DMC1A_ORYSJ
ID DMC1A_ORYSJ Reviewed; 344 AA.
AC Q7GBF8; Q2QXT3; Q8L810; Q94IB0;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
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:0000303|Ref.1};
GN Name=DMC1A {ECO:0000303|PubMed:15821864};
GN Synonyms=DMC1 {ECO:0000303|PubMed:15821864};
GN OrderedLocusNames=Os12g0143800 {ECO:0000312|EMBL:BAF29157.1},
GN LOC_Os12g04980 {ECO:0000312|EMBL:ABA96458.1};
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX AGRICOLA=IND23222213;
RA Shimazu J., Matsukura C., Senda M., Ishikawa R., Akada S., Harada T.,
RA Tabata S., Niizeki M.;
RT "Characterization of a DMC1 homologue, RiLIM15, in meiotic panicles,
RT mitotic cultured cells and mature leaves of rice (Oryza sativa L.).";
RL Theor. Appl. Genet. 102:1159-1163(2001).
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 [MRNA], AND FUNCTION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18583359; DOI=10.1093/nar/gkn405;
RA Sakane I., Kamataki C., Takizawa Y., Nakashima M., Toki S., Ichikawa H.,
RA Ikawa S., Shibata T., Kurumizaka H.;
RT "Filament formation and robust strand exchange activities of the rice DMC1A
RT and DMC1B proteins.";
RL Nucleic Acids Res. 36:4266-4276(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [9]
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 [10]
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 [11]
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).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26960731; DOI=10.1104/pp.16.00167;
RA Wang H., Hu Q., Tang D., Liu X., Du G., Shen Y., Li Y., Cheng Z.;
RT "OsDMC1 is not required for homologous pairing in rice meiosis.";
RL Plant Physiol. 171:230-241(2016).
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
CC (PubMed:18583359). Seems to be required for homologous pairing and
CC subsequent chromosome segregation during male meiosis
CC (PubMed:17562186). May be not directly required for homologous pairing
CC during male meiosis. Required for synaptonemal complex assembly and
CC crossover formation. Functions redundantly with DMC1B
CC (PubMed:26960731). {ECO:0000269|PubMed:15821864,
CC ECO:0000269|PubMed:16689935, ECO:0000269|PubMed:17562186,
CC ECO:0000269|PubMed:18583359, ECO:0000269|PubMed:26118128,
CC ECO:0000269|PubMed:26960731, ECO:0000305|PubMed:16689935}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26960731}.
CC -!- TISSUE SPECIFICITY: Expressed in meiotic young panicles.
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=ABA96458.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB065111; BAB62026.1; -; Genomic_DNA.
DR EMBL; AY123338; AAM76791.1; -; Genomic_DNA.
DR EMBL; AB079873; BAB85213.1; -; mRNA.
DR EMBL; DP000011; ABA96458.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008218; BAF29157.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT15865.1; -; Genomic_DNA.
DR EMBL; AK110641; BAG99006.1; -; mRNA.
DR RefSeq; XP_015618986.1; XM_015763500.1.
DR AlphaFoldDB; Q7GBF8; -.
DR SMR; Q7GBF8; -.
DR STRING; 4530.OS12T0143800-01; -.
DR PaxDb; Q7GBF8; -.
DR PRIDE; Q7GBF8; -.
DR EnsemblPlants; Os12t0143800-01; Os12t0143800-01; Os12g0143800.
DR GeneID; 4351482; -.
DR Gramene; Os12t0143800-01; Os12t0143800-01; Os12g0143800.
DR KEGG; osa:4351482; -.
DR eggNOG; KOG1434; Eukaryota.
DR HOGENOM; CLU_041732_0_1_1; -.
DR InParanoid; Q7GBF8; -.
DR OMA; QQIECIT; -.
DR OrthoDB; 877394at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:UniProtKB.
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:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0042148; P:strand invasion; IBA:GO_Central.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:UniProtKB.
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_0000445040"
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 117
FT /note="K -> E (in Ref. 2; AAM76791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 37542 MW; 7A63E365266A6418 CRC64;
MAPSKQYSEG GQLQLMDAER IEEEEECFES IDKLISQGIN SGDVKKLQDA GIYTCNGLMM
HTKKSLTGIK GLSEAKVDKI CEAAEKLLSQ GFITGSDLLI KRKSVVRITT GSQALDKLLG
GGIETLCITE AFGEFRSGKT QLAHTLCVSA QLPIHMHGGN GKVAYIDTEG TFRPERIVPI
AERFGMDANA VLDNIIYARA YTYEHQYNLL LGLAAKMAEE PFRLLIVDSV IALFRVDFSG
RGELAERQQK LAQMLSRLTK IAEEFNVAVY ITNQVIADPG GGMFITDLKK PAGGHVLAHA
ATIRLMLRKG KGEQRVCKIF DAPNLPEGEA VFQVTSGGIM DAKD
