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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}.
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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
 
 
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