ID   RUVB2_EMENI             Reviewed;         468 AA.
AC   Q5BGK3; C8VU13;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=RuvB-like helicase 2;
DE            EC=3.6.4.12;
GN   Name=rvb2; ORFNames=AN0327;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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 RVB1. 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   -!- SEQUENCE CAUTION:
CC       Sequence=EAA65733.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000006; EAA65733.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001308; CBF89714.1; -; Genomic_DNA.
DR   RefSeq; XP_657931.1; XM_652839.1.
DR   AlphaFoldDB; Q5BGK3; -.
DR   SMR; Q5BGK3; -.
DR   STRING; 162425.CADANIAP00002382; -.
DR   EnsemblFungi; CBF89714; CBF89714; ANIA_00327.
DR   EnsemblFungi; EAA65733; EAA65733; AN0327.2.
DR   GeneID; 2876107; -.
DR   KEGG; ani:AN0327.2; -.
DR   VEuPathDB; FungiDB:AN0327; -.
DR   eggNOG; KOG2680; Eukaryota.
DR   HOGENOM; CLU_028311_4_0_1; -.
DR   InParanoid; Q5BGK3; -.
DR   OMA; YDMGAKM; -.
DR   OrthoDB; 752343at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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: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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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; 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; 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   rRNA processing; Transcription; Transcription regulation.
FT   CHAIN           1..468
FT                   /note="RuvB-like helicase 2"
FT                   /id="PRO_0000165668"
FT   BINDING         76..83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  51460 MW;  4DCBFA3BEAD12EBE CRC64;
     MAAPISTVAE SKELRGLNLI AAHSHIRGLG VDVDSLQPRP ASQGLVGQEK ARKAAAVILQ
     MVKEGKIAGR AVLIAGPPST GKTAIAMGMA QSLGPDVPFT MLAASEIFSM EMSKTEALTQ
     AFRKSIGVRI KEESEIIEGE VVEIQIDRSV TGGNKQGKLT IKTTDMETIY DMGTKMIDSM
     TKERVMAGDI ISIDKSSGKI TKLGRSYARS RDYDAMGADV KFVQCPEGEL QVRKEIVHTV
     SLHEIDVINS RSQGFLALFS GDTGEIRSEV RDQINVKVAE WKEEGKAEII PGVLFIDEVH
     MLDIECYSYI NRALEAELAP IVIMASNRGH SRIRGTTYNS PHGLPLDFLD RVVIVSTQHY
     SADEIRQILA IRAQEEEIDL SPDALALLTK IGQESNLRYA SNIITTSHLL SQKRKAKEVS
     VDDVQRSYRL FYDPARSVKF VNQYEQRFIG DQGNVNFTAS NGDAMEIS