ID   RUVB1_SCHPO             Reviewed;         456 AA.
AC   Q9C0X6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=RuvB-like helicase 1;
DE            EC=3.6.4.12;
GN   Name=rvb1; ORFNames=SPAPB8E5.09;
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).
CC   -!- FUNCTION: DNA helicase which participates in several chromatin
CC       remodeling complexes, including the SWR1 and the INO80 complexes. The
CC       SWR1 complex mediates the ATP-dependent exchange of histone H2A for the
CC       H2A variant HZT1 leading to transcriptional regulation of selected
CC       genes by chromatin remodeling. The INO80 complex remodels chromatin by
CC       shifting nucleosomes and is involved in DNA repair. Also involved in
CC       pre-rRNA processing (By similarity). {ECO:0000250}.
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; EC=3.6.4.12;
CC   -!- SUBUNIT: May form heterododecamers with RVB2. Component of the SWR1
CC       chromatin remodeling complex, the INO80 chromatin remodeling complex,
CC       and of the R2TP complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR   EMBL; CU329670; CAC37428.1; -; Genomic_DNA.
DR   RefSeq; NP_594783.1; NM_001020211.2.
DR   AlphaFoldDB; Q9C0X6; -.
DR   SMR; Q9C0X6; -.
DR   BioGRID; 279655; 15.
DR   IntAct; Q9C0X6; 2.
DR   MINT; Q9C0X6; -.
DR   STRING; 4896.SPAPB8E5.09.1; -.
DR   iPTMnet; Q9C0X6; -.
DR   MaxQB; Q9C0X6; -.
DR   PaxDb; Q9C0X6; -.
DR   PRIDE; Q9C0X6; -.
DR   EnsemblFungi; SPAPB8E5.09.1; SPAPB8E5.09.1:pep; SPAPB8E5.09.
DR   GeneID; 2543227; -.
DR   KEGG; spo:SPAPB8E5.09; -.
DR   PomBase; SPAPB8E5.09; rvb1.
DR   VEuPathDB; FungiDB:SPAPB8E5.09; -.
DR   eggNOG; KOG1942; Eukaryota.
DR   HOGENOM; CLU_028311_1_1_1; -.
DR   InParanoid; Q9C0X6; -.
DR   OMA; VIYVEAN; -.
DR   PhylomeDB; Q9C0X6; -.
DR   Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR   PRO; PR:Q9C0X6; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0070209; C:ASTRA complex; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0031011; C:Ino80 complex; IDA:PomBase.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0097255; C:R2TP complex; IBA:GO_Central.
DR   GO; GO:0000812; C:Swr1 complex; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; NAS:PomBase.
DR   GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:PomBase.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 2.40.50.360; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR027238; RuvB-like.
DR   InterPro; IPR041048; RuvB-like_C.
DR   InterPro; IPR037938; RUVBL1.
DR   InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR   InterPro; IPR010339; TIP49_P-loop.
DR   PANTHER; PTHR11093; PTHR11093; 1.
DR   PANTHER; PTHR11093:SF6; PTHR11093:SF6; 1.
DR   Pfam; PF06068; TIP49; 1.
DR   Pfam; PF17856; TIP49_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; Chromatin regulator; DNA damage; DNA repair;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..456
FT                   /note="RuvB-like helicase 1"
FT                   /id="PRO_0000165658"
FT   BINDING         71..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  50052 MW;  BE9CE98F3705536F CRC64;
     MVQISEVKGN GRDNRITTHS HIKGLGLKED GTCESVGGGF IGQEKAREAC GIITDLIKSK
     KFGGKGVLFA GGAGTGKTAL ALAIAQELGP KVPFCPMVGS EVYSSEIKKT EALMENFRRA
     IGLRVKETKE VYEGEVTEMV PEEAENPLGG YGKTISHVLL GLKTHKGTKQ LKLDPSIYES
     LQREQVSTGD VIYIEANTGA VKRVGRSDAY ATEFDLEAEE YVPMPKGEVH KRKEIVQDVT
     LHDLDIANAR PQGGQDIMSM MGQLMKPKKT EITDKLRGEI NKVVNKYIEQ GIAELIPGVL
     FIDEVHMLDI ECFTYLNQAL ESTISPIVIF ASNRGICTIR GTEDIQAPHG IPTDLLDRLL
     IVRTLPYSES EIRSILQIRA KVENIILTDE CLDKLAQEGS RTSLRYVIQL LTPVSIIASL
     HGNKEIGVQD IEECNDLFLD ARRSAQVVKS SSGFLQ