RAD54_CHICK
ID RAD54_CHICK Reviewed; 733 AA.
AC O12944;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=DNA repair and recombination protein RAD54-like;
DE EC=3.6.4.-;
DE AltName: Full=Putative recombination factor GdRad54;
DE AltName: Full=RAD54 homolog;
DE Flags: Fragment;
GN Name=RAD54L; Synonyms=RAD54;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Bursa of Fabricius, and Testis;
RX PubMed=9108474; DOI=10.1016/s0092-8674(00)80198-1;
RA Bezzubova O.Y., Silbergleit A., Yamaguchi-Iwai Y., Takeda S.,
RA Buerstedde J.-M.;
RT "Reduced X-ray resistance and homologous recombination frequencies in a
RT RAD54-/- mutant of the chicken DT40 cell line.";
RL Cell 89:185-193(1997).
CC -!- FUNCTION: Plays an essential role in homologous recombination (HR)
CC which is a major pathway for repairing DNA double-strand breaks (DSBs),
CC single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication
CC forks. Acts as a molecular motor during the homology search and guides
CC RAD51 ssDNA along a donor dsDNA thereby changing the homology search
CC from the diffusion-based mechanism to a motor-guided mechanism. Plays
CC also an essential role in RAD51-mediated synaptic complex formation
CC which consists of three strands encased in a protein filament formed
CC once homology is recognized. Once DNA strand exchange occured,
CC dissociates RAD51 from nucleoprotein filaments formed on dsDNA.
CC {ECO:0000250|UniProtKB:P32863}.
CC -!- SUBUNIT: Homohexamer (By similarity). Interacts (via N-terminus) with
CC RAD51 (By similarity). Interacts with NAP1L1 (By similarity). Interacts
CC with BRD9; this interaction orchestrates RAD51-RAD54 complex formation
CC (By similarity). {ECO:0000250|UniProtKB:P32863,
CC ECO:0000250|UniProtKB:Q7ZV09}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in bursa, thymus, testis, and
CC ovary. Low level of expression seen in all other organs tested.
CC {ECO:0000269|PubMed:9108474}.
CC -!- PTM: Acetylated. Acetylation promotes interaction with BRD9, and
CC subsequently with RAD54, which is essential for homologous
CC recombination (HR). {ECO:0000250|UniProtKB:Q92698}.
CC -!- PTM: Phosphorylated. Phosphorylation at Ser-561 by NEK1 specifically in
CC G2 phase allows efficient removal of RAD51 filaments from DNA.
CC {ECO:0000250|UniProtKB:Q92698}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; U92461; AAB54115.1; -; mRNA.
DR RefSeq; NP_001292075.1; NM_001305146.1.
DR AlphaFoldDB; O12944; -.
DR SMR; O12944; -.
DR STRING; 9031.ENSGALP00000037559; -.
DR PaxDb; O12944; -.
DR GeneID; 424611; -.
DR KEGG; gga:424611; -.
DR CTD; 8438; -.
DR VEuPathDB; HostDB:geneid_424611; -.
DR eggNOG; KOG0390; Eukaryota.
DR InParanoid; O12944; -.
DR OrthoDB; 93727at2759; -.
DR PhylomeDB; O12944; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
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; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN <1..733
FT /note="DNA repair and recombination protein RAD54-like"
FT /id="PRO_0000074339"
FT DOMAIN 159..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 488..642
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 285..288
FT /note="DEGH box"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 504
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92698"
FT MOD_RES 561
FT /note="Phosphoserine; by NEK1"
FT /evidence="ECO:0000250|UniProtKB:Q92698"
FT NON_TER 1
SQ SEQUENCE 733 AA; 82765 MW; DB0017EF247C1C48 CRC64;
LAKRKAGGEE EDGEWRPPAT QKRQKAGSEA ESADCYRSPF RKPLTQLTNR PLCLDSSQHE
AFIRSILSKP FKVPIPNYKG PTGLRALGIK RAGLRSPLHD PFEEGALVLY EPPLLSAHEQ
LKIDKDKVPV HVVVDPVLSR VLRPHQREGV KFLWDCVTSR RIPGSHGCIM ADEMGLGKTL
QCITLMWTLL RQSPDCKPEI EKAMVVSPSS LVRNWYNEVE KWLGGRIQPL AIDGGSKEEI
DRKLVGSMNQ RGLRVPSPIL IISYETFRLH AEALQKGSVG LVICDEGHRL KNSENQTYQA
LNSLNTPRRV LISGTPIQND LLEYFSLVHF VNSGILGTAQ EFKRHFELPI LKGRDADASE
AERQKGEERL KELISIVNRC LIRRTSDILS KYLPVKIEQV VCCRLTPLQA ELYKNFLKQA
KPVEELKEGK INVSSLSSIT SLKKLCNHPA LIYDKCVEEE EGFMGALDLF PAGYSTKSVE
PQLSGKMLVL DYILAVTKST SNDKVVLVSN YTQTLDLFEK LCRNRRYLYV RLDGTMSIKK
RAKVVERFNS PSSPEFIFML SSKAGGCGLN LIGANRLVMF DPDWNPANDE QAMARVWRDG
QKKTCYIYRL LSTGTIEEKI FQRQTHKKAL SSCVVDEEQD VERHFSLGEL KELFSLNETT
ISDTHDKIKC RRCVNGHQVR PPPEGSDCTS DLSQWNHCAD KRGLQDSVLK AAWDAAVTFT
FHHHSHEEQR GIP
