RUVB2_CANAL
ID RUVB2_CANAL Reviewed; 498 AA.
AC Q5AGZ9; A0A1D8PR03; Q3MPG1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=RuvB-like helicase 2;
DE EC=3.6.4.12;
GN Name=RVB2; OrderedLocusNames=CAALFM_C701810WA;
GN ORFNames=CaJ7.0208, CaO19.13892, CaO19.6539;
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=15937140; DOI=10.1534/genetics.104.034652;
RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA Mikami Y.;
RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT syntenic analysis against the Saccharomyces cerevisiae genome.";
RL Genetics 170:1525-1537(2005).
RN [2]
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 [3]
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 [4]
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: 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; AP006852; BAE44699.1; -; Genomic_DNA.
DR EMBL; CP017629; AOW30546.1; -; Genomic_DNA.
DR RefSeq; XP_721377.1; XM_716284.1.
DR AlphaFoldDB; Q5AGZ9; -.
DR SMR; Q5AGZ9; -.
DR BioGRID; 1220149; 1.
DR STRING; 237561.Q5AGZ9; -.
DR PRIDE; Q5AGZ9; -.
DR GeneID; 3637055; -.
DR KEGG; cal:CAALFM_C701810WA; -.
DR CGD; CAL0000176498; RVB2.
DR VEuPathDB; FungiDB:C7_01810W_A; -.
DR eggNOG; KOG2680; Eukaryota.
DR HOGENOM; CLU_028311_4_0_1; -.
DR InParanoid; Q5AGZ9; -.
DR OMA; YDMGAKM; -.
DR OrthoDB; 752343at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0097255; C:R2TP complex; IBA:GO_Central.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:EnsemblFungi.
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; IBA:GO_Central.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
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 3: Inferred from homology;
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..498
FT /note="RuvB-like helicase 2"
FT /id="PRO_0000165664"
FT REGION 458..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 498 AA; 54549 MW; 5ADE8A14BCEF2786 CRC64;
MATNTITTTK VTTTTTDVTG LSLIAAHSHI SGLGLDDNLQ PKENAQGMVG QLSARKAAGV
ILKMVEAGKI AGRAVLIAGP PSTGKTAIAM GLSQSLGNQV PFTALAASEV FSLELSKTEA
LTQAFRKSIG IKIKEETEII EGEVVEIQID RTITGGHKQG KLTIKTTDME TIYELGNKMI
EGLTKEKVLA GDVISIDKAS GKITKLGRSF TRARDYDAMG PETKFVQCPE GELQKRKEVV
HTISLHEIDV INSRQQGFLA LFSGDTGEIR PEVRDQINTK VAEWKEEGKA EIVPGVLFID
EVHMLDIECF SFINRALEDE FSPIVIMATN RGVSRIRGTD YKSPHGMPMD LLDRSITIHT
TSYTADEIRT ILSIRATEEE VELSGDALAL LTKIGQETSL RYAANLISVS QQIALKKKNN
TVDLQDIKRA YMLFLDSDRS VQYLEENADQ YIDDYGRVTI GQESTDGSTQ PQAKQQEVAQ
PEATQPQSQP EDDKMETD
