RAD54_DROVI
ID RAD54_DROVI Reviewed; 786 AA.
AC B4M9A8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=DNA repair and recombination protein RAD54-like {ECO:0000250|UniProtKB:O76460};
DE EC=3.6.4.-;
DE AltName: Full=Protein okra {ECO:0000250|UniProtKB:O76460};
GN Name=okr {ECO:0000250|UniProtKB:O76460}; ORFNames=GJ18280;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW57784.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW57784.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 (By similarity).
CC {ECO:0000250|UniProtKB:O76460}.
CC -!- SUBUNIT: Interacts (via N-terminus) with spn-A/Rad51. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O76460}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000255}.
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DR EMBL; CH940654; EDW57784.1; -; Genomic_DNA.
DR RefSeq; XP_002057711.1; XM_002057675.2.
DR AlphaFoldDB; B4M9A8; -.
DR SMR; B4M9A8; -.
DR STRING; 7244.FBpp0232697; -.
DR EnsemblMetazoa; FBtr0234205; FBpp0232697; FBgn0205441.
DR GeneID; 6634100; -.
DR KEGG; dvi:6634100; -.
DR eggNOG; KOG0390; Eukaryota.
DR HOGENOM; CLU_000315_10_5_1; -.
DR InParanoid; B4M9A8; -.
DR OMA; YTEHERM; -.
DR OrthoDB; 93727at2759; -.
DR PhylomeDB; B4M9A8; -.
DR ChiTaRS; okr; fly.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0043150; P:DNA synthesis involved in double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IEA:EnsemblMetazoa.
DR GO; GO:0000711; P:meiotic DNA repair synthesis; ISS:UniProtKB.
DR GO; GO:0030716; P:oocyte fate determination; IEA:EnsemblMetazoa.
DR GO; GO:0048477; P:oogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IEA:EnsemblMetazoa.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013967; Rad54_N.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08658; Rad54_N; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Meiosis; Mitosis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..786
FT /note="DNA repair and recombination protein RAD54-like"
FT /id="PRO_0000392526"
FT DOMAIN 165..340
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 497..654
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 2..9
FT /note="Required for chromatin remodeling, strand pairing
FT activities and coupling of ATPase activity"
FT /evidence="ECO:0000250|UniProtKB:O76460"
FT REGION 740..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 291..294
FT /note="DEGH box"
FT /evidence="ECO:0000255"
FT COMPBIAS 740..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76460"
SQ SEQUENCE 786 AA; 89474 MW; EBBAA63BE70C66AE CRC64;
MRRSLAPSQR LGVRIKSKDA FTPPLQKKNK RVCQIELQKR QSALRDATNT VELPLPIRFT
ANSDYEQAIA KVLARKFKVP IANYVPDYGG NRTLGVRRSI VRRALHDPQA CNALVLYTPP
AYTEHERMSL DPSKLQVHVV VDPILSNVLR PHQREGVRFM YECVEGKRGN FNGCIMADEM
GLGKTLQCVT LTWTLLRQSP DCKPTISKAI VVSPSSLVKN WEKEFTKWLH GRMHCLAMEG
GSKEDTTRTL EQFAMNTATR CGTPVLLISY ETFRLYSHIL CKTEVGMVIC DEGHRLKNSD
NLTYQALMGL KTKRRVLLSG TPIQNDLTEY FSLVNFVNPE MLGTGSDFKR NFENAILRGQ
NADSTDAERE RALEKTQELV GLVNQCIIRR TNQILTKYLP VKFEMVVCAK LTAVQLQLYT
NFLKSDQVRR SLADCTDKTT LTALADITTL KKLCNHPDLI YEKIAAREKG FENSQNVLPP
NYKPKDVNPE LSGKFMLLDF MLAAIRANSD DKVVLISNYT QTLDLFEQLA RKRKYSYVRL
DGTMTIKKRS KVVDRFNDPA TDCFLFMLSS KAGGCGLNLI GANRLFMFDP DWNPANDEQA
MARVWRDGQK KPCYIYRLVA SGSIEEKILQ RQTHKKSLSS SIIDNNDSAE KHFTRDDLKD
LFRFEANVLS DTHNKLKCKR CFQDVQRQPP PENSDCTSHL SQWFHCSNNR GLPDSILSQA
WMASKCVSFV FHHRSQGDAK QPTCITEDNH SEQPQLNSKR NANSVLENDD DEDFDPNSSD
EKFLGF
