ID A0A397IUT5_9GLOM Unreviewed; 1670 AA.
AC A0A397IUT5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=Glove_156g94 {ECO:0000313|EMBL:RHZ78787.1};
OS Diversispora epigaea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ78787.1, ECO:0000313|Proteomes:UP000266861};
RN [1] {ECO:0000313|EMBL:RHZ78787.1, ECO:0000313|Proteomes:UP000266861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT104 {ECO:0000313|EMBL:RHZ78787.1,
RC ECO:0000313|Proteomes:UP000266861};
RA Sun X., Fei Z., Harrison M.;
RT "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RHZ78787.1}.
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DR EMBL; PQFF01000147; RHZ78787.1; -; Genomic_DNA.
DR STRING; 1348612.A0A397IUT5; -.
DR Proteomes; UP000266861; 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 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 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:UP000266861}.
FT DOMAIN 557..682
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 825..997
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1393..1553
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 626..665
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1670 AA; 190170 MW; A606CF11BFE5F48A CRC64;
MSSSYNYRDR AQSSRSYSSE NPSQRPPPPS NRTSSFNLNH LLNSDDQPLS HTSGHYSLPP
LTSSPYSQST LSFSSYASQT SSPHYGHSHN DFSTSPSLSH THPIPPSIPP IQQLPYNGSS
WDYSESASRQ LPNNSYKLDH APSVPTTSST LTFFHSNINQ NNINQSISQD QSNTTHHIHE
SKSNVLSQEP LFRPPPVMSI SGLLSRDTND DTEYSFSKLQ KDSNNSGAYD EEIFDARSNV
AQVQTTTDSA EEKESAASIS EGSLHASDRS NEGESTGDDP NSPSMIIPPP TRKIPIPEPV
NAGNGLVVKL KTNDNHPPSV SNQESQEPEK TSTSRKNNKT PTAPSTVASP LTATSSKNTR
KRTSKKFQVS PKPPSRVPKS KKSSRLDVSE VEHQVANESS TSSDSSDYII TREEKTKHRQ
PEDSSDSSSS DSSSSGSELD ERFNKELVNY MIEIYKRQKR VVDEFNKKCE TKKEIVRRKF
ASRLVRIGVK GHISEKDAIE TEGSRQKGRR TNKKESKRVN RKSDRLAGND ENEKRVVLAT
KLQKQQEAYE MEERRRIWKD IVRNAIPKMN KIVNQSITSR ANNCRKIAVL CQKEARKAAC
KSCKSPKDIQ TRSRQAMRQM LCFWKRNEKE ERELRKKAER EALERMRVEE EMREAKRQAR
KLNFLITQTE LYSHFVGKKI GTQAAEGNST QTYVSTSGRT AMDQGADSSP AELNTDEDNN
NLILPQSFKD IDFDEEDEEA LREKARASAQ NALAQVKQHT RDFDAERKIA AGGKSIDAGA
SNEYLDQMNF QNPSSMPSMS EIKQPSILVN VTLKDYQLKG LNWLANLYEQ GINGILADEM
GLGKTVQSIS LMAHLAETHS IWGPFLVIAP ASTLHNWQKE ISEFLPSLRI LPYWGTPKDR
VVLRKSLNKK NLIFNKDAPF HVVITSYQLI VQDQSYFARL KWQYMILDEA QAIKSSTSAR
WKTLLGFHCR NRLLLTGTPI QNSMQELWAL LHFIMPTLFD SHQEFSEWFS KDIESHAENK
GSLNEHQLKR LHMILKPFML RRVKKNVQNE LGEKIEKEIF CLLTARQRVL YRGLREKISV
AELLEKAATL PDNDNVDSLM NLVMQFRKVC NHPELFERAD VVSPLSFCFY GSTWLISREE
SLYLPYSSRN YITYEIPKRV FRNGGFLDVP GHSSRAGSRS KILDHLMNIW RPDYIYQSLQ
DEQNDTFAFL KFLDTSPSEA SKIFFGNLIQ RWILHLLQRK YRLRKFYMRH DARSFRDTMF
LINEMVSKLI GSSPTLNVLT NIFENKTQYE LVVLDSCYMP KAIAPPIQPV CLDKGFYNDQ
ERLLFDPFVR AALSGIIELV PQNERAQSTV GRLLVQSRDK GIIGETYRKD RGFSYIRVPP
LKKLVLDSGK LTKLDELLKE LKAGGHRVLI YFQMTRMIDL MEEYLAYRQY KYLRLDGSSK
IHDRRDMVED WQTRSDIFVF LLSTRAGGLG INLTAADTVI FYDSDWNPTV DQQAMDRAHR
LGQTKQVTVY RLITKGTIEE RILQRAKQKD EIQKVVISGG EFKQVDFKSR EIMSLLLEDD
ELEAKFKEQH LKRKADEEEN KKKGRNNKRR KKDSNGSSSK SLEDLWHEGE PAMVETEGSG
VTTPASSVGG TKRKRTNRAT STRTTAKGRA KPRTSGRTGG GGKTRTSTPI
//
