ID   DMA_VIBCH               Reviewed;         277 AA.
AC   P0C6Q8; Q08318; Q9KNV4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=DNA adenine methylase;
DE            EC=2.1.1.72;
DE   AltName: Full=DNA adenine methyltransferase;
DE   AltName: Full=Deoxyadenosyl-methyltransferase;
DE   AltName: Full=M.VchADam;
DE   AltName: Full=Orphan methyltransferase M.VchADamP {ECO:0000303|PubMed:12654995};
DE            Short=M.VchADamP {ECO:0000303|PubMed:12654995};
GN   Name=dam {ECO:0000303|PubMed:8125341}; OrderedLocusNames=VC_2626;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RX   PubMed=8125341; DOI=10.1016/0378-1119(94)90732-3;
RA   Bandyopadhyay R., Das J.;
RT   "The DNA adenine methyltransferase-encoding gene (dam) of Vibrio
RT   cholerae.";
RL   Gene 140:67-71(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [3]
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).
CC   -!- FUNCTION: An alpha subtype methylase, recognizes the double-stranded
CC       sequence 5'-GATC-3' and methylates A-2 (Probable) (PubMed:12654995).
CC       May be involved in methyl-directed DNA mismatch repair, initiation of
CC       chromosome replication and gene expression (By similarity).
CC       {ECO:0000250|UniProtKB:P0AEE8, ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:8125341}.
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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA48031.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X67820; CAA48031.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE003852; AAF95767.1; -; Genomic_DNA.
DR   PIR; H82052; H82052.
DR   PIR; S29558; S29558.
DR   RefSeq; NP_232254.1; NC_002505.1.
DR   RefSeq; WP_000744680.1; NZ_LT906614.1.
DR   AlphaFoldDB; P0C6Q8; -.
DR   SMR; P0C6Q8; -.
DR   STRING; 243277.VC_2626; -.
DR   REBASE; 4762; M.VchADamP.
DR   DNASU; 2615643; -.
DR   EnsemblBacteria; AAF95767; AAF95767; VC_2626.
DR   GeneID; 69718771; -.
DR   KEGG; vch:VC_2626; -.
DR   PATRIC; fig|243277.26.peg.2504; -.
DR   eggNOG; COG0338; Bacteria.
DR   HOGENOM; CLU_063430_0_1_6; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IBA:GO_Central.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
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.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..277
FT                   /note="DNA adenine methylase"
FT                   /id="PRO_0000087999"
FT   BINDING         10
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  31624 MW;  48D831240F9E7C60 CRC64;
     MKKQRAFLKW AGGKYSLVED IQRHLPEARE LVEPFVGAGS VFLNTDFERY LLADINPDLI
     NFYNLLKTEP QAYIHEAKRW FVPENNRKEV YLDIRKQFNQ SDDAMFRSLA FLYMNRFGFN
     GLCRYNKKGG FNVPFGSYKK PYFPEQELEF FAEKAQRATF ICASYGETFA RAQSDSVIYC
     DPPYAPLSTT ANFTSYAGNG FTLDDQAALA DIAEKTAKER GISVLISNHD TTHTRRLYRG
     AQLNVVKANR TISRNGAGRN KVDELLALFT PHLSSQA
//