ID E3Q5H9_COLGM Unreviewed; 1874 AA.
AC E3Q5H9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=GLRG_01090 {ECO:0000313|EMBL:EFQ25946.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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; GG697333; EFQ25946.1; -; Genomic_DNA.
DR RefSeq; XP_008089966.1; XM_008091775.1.
DR STRING; 645133.E3Q5H9; -.
DR EnsemblFungi; EFQ25946; EFQ25946; GLRG_01090.
DR GeneID; 24406455; -.
DR VEuPathDB; FungiDB:GLRG_01090; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_1_1; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0031011; C:Ino80 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
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:0034080; P:CENP-A containing chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0032006; P:regulation of TOR signaling; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin formation; 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 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:UP000008782}.
FT DOMAIN 778..903
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 1027..1199
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1600..1759
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1787..1874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 569..601
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 848..889
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 15..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1874 AA; 212358 MW; F5F4E1B09EA2C1C3 CRC64;
MDHPKDFRST VLQAPSRHGD RDRDRDDDRD RRRHRDIMNP TPGSTRHSGF SLRSPTQSEY
HHPQHSSYSS PKASAHSHQH HSPRSHQSGL SHPNPYSTSS SSAAAAAAAA TTGPLALGAS
GSGSGTGHHQ APPLSPLHPP SGYYPPPEAH QTREKPATSS YYDPLTDSTR ERRVSDAAWN
GNTAKGSPKT TRDPYGNYPQ SQQSEPASRE SHAYYKNGGA NAGYTSPSAA NFPPRSPRSH
SNSYSRSHQQ PTGSISPSNR ATPHMTSPSL RHAASPSVHA SSNGAPVTSL PLQGKPDPSP
LKAPASTPSR SADPMSFSNI LSNAEPISKP KSKSPPPVEE EERVAKVDSK PEHSEKPRSI
EPPIKTERSH REAEIELRPE PVKERVSTPL VRKERKERVP RKSKSRASDI RDTESTPKSS
RRASSKHDTP TPRVPSKRQA NGQPKQKTLS AEKEKKVTDL IAQLDADADD LTDSDLAAER
AQYQESGNKR RRLMQEKDSN RNVDRREDFV VVIGRRLGAL ADLGKRRYDD IYYEEAMNEV
RERELFAEKE RKKDMQRKRR REKSMAVTME QQKLALERAR LAEDETEKAK HLRDAERANK
KALQTKLILQ KGIKGPARNL VELNLDGGTM ATFQASDMEP GTKPKGKGRS GPRPKKSKEQ
KQAEKDAAEA AQAAIDAGEE LPIKEESKIR IKFSKKSKDK DKEKEKNKDK DLDEPDVEIE
GDVDVDVDED TMVEPTKEKK EKKGKKKDKE KKEDKPEEPP NKDAKFETKG FLQIYDQIWR
DLARKDVSKT YKMATESYQT KASNLKKTAI LASKEAKRWQ LRTNKGSKDQ QARAKRVMRD
MMGFWKRNER EERDLRKAAE KQEIENARKE EAEREAARQK RKLNFLISQT ELYSHFIGKK
IKTDEVERST DNPEIAAENR NEPTHKLDIE EPTGPLGAKV TDFDNLTFEE EDEETLRRAA
VANAQNAIAE AQRKARQFNE PSGPDMDEEG EMNFQNPAGM GDVAIEQPKL INAQLKEYQL
KGLNWLANLY EQGINGILAD EMGLGKTVQS ISVMAYLAEK YDIWGPFLVV APASTLHNWE
QEIRKFVPEF KILPYWGSAG DRKVLRKFWD RKHTTYKKDA SFHVCVTSYQ LVVSDVAYFQ
KMKWQYMILD EAQAIKSSQS SRWKSLLNFH CRNRLLLTGT PIQNNMQELW ALLHFIMPSL
FDSHDEFSEW FSKDIESHAQ SNTKLNEDQL KRLHMILKPF MLRRVKKHVQ KELGDKIEED
VYCDLTYRQR AIYSNLRNQI SIMDLIEKAT TGDNDDSGTL MNLVMQFRKV CNHPDLFERA
DTTSPFSFGY FAETASFVRE GNMVTVGYST RSLIEYELPR LVWREDGRLH KPGKDNLKAG
WRNKTLQHMM NIFTPEHIRA SMEGPDAFSF LRFADTSPAE VYKASHEDVF SRAVELSQKK
DRLSLMNIAY DEPEDMNFTP AHALFNIKDR NNRKPLADIT QEGVLANLMN VAREGYVDSG
LGRLEQAGRP RASAPPIEVS CCSRGTALET ESVLFNVGMR KSLFGPTMHE ERALVTEKIP
LGLFPPPKLL PAPDNEKKKF SNIAVPSMRR FVTDSGKLAT LDKLLTRLKA EGHRVLLYFQ
MTRMIDLMEE YLTYRNYKYC RLDGSTKLED RRDTVADFQT RPEIFIFLLS TRAGGLGINL
TSADTVIFYD SDWNPTIDSQ AMDRAHRLGQ TRQVTVYRLI TKGTIEERIR KRAMQKEEVQ
RVVIQGGGAS VDFSGRRAPE NRNRDIAMWL ADDEQAELIE QRERELLESG ELDKPQKKKA
TKRKRAVNED ISLDEMYHEG EGNFDDNRAG AAGTSGTATP VAETEVKGVK KRRTGGGKKA
KTLKQRLAVA DGQV
//
