ID Q9U2S8_CAEEL Unreviewed; 833 AA.
AC Q9U2S8;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 2.
DT 27-MAR-2024, entry version 163.
DE RecName: Full=DNA repair and recombination protein RAD54-like {ECO:0000256|ARBA:ARBA00015341};
DE AltName: Full=Protein okra {ECO:0000256|ARBA:ARBA00029956};
GN Name=rad-54.b {ECO:0000313|WormBase:Y116A8C.13a};
GN Synonyms=rad-54.B {ECO:0000313|EMBL:CAB55149.2};
GN ORFNames=CELE_Y116A8C.13 {ECO:0000313|EMBL:CAB55149.2}, Y116A8C.13
GN {ECO:0000313|WormBase:Y116A8C.13a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB55149.2, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAB55149.2, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB55149.2,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Involved in mitotic DNA repair and meiotic recombination.
CC Functions in the recombinational DNA repair pathway. Essential for
CC interhomolog gene conversion (GC), but may have a less important role
CC in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51
CC enhances the ATPase activity of okr/Rad54.
CC {ECO:0000256|ARBA:ARBA00024776}.
CC -!- SUBUNIT: Interacts (via N-terminus) with spn-A/Rad51.
CC {ECO:0000256|ARBA:ARBA00011467}.
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DR EMBL; BX284604; CAB55149.2; -; Genomic_DNA.
DR PIR; T31515; T31515.
DR RefSeq; NP_001255913.1; NM_001268984.1.
DR AlphaFoldDB; Q9U2S8; -.
DR SMR; Q9U2S8; -.
DR STRING; 6239.Y116A8C.13a.1; -.
DR EPD; Q9U2S8; -.
DR PaxDb; 6239-Y116A8C-13a; -.
DR PeptideAtlas; Q9U2S8; -.
DR EnsemblMetazoa; Y116A8C.13a.1; Y116A8C.13a.1; WBGene00013792.
DR GeneID; 190999; -.
DR KEGG; cel:CELE_Y116A8C.13; -.
DR UCSC; Y116A8C.13; c. elegans.
DR AGR; WB:WBGene00013792; -.
DR WormBase; Y116A8C.13a; CE35647; WBGene00013792; rad-54.B.
DR eggNOG; KOG0390; Eukaryota.
DR GeneTree; ENSGT00940000156966; -.
DR InParanoid; Q9U2S8; -.
DR OMA; KCQTHEL; -.
DR OrthoDB; 5480555at2759; -.
DR PhylomeDB; Q9U2S8; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00013792; Expressed in adult organism and 4 other cell types or tissues.
DR ExpressionAtlas; Q9U2S8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR CDD; cd18004; DEXHc_RAD54; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022776};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|EPD:Q9U2S8,
KW ECO:0007829|PeptideAtlas:Q9U2S8};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 225..392
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 527..676
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 98..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..766
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 93237 MW; 2D281B186BD551D9 CRC64;
MSRVVLNVDS YEGNDTPSAE IARFVVLYGK ASTRKHKIWE GDGLLVCFTD SCLLKSEDER
DVICRSSALK GLDQLEDGRI INIGSWSVEI QERIATGPPQ KPISAQKPEI QSPMPPMTPG
NSENVENRKR GGFSSPFLGI ELPKPLSKRS ATFVPPLIGS ESSSSGGSSS STIQEKIPPF
ILNEQDILDR KTTSAVTVDT RFARHLRPHQ KSGIQFIFDR LRRGSGKNGG GGGAILADDM
GLGKSLQTMA ATWALLKGSK TAQQLANSCL IIVPSSLVNN WKAEFDKWWR LMRFPAVIAL
TANDITTYQS TIKLMPYLVI SYDLAQRHVE KLKIIRFDVM VCDEGHKLKN LDGKLRKTLL
SLEIPRRLIL TGTPMQNDFE EFYSLLDFVR PSVFGSIVEF RKMCSDRPEQ LNELIDECML
RRTAADVDLK HLPEKHEYIL FCAASPIQKH VHSEICDYMT GDALSLIFFA RQLANHPKLL
LDNLREKTEK SKAHKHSPLL LAFDGAHMPR GGVKESGKLT ALVDMIKCFR LLQECTVIVS
NYIETLDMIQ QLCEYLNFKV LRLDGKTQVP DRQKLVRTFN DHRDPSNIFL LSTKAGGVGL
NLIGASRLVL FDSDWNPAND QQAMARIWRD GQVRPCHIYR LITTGTIEEK MLQRQIKKTG
LGCVIDAIEV GDTIATFTDE DLKDIFTFTG SATECNTHDL CECPCDGCGM LENEMDEEDD
GDDVVENDAE KIDKSGKIDK IDSDDDEEAD DEELEADVTD EVVEDSQEPP EATKPAVAAA
GLRTIASLAE LSRWRHFSPR HADTWHHFMT NAGLSQVDTD VELTFAFYQE SQY
//
