RUVB1_USTMA
ID RUVB1_USTMA Reviewed; 488 AA.
AC Q4P112; A0A0D1DMR7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=RuvB-like helicase 1;
DE EC=3.6.4.12;
GN Name=RVB1; ORFNames=UMAG_06201;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 RVB2. 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; CM003161; KIS65824.1; -; Genomic_DNA.
DR RefSeq; XP_011392567.1; XM_011394265.1.
DR AlphaFoldDB; Q4P112; -.
DR SMR; Q4P112; -.
DR STRING; 5270.UM06201P0; -.
DR EnsemblFungi; KIS65824; KIS65824; UMAG_06201.
DR GeneID; 23565873; -.
DR KEGG; uma:UMAG_06201; -.
DR VEuPathDB; FungiDB:UMAG_06201; -.
DR eggNOG; KOG1942; Eukaryota.
DR HOGENOM; CLU_028311_1_1_1; -.
DR InParanoid; Q4P112; -.
DR OMA; VIYVEAN; -.
DR OrthoDB; 752343at2759; -.
DR Proteomes; UP000000561; Chromosome 22.
DR GO; GO:0070209; C:ASTRA complex; IEA:EnsemblFungi.
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 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; IPR037938; RUVBL1.
DR InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR InterPro; IPR010339; TIP49_P-loop.
DR PANTHER; PTHR11093; PTHR11093; 1.
DR PANTHER; PTHR11093:SF6; PTHR11093:SF6; 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 Transcription; Transcription regulation.
FT CHAIN 1..488
FT /note="RuvB-like helicase 1"
FT /id="PRO_0000165659"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 488 AA; 52820 MW; B449AAA1989C01B3 CRC64;
MATANTSSGS MNGVGPVTMD SSTSGASREA RIATHSHIKG LGLSDDGTAL PSAQGFVGQK
AAREACGLVL DLIRMKKFAG KALLLAGGPG TGKTALALAV SQELGHKVPF CPMVGSEVYS
SEVKKTEVLM ENFRRAIGLR VRETKEVYEG EITELTPTEA ENPLSGYGKT IAHVVIALKT
VKGTKQLRLD PSIYESIMKE RISVGDVIYI EANTGAVKRV GRSDAYATEF DLEAEEYVPL
PKGEVHKRKE VVQDVTLHDL DMANAKPQGG QDIMSVVGQL VKGRRTEVTD KLRGEINRVV
DKYIEQGIAE LVPGVLFIDE VHMLDMECFT YLNRALESTI SPHVILATNR GQCMVRGTEY
EGPASGTGIV APHGIPLDLL DRCMIVRTMP YEKDEIREVL RLRAKVEGHL IAEDALEKLT
EEGVSSSLRF ALQLLSPSSI LAKTAGRSEI TIKDIVEANE LFIDARRSAK VLMSIGEATT
EAVPMETS