(data stored in ACNUC7421 zone)

SWISSPROT: RUVB1_ASHGO

ID   RUVB1_ASHGO             Reviewed;         459 AA.
AC   Q750R1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 104.
DE   RecName: Full=RuvB-like helicase 1;
DE            EC=3.6.4.12;
GN   Name=RVB1; OrderedLocusNames=AGL119C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(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 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}.
DR   EMBL; AE016820; AAS54372.1; -; Genomic_DNA.
DR   RefSeq; NP_986548.1; NM_211610.1.
DR   SMR; Q750R1; -.
DR   STRING; 33169.AAS54372; -.
DR   PRIDE; Q750R1; -.
DR   EnsemblFungi; AAS54372; AAS54372; AGOS_AGL119C.
DR   GeneID; 4622847; -.
DR   KEGG; ago:AGOS_AGL119C; -.
DR   HOGENOM; HOG000190885; -.
DR   InParanoid; Q750R1; -.
DR   KO; K04499; -.
DR   OMA; GNCLIRG; -.
DR   Proteomes; UP000000591; Chromosome VII.
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: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:0060303; P:regulation of nucleosome density; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; 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;
DR   PRODOM; Q750R1.
DR   SWISS-2DPAGE; Q750R1.
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..459
FT                   /note="RuvB-like helicase 1"
FT                   /id="PRO_0000165648"
FT   NP_BIND         75..82
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  49992 MW;  1800A8EB19B70CB8 CRC64;
     MVQISEVKDQ VPGSSAGART AAHTHIKGLG LDEFGAAKQV EGGFVGQVEA REACGVIVDL
     IKAKRMSGRA ILLAGGPSTG KTALALAITQ ELGPKVPFCP LVGSELFSVE VKKTETLMEN
     FRRAIGLRIK EVKEVYEGEV TELTPEEAEN PLGGYGKTIS HVIVGLKSAK GTKTLRLDPT
     IYESIQREKV SVGDVIYIES NSGAVKRVGR SDAYATEFDL EAEEYVPLPK GEVHKKKEII
     QDVTLHDLDV ANARPQGGQD VISMMGQLMK PKKTEITEKL RHEVNKVVAK YIDQGVAELV
     PGVLFIDEVN MLDIEIFTFL NRALELEIAP VVVLASNRGM TTVRGTEDVV SAHGIPPDLI
     DRLLIVRTLP YTQDEIRVII EKRSKVENLQ LEQAALDLLA AMGSDMSLRY ALQLLTPAGI
     LAATAGRTEI LLSDIEEAKM LFLDAKRSTK ILESNSNYL
//

If you have problems or comments...

PBIL Back to PBIL home page