC G5BM08;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 ORFNames=GW7_18730 {ECO:0000313|EMBL:EHB10322.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB10322.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB10322.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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; JH170984; EHB10322.1; -; Genomic_DNA.
DR STRING; 10181.G5BM08; -.
DR eggNOG; KOG0388; Eukaryota.
DR InParanoid; G5BM08; -.
DR OMA; FWKKNER; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd18002; DEXQc_INO80; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR031047; DEXQc_INO80.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368001};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:EHB10322.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368001};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813}.
FT DOMAIN 282..407
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 532..703
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1105..1260
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 46..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1496..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..393
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 210..230
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1553 AA; 176500 MW; 479D56F3052368F4 CRC64;
MASELGAGDD GGCGELAKPL YLQYLERSLR LDHLLRQTSA IFNRSISSDD SEDGLDDNNP
LLPQSGDPLI QVQEEPPNSL LGETSGASNS GMLNPYSLNG VLQSESKSDK GNLYNFSKLK
KSRKWLKSIL LSDESSEADS QSEDNDEEGE ELNLSREELH NMLRLHKYKK LHQNKYNKDK
ELQQYQYYSA GLLSTYDPFY EQQRHLLGPR KKKFKEDKKL KAKLKKVKKK RRRDEELSSE
ESPRRHHHQT KVFAKFSHDA PPPGTKKKHL SIEQLNARRR KVWLSIVKKE LPKANKQKAS
ARNLFLTNSR KLAHQCMKEV RRAALQAQKN CKETLPRARR LTKEMLLYWK KYEKVEKEHR
KRAEKEALEQ RKLDEEMREA KRQQRKLNFL ITQTELYAHF MSRKRDMGHD GIQEEILRKL
EDSSTQRQID IGGGVVVNIA QEDYDSNHFK AQALKNAENA YHIHQARTRS FDEDAKESRA
AALRAANKSG TGFGESYSLA NPSIRAGEDI PQPTVFNGKL KGYQLKGMNW LANLYEQGIN
GILADEMGLG KTVQSIALLA HLAERENIWG PFLIISPAST LNNWHQEFTR FVPKFKVLPY
WGNPHDRKVI RRFWSQKTLY TQDAPFHVVI TSYQLVVQDV KYFQRVKWQY MVLDEAQALK
SSSSVRWKIL LQFQCRNRLL LTGTPIQNTM AELWALLHFI MPTLFDSHEE FNEWFSKDIE
SHAENKSAID ENQLSRLHMI LKPFMLRRIK KDVENELSDK IEILMYCQLT SRQKLLYQAL
KNKISIEDLL QSSMGSTQQA QNTTSSLMNL VMQFRKVCNH PELFERQETW SPFHISLKPY
EISKFIYRHG QIRVFNHSRD RWLRVLSPFA PDYIQQSLFH RKGINEESCF SFLRFIDVSP
AEMANLMLQG LLARWLALFL SLKASYRLHQ LRFWGEPEGE SQQRYLRNKD FLLGVNFPLS
FPNLCSCPLL KSLVFSSHCN AVSGYSDQVI HQRRSATSSL RCCLLTKLPS FLCVASPRVT
AVPLDSYCND RSAEYERRVL KEGGSLAAKQ CLLKGSPELA TDWQNRRFQF FPEHPGGLWS
IQPQNGWSFI RIPESLITDS GKLYALDVLL TRLKSQGHRV LIYSQMTRMI DLLEEYMVYK
KHTYMRLDGS SKISERRDMV ADFQNRNDIF VFLLSTRAGG LGINLTAADT VIFYDSDWNP
TVDQQAMDRA HRLGQTKQVT VYRLICKGTI EERILQRAKE KSEIQRMVIS GGNFKPDTLK
PKEVVSLLLD DEELEKKLRL RQEEKRQQEE TNRVKERKRK REKYAEKKKK EDELDGKRKK
EGVNLVIPFV PSADNSNLSA DGDDSFISVD SAMPSPFSEI SISSELHTGS IPPDESSSDM
LVIVDDPASS APQSRATNSP ASVTGSVSDT VNGISIQEMP AAGRGQSARS RGRPRGSGST
AKAAGKGRSR KSTAGSAAAM AGAKAGASAA AYAAYGYNVS KGISASSPLQ TSLVRPAGLA
DFGPSSASSP LSSPLSKGNN VPGTPKSLHM TSSLASDSLV RKQGKGINPS GGR
//
