DMC1_HUMAN
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 03-AUG-2022, entry version 192.
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/";
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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 PDBsum; 1V5W; -.
DR PDBsum; 2ZJB; -.
DR PDBsum; 4HYY; -.
DR PDBsum; 6R3P; -.
DR PDBsum; 7C98; -.
DR PDBsum; 7C99; -.
DR PDBsum; 7C9C; -.
DR PDBsum; 7CGY; -.
DR AlphaFoldDB; Q14565; -.
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; Q14565; -.
DR PeptideAtlas; Q14565; -.
DR PRIDE; Q14565; -.
DR ProteomicsDB; 60046; -. [Q14565-1]
DR Antibodypedia; 246; 417 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 CTD; 11144; -.
DR DisGeNET; 11144; -.
DR GeneCards; DMC1; -.
DR HGNC; HGNC:2927; DMC1.
DR HPA; ENSG00000100206; Tissue enhanced (testis).
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; GGINDPD; -.
DR OrthoDB; 877394at2759; -.
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 1081 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 129 other tissues.
DR ExpressionAtlas; Q14565; baseline and differential.
DR Genevisible; Q14565; HS.
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:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:ProtInc.
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: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 GO; GO:0042148; P:strand invasion; IBA:GO_Central.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR DisProt; DP02746; -.
DR Gene3D; 3.40.50.300; -; 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; 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 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
