INO80_CANAL
ID INO80_CANAL Reviewed; 1387 AA.
AC Q59KI4; A0A1D8PSU8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
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; OrderedLocusNames=CAALFM_CR04720CA;
GN ORFNames=CaO19.1734, CaO19.9302;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017630; AOW31205.1; -; Genomic_DNA.
DR RefSeq; XP_710254.2; XM_705162.2.
DR AlphaFoldDB; Q59KI4; -.
DR SMR; Q59KI4; -.
DR STRING; 237561.Q59KI4; -.
DR PRIDE; Q59KI4; -.
DR GeneID; 3648140; -.
DR KEGG; cal:CAALFM_CR04720CA; -.
DR CGD; CAL0000196418; orf19.9302.
DR VEuPathDB; FungiDB:CR_04720C_A; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_2_1; -.
DR InParanoid; Q59KI4; -.
DR OrthoDB; 188211at2759; -.
DR PRO; PR:Q59KI4; -.
DR Proteomes; UP000000559; Chromosome R.
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; -; 1.
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..1387
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000074320"
FT DOMAIN 438..563
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 684..856
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1240..1387
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 480..551
FT /evidence="ECO:0000255"
FT MOTIF 807..810
FT /note="DEAQ box"
FT COMPBIAS 280..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 697..704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1387 AA; 158823 MW; 68C05F806CF7E43A CRC64;
MNISSMLSSD NNVSLKESMT TATDQQQQQQ AESVDHASIN GNGQTSVSAV NNVQENHLSE
FHSSNQQHSS IPPVGTTVEH ATTTTTTATN HQPVNSSPLK HSVDENSNPT TISSLKKDTN
SIIASILPES YQFDNSYTPT IDQKYKSVFE SNINVINQLD QYQQMGHHLK LMKFDEVKLN
NYLINTGQFA SNYIDRVVAE DISSRNNKIS ETNKNKELIA IDYSKPLHHN STRGKEFKWG
STRKIHKVEH KSRRRKPAAT TSTTDDSNKA VAAAANGTKD HSATAGTTAS ANGSDTPDRR
HQRQSSKPST PILIKPKTEP GKGSPEIQPR RSSRPKVKRK AFEDELETAD KQSSTQQVKK
SQESTGRDHK RVKIENKQEE QQQHQQQQQA DEEDEAEAEA EAEQKPKSGA LSEAAAAGMT
AKEFKAFMRQ YDNTYIAIWK DLSRKDGPKG SRSMQQATQG RLINLRKTAL LAAREAKRWQ
LKNTKNQKDL TTKARRAMRE MFNFWKRNER LERDLKKKHE KELLDKAKKE EEEREAKRQS
RKLNFLITQT ELYSHFIGKK IKTDELEGTN ADDNLKSNTK EHLDKYADVD GSATHDINAV
DFDNDDEEAL RRMAAQNAQN ALIEVQNKAK QFDNSEESFK NPDTNGEEMN FQNPTLLGDI
TIPQPNMLKC TLKEYQLKGL NWLANLYEQG INGILADEMG LGKTVQSISV LAYLAETYNM
WGPFLVVTPA STLHNWQQEI TKFVPEFKVL PYWGNAKDRK ILRKFWDRKS LRYDKDSPFH
VLVTSYQLIV ADIAYFQKMK WQYMILDEAQ AIKSSSSSRW KSLLNLTCRN RLLLTGTPIQ
NSMQELWALL HFIMPSIFDS HDEFSDWFAK DIESHAQSNT SLDEQQLRRL HMILKPFMLR
RIKKNVQSEL GDKVEIDVYC DLTTRQKKLY QQLRSQISMS DTDLLELESN STSSDSSLAN
LVMQFRKVCN HPDLFERADV NSPFSFGKFA ETGSFLRETN ELDVNYSTEN IVQYDLPRLI
YDELLTPNYN KSIRDSIYSK FSIYNPENMN ATGWLQGINV SPNELKHYSQ MDILSRAIEM
QNKPTETEKL ERINYLYEGD YIPKNKKLLI TDHSTSTNSS FISNSLVFSD LVSIKEKVGE
DMYLNKLEPA VTPIASAPPI TVNCSSMNFT NKMNNTLFDS NIRSSLIPLS LSTELKLMKD
QIPLEQYPKS NMLPMPIFDY SNIRMPSMDR FIAESGKLAK LDELLIDLKR GGHRILIYFQ
MTRMMQIFEE YLAYKSYKYI RLDGSTTIES RREMVQAWQT NPEIFIFMLS TRAGGLGLNL
TSADTVIFYD SDWNPTIDSQ AMDRAHRIGQ TKQVKVFRLV TRNTIEQKIL ERAKEKEEIQ
KLVVGNM
