ID H6BZZ1_EXODN Unreviewed; 1690 AA.
AC H6BZZ1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=HMPREF1120_05188 {ECO:0000313|EMBL:EHY57140.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY57140.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY57140.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY57140.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) 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}.
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DR EMBL; JH226133; EHY57140.1; -; Genomic_DNA.
DR RefSeq; XP_009157601.1; XM_009159353.1.
DR STRING; 858893.H6BZZ1; -.
DR GeneID; 20309827; -.
DR VEuPathDB; FungiDB:HMPREF1120_05188; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_0_1; -.
DR InParanoid; H6BZZ1; -.
DR OMA; NLLGFHC; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000007304; 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; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT DOMAIN 576..701
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 833..1005
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1406..1566
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 646..687
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1690 AA; 190281 MW; 9A5D65020B538B4F CRC64;
MSGSTPFATR SPTQSKQYPP YSPTHPNRPY YGHEPFQIPP QHLIQTPPPF PPASLVQSPH
HHRPPTLASP LPAPNTLPPP SVGTGPQYPP LASSPSFPLQ GTYSRHLASA SNPSPNMPAQ
YDGTPTHAHP SGPSPSSLPS PMRDQHILPN GRSTEGAFQE SRPHSKDKPD RASNPMSFAS
ILGPSHHEPT SKVADGKPSR PATPPPAKSV LESKPVPEEP LVAKLPDLGQ PRHVLNGEAK
LQSRADSLHF QRKIVAPSKP RTILTEREAE KILKALSSIE EGPLSDVEDG GLLEQKGRYK
QRSRKRAADV AESELHKRKR RRQFIIDSLI APFESQAQSA AERFRERYEP IAAKEIADKD
IRTEKERKKD MQRKRRREQL LRTETQKMEE FEQLARAAED QEEAQKYLKQ AEKSQARIRQ
TAELLEGGSA QEDMEVAAPA PNYEGGVTSS FQIGSPEPPE PPKKRTKREG AASTRPKKSK
EKKQAEKDAA EAAYAAMERD ALVQIAPKEE TKKETTAKGK KAQAKAEAAA AAAAAASAAA
AAGADAGETP DAAAPTTAGH TINYESKGYN QIYEQIWRDM ARKDIAKVYR IKQVSLNTRQ
ENLRKTAILA SKQARKWQER TNKSMKDTQA RAKRVMREMM SFWKRNEREE RDLRRMAERK
EIEDAKKAEA DREANRQKRK LNFLISQTEI YSHFIGRKIK TDEIERATND PEVAAAAEKE
RPAGDSAQAK GMDDMSLSDE HGNHKVTNFE DLDFDAEDES ELRKAAMANA ASALQDAQDK
ARNFNGDDPM SAFDSSEMNF QNPTMAGDVQ VSQPRMLQAQ LKEYQLKGLN WLVNLYEQGI
NGILADEMGL GKTVQSISVM GYLAEQHNIW GPFLVIAPAS TLHNWQQEIT KFVPAIKVLP
YWGNAKDRKI LRKFWDRKHI TYNKDSEFHV LVTSYQLVVQ DAQYFQKIRW QYMILDEAQA
IKSSSSSRWK TLLAFQCRNR LLLTGTPIQN NMQELWALLH FIMPTLFDSH DEFSDWFSKD
IESHAQSNTK LNQDQLKRLH MILKPFMLRR VKAHVQKELG DKVEKDVFCD LTYRQRAYYA
NLRSKISIMD LIEKATLGDD QDTATLMNLV MQFRKVCNHP DLFERADTTS PFSMSTFAET
ASFLREGYFV QVGYSVRNPI QYDLPRVLCN DVGRLDIAGP NNPKAGFRRA GFKKDKLSGL
MRIWTQEHIK SSAENHGAFS FLRFVDTSVQ EASSIGSSGL FERAIKLRKQ HRRILPIEDD
SEPEAPAHAM FNIVDNSPRK ALAELDPNSN LAKLCNISKE GLSSQGYSIL EPAARPKASA
PPIEVSCFDQ SSLTERQLTM FNMDVRSCLF PLEESMEVKL LQQDVDPENF PLSDMLPKPE
NQKARYTHIS IPSMRRFVTD SGKLAKLDQL LRELKNGGHR VLLYFQMTRM IDLMEEYLTY
RNYKYCRLDG STKLEDRRDT VHDFQTRPEI FIFLLSTRAG GLGINLTSAD TVIFYDSDWN
PTIDSQAMDR AHRLGQTKQV TVYRLITRGT IEERIRKRAM QKEEVQRVVI TGGDGAGVDF
NTRDRRENRT KDIAMWLADD DQAALIEQKE KEIADKPEEE TKKKSKKALA AAARKKKGEM
SLDDMYHEGE GHFEDASAKP SGAATPVSTV ETPGPKRGPR GGKGISKKAK TAKQRLAIVD
AEGDLGMGGM
//
