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RAD54_DROYA
ID   RAD54_DROYA             Reviewed;         784 AA.
AC   B4NXB8; B6UXG4;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
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=GE14966;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1] {ECO:0000312|EMBL:EDW87475.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW87475.1};
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).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:ACI97197.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 475-642.
RX   PubMed=18984573; DOI=10.1534/genetics.108.093807;
RA   Anderson J.A., Gilliland W.D., Langley C.H.;
RT   "Molecular population genetics and evolution of Drosophila meiosis genes.";
RL   Genetics 181:177-185(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDW87475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CM000157; EDW87475.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; FJ219212; ACI97197.1; -; Genomic_DNA.
DR   RefSeq; XP_002087763.2; XM_002087727.2.
DR   AlphaFoldDB; B4NXB8; -.
DR   SMR; B4NXB8; -.
DR   STRING; 7245.FBpp0259976; -.
DR   EnsemblMetazoa; FBtr0261484; FBpp0259976; FBgn0232556.
DR   GeneID; 6526655; -.
DR   KEGG; dya:Dyak_GE14966; -.
DR   eggNOG; KOG0390; Eukaryota.
DR   OrthoDB; 93727at2759; -.
DR   ChiTaRS; okr; fly.
DR   Proteomes; UP000002282; Chromosome 2L.
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.
FT   CHAIN           1..784
FT                   /note="DNA repair and recombination protein RAD54-like"
FT                   /id="PRO_0000392528"
FT   DOMAIN          172..346
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          503..660
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..54
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          751..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           297..300
FT                   /note="DEGH box"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        31..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..774
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         185..192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O76460"
FT   MOD_RES         22
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O76460"
SQ   SEQUENCE   784 AA;  89447 MW;  3D94D2010C1D2703 CRC64;
     MRRSLAPSQR GPMRPESRHS FTPPLLKKNK RSCQQELERE QELDRKRQSA LRDASNTMDL
     PLPIRFTANS EYERAIAKVL ARKFKVPMDN YVPDYGGKRV LGVRRCISRR PLHDPVACNA
     LVLFNPPAYT EHERMGMDPT KVLVHVVVDP LLSNILRPHQ REGVRFMYEC VEGKRGNFNG
     CIMADEMGLG KTLQCVTLVW TLLRQGPECK PTINKAIVVS PSSLVKNWEK EFTKWLQGRL
     LCLPMEGGTK ENTIRALEQF SMTSSRLGTP VLLISYETFR IYAEILCKYE VGMVICDEGH
     RLKNSDNLTY QALMGLKTKR RVLLSGTPIQ NDLTEYYSLV NFVNPEMLGT AAVFKRNFES
     AILRGQNTDS TEGERQRAIE KTQELIGLVD QCIIRRTNQI LTKYLPVKFE MVICAKLTSI
     QLELYTNFLK SDQVRRSLAD CNEKASLTAL ADITTLKKIC SHPDLIYEKI TAREKGFENS
     QNVLPSNYNT KDLNPELSGK FMLLDFMLAA IRADGNDKVV LISNYTQTLD LFEQLARKRK
     YGFVRLDGTM SIKKRSKVVD RFNDPESDSF LFMLSSKAGG CGLNLIGANR LFMFDPDWNP
     ANDEQAMARV WRDGQKKPCY IYRMVASGSI EEKILQRQTH KKSLSSTIID NNESAEKHFT
     RDDLKDLFTF DADILSDTHE KLKCKRCVQN VQVKPPPDNT DCTSHLSQWY HCSNNRGLPD
     NILAQAWTDC KCVSFVFHHR SQAQEIVAIA EEAASEQPEE KPDRRKRPST PPSDDSADED
     FLGF
 
 
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