MTD21_STREE
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 03-AUG-2022, entry version 133.
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; Firmicutes; 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 + H(+) + S-adenosyl-L-
CC homocysteine; 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}.
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DR EMBL; M11226; AAA26872.1; -; Genomic_DNA.
DR EMBL; M14339; AAA88580.1; -; Genomic_DNA.
DR PIR; A00556; XYSONA.
DR RefSeq; WP_000692845.1; NZ_WNIC01000007.1.
DR PDB; 2DPM; X-ray; 1.80 A; A=1-284.
DR PDBsum; 2DPM; -.
DR AlphaFoldDB; P04043; -.
DR SMR; P04043; -.
DR REBASE; 162065; M.Wso11848ORF439P.
DR REBASE; 3636; M1.DpnII.
DR GeneID; 66806924; -.
DR OMA; MNRHGFN; -.
DR BRENDA; 2.1.1.72; 1960.
DR EvolutionaryTrace; P04043; -.
DR PRO; PR:P04043; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1020.10; -; 1.
DR Gene3D; 3.40.50.150; -; 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 PANTHER; PTHR30481; PTHR30481; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00571; dam; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
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 REGION 177..178
FT /note="S-adenosyl-L-methionine"
FT /evidence="ECO:0000269|PubMed:9862809,
FT ECO:0007744|PDB:2DPM"
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 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 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
