DMC1B_ORYSJ
ID DMC1B_ORYSJ Reviewed; 344 AA.
AC Q7GBF7; Q8VWY5; Q93XI1; Q94IA9; Q94JQ1;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Meiotic recombination protein DMC1 homolog B {ECO:0000305};
DE Short=OsDMC1B {ECO:0000303|PubMed:15821864};
DE AltName: Full=RiLIM15B {ECO:0000303|Ref.2};
GN Name=DMC1B {ECO:0000303|PubMed:15821864};
GN Synonyms=DMC1 {ECO:0000303|Ref.1};
GN OrderedLocusNames=Os11g0146800 {ECO:0000312|EMBL:BAF27583.1},
GN LOC_Os11g04954 {ECO:0000305};
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare; TISSUE=Spike;
RX AGRICOLA=IND23233616; DOI=10.1007/s004970100065;
RA Ding Z.-J., Wang T., Chong K., Bai S.-N.;
RT "Isolation and characterization of OsDMC1, the rice homologue of the yeast
RT DMC1 gene essential for meiosis.";
RL Sex. Plant Reprod. 13:285-288(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Panicle;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 (By similarity).
CC Exhibits DNA-dependent ATPase activity when bound to single-stranded
CC DNA (ssDNA). Mediates renaturation of homologous complementary strands
CC as well as assimilation of single strands into homologous supercoiled
CC duplexes leading to D-loop formation (By similarity). Binds circular
CC single-stranded DNA (ssDNA) and circular double-stranded DNA (dsDNA) in
CC vitro (By similarity). Catalyzes DNA homologous renaturation and DNA
CC strand exchange. The rates of these activities are dependent on the
CC state of ATP hydrolysis (By similarity). Forms helical filaments along
CC ssDNA and dsDNA, and promotes strand exchange between ssDNA and dsDNA
CC with long DNA substrates of several thousand base pairs. The presence
CC of the 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 (By similarity).
CC May be not directly required for homologous pairing during male
CC meiosis. Required for synaptonemal complex assembly and crossover
CC formation. Functions redundantly with DMC1A (PubMed:26960731).
CC {ECO:0000250|UniProtKB:Q7GBF8, ECO:0000269|PubMed:18583359,
CC ECO:0000269|PubMed:26960731}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26960731}.
CC -!- TISSUE SPECIFICITY: Highly expressed in spikelets (Ref.1). Expressed in
CC meiotic young panicles (Ref.2). {ECO:0000269|Ref.1, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the RecA family. DMC1 subfamily. {ECO:0000305}.
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DR EMBL; AB046620; BAB84121.1; -; mRNA.
DR EMBL; AB064544; BAB61838.1; -; mRNA.
DR EMBL; AB065112; BAB62025.1; -; Genomic_DNA.
DR EMBL; AF375982; AAK55555.2; -; Genomic_DNA.
DR EMBL; AB079874; BAB85214.1; -; mRNA.
DR EMBL; DP000010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP008217; BAF27583.1; -; Genomic_DNA.
DR EMBL; AP014967; BAT12668.1; -; Genomic_DNA.
DR RefSeq; XP_015616932.1; XM_015761446.1.
DR AlphaFoldDB; Q7GBF7; -.
DR SMR; Q7GBF7; -.
DR STRING; 4530.OS11T0146800-00; -.
DR PaxDb; Q7GBF7; -.
DR PRIDE; Q7GBF7; -.
DR EnsemblPlants; Os11t0146800-01; Os11t0146800-01; Os11g0146800.
DR Gramene; Os11t0146800-01; Os11t0146800-01; Os11g0146800.
DR KEGG; osa:4349763; -.
DR eggNOG; KOG1434; Eukaryota.
DR HOGENOM; CLU_041732_0_1_1; -.
DR InParanoid; Q7GBF7; -.
DR OMA; GGINDPD; -.
DR OrthoDB; 877394at2759; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
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; 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: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 B"
FT /id="PRO_0000445042"
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 246
FT /note="E -> K (in Ref. 2; BAB62025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 37603 MW; F05759B36C67882A CRC64;
MAPSKQYDEG GQLQLMDAER IEEEEECFES IDKLISQGIN SGDVKKLQDA GIYTCNGLMM
HTKKSLTGIK GLSEAKVDKI CEAAEKLLSQ GFMTGSDLLI KRKSVVRITT GSQALDELLG
GGIETLCITE AFGEFRSGKT QLAHTLCVST QLPIHMHGGN GKVAYIDTEG TFRPERIVPI
AERFGMDANA VLDNIIYARA YTYEHQYNLL LGLAAKMAEE PFRLLIVDSV IALFRVDFSG
RGELAERQQK LAQMLSRLTK IAEEFNVAVY ITNQVIADPG GGMFITDPKK PAGGHVLAHA
ATIRLMLRKG KGEQRVCKIF DAPNLPEGEA VFQVTSGGIM DAKD
