ID MTD21_STREE Reviewed; 284 AA. AC P04043; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1986, sequence version 1. DT 02-SEP-2026, entry version 146. DE RecName: Full=Type II methyltransferase M1.DpnII {ECO:0000303|PubMed:12654995}; DE Short=M1.DpnII {ECO:0000303|PubMed:12654995}; DE EC=2.1.1.72 {ECO:0000269|PubMed:2989823}; DE AltName: Full=Adenine-specific methyltransferase DpnM {ECO:0000303|PubMed:2824782}; DE AltName: Full=M.DpnII 1; DE AltName: Full=Modification methylase DpnIIA {ECO:0000303|PubMed:2989823}; GN Name=dpnM {ECO:0000303|PubMed:2989823}; OS Streptococcus pneumoniae. OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1313; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=697; RX PubMed=2989823; DOI=10.1073/pnas.82.13.4468; RA Mannarelli B.M., Balganesh T.S., Greenberg B., Springhorn S.S., Lacks S.A.; RT "Nucleotide sequence of the Dpn II DNA methylase gene of Streptococcus RT pneumoniae and its relationship to the dam gene of Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 82:4468-4472(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=697; RX PubMed=3019562; DOI=10.1016/0092-8674(86)90698-7; RA Lacks S.A., Mannarelli B.M., Springhorn S.S., Greenberg B.; RT "Genetic basis of the complementary DpnI and DpnII restriction systems of RT S. pneumoniae: an intercellular cassette mechanism."; RL Cell 46:993-1000(1986). RN [3] RP PROTEIN SEQUENCE OF 1-14, FUNCTION, AND SUBUNIT. RX PubMed=2824782; DOI=10.1016/0022-2836(87)90024-6; RA de la Campa A.G., Purushottam K., Springhorn S.S., Lacks S.A.; RT "Proteins encoded by the DpnII restriction gene cassette. Two methylases RT and an endonuclease."; RL J. Mol. Biol. 196:457-469(1987). RN [4] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=2687877; DOI=10.1073/pnas.86.23.9223; RA Cerritelli S., Springhorn S.S., Lacks S.A.; RT "DpnA, a methylase for single-strand DNA in the Dpn II restriction system, RT and its biological function."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9223-9227(1989). RN [5] RP NOMENCLATURE, AND SUBTYPE. RX PubMed=12654995; DOI=10.1093/nar/gkg274; RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A., RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K., RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S., RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A., RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S., RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V., RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E., RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W., RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.; RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing RT endonucleases and their genes."; RL Nucleic Acids Res. 31:1805-1812(2003). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-284 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE. RC STRAIN=HB264; RX PubMed=9862809; DOI=10.1016/s0969-2126(98)00154-3; RA Tran P.H., Korszun Z.R., Cerritelli S., Springhorn S.S., Lacks S.A.; RT "Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII RT restriction system of Streptococcus pneumoniae bound to S- RT adenosylmethionine."; RL Structure 6:1563-1575(1998). CC -!- FUNCTION: An alpha subtype methylase that recognizes the double- CC stranded sequence 5'-GATC-3', methylates A-2 on both strands, and CC protects the DNA from cleavage by the DpnII endonuclease. CC {ECO:0000269|PubMed:2687877, ECO:0000269|PubMed:2824782, CC ECO:0000269|PubMed:2989823, ECO:0000303|PubMed:12654995}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an CC N(6)-methyl-2'-deoxyadenosine in DNA + S-adenosyl-L-homocysteine + CC H(+); Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA- CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72; CC Evidence={ECO:0000269|PubMed:2687877, ECO:0000269|PubMed:2989823}; CC -!- SUBUNIT: Monomer (PubMed:9862809). Homodimer (Probable). CC {ECO:0000269|PubMed:9862809, ECO:0000305|PubMed:2824782}. CC -!- MISCELLANEOUS: The DpnII restriction system has two different CC methylases. {ECO:0000269|PubMed:2824782}. