INO80_SCLS1
ID INO80_SCLS1 Reviewed; 1707 AA.
AC A7EQA8;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=INO80; ORFNames=SS1G_07509;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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}.
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DR EMBL; CH476629; EDO05024.1; -; Genomic_DNA.
DR RefSeq; XP_001592061.1; XM_001592011.1.
DR AlphaFoldDB; A7EQA8; -.
DR SMR; A7EQA8; -.
DR STRING; 665079.A7EQA8; -.
DR EnsemblFungi; EDO05024; EDO05024; SS1G_07509.
DR GeneID; 5488199; -.
DR KEGG; ssl:SS1G_07509; -.
DR VEuPathDB; FungiDB:sscle_06g048760; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_0_1; -.
DR InParanoid; A7EQA8; -.
DR OMA; DDMYHEG; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
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:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0035065; P:regulation of histone acetylation; IEA:EnsemblFungi.
DR GO; GO:0032006; P:regulation of TOR signaling; IEA:EnsemblFungi.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; 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 Gene3D; 3.40.50.300; -; 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-rel_dom; 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; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1707
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350964"
FT DOMAIN 603..728
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 853..1025
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1426..1586
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1610..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 369..470
FT /evidence="ECO:0000255"
FT MOTIF 976..979
FT /note="DEAQ box"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1610..1625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 866..873
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1707 AA; 192466 MW; 39AC24CB0CC3F5F9 CRC64;
MSTSSSNIPY DVGSPRQQSQ TEIRSILNPS TTSTGAHPSF NQYHPPTAAP PLIPSHIPLQ
STTPSTLGLS LGTPLYQSER DIGYPRDQKP TSNYYDPTSD SSERRPATAE SKWSDREAKT
SQRRDSYPYQ QNQPPAPSTD GPMNLYNGGY KSPVNSHFPP GSPISHAHPQ GRVPPLVTQS
PRMPAMESPI SRHNGLGGGP ELQDKPVIKQ EPVPASTPSR PVDPMAFSSI LSSAAPEPTP
KPQPTPTPIV SKPRKASRQP IPTLKPEPSS APSSRQSSVA PAPQPPTSRV PAKRKANGET
KPTPKPKPFT KDQERDIVIL MSKLDGEPED SDVEFAEEKR LYQTRSLKRK LEVEKIETSK
TKQRRTDFTN KMAKRLEKHA KAGEERYREV EGDAAISKVQ ADEIQTEKER KKDMQRKRRR
EKTVQNNMEQ KEIALAKAQA AQDDQERHKF LRDAQRAEKK AQQTKQILAR GDKGPEIRAV
SPMEPNMQGG SMSTFTAVDP DSTKKPKRGG ARPRKSKEQK QAEKDSAAAA QEAIDKGESP
ALMPIRDAAE FKDMKPLPSK EGVTKIKLKF KAPAEPVEVK EESPSAPVDQ HNTKMYHVVY
DQIWKDLARK EVPKVFKLAV DSYSIRASNL KKTAILASKE AKRWQLRTNK GTKDLQARAK
RVMREMMSFW KRNEREERDT RRAAEKQEIE NAKKAEADRE ANRQKRKLNF LISQTELYSH
FIGKKIKTDE VERSTDHPDV AVPDKADHAK PDHGDLPEGT APAKVTNFED LDFDAEDESV
LKAAAMANAQ NAIQEAQNKA RAFNKKDDAP AMDDEGEMNF QNPAGMGDVD IEQPKMLQAQ
LKEYQLKGLN WLVNLYEQGI NGILADEMGL GKTVQSISVM AYLAEKHGIW GPFLVVAPAS
TLHNWQQEIT KFVPRLKVLP YWGTAADRKV LRKFWDRKHI TYTEDAPFHV LVTSYQLVVS
DVAYFQKMKW QYMILDEAQA IKSSQSSRWK SLLGFHCRNR LLLTGTPIQN NMQELWALLH
FIMPSLFDSH DEFSEWFSKD IESHAQSNTK LNEDQLKRLH MILKPFMLRR VKKHVQKELG
DKIEEDIFCD LTYRQRAYYS NLRNQISIMD LIEKATIGDD NDTGTLMNLV MQFRKVCNHP
DLFERAETTS PLSFSYFAEA GSFLREGSNV TVAYSARNMI EYSLPRLIWR EGGRLDLPGH
DNEHAGVKAK CLESLFNVWK PENIVDSAKE DGAFSWLRFT NTSVQELSTA SRKDVFARAV
DLVKRPQTLG RLNIVYDEEE DKNYTPVHSM LQIVNRKDRK PLAEVTNEGY LNKLFNVAKD
VWGQSGMSRM EQCGRPSATA PPIEVTCSSR GAVIERQKIL FNVPMRRALF GPSPVEEKAL
ITSKVSPLFY PPKPMLPLPT SEKQRFTNIK VPSMRRFVTD SGKLAKLDSL LTKLKEGGHR
VLLYFQMTRM IDLMEEYLTY RNYKYLRLDG STKLEDRRDT VHDFQTRPEI FIFLLSTRAG
GLGINLTSAD TVIFYDSDWN PTIDSQAMDR AHRLGQTRQV TVYRMITRGT IEERIRKRAL
QKEEVQKVVM TGGAGGGVDF NTRSKENRTK DIAMWLVDDE EAAEIERKEA EQLRYEAENP
TASKKGKGKG KKGKEGGGGS LEDLYHEGEG HFDDGSNRPS GTATPIAVDA SKKKGSSSRK
SGGGGRSKKA KTAKERLAMA DGDVDMA
