RAD54_DROPE
ID RAD54_DROPE Reviewed; 782 AA.
AC B4GS98;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=GL26701;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1] {ECO:0000312|EMBL:EDW25645.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479189; EDW25645.1; -; Genomic_DNA.
DR RefSeq; XP_002021802.1; XM_002021766.1.
DR AlphaFoldDB; B4GS98; -.
DR SMR; B4GS98; -.
DR STRING; 7234.FBpp0190808; -.
DR EnsemblMetazoa; FBtr0192316; FBpp0190808; FBgn0164282.
DR GeneID; 6596280; -.
DR KEGG; dpe:6596280; -.
DR eggNOG; KOG0390; Eukaryota.
DR HOGENOM; CLU_000315_10_5_1; -.
DR OMA; YTEHERM; -.
DR PhylomeDB; B4GS98; -.
DR ChiTaRS; okr; fly.
DR Proteomes; UP000008744; 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..782
FT /note="DNA repair and recombination protein RAD54-like"
FT /id="PRO_0000392524"
FT DOMAIN 168..343
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 501..658
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 741..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 294..297
FT /note="DEGH box"
FT /evidence="ECO:0000255"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..188
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 782 AA; 89103 MW; 624DA2738D2CFDE7 CRC64;
MRRSLAPSQR GGQRLSSRND FTPPLLKKNK RACQQDLEQE RLRQSALRDA TNTSDLPLPI
RFTANTEYEM AIAKVLARKF KVPIDNYVPD YGGNRTLGVR RRIVRRPLHD PLACNALVLY
HAPNYTDHER MSMEPSSVLV HVVVDPLLSN ILRPHQREGV RFMYECVEGK RGNFNGCIMA
DEMGLGKTLQ CVALVWTLLK QSAECKPTIN KCIIVSPSSL VKNWEKEFTK WLHGRMHCLA
MEGGSKENTV RALEQFSMNA STRLGTPVLL ISYETFRIYA EILCKYEVGM VICDEGHRLK
NSDNLTYQAL MGLKTKRRVL LSGTPIQNDL TEYFSLVNFV NPEMLGTAAD FKRNFENCIL
RGQNADSTDK ERDRALEKTQ ELIKLVDQCI IRRTNQILTK YLPVKFEMVI CAKLTPIQLQ
LYTNFLKSDQ VRRSLADCKE KASLTALADI TTLKKLCSHP NLICEKIAAG EKGFENSQNI
LPINYNPKGE INPELSGKFK LLDFMLAAIR AHGNDKVVLI SNYTQTLDLF ELLARKRKYG
FVRLDGTMSI KKRSKVVDRF NDPESDCFLF MLSSKAGGCG LNLIGANRLF MFDPDWNPAN
DEQAMARVWR DGQKKPCYIY RLVASGSIEE KILQRQTHKK SLSSTIIDNN ESAEKHFTRD
DLKDLFSFDP DILSDTHDKL KCKRCVQNVQ MMPPPDDTDC TSHLSQWYHC SNNRGLPDNI
LAQAWTDSKC VSFVFHHRSQ SQKIEATPAT ETSVEAKLEP ERRKRPAMPL SDDSADEDFQ
GF
