DMA_VIBC3
ID DMA_VIBC3 Reviewed; 277 AA.
AC A5F520; C3LXM4; Q08318; Q9KNV4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Orphan methyltransferase M.VchO395Dam/M.VchO395CDamP {ECO:0000303|PubMed:12654995};
DE Short=M.VchO395Dam/M.VchO395CDamP {ECO:0000303|PubMed:12654995};
GN Name=dam {ECO:0000303|PubMed:11705940};
GN OrderedLocusNames=VC0395_A2203, VC395_2739;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=11705940; DOI=10.1128/iai.69.12.7610-7615.2001;
RA Julio S.M., Heithoff D.M., Provenzano D., Klose K.E., Sinsheimer R.L.,
RA Low D.A., Mahan M.J.;
RT "DNA adenine methylase is essential for viability and plays a role in the
RT pathogenesis of Yersinia pseudotuberculosis and Vibrio cholerae.";
RL Infect. Immun. 69:7610-7615(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
RN [4]
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:11705940}.
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 -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:11705940}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF274317; AAG23174.1; -; Genomic_DNA.
DR EMBL; CP000627; ABQ21457.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10724.1; -; Genomic_DNA.
DR RefSeq; WP_000744680.1; NZ_JAACZH010000007.1.
DR AlphaFoldDB; A5F520; -.
DR SMR; A5F520; -.
DR STRING; 345073.VC395_2739; -.
DR REBASE; 20804; M.VchO395CDamP.
DR REBASE; 5786; M.VchO395Dam.
DR EnsemblBacteria; ABQ21457; ABQ21457; VC0395_A2203.
DR GeneID; 57741227; -.
DR KEGG; vco:VC0395_A2203; -.
DR KEGG; vcr:VC395_2739; -.
DR PATRIC; fig|345073.21.peg.2639; -.
DR eggNOG; COG0338; Bacteria.
DR HOGENOM; CLU_063430_0_1_6; -.
DR OMA; MNRHGFN; -.
DR BRENDA; 2.1.1.72; 6626.
DR Proteomes; UP000000249; Chromosome 2.
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:0006260; P:DNA replication; 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 3: Inferred from homology;
KW DNA replication; DNA-binding; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..277
FT /note="DNA adenine methylase"
FT /id="PRO_0000324810"
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
