RUVB1_CRYNJ
ID RUVB1_CRYNJ Reviewed; 484 AA.
AC P0CR26; Q560Z7; Q5KPZ8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=RuvB-like helicase 1;
DE EC=3.6.4.12;
GN Name=RVB1; OrderedLocusNames=CNA00990;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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 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; AE017341; AAW40710.1; -; Genomic_DNA.
DR RefSeq; XP_566529.1; XM_566529.1.
DR AlphaFoldDB; P0CR26; -.
DR SMR; P0CR26; -.
DR STRING; 5207.AAW40710; -.
DR PaxDb; P0CR26; -.
DR EnsemblFungi; AAW40710; AAW40710; CNA00990.
DR GeneID; 3253447; -.
DR KEGG; cne:CNA00990; -.
DR VEuPathDB; FungiDB:CNA00990; -.
DR eggNOG; KOG1942; Eukaryota.
DR HOGENOM; CLU_028311_1_1_1; -.
DR InParanoid; P0CR26; -.
DR OMA; VIYVEAN; -.
DR OrthoDB; 752343at2759; -.
DR Proteomes; UP000002149; Chromosome 1.
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..484
FT /note="RuvB-like helicase 1"
FT /id="PRO_0000165652"
FT REGION 1..27
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 484 AA; 52462 MW; 75A70D8ABD730A03 CRC64;
MSMAASSSTA TVQPSGIITQ PPPPSTLREQ RIATHSHIKG LGLADDGTAM SSSQGFIGQI
LAREALGLHL SLLKGGKYSG RPLLLVGPPG TGKTALALAL SQELGSKVPF CAMVGSEVYS
GEVKKTEVLG SCFRRAIGLR IKETKEVYEG EVTELTPSEA ENPLSGYGKT ISHVIVGLKT
VKGTKQLRLD PSVYESIQKE RVVVGDVIYI EANTGAVKRV GRSDAYASEY DLEAEEYVPL
PKGDVHKRKE LVQDVTLHDL DMANARPQGG QDIMSVMGQL VKGGRTEVTD KLRREINKVV
DRYIEQGVAE LVPGVLFIDE VHMLDMECFT YLNRALESPM SPYVVLASNR GISTIRGTEY
DGVAGSASEG IRAPHGLPVD LLDRCMIVKT QLYTRDEIRR IVEMRCKVEG IAISSEAVDK
LADEGERSSL RYALQLLTPA GIVSKNKGKG EVGVADVEEL GELFLDAKRS AGVLRSTEDF
EKRY
