GenomeNet

Database: UniProt
Entry: Q1DUF9
LinkDB: Q1DUF9
Original site: Q1DUF9 
ID   INO80_COCIM             Reviewed;        1662 AA.
AC   Q1DUF9; J3K7T6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   31-JUL-2019, entry version 89.
DE   RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN   Name=INO80; ORFNames=CIMG_06054;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J.,
RA   Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E.,
RA   Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M.,
RA   Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J.,
RA   Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens
RT   Coccidioides and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- FUNCTION: ATPase component of the INO80 complex which remodels
CC       chromatin by shifting nucleosomes and is involved in DNA repair.
CC       {ECO:0000255|PROSITE-ProRule:PRU00746}.
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:0000250|UniProtKB:P53115};
CC   -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex.
CC       {ECO:0000255|PROSITE-ProRule:PRU00746}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00746}.
CC   -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC       {ECO:0000250|UniProtKB:Q9ULG1}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
DR   EMBL; GG704912; EAS30575.3; -; Genomic_DNA.
DR   RefSeq; XP_001242158.1; XM_001242157.2.
DR   SMR; Q1DUF9; -.
DR   PRIDE; Q1DUF9; -.
DR   EnsemblFungi; EAS30575; EAS30575; CIMG_06054.
DR   GeneID; 4561120; -.
DR   KEGG; cim:CIMG_06054; -.
DR   EuPathDB; FungiDB:CIMG_06054; -.
DR   eggNOG; KOG0388; Eukaryota.
DR   eggNOG; ENOG410XP0A; LUCA.
DR   InParanoid; Q1DUF9; -.
DR   KO; K11665; -.
DR   OMA; DDMYHEG; -.
DR   OrthoDB; 188211at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR020838; DBINO.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR031047; Ino80.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45685:SF2; PTHR45685:SF2; 1.
DR   Pfam; PF13892; DBINO; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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   Activator; ATP-binding; Coiled coil; Complete proteome; DNA damage;
KW   DNA repair; DNA-binding; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN         1   1662       Chromatin-remodeling ATPase INO80.
FT                                /FTId=PRO_0000350958.
FT   DOMAIN      558    683       DBINO. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00746}.
FT   DOMAIN      808    980       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1384   1544       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     821    828       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED      356    439       {ECO:0000255}.
FT   COILED      581    671       {ECO:0000255}.
FT   MOTIF       931    934       DEAQ box.
FT   COMPBIAS      5    225       Pro-rich.
FT   COMPBIAS   1635   1642       Poly-Gly.
SQ   SEQUENCE   1662 AA;  187850 MW;  397D69D7F19956C0 CRC64;
     MAGVPPYGMH SPTQQPRYPS YSPSTRDRQP YSGNDPYQHP PRTPPSFAPP SSLSRSPHFA
     RPPSPMNTTL PPLNGTVVNA DGSPPYHGHS GSATSGYTLP RPFGGSLMSA TSHSPPPSYS
     HASGSHSHPS NIPDSFSQSP KRESEPYDVR SDRTGPVSQT PARPASPKES KSARSNPMSF
     ANILSGPADE PPPRRSSPPP QTYKSSTLPP IAPTPKVDKE PLSEPEKRRG SSHYETAYNE
     MPHRPAMNGF TPAKSPLAAM PSPLSKSRKL VDEEEIDKIS RENIARALEQ IDALDNSDVE
     APGFEQEWER YMAKSRKRAR ELDAIEGRKR KRRRTEFLGK LAKMFEKQAL QGIERFNRIH
     EAEVQMEVQQ KEIQEEKERK KDMQRKRRRE NTVRHEMEKL NAAQKKANKI EDEAEKQKLA
     KEIARSKKKI KDTTLALERG EASQEISEVN PLAPNLEGGT TSSFHIRTKS PPPPKKRAAK
     GTSSRPRKSK EKKQAEKDAA EAAYAAMENE DLVPLAPKED PRKTSLKKES KAARSKEPSP
     VPATPYDSKG YNQFYEQLWR DIARKDIPKV YRIKVVSLST RQENLRKTAQ LAAKQARKWQ
     EKTNRSMKDT QARAKRTMRE MMTFWRRNER EERDMRRLAQ RQELELAKKA EADREANRQR
     RKLNFLISQT ELYSHFIGRK IKTDKAQDSG DATTTAAIEG NGEGKVPDSL VPLPDGGAKV
     TSFDDLDFDA EDETALRQAA MANAQSAVQE AQDRARAFNG EENKMADFDE GEMNFQNPTS
     LGDVEVSQPK MLTCQLKEYQ LKGLNWLVNL YEQGINGILA DEMGLGKTVQ SISVMAYLAE
     VHDIWGPFLV VAPSSTLHNW QQEIVKFVPD LKVLPYWGSA KDRKVLRKFW DRRNITYRKQ
     SEFHVLVTSY QLVVGDAQYF QKIKWQYMIL DEAQAIKSSQ SSRWKSLLGM HCRNRLLLTG
     TPIQNNMQEL WALLHFIMPT LFDSHDEFSE WFSKDIESHA QSNTKLNEDQ LKRLHMILKP
     FMLRRIKKHV QKELGDKVEK DVFCDLTYRQ RAYYTSLRNR VSIMDLIEKA AIGDDTDSTT
     LMNLVMQFRK VCNHPDLFER AETTSPFSVC YFAETASFVR EGPFVDVGYS TRNLVEYDLP
     RLLCSPEGRL DVAGPGNNKA GFEGRYLSHL MNIWTPENIR ESMSHNDAFS WLRFADTSVG
     EAYEVSHKGV FERAVRRRDY STRLSLLDVA YDAEDGVNIN SVHVHSLFNI VERNDRRALA
     DITATGYMRE LLNVASNVAE RGGIRTIEPC AKPGASAPPI TISCSGQAAI AEARATFFNT
     AVRHALFAAP TKAMEEEILS NKLDPAPYSL RPLLPQPGSM KGRYTNITVP SMRRFVTDSG
     KLAKLDELLR ELKNGGHRVL LYFQMTRMID LMEEYLTYRN YKYCRLDGST KLEDRRDTVS
     DFQQRPEIFV FLLSTRAGGL GINLTAADTV IFYDSDWNPT IDSQAMDRAH RLGQTKQVTV
     YRLITRGTIE ERIRKRALQK EEVQRVVISG GAAGGVDFNA RSRENRTKDI AMWLADDEQA
     EILEQKEKEA LEKGEELGAK KGRKAAGKRK RDITLDDMYH EGEGHFEDNS TKPSGAATPV
     SGDVSGVPGV KGRRGRGGGG VGRSKKAKTM KERLRLVDGE VD
//
DBGET integrated database retrieval system