ID DMC1_HUMAN Reviewed; 340 AA. AC Q14565; A8K9A2; B4DMW6; Q08AI1; Q99498; Q9UH11; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 27-MAR-2024, entry version 201. DE RecName: Full=Meiotic recombination protein DMC1/LIM15 homolog; GN Name=DMC1; Synonyms=DMC1H, LIM15; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=8590282; DOI=10.1093/dnares/2.4.183; RA Sato S., Seki N., Hotta Y., Tabata S.; RT "Expression profiles of a human gene identified as a structural homologue RT of meiosis-specific recA-like genes."; RL DNA Res. 2:183-185(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=8602360; DOI=10.1093/nar/24.3.470; RA Habu T., Taki T., West A., Nishimune Y., Morita T.; RT "The mouse and human homologs of DMC1, the yeast meiosis-specific RT homologous recombination gene, have a common unique form of exon-skipped RT transcript in meiosis."; RL Nucleic Acids Res. 24:470-477(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Heart, and Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-200. RG NIEHS SNPs program; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP INTERACTION WITH BRCA2. RX PubMed=20729832; DOI=10.1038/nature09399; RA Jensen R.B., Carreira A., Kowalczykowski S.C.; RT "Purified human BRCA2 stimulates RAD51-mediated recombination."; RL Nature 467:678-683(2010). RN [9] RP INTERACTION WITH RAD51AP1. RX PubMed=21903585; DOI=10.1074/jbc.m111.290015; RA Dunlop M.H., Dray E., Zhao W., Tsai M.S., Wiese C., Schild D., Sung P.; RT "RAD51-associated protein 1 (RAD51AP1) interacts with the meiotic RT recombinase DMC1 through a conserved motif."; RL J. Biol. Chem. 286:37328-37334(2011). RN [10] RP FUNCTION, AND INTERACTION WITH RAD51AP1. RX PubMed=21307306; DOI=10.1073/pnas.1016454108; RA Dray E., Dunlop M.H., Kauppi L., San Filippo J., Wiese C., Tsai M.S., RA Begovic S., Schild D., Jasin M., Keeney S., Sung P.; RT "Molecular basis for enhancement of the meiotic DMC1 recombinase by RAD51 RT associated protein 1 (RAD51AP1)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:3560-3565(2011). RN [11] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), SUBUNIT, DNA-BINDING SITES, AND RP MUTAGENESIS OF ARG-230; PHE-233; ARG-236; ARG-242; GLU-258 AND ARG-311. RX PubMed=15125839; DOI=10.1016/s1097-2765(04)00218-7; RA Kinebuchi T., Kagawa W., Enomoto R., Tanaka K., Miyagawa K., Shibata T., RA Kurumizaka H., Yokoyama S.; RT "Structural basis for octameric ring formation and DNA interaction of the RT human homologous-pairing protein Dmc1."; RL Mol. Cell 14:363-374(2004). CC -!- FUNCTION: Participates in meiotic recombination, specifically in CC homologous strand assimilation, which is required for the resolution of CC meiotic double-strand breaks. {ECO:0000269|PubMed:21307306}. CC -!- SUBUNIT: Double stacked ring-shaped homooctamer (PubMed:15125839). CC Interacts with BRCA2 (PubMed:20729832). Interacts with the MND1-PSMC3IP CC heterodimer (By similarity). Interacts with RAD51AP1; the interaction CC is direct and stimulates DMC1-mediated homologous recombination CC (PubMed:21307306, PubMed:21903585). {ECO:0000250|UniProtKB:Q61880, CC ECO:0000269|PubMed:15125839, ECO:0000269|PubMed:20729832, CC ECO:0000269|PubMed:21307306, ECO:0000269|PubMed:21903585}. CC -!