RAD54_DROMO
ID RAD54_DROMO Reviewed; 783 AA.
AC B4KHL5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=GI10760;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW12294.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW12294.1};
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; CH933807; EDW12294.1; -; Genomic_DNA.
DR RefSeq; XP_002002852.1; XM_002002816.2.
DR AlphaFoldDB; B4KHL5; -.
DR SMR; B4KHL5; -.
DR STRING; 7230.FBpp0159977; -.
DR EnsemblMetazoa; FBtr0161485; FBpp0159977; FBgn0133523.
DR GeneID; 6576868; -.
DR KEGG; dmo:Dmoj_GI10760; -.
DR eggNOG; KOG0390; Eukaryota.
DR HOGENOM; CLU_000315_10_2_1; -.
DR InParanoid; B4KHL5; -.
DR OMA; YTEHERM; -.
DR OrthoDB; 93727at2759; -.
DR PhylomeDB; B4KHL5; -.
DR ChiTaRS; okr; fly.
DR Proteomes; UP000009192; 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:0000711; P:meiotic DNA repair synthesis; ISS:UniProtKB.
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..783
FT /note="DNA repair and recombination protein RAD54-like"
FT /id="PRO_0000392523"
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 737..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 291..294
FT /note="DEGH box"
FT /evidence="ECO:0000255"
FT COMPBIAS 739..766
FT /note="Basic and acidic 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 783 AA; 89247 MW; D122BA835CC26755 CRC64;
MRRSLAPSQR LGVRIKSKDA FTPPLQKKNK RVCQEELQKR QSALRDATNR VELPLPIRFT
ANSEYEQAIA KVLARKFKVP IANYVPDYGG NRTLGVRRTI VRRALHDPQA CNALVLYVPP
AYTEHERMSM DPSKVQVHVV VDPILSNVLR PHQREGVRFM YECVEGKRGN FNGCIMADEM
GLGKTLQCVT LTWTLLRQSP DCKPTISKAI IVSPSSLVKN WEKEFTKWLH GRMHCLAMEG
GSKEDTTRAL EQFAMNTATR CGTPVLLISY ETFRLYAHIL CKTEVGMVIC DEGHRLKNSD
NLTYQALMGL KTKRRVLLSG TPIQNDLTEY FSLVNFVNPE MLGTAADFKR NFENSILRGQ
NADSTDAERQ RALQKTQELI GLVNQCIIRR TNQILTKYLP VKFEMVVCVK LTPVQLQIYT
NFLKSDQVRR SLADCNEKAS LTALADITTL KKLCNHPDLI YEKIAAKEKG FENSQNVLPP
NYKPKDVNPE LSGKFMLLDF MLAAIRANSD DKVVLISNYT QTLDLFEQLA RKRKYTYVRL
DGTMTIKKRS KVVDRFNDPS TDCFLFMLSS KAGGCGLNLI GANRLFMFDP DWNPANDEQA
MARVWRDGQK KPCYIYRLVA SGSIEEKILQ RQTHKKSLSS TIIDNNESSE KHFTRDDLKD
LFSFEANVLS DTHNKLKCKR CFQDVQRQPP AENTDCTSHL SQWFHCSNNR GLPDSILSQA
WTASKCVSFV FHHRSQAESK PAAITEDDES EQQQQSPKRT SKNDDNDEDF DPENSAEEQF
LGF
