RA51B_XENLA
ID RA51B_XENLA Reviewed; 336 AA.
AC Q91917; Q5D0A9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA repair protein RAD51 homolog B;
DE Short=xRAD51.2;
GN Name=rad51-b; Synonyms=rad51-2, rad51.2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=7642095; DOI=10.1016/0378-1119(95)00148-y;
RA Maeshima K., Morimatsu K., Shinohara A., Horii T.;
RT "RAD51 homologues in Xenopus laevis: two distinct genes are highly
RT expressed in ovary and testis.";
RL Gene 160:195-200(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR EMBL; D38488; BAA07500.1; -; mRNA.
DR EMBL; BC046650; AAH46650.1; -; mRNA.
DR EMBL; BC108486; AAI08487.1; -; mRNA.
DR RefSeq; NP_001080559.1; NM_001087090.1.
DR RefSeq; XP_018084142.1; XM_018228653.1.
DR RefSeq; XP_018084143.1; XM_018228654.1.
DR AlphaFoldDB; Q91917; -.
DR SMR; Q91917; -.
DR BioGRID; 98493; 1.
DR DNASU; 380251; -.
DR GeneID; 380251; -.
DR KEGG; xla:380251; -.
DR CTD; 380251; -.
DR Xenbase; XB-GENE-6256559; rad51.L.
DR OMA; TFRIYLR; -.
DR OrthoDB; 877394at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 380251; Expressed in ovary and 16 other tissues.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
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:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0000730; P:DNA recombinase assembly; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
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..336
FT /note="DNA repair protein RAD51 homolog B"
FT /id="PRO_0000122937"
FT DOMAIN 45..74
FT /note="HhH"
FT MOTIF 242..257
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 336 AA; 36621 MW; CC81A1D2DA6A07BD CRC64;
MAMQAHYQAE ATEEENFGPQ AITRLEQCGI NANDVKKLED AGFHTVEAVA YAPKKELLNI
KGISEAKAEK ILAEAAKLVP MGFTTATEFH QRRSEIIQIG TGSKELDKLL QGGIETGSIT
EMFGEFRTGK TQLCHTLAVT CQLPIDRGGG EGKAMYIDTE GTFRPERLLA VAERYGLSGS
DVLDNVAYAR AFNTDHQTQL LYQASAMMAE SRYALLIVDS ATALYRTDYS GRGELSARQM
HLARFLRMLL RLADEFGVAV VITNQVVAQV DGAAMFAADP KKPIGGNIIA HASTTRLYLR
KGRGETRICK IYDSPCLPEA EAMFAINADG VGDAKD