- INTERACTION: CC Q14565; P51587: BRCA2; NbExp=12; IntAct=EBI-930865, EBI-79792; CC Q14565; Q14565: DMC1; NbExp=3; IntAct=EBI-930865, EBI-930865; CC Q14565; Q9H8Y8: GORASP2; NbExp=8; IntAct=EBI-930865, EBI-739467; CC Q14565; Q8N5Z5: KCTD17; NbExp=4; IntAct=EBI-930865, EBI-743960; CC Q14565; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-930865, EBI-739832; CC Q14565; Q9GZT8: NIF3L1; NbExp=9; IntAct=EBI-930865, EBI-740897; CC Q14565; O75928-2: PIAS2; NbExp=3; IntAct=EBI-930865, EBI-348567; CC Q14565; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-930865, EBI-79165; CC Q14565; P25788: PSMA3; NbExp=7; IntAct=EBI-930865, EBI-348380; CC Q14565; Q96B01-2: RAD51AP1; NbExp=3; IntAct=EBI-930865, EBI-1178743; CC Q14565; O00560: SDCBP; NbExp=7; IntAct=EBI-930865, EBI-727004; CC Q14565; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-930865, EBI-742426; CC Q14565; P36406: TRIM23; NbExp=3; IntAct=EBI-930865, EBI-740098; CC Q14565; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-930865, EBI-10180829; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61880}. CC Chromosome {ECO:0000250|UniProtKB:Q61880}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14565-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14565-2; Sequence=VSP_055357; CC -!- SIMILARITY: Belongs to the RecA family. DMC1 subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/dmc1/"; 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; D63882; BAA09932.1; -; mRNA. DR EMBL; D64108; BAA10970.1; -; mRNA. DR EMBL; CR456486; CAG30372.1; -; mRNA. DR EMBL; AK292617; BAF85306.1; -; mRNA. DR EMBL; AK297664; BAG60028.1; -; mRNA. DR EMBL; AY520538; AAR89915.1; -; Genomic_DNA. DR EMBL; AL022320; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC125163; AAI25164.1; -; mRNA. DR EMBL; BC125164; AAI25165.1; -; mRNA. DR CCDS; CCDS13973.1; -. [Q14565-1] DR CCDS; CCDS63477.1; -. [Q14565-2] DR PIR; S62354; S62354. DR RefSeq; NP_001265137.1; NM_001278208.1. [Q14565-2] DR RefSeq; NP_008999.2; NM_007068.3. [Q14565-1] DR RefSeq; XP_006724175.1; XM_006724112.2. DR PDB; 1V5W; X-ray; 3.20 A; A/B=1-340. DR PDB; 2ZJB; X-ray; 3.50 A; A/B=1-340. DR PDB; 4HYY; X-ray; 2.60 A; A/B/C/D=84-340. DR PDB; 6R3P; X-ray; 2.05 A; A/B/C/D=83-340. DR PDB; 7C98; EM; 3.47 A; A/B/C=1-340. DR PDB; 7C99; EM; 3.36 A; A/B/C=1-340. DR PDB; 7C9C; EM; 3.33 A; A/B/C=1-340. DR PDB; 7CGY; EM; 3.20 A; A/B/C=1-340. DR PDB; 8R2G; X-ray; 3.45 A; A/B/C/D/E/F/G/H=83-340. DR PDBsum; 1V5W; -. DR PDBsum; 2ZJB; -. DR PDBsum; 4HYY; -. DR PDBsum; 6R3P; -. DR PDBsum; 7C98; -. DR PDBsum; 7C99; -. DR PDBsum; 7C9C; -. DR PDBsum; 7CGY; -. DR PDBsum; 8R2G; -. DR AlphaFoldDB; Q14565; -. DR EMDB; EMD-30308; -. DR EMDB; EMD-30309; -. DR EMDB; EMD-30311; -. DR EMDB; EMD-30366; -. DR SMR; Q14565; -. DR BioGRID; 116316; 30. DR DIP; DIP-24192N; -. DR IntAct; Q14565; 22. DR MINT; Q14565; -. DR STRING; 9606.ENSP00000216024; -. DR DrugBank; DB03366; Imidazole. DR PhosphoSitePlus; Q14565; -. DR BioMuta; DMC1; -. DR DMDM; 13878923; -. DR MassIVE; Q14565; -. DR PaxDb; 9606-ENSP00000216024; -. DR PeptideAtlas; Q14565; -. DR ProteomicsDB; 60046; -. [Q14565-1] DR Antibodypedia; 246; 443 antibodies from 34 providers. DR DNASU; 11144; -. DR Ensembl; ENST00000216024.7; ENSP00000216024.2; ENSG00000100206.11. [Q14565-1] DR Ensembl; ENST00000428462.6; ENSP00000412703.2; ENSG00000100206.11. [Q14565-2] DR GeneID; 11144; -. DR KEGG; hsa:11144; -. DR MANE-Select; ENST00000216024.7; ENSP00000216024.2; NM_007068.4; NP_008999.2. DR UCSC; uc003avz.3; human. [Q14565-1] DR AGR; HGNC:2927; -. DR CTD; 11144; -. DR DisGeNET; 11144; -. DR GeneCards; DMC1; -. DR HGNC; HGNC:2927; DMC1. DR HPA; ENSG00000100206; Tissue enhanced (testis). DR MalaCards; DMC1; -. DR MIM; 602721; gene. DR neXtProt; NX_Q14565; -. DR OpenTargets; ENSG00000100206; -. DR Orphanet; 619; NON RARE IN EUROPE: Primary ovarian failure. DR PharmGKB; PA27377; -. DR VEuPathDB; HostDB:ENSG00000100206; -. DR eggNOG; KOG1434; Eukaryota. DR GeneTree; ENSGT00760000119398; -. DR