INO80_USTMA
ID INO80_USTMA Reviewed; 1910 AA.
AC Q4PGL2; A0A0D1EAT0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=INO80; ORFNames=UMAG_00751;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003140; KIS72346.1; -; Genomic_DNA.
DR RefSeq; XP_011386530.1; XM_011388228.1.
DR AlphaFoldDB; Q4PGL2; -.
DR SMR; Q4PGL2; -.
DR STRING; 5270.UM00751P0; -.
DR PRIDE; Q4PGL2; -.
DR EnsemblFungi; KIS72346; KIS72346; UMAG_00751.
DR GeneID; 23561963; -.
DR KEGG; uma:UMAG_00751; -.
DR VEuPathDB; FungiDB:UMAG_00751; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_25_0_1; -.
DR InParanoid; Q4PGL2; -.
DR OMA; DAHRRIW; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000000561; Chromosome 1.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
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:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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..1910
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000074328"
FT DOMAIN 726..851
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 1010..1182
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1583..1747
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1760..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 790..840
FT /evidence="ECO:0000255"
FT MOTIF 1133..1136
FT /note="DEAQ box"
FT COMPBIAS 66..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1760..1790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1823..1837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1023..1030
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1910 AA; 214514 MW; 8B2651333E23956F CRC64;
MSGEDRGAPY RYAGERPPAY PADGYASYQR GLKSSIPSRS YDTAYPEQGY DRHLRERVHP
AYTTGPSYGV PPPPPTDYRR PPPQAAYRYE EDYHHRRAPA QPHLEYAPEH RRQPVHSDAY
READDRRSFE QARSDPYASP SRHAYQDSYR SELPHERRHA PAAYERISVR DDARSAPENR
HIDEPAVYRR DEYDAHSREI QPSYRRGAHR SPRLSPQPVV SAHERSSEYA TRDYSASAAR
YAEPVHQPES PPRPSMSIFN MLNDRSANGA VESVHSSPTK SSIAAEHESY PTTAQEPSHA
SRAAFDPARE QSYSTARDSQ AYSRGSEARA GAARVNYTVH PEDEAAISQR RNSSAHQQSS
IKSVRHPANA VDEPLIRVKH EEATSASLDA QMSAEPPVSH TLNNGERLSA QDAKVATEDS
SLAANGNGKV DSAGGTARPA PAKTQLKLRN NPLPASKSNS SFVAPPPPAK KNRDPDGWES
DLSNEENQPF WQTELDDYIF DVRERQRLIE DAFVASMREK HVEVERRLAR AYEGRYFAVI
RQIRLREQQE ASQRDMERRQ DHVRQQRDHE IDLELLGTLS DGQQNMGTRK KKGGRGTDDD
GLLQADDDDD DDSDDVALAD LAARNGSKSN IIKLKRSKGK PAAADPRNKK RRLENGAALS
PAPGSEVDST LADFGGNFDG DDSAFASHQA SPTPDDVSFA LDVDASGKVP IDARRAQQLE
DAHRRIWTTI AKRDVPKVYR TVLQSASSKT MYWRRISSVV QREAKRGAAR NNKTVKDVQL
RARKVMREVL VFWKRNEKEE RELRKKAERE ALEKAKKEEE MREAKRQARK LNFLISQTEL
YSHFVGSKLK TAEAEESEET AGSSKIIDPN AQPSDATVLP INPHSELADA EARLAELDDI
DFDDEDESNL RAHAARNAQE AVRLAKEKAQ AFDVAAAEER RRNEAAARER EGLDAGPVKQ
IEEKDLGKAF DSDDMNFLNP TSMGQTEIKQ PKMLTCQLKE YQLKGLNWLA NLYEQGINGI
LADEMGLGKT VQSISLMAYL AEVHDIWGPF LVIAPASTLH NWQQEISKFV PTLKALPYWG
NVKDRAVLRK FWNRKQISYN RDAPFHVLVT SYQLVVSDEK YFQRVKWQYM ILDEAQAIKS
SSSIRWKTLL GFNCRNRLLL TGTPVQNSMQ ELWALLHFIM PSLFDSHDEF SEWFSKDIES
HAEQKGTLNE HQLRRLHMIL KPFMLRRIKK NVQNELGDKI EIDVFCDLSA RQKMLYRGLR
ANISVAELMD RATSNDEAGL KSLMNLVMQF RKVCNHPELF ERADVRAPFA LADFARSGSL
AREGDLLNLP DSTTSLIELQ VPKLLVREGG IFDIPGHNSR KGFDTGYLQN LFNIWRAPHI
HESLQEERST FASLPLIGVS PSEAQKTFHS TGIKRILAAA AEERHWRSLE AFASDDTFAA
ASVRPLAKML RPMPTTSGRS PSVLMPLEEV AADYRRHSYL AKDSARAVVA PAVAPPIKLY
SNDGPFMQAQ ERFSRDAQVS VTLFGLSPEG RESVKRVEEL QSELPEVPPQ GVMRDSSIDQ
LPYNGMQVPQ MNKLIVDSSK LAKLDVLLRE LKANGHRVLI YFQMTRMIDL MEEYLIYRQY
KYLRLDGASK ISDRRDMVTD WQTKPELFIF LLSTRAGGLG INLTAADTVI FYDHDWNPSN
DSQAMDRAHR LGQTKQVTVY RLITKGTIDE RIVRLARNKK EVQDIVVGTK AYSETGMAKP
QEIVSLLLDD DELAESMLRK KQAEEAQTAQ EKADLARASH AKRRLNKDRA AAAVESPAPV
GSTWSLEDDE DDFFGARPPS KADTDTAETT PQLQSKKRSV GGGGGGSGGA KRGRISEVAS
PRMTPLSLDD GALMASGEQL ASPSKGAAAK RKSKSHRKKT VDELAGVDLD
