ID B5VII0_YEAS6 Unreviewed; 934 AA.
AC B5VII0;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000256|RuleBase:RU368001};
DE EC=3.6.4.- {ECO:0000256|RuleBase:RU368001};
DE Flags: Fragment;
GN ORFNames=AWRI1631_71030 {ECO:0000313|EMBL:EDZ72255.1};
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ72255.1, ECO:0000313|Proteomes:UP000008988};
RN [1] {ECO:0000313|EMBL:EDZ72255.1, ECO:0000313|Proteomes:UP000008988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ72255.1,
RC ECO:0000313|Proteomes:UP000008988};
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
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|ARBA:ARBA00001836,
CC 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|RuleBase:RU368001}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDZ72255.1}.
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DR EMBL; ABSV01000851; EDZ72255.1; -; Genomic_DNA.
DR AlphaFoldDB; B5VII0; -.
DR Proteomes; UP000008988; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
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; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51413; DBINO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {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|RuleBase:RU368001};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU368001};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 476..601
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 718..890
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 137..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 550..587
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 138..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 934
FT /evidence="ECO:0000313|EMBL:EDZ72255.1"
SQ SEQUENCE 934 AA; 108806 MW; 0E5A6703297BEA15 CRC64;
MSLAVLLNKE DKDISDFSKT TAGKSAKKNS RERVADVAPT RVLDKKQAYL SQLNSEFNRI
KRRDSIEQLY QDWKFINLQE FELISEWNQQ SKDWQFDNTN DSQDLHFKKL YRDMSMINKE
WAEYQSFKNA NLSDIINEKD ADEDEEDDED ELEDGEEDME EDEASTGRHT NGKSMRGNGI
QKSRKKDAAA AAAIGKAIKD DQTHADTVVT VNGDENEDGN NGEDEDNDND NENNNDNDND
NENENDNDSD NDDEEENGEE DEEEEEIEDL DEEDFAAFEE QDDNDDEDFN PDVEKRRKRS
SSSSSSTKLS MNSLSLITSK KINKNITINS DRPKIVRELI KMCNKNKHQK IKKRRFTNCI
VTDYNPIDSK LNIKITLKQY HVKRLKKLIN DAKREREREE ALKNNVGLDG NDLDNDEDGS
ESHKRRKLNN NTANGADDAN KRKFNTRHGL PTYGMKMNAK EARAIQRHYD NTYTTIWKDM
ARKDSTKMSR LVQQIQSIRS TNFRKTSSLC AREAKKWQSK NFKQIKDFQT RARRGIREMS
NFWKKNEREE RDLKKKIEKE AMEQAKKEEE EKESKRQAKK LNFLLTQTEL YSHFIGRKIK
TNELEGNNVS SNDSESQKNI DISALAPNKN DFHAIDFDNE NDEQLRLRAA ENASNALAET
RAKAKQFDDH ANAHEEEEEE DELNFQNPTS LGEITIEQPK ILACTLKEYQ LKGLNWLANL
YDQGINGILA DEMGLGKTVQ SISVLAHLAE NHNIWGPFLV VTPASTLHNW VNEISKFLPQ
FKILPYWGNA NDRKVLRKFW DRKNLRYNKN APFHVMVTSY QMVVTDANYL QKMKWQYMIL
DEAQAIKSSQ SSRWKNLLSF HCRNRLLLTG TPIQNSMQEL WALLHFIMPS LFDSHDEFNE
WFSKDIESHA EANTKLNQQQ LRRLHMILKP FMLR
//
