INO80_SCHPO
ID INO80_SCHPO Reviewed; 1604 AA.
AC O14148; O14025;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 4.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=ino80; ORFNames=SPAC29B12.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179 AND SER-518, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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; CU329670; CAB16246.2; -; Genomic_DNA.
DR RefSeq; NP_001018299.1; NM_001020410.2.
DR AlphaFoldDB; O14148; -.
DR SMR; O14148; -.
DR BioGRID; 280642; 18.
DR STRING; 4896.SPAC29B12.01.1; -.
DR iPTMnet; O14148; -.
DR MaxQB; O14148; -.
DR PaxDb; O14148; -.
DR PRIDE; O14148; -.
DR EnsemblFungi; SPAC29B12.01.1; SPAC29B12.01.1:pep; SPAC29B12.01.
DR GeneID; 3361566; -.
DR KEGG; spo:SPAC29B12.01; -.
DR PomBase; SPAC29B12.01; ino80.
DR VEuPathDB; FungiDB:SPAC29B12.01; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_2_1; -.
DR InParanoid; O14148; -.
DR OMA; CKLKEYQ; -.
DR PhylomeDB; O14148; -.
DR PRO; PR:O14148; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0031011; C:Ino80 complex; IDA:PomBase.
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; NAS:PomBase.
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; IMP:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IDA:PomBase.
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; -; 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 1: Evidence at protein level;
KW Activator; ATP-binding; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1604
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350963"
FT DOMAIN 626..751
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 854..1026
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1433..1591
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 977..980
FT /note="DEAQ box"
FT COMPBIAS 406..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 867..874
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1604 AA; 183049 MW; 10B80307F3308619 CRC64;
MDPSRETFDG STRDSYKPPN GAEMMGQSEL NTQNRIPYNT SANNRNWQIP LYWQQRGNEF
QASPPPPLGY VTPEYGATGT PVNANNASRV DYATTAANVP EEYANDYSSE LAYIHNVNDM
PHVDGLSNHS PATQPDLFET PAQSDPILFS SYPHAAQARV DPSISKDLYN MVPRPDANTV
SPHAARSASS LPVPKEASET PFRDASTDLF DEHAHAAPMH SSISISTLLS DSDRYEPHVS
LTENISPVMA PSIDARLSQT ILRGLPPAQK LSPNSSQSQI THNRRKHKLP LNATTNNSVV
LTPDTSPLLD SDEVVSDDDS NEQQTMMMKF NYLQHLRNKR DEAVHAEKRR LLDIRGSIHD
RLVCRYENRY NKLHASEYNH HHDWAVRQAI REEVAAVEAA KIRADEEKKK KEREEQVRLL
QESADKDAEM NEASTATSEN EDLKDDLSLA DLSSKKTANS QATENNNTPS KAKVKAESKV
RSKAKSDKSR AKLSSDTNKD SEKNDNNDAS LQSAGVASDG ESSPETPLTK ASKSKKAKAS
KLANDTSKNA NGETKSTPKK SKKKTSKAQQ EANSTTAEGK EKLSGDSTET GNSTNKEAST
EDTKANATAS APNKKKKTVE TLQQQVIKEI ARKEIPRVYK IIQQNQYNRS TNARKTSQLC
GREARRWQFR TIKNNKDMQT KAKRAMRETM VFWKRNERVE RDLRKKAERE ALDRAKKEEE
LRESRRQARK LDFLITQTEL YSHFVGRKMD REQDLPSATN TASVSEINFD SDEEEDIRRL
AVESAQEAVQ KAREHSQLFD ANRQQSPNNS SSDMNEGEMN FQNPTLVNAF EVKQPKMLMC
KLKEYQLKGL NWLANLYEQG INGILADEMG LGKTVQSISV MAYLAETHNI WGPFLVIAPA
STLHNWQQEI TRFVPKLKCI PYWGSTKDRK ILRKFWCRKN MTYDENSPFH VVVTSYQLVV
LDAQYFQSVK WQYMILDEAQ AIKSSSSSRW KSLLAFKCRN RLLLTGTPIQ NTMQELWALL
HFIMPSLFDS HNEFSEWFSK DIESHAQSNT QLNEQQLKRL HMILKPFMLR RVKKNVQSEL
GEKIEKEVYC DLTQRQKILY QALRRQISIA ELLEKAILGG DDTVASIMNL VMQFRKVCNH
PDLFEREDVR SPLSLATWSK SIYINREGNF LDVPYNTRNF ITFSIPRLLY EQGGILSVPG
LNTSRGFETK YLYNLMNIWN PEYTNDSIKS NPEGSPFSWL RFVDESPQTL FQTFQNPVVH
YLDEAEASSS LKEEQLCRQE FCYGKDYSNV RKMLLLPKSI TKVDVLGSDF KEDSPFYHLT
HVLEESDSQL DLTLLDSVLV QRASAPPIDI YCPGSRQFTV LQSRFQRDHL WSHYLYQPLK
GEEDLIINNQ AVSKLPIPRK PLLPSFGIAK GSYSNVRIPS MLRFIADSGK LSKLDKLLVE
LKANDHRVLI YFQMTRMIDL MEEYLTFRQY KYLRLDGSSK ISQRRDMVTE WQTRPELFVF
LLSTRAGGLG INLTAADTVI FYDSDWNPSI DSQAMDRAHR IGQQKQVTVY RFITRGTIEE
RIVIRAKEKE EVQKVVISGG ETRPTKQMDL KGNSREMVSW LLEE
