ID A0A094C9A7_9PEZI Unreviewed; 1703 AA.
AC A0A094C9A7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=V494_01682 {ECO:0000313|EMBL:KFY44035.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY44035.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY44035.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY44035.1}.
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DR EMBL; JPJW01000553; KFY44035.1; -; Genomic_DNA.
DR STRING; 1420907.A0A094C9A7; -.
DR HOGENOM; CLU_000315_26_1_1; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000029288; 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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368001};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000029288}.
FT DOMAIN 610..735
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 858..1030
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1422..1582
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 682..721
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1703 AA; 191430 MW; 0D6CD5CEAE56E407 CRC64;
MDSSFHSTVM QRPQDEEDER LRRERLNHVA NQNSPLPLYA GQSPTQAVYN GPSSSYSPTK
SLPRRPSFTK QYHHPPPTPS SQLPPPPPPG SAHRAPSEAS PLIPSATPYQ SSEYHSAPRD
KPTSSYYDPT SDSGEPRPAD PTRHNGQNPA PQNNRDSYTW SQTGTESRNY RNGAFTSPVN
ATFPGPQSPG TSHSHPPSQL GSTAQSPSVT AAMETPVARQ NNGVAPVLPA EPTMASPSKP
TRTTDPMSFS SILTESAPAA PTPTMPSSPP PAKVPRKSSR ASIPPPPPAD ETPIKEESRR
AAPLHATTPV SSSRVPAKRQ ANGSLKGKKS AAEHDEEIQA ILAEIDANAS DLETSEFEDE
MWLFKARCLK RRVELDEGEE RRRKIRRRKY VDDMTSKLMK HAETGEKRYR EIHGEEAIAS
VQEKEILAEK ERKKDMQRKR RREKTVATNL EQKEALLKKA QQTADDNERK KLLKEAERAE
KKAQHTKIIL ARGDKGPEIR TVSPIEPNFS GGTMTTFAAE PETFTGKGKG KGRGGARLRK
SKEQKQAEKD SAVAAQAAID AGEEPAPPPP SEPKIRLKLG PKSKEEPREE SPAVIEPFVS
KTYNQIYDQI WKDIAKKDIT KVSKIVTDSQ SVKASNLKKT AILASKEAKR WQMRTNKGTK
DLQARAKRVM REMMSFWKRN EREERDLRRQ AEKQEIENAK KAEADREANR QKRKLNFLIS
QTELYSHFIG KKIKTDEVER STDHPDVAVV KDAEGHTHKI DVPDSGTAAG KVTNFEDLDF
DAEDESALTA AAMANAQNAI QEAQNKARAF NNPEPAMDEE GELNFQNPAG MGDVDIEQPK
MLHAQLKEYQ LKGLNWLVNL YEQGINGILA DEMGLGKTIQ SISVMAYLAE KHGIWGPFLV
VAPASTLHNW QQEITKFVPK LKVLPYWGTA ADRKVLRKFW DRKHITYTED APFHVLITSY
QLVVSDVAYF QKMRWQYMIL DEAQAIKSSQ SSRWKSLLGF HCRNRLLLTG TPIQNNMQEL
WALLHFIMPS LFDSHDEFSE WFSKDIESHA QSNTKLNEDQ LKRLHMILKP FMLRRVKKHV
QKELGDKIEL DIFCDLTYRQ RAYYSNLRNQ ISIMDLIEKA TVGDDGDAGT LMNLVMQFRK
VCNHPDLFER AETTSPFSFG FFAETGSFMR EGPLINVVYS TRNLIEYPLP RLIWRNGGRL
DMPGSDNEKA GFRQKWIDNE LNIWKPTNTI QSEAFSWARL AGCSSNELTL ATDDLFVRAV
DLAKKRDNLG RANVIYDENE FTPVESMLRI VDRNDRKPLA EVTEGYIGKL LNVSKDVFAN
SGMPRMEQCG RPAASAPPIQ VSCSSRGAVI ETENTLFNAP MRKALFGPSS RDETSLVESK
APLELFPEPQ MLPAPSSEKQ RFTNILVPSM SRFVTDSGKL AKLDSLLFKL KEGGHRVLLY
FQMTRMIDLM EEYLTYRNYK YLRLDGSTKL EDRRDTVHDF QTRPEIFIFL LSTRAGGLGI
NLTSADTVIF YDSDWNPTID SQAMDRAHRL GQTRQVTVYR MITRGTIEER IRKRALQKEE
VQRVVISGGA GGGVDFNTRS RENKAKDIAM WLADDDQAAE IERKERELAA MEAAEVGKPK
KKAGRKKKVE ERSLEELYHE GEGHFDDGSA KPSGTATPIE GGPAAKKAKV DKKKAGGKKA
KTAKQRLAMA DGDVDADMDD MEM
//
