R51A2_MAIZE
ID R51A2_MAIZE Reviewed; 340 AA.
AC Q9XED7;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=DNA repair protein RAD51 homolog B;
DE AltName: Full=Rad51-like protein B;
DE Short=RAD51B;
DE AltName: Full=ZmRAD51b;
GN Name=RAD51B;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. A632;
RX PubMed=10330467; DOI=10.2307/3870816;
RA Franklin A.E., McElver J., Sunjevaric I., Rothstein R., Bowen B.,
RA Cande W.Z.;
RT "Three-dimensional microscopy of the Rad51 recombination protein during
RT meiotic prophase.";
RL Plant Cell 11:809-824(1999).
RN [2]
RP FUNCTION.
RX PubMed=12897254; DOI=10.1105/tpc.012898;
RA Pawlowski W.P., Golubovskaya I.N., Cande W.Z.;
RT "Altered nuclear distribution of recombination protein RAD51 in maize
RT mutants suggests the involvement of RAD51 in meiotic homology
RT recognition.";
RL Plant Cell 15:1807-1816(2003).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=12811575; DOI=10.1007/s00412-003-0242-8;
RA Franklin A.E., Golubovskaya I.N., Bass H.W., Cande W.Z.;
RT "Improper chromosome synapsis is associated with elongated RAD51 structures
RT in the maize desynaptic2 mutant.";
RL Chromosoma 112:17-25(2003).
CC -!- FUNCTION: Binds to single and double-stranded DNA and exhibits DNA-
CC dependent ATPase activity. Unwinds duplex DNA (By similarity).
CC Component of the meiotic recombination pathway. Seems to play a role in
CC mediating chromosome homology search, chromosome pairing and synapsis
CC at early stages and probably chromosome crossing-over at later stages
CC in meiosis. Probably is involved in the repair of meiotic double strand
CC breaks (DBSs) and in homologous recombination. {ECO:0000250,
CC ECO:0000269|PubMed:10330467, ECO:0000269|PubMed:12897254}.
CC -!- SUBUNIT: Self-associates and may interact with XRCC3 homolog.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12811575}.
CC -!- TISSUE SPECIFICITY: Highly expressed in mitotic and meiotic tissues,
CC but low levels in differentiated tissues.
CC {ECO:0000269|PubMed:10330467}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF079429; AAD32030.1; -; mRNA.
DR RefSeq; NP_001104919.1; NM_001111449.2.
DR AlphaFoldDB; Q9XED7; -.
DR SMR; Q9XED7; -.
DR STRING; 4577.GRMZM2G084762_P01; -.
DR PaxDb; Q9XED7; -.
DR PRIDE; Q9XED7; -.
DR EnsemblPlants; Zm00001eb138190_T001; Zm00001eb138190_P001; Zm00001eb138190.
DR GeneID; 541710; -.
DR Gramene; Zm00001eb138190_T001; Zm00001eb138190_P001; Zm00001eb138190.
DR KEGG; zma:541710; -.
DR MaizeGDB; 112974; -.
DR eggNOG; KOG1433; Eukaryota.
DR HOGENOM; CLU_041732_0_2_1; -.
DR OMA; TFRIYLR; -.
DR OrthoDB; 877394at2759; -.
DR Proteomes; UP000007305; Chromosome 3.
DR ExpressionAtlas; Q9XED7; baseline and differential.
DR Genevisible; Q9XED7; ZM.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
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:0000150; F:DNA strand exchange activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central.
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:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0042148; P:strand invasion; IBA:GO_Central.
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; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..340
FT /note="DNA repair protein RAD51 homolog B"
FT /id="PRO_0000122929"
FT DOMAIN 49..78
FT /note="HhH"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 340 AA; 36727 MW; 03AF36A88FB283B7 CRC64;
MSSSSAHQKA SPPIEEEATE HGPFPIEQLQ ASGIAALDVK KLKDAGLCTV ESVAYSPRKD
LLQIKGISEA KVDKIIEAAS KLVPLGFTSA SQLHAQRLEI IQLTTGSREL DQILDGGIET
GSITEMYGEF RSGKTQLCHT LCVTCQLPLD QGGGEGKALY IDAEGTFRPQ RILQIADRFG
LNGADVLENV AYARAYNTDH QSRLLLEAAS MMVETRFALM VVDSATALYR TDFSGRGELS
ARQMHLAKFL RSLQKLADEF GVAVVITNQV VAQVDGAAMF AGPQIKPIGG NIMAHASTTR
LFLRKGRGEE RICKVISSPC LAEAEARFQI SSEGVTDVKD
