GenomeNet

Database: UniProt
Entry: A1C9W6
LinkDB: A1C9W6
Original site: A1C9W6 
ID   INO80_ASPCL             Reviewed;        1707 AA.
AC   A1C9W6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   11-DEC-2019, entry version 82.
DE   RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN   Name=ino80; ORFNames=ACLA_009570;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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-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. {ECO:0000305}.
DR   EMBL; DS027049; EAW12534.1; -; Genomic_DNA.
DR   RefSeq; XP_001273960.1; XM_001273959.1.
DR   STRING; 5057.CADACLAP00001450; -.
DR   PRIDE; A1C9W6; -.
DR   EnsemblFungi; EAW12534; EAW12534; ACLA_009570.
DR   GeneID; 4706087; -.
DR   KEGG; act:ACLA_009570; -.
DR   EuPathDB; FungiDB:ACLA_009570; -.
DR   HOGENOM; HOG000048482; -.
DR   KO; K11665; -.
DR   OMA; DDMYHEG; -.
DR   OrthoDB; 188211at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0031011; C:Ino80 complex; IEA:EnsemblFungi.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
DR   GO; GO:0042766; P:nucleosome mobilization; IEA:EnsemblFungi.
DR   GO; GO:0016584; P:nucleosome positioning; IEA:EnsemblFungi.
DR   GO; GO:0080040; P:positive regulation of cellular response to phosphate starvation; IEA:EnsemblFungi.
DR   GO; GO:0090053; P:positive regulation of chromatin silencing at centromere; IEA:EnsemblFungi.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0051983; P:regulation of chromosome segregation; IEA:EnsemblFungi.
DR   GO; GO:0060303; P:regulation of nucleosome density; IEA:EnsemblFungi.
DR   GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:EnsemblFungi.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:EnsemblFungi.
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; DNA damage; DNA repair; DNA-binding;
KW   Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1707
FT                   /note="Chromatin-remodeling ATPase INO80"
FT                   /id="PRO_0000350954"
FT   DOMAIN          593..718
FT                   /note="DBINO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT   DOMAIN          847..1019
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1423..1583
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         860..867
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COILED          395..478
FT                   /evidence="ECO:0000255"
FT   COILED          635..706
FT                   /evidence="ECO:0000255"
FT   MOTIF           970..973
FT                   /note="DEAQ box"
FT   COMPBIAS        5..263
FT                   /note="Pro-rich"
SQ   SEQUENCE   1707 AA;  191994 MW;  877FE262C23F9D8D CRC64;
     MTGGPPYNSQ SPTQQPRYPV YSPPSKTRPY YPNNDQYQQH PPQTPPAFPP QPPLARSPHY
     SHAPSPLPAT LPPLNGGAPP SHHQESSSQY QAHQSSGTPQ FPLPRPYSAS VLSSNGASPY
     NHPTPSHAHP SSGRLDSLSQ SPPKKDQESL YPIGGNVASG FSSSIMLSPP CILSDSIQKP
     ARAADPMSFA SILSGPTEER PLPRKQSPLP EPAPVQTPAP APPVLAPVPA ARKATPPPPT
     APVPVPAPLP EIKEPEPLPT PLPRLEKKPS AEKRRRNVDQ ESRASESLPV PPTNGVSEPA
     KVSRASNVRK TMSERDTEAI NKIIAEIDNA EKSDVESPGF EAEYERYIAK GKKRALDAEK
     AESIRRKRRR HDFLVKLGKT FEKQANAGMD RFRVANEASV IAEVQAKEIQ DEKERKKDMQ
     RKRRRENTVR LEMQKKIEAE RKANKANDAA EKAKFLREAE RAQRKIKSTK RALEGVTSPE
     EIGEVTPLAP NLEGGTTSSF HIGRSSPSRR KSGRSGGSSR PKKSKEQKQA EKDAAEAAYA
     AMENDEPLPL APKEDPRKES LKKEAKGARS KEPTPQPLSA FESKGYNQIY EQIWRDIARK
     DIPKVYRIKA LSLSTRQENL RKTAQLASKQ SRKWQERTNK SMKDTQARAK RTMREMMSFW
     KRNEREERDL RRLAEKQEIE SAKKAEAERE ANRQRRKLNF LISQTELYSH FIGRKIKGAE
     ADASGDAAVD GSDETVRPGK AGDHTIDLPS SVADLSTKVT NFEDLDFDAE DETALRQAAM
     ANAQNAVKEA QDRARAFNAE ENPMAALDEG ELNFQNPTSL GDIEISQPNM LTAKLKEYQL
     KGLNWLVNLY EQGINGILAD EMGLGKTIQS ISVMAYLAEV HNIWGPFLVI APASTLHNWQ
     QEITKFVPDI KVLPYWGSAK DRKVLRKFWD RKHITYTKES EFHVLVTSYQ LVVLDSQYFQ
     KVKWQYMILD EAQAIKSSQS SRWKNLLGFS CRNRLLLTGT PIQNNMQELW ALLHFIMPTL
     FDSHDEFSEW FSKDIESHAQ SNTKLNEDQL RRLHMILKPF MLRRVKKHVQ QELGDKVEKD
     VFCDLTYRQR AYYTNLRNRV SIMDLIEKAA VGDEADSTTL MNLVMQFRKV CNHPDLFERA
     ETKSPFSLAH FAETASFVRE GQNVDVRYST RNLIEYDLPR LLFSSSGRLD VAGPDNEKVG
     FQNKYLQHLM NIFTPENIKR SVEDDGAFSF LRFADTSINE AYEQSHLGVF ERAVRRRGQS
     DRLSQLGVIY DNEGDQTANS VLPHSLFNIV ERNDRQAVYD VAPEGYMRDL MTVSESSFER
     QGLNVIEPCA SPAASAPPIF ISCSGQTALR ETNDTFFSVP VRHALYSTPS RQLEEQILEK
     KLDPAPFSLP PMLPKPLSAK GRYTHIEVPS MRRFVTDSGK LAKLDELLRE LKAGGHRVLL
     YFQMTRMIDL MEEYLTYRNY KYCRLDGSTK LEDRRDTVAD FQQRPDIFVF LLSTRAGGLG
     INLTAADTVI FYDSDWNPTI DSQAMDRAHR LGQTRQVTVY RLITRGTIEE RIRKRALQKE
     EVQRVVISGG AAGGVDFNTR NRESRTKDIA MWLADDEQAE LIEQKEKEAL DRGEVFGAGK
     GGKKAALKRK KDLTLDDMYH EGEGNFDDIS AKPSGAATPV STADNIATPS STPVPKRGRG
     RGTVKGSSKR AKTTTERLRL IDGDGGL
//
DBGET integrated database retrieval system