DMC1_YEAST
ID DMC1_YEAST Reviewed; 334 AA.
AC P25453; D3DM88;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Meiotic recombination protein DMC1;
GN Name=DMC1; Synonyms=ISC2; OrderedLocusNames=YER179W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RX PubMed=1581960; DOI=10.1016/0092-8674(92)90446-j;
RA Bishop D.K., Park D., Xu L., Kleckner N.;
RT "DMC1: a meiosis-specific yeast homolog of E. coli recA required for
RT recombination, synaptonemal complex formation, and cell cycle
RT progression.";
RL Cell 69:439-456(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RX PubMed=8455558; DOI=10.1007/bf00282804;
RA Kobayashi T., Hotta Y., Tabata S.;
RT "Isolation and characterization of a yeast gene that is homologous with a
RT meiosis-specific cDNA from a plant.";
RL Mol. Gen. Genet. 237:225-232(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, INTERACTION WITH RDH54, AND MUTAGENESIS OF LYS-69 AND GLY-126.
RX PubMed=9335591; DOI=10.1093/genetics/147.2.533;
RA Dresser M.E., Ewing D.J., Conrad M.N., Dominguez A.M., Barstead R.,
RA Jiang H., Kodadek T.;
RT "DMC1 functions in a Saccharomyces cerevisiae meiotic pathway that is
RT largely independent of the RAD51 pathway.";
RL Genetics 147:533-544(1997).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MEI5 AND SAE3.
RX PubMed=15620352; DOI=10.1016/j.cell.2004.10.031;
RA Hayase A., Takagi M., Miyazaki T., Oshiumi H., Shinohara M., Shinohara A.;
RT "A protein complex containing Mei5 and Sae3 promotes the assembly of the
RT meiosis-specific RecA homolog Dmc1.";
RL Cell 119:927-940(2004).
RN [7]
RP SUBUNIT.
RX PubMed=15835894; DOI=10.1021/bi048897q;
RA Chang Y.-C., Lo Y.-H., Lee M.-H., Leng C.-H., Hu S.-M., Chang C.-S.,
RA Wang T.-F.;
RT "Molecular visualization of the yeast Dmc1 protein ring and Dmc1-ssDNA
RT nucleoprotein complex.";
RL Biochemistry 44:6052-6058(2005).
CC -!- FUNCTION: Required for meiotic recombination, synaptonemal complex
CC formation and cell cycle progression. Recruited to meiosis
CC recombination hotspots by MEI5 and SAE3. {ECO:0000269|PubMed:15620352,
CC ECO:0000269|PubMed:9335591}.
CC -!- SUBUNIT: Double stacked ring-shaped homooctamer (By similarity). Forms
CC a ternary complex with MEI5 and SAE3. Interacts with RDH54.
CC {ECO:0000250, ECO:0000269|PubMed:15620352, ECO:0000269|PubMed:15835894,
CC ECO:0000269|PubMed:9335591}.
CC -!- INTERACTION:
CC P25453; P32489: MEI5; NbExp=4; IntAct=EBI-5955, EBI-10685;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15620352}.
CC -!- DEVELOPMENTAL STAGE: Expressed 2.5 hours after induction of meiosis.
CC -!- SIMILARITY: Belongs to the RecA family. DMC1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M87549; AAA34571.1; -; Genomic_DNA.
DR EMBL; D10865; BAA01637.1; -; Genomic_DNA.
DR EMBL; U18922; AAB64706.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07842.1; -; Genomic_DNA.
DR PIR; A38214; A38214.
DR RefSeq; NP_011106.1; NM_001179069.1.
DR AlphaFoldDB; P25453; -.
DR SMR; P25453; -.
DR BioGRID; 36932; 92.
DR DIP; DIP-110N; -.
DR IntAct; P25453; 45.
DR MINT; P25453; -.
DR STRING; 4932.YER179W; -.
DR PaxDb; P25453; -.
DR PRIDE; P25453; -.
DR TopDownProteomics; P25453; -.
DR EnsemblFungi; YER179W_mRNA; YER179W; YER179W.
DR GeneID; 856926; -.
DR KEGG; sce:YER179W; -.
DR SGD; S000000981; DMC1.
DR VEuPathDB; FungiDB:YER179W; -.
DR eggNOG; KOG1434; Eukaryota.
DR GeneTree; ENSGT00760000119398; -.
DR HOGENOM; CLU_041732_0_0_1; -.
DR InParanoid; P25453; -.
DR OMA; GGINDPD; -.
DR BioCyc; YEAST:G3O-30337-MON; -.
DR PRO; PR:P25453; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P25453; protein.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
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:0042030; F:ATPase inhibitor activity; IDA:SGD.
DR GO; GO:0000150; F:DNA strand exchange activity; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
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:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0000709; P:meiotic joint molecule formation; IMP:SGD.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0042148; P:strand invasion; IBA:GO_Central.
DR GO; GO:0007130; P:synaptonemal complex assembly; IGI:SGD.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; DNA-binding; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Sporulation.
FT CHAIN 1..334
FT /note="Meiotic recombination protein DMC1"
FT /id="PRO_0000122915"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 223
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 223
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 226
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 229
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 229
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
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 305
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT MUTAGEN 69
FT /note="K->E: Recessive mutant; phenotypically null.
FT Eliminates the ability for self-association."
FT /evidence="ECO:0000269|PubMed:9335591"
FT MUTAGEN 126
FT /note="G->D: Dominant mutant; phenotypically null."
FT /evidence="ECO:0000269|PubMed:9335591"
SQ SEQUENCE 334 AA; 36613 MW; 00B0503D7FAF5CB3 CRC64;
MSVTGTEIDS DTAKNILSVD ELQNYGINAS DLQKLKSGGI YTVNTVLSTT RRHLCKIKGL
SEVKVEKIKE AAGKIIQVGF IPATVQLDIR QRVYSLSTGS KQLDSILGGG IMTMSITEVF
GEFRCGKTQM SHTLCVTTQL PREMGGGEGK VAYIDTEGTF RPERIKQIAE GYELDPESCL
ANVSYARALN SEHQMELVEQ LGEELSSGDY RLIVVDSIMA NFRVDYCGRG ELSERQQKLN
QHLFKLNRLA EEFNVAVFLT NQVQSDPGAS ALFASADGRK PIGGHVLAHA SATRILLRKG
RGDERVAKLQ DSPDMPEKEC VYVIGEKGIT DSSD
