INO80_PHANO
ID INO80_PHANO Reviewed; 1673 AA.
AC Q0UG82;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=INO80; ORFNames=SNOG_09232;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445338; EAT83424.2; -; Genomic_DNA.
DR RefSeq; XP_001799531.1; XM_001799479.1.
DR AlphaFoldDB; Q0UG82; -.
DR SMR; Q0UG82; -.
DR STRING; 13684.SNOT_09232; -.
DR EnsemblFungi; SNOT_09232; SNOT_09232; SNOG_09232.
DR GeneID; 5976432; -.
DR KEGG; pno:SNOG_09232; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_0_1; -.
DR InParanoid; Q0UG82; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000001055; 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; -; 2.
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; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1673
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350962"
FT DOMAIN 583..708
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 833..1005
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1403..1563
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..466
FT /evidence="ECO:0000255"
FT COILED 647..697
FT /evidence="ECO:0000255"
FT MOTIF 956..959
FT /note="DEAQ box"
FT COMPBIAS 20..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 846..853
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1673 AA; 188809 MW; 5E219042B5EED3A9 CRC64;
MFRDPVLRRS VDGEGETMQQ GDHQAHSPTQ TQGHQPRIHS ATNYPPHQQS RPPPSPSHTT
ELPPISTALH SRDTSASKYY DPTSDHGERG LARDTARYDP QHSPQTRETH TYSDARPAHS
PYEKPYQSPI ASSYAHQSPL QRPLSQHHHT GGMEAMSHSP VSPSVYHANR GAVQPPPANY
ARRPSMKDEA RENRPFPLQH HLLTVTQAPP PTRADPMSLS SIMSAGTDSD PPAKAQPPAS
LNHDHGHLSK PPNAHFVKQE PMASPAPADL APHDNGILHR APYDPIHPVA PSHALQSFAT
PRDLPAPDEA EIEAALAHIE TKQMNDLDGP GAPFEHEEWR ERSLKRGLDV ISGETVKRKK
RRHATLTRYH DVLAAHRDYA KHSYNLEHEG DAWQQVQSQE IAEEKERKKD MQRKRRREKT
IQNEEAKRAE ALAKAGQADN EEEKERHLAA AQKAERKAKN TSQLLQGNAP SKDIREVTPH
GPNLEGGTMS SFQASDDLGT GGKRKGNRGT GRLKKSKEQK QAEKDAAAAG QAAIDRGDDL
PSIAPREEAR LGSLRDRSYT EELGNGFVTS HDSSAYRNLY AQIIKDLARK DVPKVVRIKE
NSLSTKQSNL RKTAQLAAKE ARRWQMRTNK NQKDTQARAK RGMREMLAFW KRNERDERES
RKNAERQELE NAKKVEAERE ANRQKRKLNF LISQTELYSH FIGKKARTAE IERSTDDAET
AASAPAEAEK PGIDVDGMDG NPTAKVTNFE DLDFDNDDES ALNAAAMANA QHAIQEAQDR
ARAFNNPEGQ EDDGELNFQN PSGLQNKEDW IPQPKLLNCT LKEYQLKGLN WLVNLYEQGI
NGILADEMGL GKTVQSISVM AYLAERYNIW GPFLVIAPAS TLHNWQQEIA KFVPDLNVIP
YWGTAKDRKV LRKLWDRKHV TYTRDSPFHV VVSSYQLVVQ DAQYFQKMRW QYMILDEAQA
IKSSNSSRWK SLLNFHSRNR LLLTGTPIQN NMQELWALLH FIMPSLFDSH DEFSEWFSKD
IESHAQSNTK LNEDQLRRLH MILKPFMLRR VKKHVQKELG DKIELDVYCD LTYRQRAYYA
NLRNKISIMD LIEKAVGDEQ DSATLMNLVM QFRKVCNHPD LFERADTWSP FTFASFAETP
SFLREGQNVR VAYTTRNFIE YSLPRLIGRN GGRLEIAGPD NEKAGFRGHY LDNLFNIWSP
HNMEQSAREA DAHSWLRFSD LSATEVSKIA KSDLFERALE TGSSPNKLGQ YETLYDDEND
KYEPKHSMLR IIDRKDRAPL TDLTSEGYMR NLMNVSQSAF ERTGLDVIEP CAKPAAAAPP
VELYCASQDV IAEKQRVFFN PAIRNALYGV SDKTEQVLLD TKSHSTALVR NTLPSPTNAR
TRYTHIEAPS MSRFVTDSGK LARLDALLKG LKAGDHRVLL YFQMTRMIDL MEEYLTYRNY
KYCRLDGSTK LEDRRDTVAD FQSDPTIFVF LLSTRAGGLG INLTSADTVI FYDSDWNPTI
DSQAMDRAHR LGQTRQVTVY RLITSGTIEE RIRKRALQKE EVQRVVISGG AGGAVDFNTR
SRENRTKDMA MWLVDDEQAA EIEKKEAELA EAEKNAPPGK KRSKKKRVEA NLDDMYHEGE
GHFDESAKGS GAATPVPGTE GAPGAPGGKK GKKGLSKKAK TAKQRLAVAD GEV
