ID U5H0C5_USTV1 Unreviewed; 2312 AA.
AC U5H0C5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=MVLG_00860 {ECO:0000313|EMBL:KDE09147.1};
OS Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE09147.1};
RN [1] {ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KDE09147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE09147.1};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KDE09147.1, ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200}, and P1A1
RC Lamole {ECO:0000313|EMBL:KDE09147.1};
RX PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA Hood M.E., Schultz D.J., Cuomo C.A.;
RT "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT fungus.";
RL BMC Genomics 16:461-461(2015).
RN [4] {ECO:0000313|EnsemblFungi:MVLG_00860T0}
RP IDENTIFICATION.
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, 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 DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
CC -!- SIMILARITY: Belongs to the EMC6 family.
CC {ECO:0000256|ARBA:ARBA00009436}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025, ECO:0000256|RuleBase:RU368001}.
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DR EMBL; AEIJ01000075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL541646; KDE09147.1; -; Genomic_DNA.
DR STRING; 683840.U5H0C5; -.
DR EnsemblFungi; MVLG_00860T0; MVLG_00860T0; MVLG_00860.
DR HOGENOM; CLU_000315_20_4_1; -.
DR InParanoid; U5H0C5; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000017200; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031011; C:Ino80 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd18002; DEXQc_INO80; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR031047; DEXQc_INO80.
DR InterPro; IPR029008; EMC6-like.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45685:SF2; CHROMATIN-REMODELING ATPASE INO80; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF13892; DBINO; 1.
DR Pfam; PF07019; EMC6; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368001};
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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368001};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000017200};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT TRANSMEM 2245..2264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2285..2308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 413..537
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 670..842
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1247..1398
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1906..1936
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1994..2024
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2027..2063
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2064..2091
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2092..2121
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2122..2151
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2152..2179
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1876..1903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1503..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1880..1901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2312 AA; 255574 MW; 5CA3039F1FE8ED78 CRC64;
MSLSRLLNNN PSGSSSAAMN GVSAHAPAAV ASGSASTEST TRKRSRASRA SVSFHDDLDG
DEEGSSARRS SRRSIQPKRY IDDIYADIED VADTSFDLNS SRNGAEAVAP PEADEDSDSD
SETLLRATAH IWREPLQAYL DRIHAERQQL EQDWIANEAS RHFATAARIA SFTERRIDEM
RARKEAKLLE REQELQAAAR LAEQERQRIE FEAERNAIKE REKEDRLRKQ REAAKRKRDE
DREKKGKAEE ARKIRSEKDR EARRLEFERW EALTPEQRAE EEKLYGERFK FDRDEMLNRF
DLDQYGKGAR KKKRLENDDP SGLGYEDGDL EEDVDELAEG AHGSSRGANG ASSHDMLRQS
SSHLMHSPTS SRAGSNAPGY ASDDVDHESA RDLNSSPVKA KKTRSAEELE RKLWIHIAKR
DIPKVSKIQQ QSSQSRQFFA KRVGSIVARE ARRAATRTKT VKDVQVRAKR VVREMMLFMK
GNEKRERESR KKAEKEALDK AKKEEEMREA KRQARKLNFL ITQTELYSHF IGNKIKTSEA
EESEDTASDA KIAAPAESNP SVIAALAKPA ASNGALKDLN FDVDDEANVA EHARRGAQAA
VDAAKNAASA FDAAAGQAKP ANGAEGLSFD DSDDLNFQNP TMTGAAIVTQ PRILTCTLKE
YQLKGLNWLA NLYEQGINGI LADEMGLGKT VQSISLMAYL AEVHDIWGPF LVIAPASTLH
NWQQEITRFV PALKALPYWG NTKDRAILRK FWNRKSLRYD KDAPFHILVT SYQLVVQDEQ
YFRGVKWQYM VLDEAQAIKS SSSTRWKTLL SFKCRNRLLL TGTPIQNSMH ELWALLHFIM
PSLFDSHDEF SEWFSKDIEG NAENKGAMNE HQLRRLHMIL KPFMLRRIKK NVQNELGDKI
EIDVYCDLTP RQKAMYRTLR EHISITDLVS RATSLNDDDS VKRLMNLIMQ FRKVCNHPEL
FERADVTAPF AFANFPVTSN LVRDPEMLEV AYATRSVIEY AIPKLLYRDG GLLNVPGQNS
RAGSDSLHLD RLLNIWSPDY IQHSLRQGES TFAFAQSLGF SPSELSKVAL AHDVIRIGLA
LENEATKSVR GDYDAISLEG EAPAPFSLVI PNKTTSLLSN ISWREGGLVP LAEVEQEHRV
HSRLAKPDAR FYMDKVVAPS IDAVCSDRSF AYDQERQRFD PLFSAAIYGL PGSSQNTRTD
IQSFESALPG LPAQGVLGAS SPAQLPFPPM QVPQLHKLIL DSGKLAKLDS LLAELKTGDH
RVLLYFQMTR MIDLMEEYLA FRQYKYLRLD GSSTISERRD MVMDWQTKPE LFIFLLSTRA
GGLGINLTAA DTVIFYDSDW NPSNDAQAMD RAHRLGQTKQ VTVYRLITKD TVDERIVQLA
RNKKLVQDAV VQSSSGLGPT DSGAKTNEVV SLLLDDQELE ESIRNAEIKR KKAEEKAKED
GHRGVRMREE AKRQKKAAAL AAANKPSRWD AEDDEEDAFG FFAANKAVVA DDEDGMTSMV
ATPGESGADS VNPTKTKGKG GRKSTGEAGA SKAKRRASKV AGSDPFLFGI VRGGMGHHHD
HNPHAGAAQG AAGGAGGAGA IATTSRIGLI DCTSCEGLIH SILPLGCLGH DSQHHNAHPL
PHGYPAPISA NSTSSAGHLT HPSQLGVGVV CCEQPACFPP PSLPQQNRRL LGFPLTSSAS
SSVSAATSSS ECDATCLEGP GTPWSSTSAS SSSLLFDKCD QCQADPTAAS SSANSLLIKS
FLSAHHLDCC SSLLAPPPPT PTSNLASYSC CSFDDCFGIS TTASITPTSD CPDCFTPLDQ
QPQNQQHHQL NQDASNSSFL AELMKGLDEQ AIQEILHCCC CAPEIEQNPA AWDVSHHDSH
RHANVEPSRA LLELSSAANQ DHPSHEHNHQ QHEHEHPHQP GPATRYDCGW RECKASFDSY
ALLVVHVNTL HLAPPSIATL SAPTAPPSSV LRPEVRAHRH ATHSSHPYNH FASNLTLAHE
SAVKEESVSA PGPHACRWKG CSATFPSSAE LMSHLSLVHV GSGKSSYSCE WEGCSRSNQE
GGRQFSQRQK VIRHLQTHAQ DKPFACDLCD RKFSEALSLA QHKRTHTGER PYECTWERCD
KAFASASALT IHMRTHTGDR PFVCDFPGCK AAFAESSNLA KHARTHRGER SHQCPECDKT
FLRSDQLARH MKIHEREAAG QISAGSGSGE TSAQVAALST TPTSVDEAYY VPNLISNNNS
LYYVKSTSAS ISGATAGVLG LTNTFGFLFY LVTSTLIGSL FLLTKGTAEG KGYFPGDRVS
AWRTVVLSGL LEHVFPYILF WTLFYALVHI YD
//
