ID A0A229XIA3_9EURO Unreviewed; 469 AA.
AC A0A229XIA3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 08-NOV-2023, entry version 25.
DE RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
GN Name=RVB2 {ECO:0000313|EMBL:RLL99153.1};
GN ORFNames=CDV55_102096 {ECO:0000313|EMBL:RHZ72332.1}, CFD26_103786
GN {ECO:0000313|EMBL:RLL99153.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL99153.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL99153.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ72332.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA helicase participates in several chromatin remodeling
CC complexes, including the SWR1 and the INO80 complexes.
CC {ECO:0000256|RuleBase:RU363048}.
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 Evidence={ECO:0000256|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU363048};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU363048}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|ARBA:ARBA00007519,
CC ECO:0000256|RuleBase:RU363048}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLL99153.1}.
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DR EMBL; NKHV02000014; RHZ72332.1; -; Genomic_DNA.
DR EMBL; NIDN02000037; RLL99153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229XIA3; -.
DR STRING; 1245748.A0A229XIA3; -.
DR OrthoDB; 5479950at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.50.360; RuvB-like helicase, domain II; 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; IPR010339; TIP49_P-loop.
DR PANTHER; PTHR11093:SF2; RUVB-LIKE 2; 1.
DR PANTHER; PTHR11093; RUVB-RELATED REPTIN AND PONTIN; 1.
DR Pfam; PF06068; TIP49; 1.
DR Pfam; PF17856; TIP49_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363048};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU363048};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU363048};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU363048};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363048};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363048};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363048};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU363048};
KW Reference proteome {ECO:0000313|Proteomes:UP000215289};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU363048};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU363048}.
FT DOMAIN 68..359
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 469 AA; 51379 MW; 2E4D0DC2786B3422 CRC64;
MAVPISTVAE TKELRGLNLI AAHSHIRGLG VDADSLQPRT SSQGLVGQEK ARKAAAVILQ
MVKEGKIAGR AVLIAGPPST GKTAIAMGMA QSLGSDVPFT MLAASEIFSM EMSKTEALTQ
AFRKSIGVRI KEESEIIEGE VVEIQIDRSV TGGNKQGKLT IKTTDMETIY DMGTKMIDSM
TKERVMAGDV ISIDKSSGKI TKLGRSYARS RDYDAMGADT KFVQCPEGEL QVRKEIVHTV
SLHEIDVINS RTQGFLALFS GDTGEIRSEV RDQINTKVAE WKEEGKAEII PGVLFIDEVH
MLDIECFSYI NRALEAELAP IVIMASNRGQ ARIRGTTYTS PHGLPLDFLD RVVIVSTQPY
SADEIRQILA IRAQEEEIDL SPDALALLTK IGQESNLRYA SNIITTSHLL SQKRKAKEVS
IDDVQRSYRL FYDPARSVKF VNTYEQRFIG DQGAVNFSAA ANGDAMEIS
//
