DMC1_SCHPO
ID DMC1_SCHPO Reviewed; 332 AA.
AC O42634; O42880;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Meiotic recombination protein dmc1;
GN Name=dmc1; Synonyms=dmp1; ORFNames=SPAC8E11.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10908327; DOI=10.1093/nar/28.14.2709;
RA Fukushima K., Tanaka Y., Nabeshima K., Yoneki T., Tougan T., Tanaka S.,
RA Nojima H.;
RT "Dmc1 of Schizosaccharomyces pombe plays a role in meiotic recombination.";
RL Nucleic Acids Res. 28:2709-2716(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yamazaki A.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP HOMODIMERIZATION, AND INTERACTION WITH RDH54.
RX PubMed=14551247; DOI=10.1091/mbc.e03-05-0288;
RA Catlett M.G., Forsburg S.L.;
RT "Schizosaccharomyces pombe Rdh54 (TID1) acts with Rhp54 (RAD54) to repair
RT meiotic double-strand breaks.";
RL Mol. Biol. Cell 14:4707-4720(2003).
RN [5]
RP FUNCTION, AND HOMOOLIGOMERIZATION.
RX PubMed=15899844; DOI=10.1128/mcb.25.11.4377-4387.2005;
RA Sauvageau S., Stasiak A.Z., Banville I., Ploquin M., Stasiak A.,
RA Masson J.-Y.;
RT "Fission yeast rad51 and dmc1, two efficient DNA recombinases forming
RT helical nucleoprotein filaments.";
RL Mol. Cell. Biol. 25:4377-4387(2005).
CC -!- FUNCTION: Required for meiotic recombination and cell cycle
CC progression. Binds to single and double-stranded DNA, in the presence
CC of magnesium, and exhibits DNA-dependent ATPase activity. Promotes DNA
CC strand annealing and strand exchange via DNA recombinase activity and
CC forms helical and stacked ring nucleoprotein filaments.
CC {ECO:0000269|PubMed:10908327, ECO:0000269|PubMed:15899844}.
CC -!- SUBUNIT: Double stacked ring-shaped homooctamer (By similarity).
CC Interacts with rdh54. {ECO:0000250, ECO:0000269|PubMed:14551247}.
CC -!- INTERACTION:
CC O42634; O42634: dmc1; NbExp=3; IntAct=EBI-1109558, EBI-1109558;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the RecA family. DMC1 subfamily. {ECO:0000305}.
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DR EMBL; AB008545; BAA28671.1; -; Genomic_DNA.
DR EMBL; D64035; BAA23984.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA17024.1; -; Genomic_DNA.
DR PIR; T39157; T39157.
DR PIR; T51302; T51302.
DR RefSeq; NP_594166.1; NM_001019590.2.
DR AlphaFoldDB; O42634; -.
DR SMR; O42634; -.
DR BioGRID; 278582; 66.
DR DIP; DIP-29236N; -.
DR IntAct; O42634; 3.
DR STRING; 4896.SPAC8E11.03c.1; -.
DR PaxDb; O42634; -.
DR EnsemblFungi; SPAC8E11.03c.1; SPAC8E11.03c.1:pep; SPAC8E11.03c.
DR GeneID; 2542106; -.
DR KEGG; spo:SPAC8E11.03c; -.
DR PomBase; SPAC8E11.03c; dmc1.
DR VEuPathDB; FungiDB:SPAC8E11.03c; -.
DR eggNOG; KOG1434; Eukaryota.
DR HOGENOM; CLU_041732_0_0_1; -.
DR InParanoid; O42634; -.
DR OMA; GGINDPD; -.
DR PhylomeDB; O42634; -.
DR PRO; PR:O42634; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:PomBase.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:1905334; F:Swi5-Sfr1 complex binding; IPI:PomBase.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0000730; P:DNA recombinase assembly; IDA:UniProtKB.
DR GO; GO:0006311; P:meiotic gene conversion; IMP:PomBase.
DR GO; GO:0000709; P:meiotic joint molecule formation; IDA:PomBase.
DR GO; GO:0010774; P:meiotic strand invasion involved in reciprocal meiotic recombination; IDA:PomBase.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:0042148; P:strand invasion; IDA:PomBase.
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 recombination; DNA-binding; Magnesium;
KW Meiosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..332
FT /note="Meiotic recombination protein dmc1"
FT /id="PRO_0000122916"
FT BINDING 120..127
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 304
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT CONFLICT 25
FT /note="G -> GKLKG (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="Q -> K (in Ref. 2; BAA23984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 36409 MW; 86B73EAA491F7B02 CRC64;
MEEFAEGNDD EQMIFSDIED LTAHGIGMTD IIKLKQAGVC TVQGVHMSTK RFLLKIKGFS
EAKVDKLKEA ASKMCPANFS TAMEISQNRK KVWSISTGSE ALNGILGGGI QSMSITEVFG
EFRCGKTQMS HTLCVTAQLP RDMGGAEGKV AFIDTEGTFR PDRIKAIAER FGVDADQAME
NIIVSRAYNS EQQMEYITKL GTIFAEDGQY RLLIVDSIMA LFRVDYSGRG ELSERQQKLN
IMLARLNHIS EEFNVAVFVT NQVQADPGAA MMFASNDRKP VGGHVMAHAS ATRLLLRKGR
GEERVAKLND SPDMPEAECS YVITPGGIAD VS