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {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; M11226; AAA26872.1; -; Genomic_DNA. DR EMBL; M14339; AAA88580.1; -; Genomic_DNA. DR PIR; A00556; XYSONA. DR RefSeq; WP_000692845.1; NZ_AP026918.1. DR PDB; 2DPM; X-ray; 1.80 A; A=1-284. DR AlphaFoldDB; P04043; -. DR SMR; P04043; -. DR REBASE; 162065; M.Wso11848ORF439P. DR REBASE; 3636; M1.DpnII. DR OMA; YMNRHGF; -. DR BRENDA; 2.1.1.72; 1960. DR EvolutionaryTrace; P04043; -. DR PRO; PR:P04043; -. DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:TreeGrafter. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:TreeGrafter. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; EXP:UniProtKB. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro. DR GO; GO:0006298; P:mismatch repair; IEA:TreeGrafter. DR Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR023095; Ade_MeTrfase_dom_2. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR012263; M_m6A_EcoRV. DR InterPro; IPR012327; MeTrfase_D12. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00571; dam; 1. DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1. DR PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1. DR Pfam; PF02086; MethyltransfD12; 1. DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1. DR PRINTS; PR00505; D12N6MTFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS00092; N6_MTASE; 1. DR PDBsum; 2DPM; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; DNA-binding; Methyltransferase; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..284 FT /note="Type II methyltransferase M1.DpnII" FT /id="PRO_0000087957" FT BINDING 17 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:9862809, FT ECO:0007744|PDB:2DPM" FT BINDING 21 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0007744|PDB:2DPM" FT BINDING 46 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:9862809, FT ECO:0007744|PDB:2DPM" FT BINDING 62 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:9862809, FT ECO:0007744|PDB:2DPM" FT BINDING 177 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:9862809, FT ECO:0007744|PDB:2DPM" FT BINDING 178 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:9862809, FT ECO:0007744|PDB:2DPM" FT BINDING 194 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:9862809, FT ECO:0007744|PDB:2DPM" FT HELIX 22..24 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 25..31 FT /evidence="ECO:0007829|PDB:2DPM" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 48..53 FT /evidence="ECO:0007829|PDB:2DPM" FT STRAND 56..63 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 65..76 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 78..91 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 94..101 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 102..105 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 108..111 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 114..127 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 156..168 FT /evidence="ECO:0007829|PDB:2DPM" FT STRAND 169..176 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 178..182 FT /evidence="ECO:0007829|PDB:2DPM" FT STRAND 190..193 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 195..199 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 216..230 FT /evidence="ECO:0007829|PDB:2DPM" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:2DPM" FT STRAND 235..242 FT /evidence="ECO:0007829|PDB:2DPM" FT HELIX 244..249 FT /evidence="ECO:0007829|PDB:2DPM" FT TURN 250..252 FT /evidence="ECO:0007829|PDB:2DPM" FT STRAND 253..258 FT /evidence="ECO:0007829|PDB:2DPM" FT STRAND 276..281 FT /evidence="ECO:0007829|PDB:2DPM" SQ SEQUENCE 284 AA; 32907 MW; 9F1525575CFA3E1E CRC64; MKIKEIKKVT LQPFTKWTGG KRQLLPVIRE LIPKTYNRYF EPFVGGGALF FDLAPKDAVI NDFNAELINC YQQIKDNPQE LIEILKVHQE YNSKEYYLDL RSADRDERID MMSEVQRAAR ILYMLRVNFN GLYRVNSKNQ FNVPYGRYKN PKIVDEELIS AISVYINNNQ LEIKVGDFEK AIVDVRTGDF VYFDPPYIPL SETSAFTSYT HEGFSFADQV RLRDAFKRLS DTGAYVMLSN SSSALVEELY KDFNIHYVEA TRTNGAKSSS RGKISEIIVT NYEK //