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RUVB1_NEUCR
ID   RUVB1_NEUCR             Reviewed;         458 AA.
AC   Q8WZS3; Q1K4L8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=RuvB-like helicase 1;
DE            EC=3.6.4.12;
GN   Name=hel-1; Synonyms=rvb1; ORFNames=B8L21.150, NCU03482;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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 H2A.Z 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 hel-2/rvb2. Component of the
CC       SWR1 chromatin remodeling complex, the INO80 chromatin remodeling
CC       complex, and of the R2TP complex (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; AL669989; CAD21100.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA26533.1; -; Genomic_DNA.
DR   RefSeq; XP_955769.1; XM_950676.2.
DR   AlphaFoldDB; Q8WZS3; -.
DR   SMR; Q8WZS3; -.
DR   STRING; 5141.EFNCRP00000002514; -.
DR   EnsemblFungi; EAA26533; EAA26533; NCU03482.
DR   GeneID; 3871916; -.
DR   KEGG; ncr:NCU03482; -.
DR   VEuPathDB; FungiDB:NCU03482; -.
DR   HOGENOM; CLU_028311_1_1_1; -.
DR   InParanoid; Q8WZS3; -.
DR   OMA; VIYVEAN; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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..458
FT                   /note="RuvB-like helicase 1"
FT                   /id="PRO_0000165657"
FT   BINDING         71..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   458 AA;  49811 MW;  74F74EA256BEE7BE CRC64;
     MVQISEVKGN SRDNRTAAHT HIKGLGLNSQ GIAEKQASGF VGQTTAREAC GVVVDLIKAH
     KMAGRGVLLA GGPGTGKTAL ALAISQELGT KIPFCPITGS EIYSTEVKKT EVLMENFRRA
     IGLKVRETKE VYEGEVTELT PEEAENPLGG YGKTITTLLI GLKSAKGQKK LRLDPSIYEA
     IQKERVTVGD VIYIEANTGA CKRVGRSDAY ATEFDLEAEE YVPIPKGEVH KKKEIVQDVS
     LHDLDVANAR PQGGQDIMSM MGQLMKPKMT EITDKLRSEI NKVVSKYIDQ GVAELVPGVL
     FIDEAHMLDV ECFTYLNKAL ESPISPIVVL ASNRGMTGIR GAEDLVAAHG IPPDFLSRLL
     IIPTTAYDPE EIKRIVKIRS TTEGVKITEA AIDKIAEHGV RISLRYCLQL LTPASILAKV
     NGRNEIDVQD VAECEDLFLD ARRSAALLSS EQGQEFIC
 
 
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