DMC1B_ORYSI
ID DMC1B_ORYSI Reviewed; 344 AA.
AC Q7EAG4; Q8W2E5;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Meiotic recombination protein DMC1 homolog B {ECO:0000305};
DE Short=OsDMC1B {ECO:0000303|PubMed:15821864};
DE AltName: Full=RiLIM15B {ECO:0000305};
GN Name=DMC1B {ECO:0000303|Ref.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], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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].
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).
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 (By
CC similarity). Seems to be required for homologous pairing and subsequent
CC chromosome segregation during male meiosis (By similarity). May be not
CC directly required for homologous pairing during male meiosis. Required
CC for synaptonemal complex assembly and crossover formation. Functions
CC redundantly with DMC1A (By similarity). {ECO:0000250|UniProtKB:B8BM09,
CC ECO:0000250|UniProtKB:Q7GBF7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7GBF7}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen mother cells and root tips.
CC {ECO:0000269|Ref.1}.
CC -!- DEVELOPMENTAL STAGE: Expressed in haploid male gametophytes during
CC pollen maturation and in diploid zygotic embryos and endosperm after
CC pollination. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the RecA family. DMC1 subfamily. {ECO:0000305}.
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DR EMBL; AF265549; AAL71908.1; -; Genomic_DNA.
DR EMBL; AY123339; AAM76792.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7EAG4; -.
DR SMR; Q7EAG4; -.
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.
FT CHAIN 1..344
FT /note="Meiotic recombination protein DMC1 homolog B"
FT /id="PRO_0000445043"
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 4
FT /note="S -> F (in Ref. 1; AAL71908)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="G -> V (in Ref. 1; AAL71908)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="E -> G (in Ref. 1; AAL71908)"
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