ID A0A109FMW3_9BASI Unreviewed; 464 AA.
AC A0A109FMW3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
GN ORFNames=RHOSPDRAFT_28009 {ECO:0000313|EMBL:KWU47402.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU47402.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU47402.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU47402.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) 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 -!- 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. {ECO:0000256|ARBA:ARBA00025345}.
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|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU363048}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|ARBA:ARBA00007519,
CC ECO:0000256|RuleBase:RU363048}.
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DR EMBL; KQ954464; KWU47402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FMW3; -.
DR STRING; 1305733.A0A109FMW3; -.
DR OrthoDB; 5479950at2759; -.
DR Proteomes; UP000062823; 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:SF6; RUVB-LIKE 1; 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 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:UP000062823};
KW Transcription {ECO:0000256|RuleBase:RU363048};
KW Transcription regulation {ECO:0000256|RuleBase:RU363048}.
FT DOMAIN 60..372
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 464 AA; 50762 MW; E81FB784466AE1B6 CRC64;
MATGVPQSQR ESRVASHSHI KGLGLDDDGF AQDRAGFVGQ RAAREACGLV LELIKSRRFS
GRALLLAGAP GTGKTALALA IAQELGQKVP FCPMVGSEVF SSEVKKTEVL MENFRRAIGL
RVKETKEVYE GEVTELTPAE TENPLSGYGK TISHVVVALK TAKGTKQLRL DPSIYESIQK
ERVTVGDVIY IEANTGAVKR VGRSDAYATE YDLEAEEYVP LPKGDVHKKK EIVQDVTLHD
LDMANARPQG GQDIMSVMGQ LVKGRRTEVT DKLRAEINKV VNSYIDQGIA ELIPGVLFID
EVHMLDIEAF TYLNRALESP ISPHVIFATN RGLCTIRGTE NEPGSNGGEG IVSPHGVPID
LLDRCMIVRT MPYSRDEIKT VLQTRLKIEG LAIQPDALEK LSDDGVRTSL RYALQLLTPA
SILSKVQGRT EIALEDVAET DGLFLDAKSS ARMLHERGEG QYLR
//
