RAD54_DROAN
ID RAD54_DROAN Reviewed; 791 AA.
AC B3MMA5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=GF14336;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:EDV31865.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV31865.1};
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; CH902620; EDV31865.1; -; Genomic_DNA.
DR RefSeq; XP_001962644.1; XM_001962608.2.
DR AlphaFoldDB; B3MMA5; -.
DR SMR; B3MMA5; -.
DR STRING; 7217.FBpp0117528; -.
DR EnsemblMetazoa; FBtr0119036; FBpp0117528; FBgn0091363.
DR GeneID; 6497163; -.
DR KEGG; dan:6497163; -.
DR eggNOG; KOG0390; Eukaryota.
DR HOGENOM; CLU_000315_10_5_1; -.
DR InParanoid; B3MMA5; -.
DR OMA; YTEHERM; -.
DR OrthoDB; 93727at2759; -.
DR PhylomeDB; B3MMA5; -.
DR ChiTaRS; okr; fly.
DR Proteomes; UP000007801; 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..791
FT /note="DNA repair and recombination protein RAD54-like"
FT /id="PRO_0000392519"
FT DOMAIN 175..349
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 506..663
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..53
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 747..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 300..303
FT /note="DEGH box"
FT /evidence="ECO:0000255"
FT COMPBIAS 7..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188..195
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 791 AA; 89833 MW; B14A79CA1DA0D07C CRC64;
MRRSLAPSQR IGQSTASRNA FTPPLLQKKN KRACQKDLRL DTDADEDKER KRFGLRDATN
SEIPLPIRFT ANSAYELAIA QVLARKFKVP IDNYVPDYGG NRCLGVRRVV VRRPLHDPQA
CNALVLFQPP NYTEHERMSM DPSKVLVHVV VDPLLSNILR PHQREGVRFM YECVEGKKGD
FNGCIMADEM GLGKTLQCVT LVWTLLRQGP ESKPTINKAI VVSPSSLVKN WEKEFTKWLQ
GRLLCLAMEG GTKENTIRVL EQFSMTSSKL GTPVLLISYE TFRIYAEILC KYEVGMVICD
EGHRLKNSDN LTYQALMGLK TKRRVLLSGT PIQNDLTEYF SLVNFVNPEM LGTAADFKRN
FENSILRGQN ADSTEGERKK AIEKTQELIG LVDQCIIRRT NQILTKYLPI KFEMVICVKL
TAIQLQLYTN FLNSDQVRRS LADCNEKASL TALADITTLK KICSHPDLIH QKIEAKEKGF
ENSQNVLPSN YKPKEICPEW SGKFMLLDFM LAAIRAAGND KVVLISNYTQ TLDLFEQLAR
KRKYGFVRLD GTMSIKKRSK VVDKFNDPDS ECFLFMLSSK AGGCGLNLIG ANRLFMFDPD
WNPANDEQAM ARVWRDGQKK PCYIYRLVAS GTIEEKILQR QTHKKSLSST IIDNNESSEK
HFTRDDLKDL FSFDQKILSD THEKLKCKRC VQNIQTKPPS ESTDCTSHLS QWYHCSNNRG
LPDSILAQAW TDSKCVSFVF HHRSQAKEVV ESPESAAAEA ESVEEESQPT QRKRPSPPLS
DDSADEDFIG F
