ID M3YBK9_MUSPF Unreviewed; 1561 AA.
AC M3YBK9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
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|Ensembl:ENSMPUP00000008716.1,
GN ECO:0000313|RefSeq:XP_044923837.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000008716.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000008716.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_044923837.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_044923837.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; AEYP01028225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004751184.1; XM_004751127.2.
DR RefSeq; XP_044923837.1; XM_045067902.1.
DR STRING; 9669.ENSMPUP00000008716; -.
DR Ensembl; ENSMPUT00000008859.1; ENSMPUP00000008716.1; ENSMPUG00000008786.1.
DR KEGG; mpuf:101683934; -.
DR eggNOG; KOG0388; Eukaryota.
DR GeneTree; ENSGT00900000141110; -.
DR HOGENOM; CLU_000315_19_1_1; -.
DR OMA; FWKKNER; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031011; C:Ino80 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IEA:Ensembl.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IEA:Ensembl.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0051225; P:spindle assembly; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR GO; GO:0070914; P:UV-damage excision repair; IEA:Ensembl.
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; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368001};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715}.
FT DOMAIN 284..409
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 534..705
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1110..1265
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 48..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..395
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 137..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1561 AA; 177145 MW; 89EA8B2119D36AC6 CRC64;
MASELGAGDD GGCTELAKPL YLQYLERALR LDHFLRQTSA IFNRNISSDE SEDGLDDSNP
LLPQSGDPLI QVKEEPPNSL LGETSGAGNS GMLNAYSLNG VLQSESKSDK GNLYNFSKLK
KSRKWLKSIL LSDESSEADS QSEDNEEEEE EEELHLSREE LHNMLRLHKY KKLHQNKYSK
DKELQQYQYY SAGLLSTYDP FYEQQRHLLG PKKKKFKEEK KLKAKLKKVK KKRRRDEELS
SEESPRCHHH QTKVFAKFSH DAPPPGTKKK HLSIEQLNAR RRKVWLSIVK KELPKANKQK
ASARNLFLTN SRKLAHQCMK EVRRAALQAQ KNCKETLPRA RRLTKEMLLY WKKYEKVEKE
HRKRAEKEAL EQRKLDEEMR EAKRQQRKLN FLITQTELYA HFMSRKRDMG HDGIQEEILR
KLEDSSTQRQ IDIGGGVVVN ITQEDYDSNH FKAQALKNAE NAYHIHQART RSFDEDAKES
RAAALRAANK SGTGFGESYS LANPSIRAGE DIPQPTIFNG KLKGYQLKGM NWLANLYEQG
INGILADEMG LGKTVQSIAL LAHLAERENI WGPFLIISPA STLNNWHQEF TRFVPKFKVL
PYWGNPHDRK VIRRFWSQKT LYTQDAPFHV VITSYQLVVQ DVKYFQRVKW QYMVLDEAQA
LKSSSSVRWK ILLQFQCRNR LLLTGTPIQN TMAELWALLH FIMPTLFDSH EEFNEWFSKD
IESHAENKSA IDENQLSRLH MILKPFMLRR IKKDVENELS DKIEILMYCQ LTSRQKLLYQ
ALKNKISIED LLQSSMGSTQ QAQTTTSSLM NLVMQFRKVC NHPELFERQE TWSPFHISLK
PYHISKFIYR HGQIRVFNHS RDRWLRVLLS PFAPDYIQQS LFHRKGVNEE SCFSFLRFID
VSPAEMANLM LQGLLARWLA LFLSLKASYR LHQLRSWGEP EGESQQRYLR NKDFLLGVNF
PLSFPNLCSC PLLKSLVFSS HCKAVSGYSD QVIHQRRSAT SSLRCCLLTE LPSFLCVASP
RVTAVPLDSY CNDRSAEYER RVLKEGGSLA AKQCLLNGAP ELAADWLNRR SQFFPEPAGG
LWSIRPQNGW SFIRIPGKES LITDSGKLYA LDVLLTRLKS QGHRVLIYSQ MTRMIDLLEE
YMVYRKHTYM RLDGSSKISE RRDMVADFQN RNDIFVFLLS TRAGGLGINL TAADTVIFYD
SDWNPTVDQQ AMDRAHRLGQ TKQVTVYRLI CKGTIEERIL QRAKEKSEIQ RMVISGGNFK
PDTLKPKEVV SLLLDDEELE KKLRLRQEEK RQQEETNRVK ERKRKREKYA EKKKKEDELD
GKRRKEGVNL VIPFVPSADN SNLSADGDDS FISVDSAMPS PFSEISISSE LHTGSIPPDE
SSSDMLVIVD DPASSAPQSR ATNSPASITG SVSDTVNGIS IQEMPSAGRG HSARSRGRPK
GSGSTAKGAG KGRSRKSTAG SAAAMAGAKA GAAAASAAAY AAYGYNVSKG ISASSPLQTS
LVRPAGLADF GPSSASSPLS SPLSKGNNVP GTPKSLHLTS SLAPDSLVRK QGKGTNPSGG
R
//
