RUVB2_DICDI
ID RUVB2_DICDI Reviewed; 469 AA.
AC Q54UW5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=RuvB-like helicase 2;
DE EC=3.6.4.12;
GN Name=rvb2; ORFNames=DDB_G0280775;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 26-49; 68-93; 161-173; 389-396 AND 425-434, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
CC -!- FUNCTION: Has double-stranded DNA-stimulated ATPase and ATP-dependent
CC DNA helicase (5' to 3') activity suggesting a role in nuclear processes
CC such as recombination and transcription. {ECO:0000250}.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling Ino80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. {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: Forms homohexameric rings. May form a dodecamer with rvb1 made
CC of two stacked hexameric rings. Component of the chromatin remodeling
CC Ino80 complex. Component of the RNA polymerase II holoenzyme complex
CC (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; AAFI02000038; EAL67045.1; -; Genomic_DNA.
DR RefSeq; XP_641022.1; XM_635930.1.
DR AlphaFoldDB; Q54UW5; -.
DR SMR; Q54UW5; -.
DR STRING; 44689.DDB0233014; -.
DR PaxDb; Q54UW5; -.
DR EnsemblProtists; EAL67045; EAL67045; DDB_G0280775.
DR GeneID; 8622724; -.
DR KEGG; ddi:DDB_G0280775; -.
DR dictyBase; DDB_G0280775; rvb2.
DR eggNOG; KOG2680; Eukaryota.
DR HOGENOM; CLU_028311_4_0_1; -.
DR InParanoid; Q54UW5; -.
DR OMA; YDMGAKM; -.
DR PhylomeDB; Q54UW5; -.
DR PRO; PR:Q54UW5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0031011; C:Ino80 complex; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
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; ISS:dictyBase.
DR Gene3D; 2.40.50.360; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; DNA damage; DNA recombination;
KW DNA repair; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..469
FT /note="RuvB-like helicase 2"
FT /id="PRO_0000327829"
FT BINDING 73..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 51971 MW; 8A14929657FD896A CRC64;
MSIPKISQVK DLTRIERIGA HSHIRGLGID DSLEPREISQ GMVGQVGARK AAGLILQMIK
EGKIAGRAIL IGGEPGTGKT AIAMGMAQSL GEKTPFTAIA ASEIFSLEMS KTEALTQAFR
RSIGVRIKEE TEVICGEVVD IQIDRPATGS GAKVGKLTLK TTSMDALYDL GAKMIDSLTK
EKVQNGDIIR IDKGTGKITK LGRSLSRVRD HEISGSKVNF IECPEGEIQQ RRTETHTVSL
HEIDVINSRA QGFFALFAGD IGEIKSEVRE QINQKVAEWK EEGKAEIVPG VLFIDEVHML
DIECFSYLNR ALEDDMSPIL IIATNRGNTT IRGTDYKAPH GIPLDLLDRL LIINTQPYTE
KDIYKILKIR CEEEDVDIQE DALQLLTKIG VETSLRYAIH LITSSSLVSV KRKGTDVSVD
DIKKVYDLFV DVKRSTKYLK DYQDEYLYNS QPETTATKTN EEQQTMQTA
