RUVB2_DEBHA
ID RUVB2_DEBHA Reviewed; 480 AA.
AC Q6BSB8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=RuvB-like helicase 2;
DE EC=3.6.4.12;
GN Name=RVB2; OrderedLocusNames=DEHA2D10054g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382136; CAG87056.1; -; Genomic_DNA.
DR RefSeq; XP_458902.1; XM_458902.1.
DR AlphaFoldDB; Q6BSB8; -.
DR SMR; Q6BSB8; -.
DR STRING; 4959.XP_458902.1; -.
DR EnsemblFungi; CAG87056; CAG87056; DEHA2D10054g.
DR GeneID; 2901300; -.
DR KEGG; dha:DEHA2D10054g; -.
DR VEuPathDB; FungiDB:DEHA2D10054g; -.
DR eggNOG; KOG2680; Eukaryota.
DR HOGENOM; CLU_028311_4_0_1; -.
DR InParanoid; Q6BSB8; -.
DR OMA; YDMGAKM; -.
DR OrthoDB; 752343at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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; Reference proteome;
KW rRNA processing; Transcription; Transcription regulation.
FT CHAIN 1..480
FT /note="RuvB-like helicase 2"
FT /id="PRO_0000165667"
FT BINDING 76..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 52396 MW; 88D588608822F9DD CRC64;
MSANTISTKV QSKDLNGLSL IAAHSHISGL GLDDNLQPKE SGQGMVGQLK ARKAAGVILK
MIQAGKIAGR AVLVAGPPST GKTAIAMGLS QNLGSEVPFT AIAGSEIFSL ELSKTESLTQ
AFRKSIGIKI KEETEMIEGE VVEIQIDRSI TGGHKQGKLT IKTTDMETIY ELGNKMIEGL
TKEKVLAGDV ISIDKASGKI TKLGKSFTRA RDYDAMGPET KFVQCPEGEL QKRKEVVHTV
SLHEIDVINS RQQGFLALFS GDTGEIRSEV RDQINTKVAE WKEEGKAEIV PGVLFIDEVH
MLDIECFSFI NRALEDDFAP IVIMATNRGI SKTRGTNYKS PHGLPMDLLD RSIIIHTAPY
NADEIRTILL IRATEEEVEL TGDALALLTK IGQETSLRYA SNLISVSQQI ALKRRSNSVD
LPDIKRSYML FLDSDRSVQY LEEFSTQFID DSGNVTFGTN DASVKQTKGA ANGEDKMETD