HOGENOM; CLU_041732_0_0_1; -. DR InParanoid; Q14565; -. DR OMA; REATYVI; -. DR OrthoDB; 5477610at2759; -. DR PhylomeDB; Q14565; -. DR TreeFam; TF300698; -. DR PathwayCommons; Q14565; -. DR Reactome; R-HSA-912446; Meiotic recombination. DR SignaLink; Q14565; -. DR SIGNOR; Q14565; -. DR BioGRID-ORCS; 11144; 5 hits in 1159 CRISPR screens. DR ChiTaRS; DMC1; human. DR EvolutionaryTrace; Q14565; -. DR GeneWiki; DMC1_(gene); -. DR GenomeRNAi; 11144; -. DR Pharos; Q14565; Tbio. DR PRO; PR:Q14565; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q14565; Protein. DR Bgee; ENSG00000100206; Expressed in buccal mucosa cell and 131 other cell types or tissues. DR ExpressionAtlas; Q14565; baseline and differential. DR GO; GO:0005694; C:chromosome; ISS:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl. DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central. DR GO; GO:0000800; C:lateral element; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; TAS:ProtInc. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:UniProtKB. DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. 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:0042802; F:identical protein binding; IPI:IntAct. 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:0042148; P:DNA strand invasion; IBA:GO_Central. DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IEA:Ensembl. DR GO; GO:0007292; P:female gamete generation; TAS:ProtInc. DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IEA:Ensembl. DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl. DR GO; GO:0051321; P:meiotic cell cycle; TAS:ProtInc. DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central. DR GO; GO:0001556; P:oocyte maturation; IEA:Ensembl. DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl. DR GO; GO:0007131; P:reciprocal meiotic recombination; IDA:UniProtKB. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc. DR CDD; cd19514; DMC1; 1. DR DisProt; DP02746; -. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR IDEAL; IID00078; -. 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; IPR020588; RecA_ATP-bd. DR InterPro; IPR020587; RecA_monomer-monomer_interface. DR NCBIfam; TIGR02238; recomb_DMC1; 1. DR PANTHER; PTHR22942:SF30; MEIOTIC RECOMBINATION PROTEIN DMC1_LIM15 HOMOLOG; 1. DR PANTHER; PTHR22942; RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER; 1. DR Pfam; PF14520; HHH_5; 1. DR Pfam; PF08423; Rad51; 1. DR PIRSF; PIRSF005856; Rad51; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47794; Rad51 N-terminal domain-like; 1. DR PROSITE; PS50162; RECA_2; 1. DR PROSITE; PS50163; RECA_3; 1. DR Genevisible; Q14565; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell cycle; Chromosome; KW DNA-binding; Meiosis; Nucleotide-binding; Nucleus; Reference proteome. FT CHAIN 1..340 FT /note="Meiotic recombination protein DMC1/LIM15 homolog" FT /id="PRO_0000122918" FT BINDING 126..133 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305" FT BINDING 230 FT /ligand="dsDNA" FT /ligand_id="ChEBI:CHEBI:4705" FT /evidence="ECO:0000269|PubMed:15125839" FT BINDING 230 FT /ligand="ssDNA" FT /ligand_id="ChEBI:CHEBI:9160" FT /evidence="ECO:0000269|PubMed:15125839" FT BINDING 233 FT /ligand="ssDNA" FT /ligand_id="ChEBI:CHEBI:9160" FT /evidence="ECO:0000269|PubMed:15125839" FT BINDING 236 FT /ligand="dsDNA" FT /ligand_id="ChEBI:CHEBI:4705" FT /evidence="ECO:0000269|PubMed:15125839" FT BINDING 236 FT /ligand="ssDNA" FT /ligand_id="ChEBI:CHEBI:9160" FT /evidence="ECO:0000269|PubMed:15125839" FT BINDING 242 FT /ligand="dsDNA" FT /ligand_id="ChEBI:CHEBI:4705" FT /evidence="ECO:0000269|PubMed:15125839" FT BINDING 242 FT /ligand="ssDNA" FT /ligand_id="ChEBI:CHEBI:9160" FT /evidence="ECO:0000269|PubMed:15125839" FT BINDING 311 FT /ligand="ssDNA" FT /ligand_id="ChEBI:CHEBI:9160" FT /evidence="ECO:0000269|PubMed:15125839" FT VAR_SEQ 141..196 FT /note="VTAQLPGAGGYPGGKIIFIDTENTFRPDRLRDIADRFNVDHDAVLDNVLYAR FT AYTS -> G (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055357" FT VARIANT 150 FT /note="G -> D (in dbSNP:rs58396845)" FT /id="VAR_061757" FT VARIANT 200 FT /note="M -> V (in dbSNP:rs2227914)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_018960" FT MUTAGEN 230 FT /note="R->A: Abolishes binding to ssDNA or dsDNA." FT /evidence="ECO:0000269|PubMed:15125839" FT MUTAGEN 233 FT /note="F->A: Abolishes binding to ssDNA." FT /evidence="ECO:0000269|PubMed:15125839" FT MUTAGEN 236 FT /note="R->A: Abolishes binding to ssDNA or dsDNA." FT /evidence="ECO:0000269|PubMed:15125839" FT MUTAGEN 242 FT /note="R->A: Abolishes binding to ssDNA or dsDNA." FT /evidence="ECO:0000269|PubMed:15125839" FT MUTAGEN 258 FT /note="E->A,Q: Decreases octamer stability." FT /evidence="ECO:0000269|PubMed:15125839" FT MUTAGEN 311 FT /note="R->A: Abolishes binding to ssDNA." FT /evidence="ECO:0000269|PubMed:15125839" FT CONFLICT 37 FT /note="I -> N (in Ref. 2; BAA10970)" FT /evidence="ECO:0000305" FT CONFLICT 183 FT /note="A -> P (in Ref. 1; BAA09932)" FT /evidence="ECO:0000305" FT TURN 24..27 FT /evidence="ECO:0007829|PDB:7C99" FT TURN 28..31 FT /evidence="ECO:0007829|PDB:7CGY" FT HELIX 34..40 FT /evidence="ECO:0007829|PDB:7CGY" FT TURN 41..44 FT /evidence="ECO:0007829|PDB:7CGY" FT STRAND 47..54 FT /evidence="ECO:0007829|PDB:7CGY" FT HELIX 56..59 FT /evidence="ECO:0007829|PDB:7CGY" FT HELIX 67..70 FT /evidence="ECO:0007829|PDB:7CGY" FT HELIX 72..77 FT /evidence="ECO:0007829|PDB:7CGY" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:7CGY" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:1V5W" FT HELIX 88..95 FT /evidence="ECO:0007829|PDB:6R3P" FT HELIX 106..112 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 114..127 FT /evidence="ECO:0007829|PDB:6R3P" FT HELIX 132..142 FT /evidence="ECO:0007829|PDB:6R3P" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 155..163 FT /evidence="ECO:0007829|PDB:6R3P" FT HELIX 167..176 FT /evidence="ECO:0007829|PDB:6R3P" FT HELIX 181..186 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 188..192 FT /evidence="ECO:0007829|PDB:6R3P" FT HELIX 196..212 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 216..223 FT /evidence="ECO:0007829|PDB:6R3P" FT HELIX 227..232 FT /evidence="ECO:0007829|PDB:6R3P" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:1V5W" FT HELIX 239..259 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:7C9C" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:4HYY" FT HELIX 290..296 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 298..305 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 310..315 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:7C99" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 325..331 FT /evidence="ECO:0007829|PDB:6R3P" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:6R3P" SQ SEQUENCE 340 AA; 37681 MW; 040A6E4CF1FEBFA2 CRC64; MKEDQVVAEE PGFQDEEESL FQDIDLLQKH GINVADIKKL KSVGICTIKG IQMTTRRALC NVKGLSEAKV DKIKEAANKL IEPGFLTAFE YSEKRKMVFH ITTGSQEFDK LLGGGIESMA ITEAFGEFRT GKTQLSHTLC VTAQLPGAGG YPGGKIIFID TENTFRPDRL RDIADRFNVD HDAVLDNVLY ARAYTSEHQM ELLDYVAAKF HEEAGIFKLL IIDSIMALFR VDFSGRGELA ERQQKLAQML SRLQKISEEY NVAVFVTNQM TADPGATMTF QADPKKPIGG HILAHASTTR ISLRKGRGEL RIAKIYDSPE MPENEATFAI TAGGIGDAKE //