ID   RUVB2_CRYNB             Reviewed;         463 AA.
AC   P0CR29; Q55Z22; Q5KND8;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=RuvB-like helicase 2;
DE            EC=3.6.4.12;
GN   Name=RVB2; OrderedLocusNames=CNBA6650;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
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: 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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR   EMBL; AAEY01000005; EAL22896.1; -; Genomic_DNA.
DR   RefSeq; XP_777543.1; XM_772450.1.
DR   AlphaFoldDB; P0CR29; -.
DR   SMR; P0CR29; -.
DR   EnsemblFungi; AAW41095; AAW41095; CNA06840.
DR   EnsemblFungi; EAL22896; EAL22896; CNBA6650.
DR   GeneID; 4933930; -.
DR   KEGG; cnb:CNBA6650; -.
DR   VEuPathDB; FungiDB:CNBA6650; -.
DR   HOGENOM; CLU_028311_4_0_1; -.
DR   Proteomes; UP000001435; Chromosome 1.
DR   GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:InterPro.
DR   GO; GO:0097255; C:R2TP complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Activator; ATP-binding; Chromatin regulator; DNA damage; DNA repair;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; rRNA processing;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..463
FT                   /note="RuvB-like helicase 2"
FT                   /id="PRO_0000410276"
FT   BINDING         76..83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   463 AA;  50890 MW;  EF9494566F53663B CRC64;
     MAANISLQPT SMRDVTKMER IGVHSHIHGL GLDSNLEPRA SSQGMIGQGK ARKAAGVILK
     MVQEGRIAGR AILMAGPPST GKTALAMAMT QTLGSDVPFV MLTASEVFSL EISKTESLTQ
     AFRRAIGVRI KEETELIEGE VVEIQVDRSV TGATKTGRLT LKTTDMETVY DLGSKMIDQL
     QKEKVLAGDV VSIDKASGRI SKLGRSFGRA KDYDAMGADT RFVACPDGEL QTRKEVVHTV
     SLHEIDVINS RTQGFLALFA GDTGEIKPEL RAQINGKVAE WREEGKAEIV PGVLFIDEVH
     MLDIECFSFL NRAMENELAP LVVMASNRGI TRIRGTKYKS PHGIPADLLD RMLIISTNRY
     EEDEMREIVK IRAEEEDVRL SPAALDLLAT MGIQTSLRYS LNLIAPSSLL AQRRKSPQTD
     VEDVRMAYKY FCDVERSAQY AKETSGMMFG ETEEINGGME VDA