RAD51_CHICK
ID RAD51_CHICK Reviewed; 339 AA.
AC P37383;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=DNA repair protein RAD51 homolog 1;
GN Name=RAD51A; Synonyms=RAD51;
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.
RX PubMed=8479908; DOI=10.1093/nar/21.7.1577;
RA Bezzubova O.Y., Shinohara A., Mueller R.G., Ogawa H., Buerstedde J.-M.;
RT "A chicken RAD51 homologue is expressed at high levels in lymphoid and
RT reproductive organs.";
RL Nucleic Acids Res. 21:1577-1580(1993).
CC -!- FUNCTION: Plays an important role in homologous strand exchange, a key
CC step in DNA repair through homologous recombination (HR). Binds to
CC single-stranded DNA in an ATP-dependent manner to form nucleoprotein
CC filaments which are essential for the homology search and strand
CC exchange. Catalyzes the recognition of homology and strand exchange
CC between homologous DNA partners to form a joint molecule between a
CC processed DNA break and the repair template. Recruited to resolve
CC stalled replication forks during replication stress. Also involved in
CC interstrand cross-link repair. {ECO:0000250|UniProtKB:Q06609}.
CC -!- SUBUNIT: Forms linear homooligomers, giving rise to a RAD51
CC nucleoprotein filament, which is essential for strand-pairing reactions
CC during DNA recombination. {ECO:0000250|UniProtKB:Q06609}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q06609}. Chromosome
CC {ECO:0000250|UniProtKB:Q06609}. Note=Accumulated at sites of DNA
CC damage. Recruited to stalled replication forks during replication
CC stress. {ECO:0000250|UniProtKB:Q06609}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in lymphoid and
CC reproductive organs. {ECO:0000269|PubMed:8479908}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR EMBL; L09655; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S59426; AAB26354.1; -; mRNA.
DR PIR; S35642; S35642.
DR RefSeq; NP_990504.1; NM_205173.1.
DR RefSeq; XP_015141632.1; XM_015286146.1.
DR RefSeq; XP_015141633.1; XM_015286147.1.
DR AlphaFoldDB; P37383; -.
DR SMR; P37383; -.
DR BioGRID; 676352; 3.
DR STRING; 9031.ENSGALP00000032107; -.
DR PaxDb; P37383; -.
DR Ensembl; ENSGALT00000070280; ENSGALP00000046453; ENSGALG00000030313.
DR GeneID; 396086; -.
DR KEGG; gga:396086; -.
DR CTD; 5888; -.
DR VEuPathDB; HostDB:geneid_396086; -.
DR eggNOG; KOG1433; Eukaryota.
DR GeneTree; ENSGT00940000156157; -.
DR HOGENOM; CLU_041732_0_2_1; -.
DR InParanoid; P37383; -.
DR OMA; TFRIYLR; -.
DR OrthoDB; 877394at2759; -.
DR PhylomeDB; P37383; -.
DR TreeFam; TF101218; -.
DR Reactome; R-GGA-265976; Homologous DNA pairing and strand exchange.
DR Reactome; R-GGA-351433; ATM mediated phosphorylation of repair proteins.
DR Reactome; R-GGA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-GGA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-GGA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-GGA-5693579; Homologous DNA Pairing and Strand Exchange.
DR PRO; PR:P37383; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000030313; Expressed in testis and 13 other tissues.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000800; C:lateral element; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0070182; F:DNA polymerase binding; IEA:Ensembl.
DR GO; GO:0000150; F:DNA strand exchange activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0072757; P:cellular response to camptothecin; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; IEA:Ensembl.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0000730; P:DNA recombinase assembly; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:BHF-UCL.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:Ensembl.
DR GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
DR GO; GO:0051106; P:positive regulation of DNA ligation; IEA:Ensembl.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IEA:Ensembl.
DR GO; GO:0042148; P:strand invasion; IBA:GO_Central.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:Ensembl.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IEA:Ensembl.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011941; DNA_recomb/repair_Rad51.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02239; recomb_RAD51; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chromosome; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..339
FT /note="DNA repair protein RAD51 homolog 1"
FT /id="PRO_0000122935"
FT DOMAIN 48..77
FT /note="HhH"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 339 AA; 36904 MW; 549C59DBD3529DA4 CRC64;
MAMQVQFEAS TDTSAEEESF GPEPISRLEQ CGINANDVKK LEEAGYHTVE SVAHAPKKEL
LNIKGISEAK ADKILAEAAK LVPMGFTTAT EFHQRRSEII QITTGSKELD KLLQGGIETG
SITELFGEFR TGKTQLCHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL
SGSDVLDNVA YARGFNTDHQ TQLLYQASAM MAESRYALLI VDSATALYRT DYSGRGELSA
RQMHLARFLR MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL
YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKE
