ID   RUVB2_SCHPO             Reviewed;         465 AA.
AC   O94692;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=RuvB-like helicase 2;
DE            EC=3.6.4.12;
GN   Name=rvb2; ORFNames=SPBC83.08;
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   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DIL1.
RX   PubMed=20404563; DOI=10.4161/cc.9.9.11526;
RA   Rumpf C., Cipak L., Novatchkova M., Li Z., Polakova S., Dudas A.,
RA   Kovacikova I., Miadokova E., Ammerer G., Gregan J.;
RT   "High-throughput knockout screen in Schizosaccharomyces pombe identifies a
RT   novel gene required for efficient homolog disjunction during meiosis I.";
RL   Cell Cycle 9:1802-1808(2010).
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 RVB1. Component of the SWR1
CC       chromatin remodeling complex, the INO80 chromatin remodeling complex,
CC       and of the R2TP complex (By similarity). Interacts with dil1.
CC       {ECO:0000250, ECO:0000269|PubMed:20404563}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB36870.1; -; Genomic_DNA.
DR   PIR; T40697; T40697.
DR   RefSeq; NP_595640.1; NM_001021534.2.
DR   AlphaFoldDB; O94692; -.
DR   SMR; O94692; -.
DR   BioGRID; 277592; 19.
DR   IntAct; O94692; 2.
DR   MINT; O94692; -.
DR   STRING; 4896.SPBC83.08.1; -.
DR   iPTMnet; O94692; -.
DR   MaxQB; O94692; -.
DR   PaxDb; O94692; -.
DR   PRIDE; O94692; -.
DR   EnsemblFungi; SPBC83.08.1; SPBC83.08.1:pep; SPBC83.08.
DR   GeneID; 2541077; -.
DR   KEGG; spo:SPBC83.08; -.
DR   PomBase; SPBC83.08; rvb2.
DR   VEuPathDB; FungiDB:SPBC83.08; -.
DR   eggNOG; KOG2680; Eukaryota.
DR   HOGENOM; CLU_028311_4_0_1; -.
DR   InParanoid; O94692; -.
DR   OMA; YDMGAKM; -.
DR   PhylomeDB; O94692; -.
DR   PRO; PR:O94692; -.
DR   Proteomes; UP000002485; Chromosome II.
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; ISS: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   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR   InterPro; IPR037942; RUVBL2.
DR   InterPro; IPR010339; TIP49_P-loop.
DR   PANTHER; PTHR11093; PTHR11093; 1.
DR   PANTHER; PTHR11093:SF2; PTHR11093:SF2; 1.
DR   Pfam; PF06068; TIP49; 1.
DR   Pfam; PF17856; TIP49_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Activator; ATP-binding; Chromatin regulator; DNA damage; DNA repair;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW   rRNA processing; Transcription; Transcription regulation.
FT   CHAIN           1..465
FT                   /note="RuvB-like helicase 2"
FT                   /id="PRO_0000165672"
FT   BINDING         72..79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  51562 MW;  150EE10A1D31F847 CRC64;
     MSISVTSHND VSKLERIGAH SHIKGIGLND NLEPKESSQG MVGQVKARRA AGVILKMIQE
     GRIAGRAILM AGPPSTGKTA IAMGMAQSLG SDTPFVTLSA SEVYSLEMSK TEALLQALRK
     SIGVRIKEET EIIEGEVVEV QIDRSITGGN KQGKLTIRST DMETVYDLGT KMIDSLTKEK
     VLAGDVISID KSVGRVTKLG RSFSRARDYD AMGADTRFVQ CPQGEIQKRK EVVHTVSLHD
     IDVINSRTQG FLALFSGDTG EIKPEVREQI NTKVSEWREE GKAEIVPGVL FVDEVHMLDI
     ECFSFFNRAL EDDLAPIVIM ASNRGITRIR GTNYRSPHGI PVDLLDRMLI ISTLPYSHEE
     VKEILKIRCQ EEDVDMEPSA LDYLSTIGQE TSLRYALLLI SSSNQVALKR KSATIEESDI
     RRVYELFLDQ KRSVEYLEEY GKNYITENEW SASGAQDNAV AMQED