DMC1A_ORYSI
ID DMC1A_ORYSI Reviewed; 344 AA.
AC B8BM09; Q8L809; Q8W2E6; Q949I5;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Meiotic recombination protein DMC1 homolog A {ECO:0000305};
DE Short=OsDMC1A {ECO:0000303|PubMed:15821864};
DE AltName: Full=OsDMC1 {ECO:0000303|PubMed:15821864};
DE AltName: Full=RiLIM15A {ECO:0000305};
GN Name=DMC1A {ECO:0000303|Ref.1};
GN Synonyms=DMC1 {ECO:0000303|PubMed:15821864};
GN ORFNames=OsI_37443 {ECO:0000312|EMBL:EEC68851.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. IR64;
RX AGRICOLA=IND23274239; DOI=10.1007/s00497-001-0113-5;
RA Kathiresan A., Khush G.S., Bennett J.;
RT "Two rice DMC1 genes are differentially expressed during meiosis and during
RT haploid and diploid mitosis.";
RL Sex. Plant Reprod. 14:257-267(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=15821864; DOI=10.1007/s11103-004-5828-x;
RA Kant C.R., Rao B.J., Sainis J.K.;
RT "DNA binding and pairing activity of OsDmc1, a recombinase from rice.";
RL Plant Mol. Biol. 57:1-11(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. IR36;
RA Sato S., Asamizu E., Tabata S.;
RT "Genome structure of RiLIM15, a rice homologue of meiosis-specific recA-
RT like genes.";
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP FUNCTION.
RX PubMed=16689935; DOI=10.1111/j.1742-4658.2006.05170.x;
RA Rajanikant C., Kumbhakar M., Pal H., Rao B.J., Sainis J.K.;
RT "DNA strand exchange activity of rice recombinase OsDmc1 monitored by
RT fluorescence resonance energy transfer and the role of ATP hydrolysis.";
RL FEBS J. 273:1497-1506(2006).
RN [6]
RP FUNCTION.
RX PubMed=17562186; DOI=10.1007/s11103-007-9195-2;
RA Deng Z.Y., Wang T.;
RT "OsDMC1 is required for homologous pairing in Oryza sativa.";
RL Plant Mol. Biol. 65:31-42(2007).
RN [7]
RP FUNCTION.
RX PubMed=26118128;
RA Chittela R.K., Melzer M., Sainis J.K.;
RT "Comparison of activity of OsDmc1A recombinase of rice (Oryza sativa) in
RT presence of Ca2+ and Mg2+ ions.";
RL Indian J. Biochem. Biophys. 52:161-168(2015).
CC -!- FUNCTION: Recombinase that may participate in meiotic recombination,
CC specifically in homologous strand assimilation, which is required for
CC the resolution of meiotic double-strand breaks (Probable). Exhibits
CC DNA-dependent ATPase activity when bound to single-stranded DNA
CC (ssDNA). Mediates renaturation of homologous complementary strands as
CC well as assimilation of single strands into homologous supercoiled
CC duplexes leading to D-loop formation (PubMed:15821864). Binds circular
CC single-stranded DNA (ssDNA) and circular double-stranded DNA (dsDNA) in
CC vitro (PubMed:15821864, PubMed:26118128). Catalyzes DNA homologous
CC renaturation and DNA strand exchange. The rates of these activities are
CC dependent on the state of ATP hydrolysis (PubMed:16689935,
CC PubMed:26118128). Forms helical filaments along ssDNA and dsDNA, and
CC promotes strand exchange between ssDNA and dsDNA with long DNA
CC substrates of several thousand base pairs. The presence of the
CC replication protein A is not required for this activity (By
CC similarity). Seems to be required for homologous pairing and subsequent
CC chromosome segregation during male meiosis (PubMed:17562186). May be
CC not directly required for homologous pairing during male meiosis.
CC Required for synaptonemal complex assembly and crossover formation.
CC Functions redundantly with DMC1B (By similarity).
CC {ECO:0000250|UniProtKB:Q7GBF8, ECO:0000269|PubMed:15821864,
CC ECO:0000269|PubMed:16689935, ECO:0000269|PubMed:17562186,
CC ECO:0000269|PubMed:26118128, ECO:0000305|PubMed:16689935}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7GBF8}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen mother cells and root tips.
CC {ECO:0000269|Ref.1}.
CC -!- MISCELLANEOUS: Plant silencing DMC1A are sterile due to defects in
CC homologous pairing and subsequent chromosome segregation during male
CC meiosis. {ECO:0000269|PubMed:17562186}.
CC -!- SIMILARITY: Belongs to the RecA family. DMC1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEC68851.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF265548; AAL71907.1; -; Genomic_DNA.
DR EMBL; AY123340; AAM76793.1; -; Genomic_DNA.
DR EMBL; D70898; BAB61097.1; -; Genomic_DNA.
DR EMBL; CM000137; EEC68851.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B8BM09; -.
DR SMR; B8BM09; -.
DR STRING; 39946.B8BM09; -.
DR HOGENOM; CLU_041732_0_1_1; -.
DR Proteomes; UP000007015; Chromosome 12.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000150; F:DNA strand exchange activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IEA:InterPro.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011940; Dmc1.
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 SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02238; recomb_DMC1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; DNA-binding; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..344
FT /note="Meiotic recombination protein DMC1 homolog A"
FT /id="PRO_0000445041"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 235
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 235
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 238
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 241
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 241
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 247
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 247
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 315
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT CONFLICT 116
FT /note="D -> Y (in Ref. 3; BAB61097)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="T -> A (in Ref. 2; AAM76793)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="E -> K (in Ref. 2; AAM76793)"
FT /evidence="ECO:0000305"
FT CONFLICT 296..297
FT /note="VL -> RV (in Ref. 3; BAB61097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 37572 MW; 3B73EE085A0B6975 CRC64;
MAPSKQYSEG GQLQLMDAER IEEEEECFES IDKLISQGIN SGDVKKLQDA GIYTCNGLMM
HTKKSLTGIK GLSEAKVDKI CEAAEKLLSQ GFITGSDLLI KRKSVVRITT GSQALDKLLG
GGIETLCITE AFGEFRSGKT QLAHTLCVST QLPIHMHGGN GKVAYIDTEG TFRPERIVPI
AERFGMDANA VLDNIIYARA YTYEHQYNLL LGLAAKMAEE PFRLLIVDSV IALFRVDFSG
RGELAERQQK LAQMLSRLTK IAEEFNVAVY ITNQVIADPG GGMFITDLKK PAGGHVLAHA
ATIRLMLRKG KGEQRVCKIF DAPNLPEGEA VFQVTSGGIM DAKD
