ID   RUVB2_ASPFU             Reviewed;         469 AA.
AC   Q4WKH9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=RuvB-like helicase 2;
DE            EC=3.6.4.12;
GN   Name=rvb2; ORFNames=AFUA_1G02410;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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 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}.
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DR   EMBL; AAHF01000007; EAL87953.1; -; Genomic_DNA.
DR   RefSeq; XP_749991.1; XM_744898.1.
DR   AlphaFoldDB; Q4WKH9; -.
DR   SMR; Q4WKH9; -.
DR   STRING; 746128.CADAFUBP00000275; -.
DR   PRIDE; Q4WKH9; -.
DR   EnsemblFungi; EAL87953; EAL87953; AFUA_1G02410.
DR   GeneID; 3507931; -.
DR   KEGG; afm:AFUA_1G02410; -.
DR   VEuPathDB; FungiDB:Afu1g02410; -.
DR   eggNOG; KOG2680; Eukaryota.
DR   HOGENOM; CLU_028311_4_0_1; -.
DR   InParanoid; Q4WKH9; -.
DR   OMA; YDMGAKM; -.
DR   OrthoDB; 752343at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
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..469
FT                   /note="RuvB-like helicase 2"
FT                   /id="PRO_0000165663"
FT   BINDING         76..83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  51347 MW;  7F1A9B713AEE074E CRC64;
     MAVPISTVAE TKELRGLNLI AAHSHIRGLG VDADSLQPRT SSQGLVGQEK ARKAAAVILQ
     MVKEGKIAGR AVLIAGPPST GKTAIAMGMA QSLGSDVPFT MLAASEIFSM EMSKTEALTQ
     AFRKSIGVRI KEESEIIEGE VVEIQVDRSV TGGNKQGKLT IKTTDMETIY DMGTKMIDSM
     TKERVMAGDV ISIDKSSGKI TKLGRSYARS RDYDAMGADT KFVQCPEGEL QVRKEIVHTV
     SLHEIDVINS RTQGFLALFS GDTGEIRSEV RDQINTKVAE WKEEGKAEII PGVLFIDEVH
     MLDIECFSYI NRALEAELAP IVIMASNRGQ ARIRGTTYTS PHGLPLDFLD RVVIVSTQPY
     SGDEIRQILA IRAQEEEIDL SPDALALLTK IGQESNLRYA SNIITTSHLL SQKRKAKEVS
     IDDVQRSYRL FYDPARSVKF VNAYEQRFIG DQGAVNFSAP ANGDAMEIS