INO80_CRYNJ
ID INO80_CRYNJ Reviewed; 1765 AA.
AC P0CO16; Q55US0; Q5KHM0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=INO80; OrderedLocusNames=CND06010;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017344; AAW43182.1; -; Genomic_DNA.
DR RefSeq; XP_570489.1; XM_570489.1.
DR AlphaFoldDB; P0CO16; -.
DR SMR; P0CO16; -.
DR STRING; 5207.AAW43182; -.
DR PaxDb; P0CO16; -.
DR PRIDE; P0CO16; -.
DR EnsemblFungi; AAW43182; AAW43182; CND06010.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_002244_0_0_1; -.
DR InParanoid; P0CO16; -.
DR OMA; MNIWRED; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000002149; Chromosome 4.
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: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..1765
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000074322"
FT DOMAIN 629..759
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 883..1055
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1457..1607
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1680..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 702..745
FT /evidence="ECO:0000255"
FT MOTIF 1006..1009
FT /note="DEAQ box"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 896..903
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1765 AA; 196403 MW; C5E120034EEC0A86 CRC64;
MGAMDDRRYS YPPPRTSYVQ PSTHPSPTAS DYRYRSPVLP QHPPTHHSPS SYSASLYGQP
KEDPAIAYAR MREEMRTAEE ARREAEALEY RRKRDMEFAA RRPGSELMDD PRRIPHSSFP
RSQMYGPSAD QSRVMPSRNG KDYISEPPSP SELYPTDEDT ERLPIDRYRR DIDVPPLPRQ
LPPPPSEIGR MADRARSPSA PIAPPLLKVV RKRTKVIRPN DFLVGNEDVW EDGLIRYQSK
REDEVRAIAQ WAASCQVRNG VGEPSLPQTQ DESIKVRKIN GDIATPTNKK KRKSRKLNLD
DELLGLASSP PGSPNAAAEA EKSESKHHIY GMNGPIDPAN PPSPSTIVYP SGLTRAEVIA
KCEAGDVEGL TEDDVKAVQD EMWMREKAAQ AAENGGVLPT NKDGTVRRKP GPAKGWRKIR
GIDKKKETTP GKAQSTTAGS VAGSVADEEA EADIAALLDD SIAKKGKKVK RRKLEEPGAE
SPRFADAEDE YNEHRPSDSV LLDEIEDEHS RAGSVGESNA LDTLPAASAP PKKKNSKTKE
PGVGKGRWTR PTKPEKELVK KAEALASRTS KASLAGPSDD TFGVGPGPAE EVQEEIKHEY
APNTHDPRGV SENEAKIRHE LVEDLQKQAW SNIVRDVPRI YRVFQGYDQS MKQIAQRRAQ
ACVRNAFGQR NQKTMQRQSG KVNKEGAAKA KRIVKELAAF WRKNEKDEVI ARKKAEREAL
ERAKAEEEAR ETKRQSRKLN FLLTQTELYS HFIGKKIKTK EAEAAEGMDV EEEEKRGMEE
IAIGEDGEPL PDLDYDEDDE ENLRKHAARG AQAAIQAARD KARAFDDSIV GRGAPLPGDD
TMDGDELNFQ NPSLGENSVT ITQPKMLMAQ LKEYQLKGLT WLGNLYEQGI NGILADEMGL
GKTIQSISLL AYLAEHHNLW GPFLVIAPAS TLHNWQQELA RFVPRLKALP YWGSPKDRET
LRKIWSRKNQ TFSEDSPFHI LITSYQLAVQ DEKYLQGMKW QYMILDEAQA IKSSSSARWK
SLLSLHCRNR LLLTGTPIQN SMHELWALLH FIMPQLFDSH EEFAEWFSKD IESSSGGVTG
NLKPEQLKRL HMILKPFMLR RVKKHVQKEL GDKIEIDLLV DLSQRQREIY KALRQRVSIT
DLLATAENNT DNGNPKNMRS LVNLVMQFRK VCNHPDLFER ADVVSPFVFG EFSQSGNLAR
EGDGMYLPDS ARNAIEVQIP RILWTDGGKL DIPGEQSLAG SDTKILQNLL NIWTPEWINE
RTKCADAEFG FVKLVGSSPG ETSRSAKSPV LVQLLEGAEK ERRWTEEGRF VDDSEFAASV
KKGFRVPSVI PVLTQPGQVS LREISRRVWD ESYLSRDDAR CIGDYAIAPI VKPIASNRSF
LNAQDRILNQ PLAHSTLYGL APSELHDPLA AEQFSRIAPS VPLTGLIPSS ASSQTPVSPL
HIPPTKRLIV DSAKLARLDS LLRELKAGGH RVLLYFQMTK MMDLIEEYLI FRQYKYLRLD
GSSPIAERRD MVTSWQTNPD IFVFCLSTRA GGLGINLTAA DTVIFYDHDW NPSSDAQAMD
RAHRVGQTKQ VTVYRLVARG TIEERILQMA RGKKDIQDVV VGTKSVSDVA KPSEIVSLFM
DDEELAESVA KRKQAEAHGY IAPTIIPNGR RSQFGDGLVL DDGEGDDGFF NAAAAARANA
EEEEGLGAEE ESKGKGKAKA AAAVTFPVPG EKRSHKKGMG KKAQAAAAAA ALERVIAGNE
EPLAASKPPA KKKVKIALGP DGLPL
