ID Q7MW04_PORGI Unreviewed; 1132 AA.
AC Q7MW04;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=PG_0862 {ECO:0000313|EMBL:AAQ66010.1};
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ66010.1, ECO:0000313|Proteomes:UP000000588};
RN [1] {ECO:0000313|EMBL:AAQ66010.1, ECO:0000313|Proteomes:UP000000588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588};
RX PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J.,
RA Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J.,
RA Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., Tettelin H.,
RA Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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:0000256|ARBA:ARBA00001279};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; AE015924; AAQ66010.1; -; Genomic_DNA.
DR RefSeq; WP_010956144.1; NC_002950.2.
DR AlphaFoldDB; Q7MW04; -.
DR STRING; 242619.PG_0862; -.
DR REBASE; 7383; PgiTORF862P.
DR EnsemblBacteria; AAQ66010; AAQ66010; PG_0862.
DR KEGG; pgi:PG_0862; -.
DR PATRIC; fig|242619.8.peg.798; -.
DR eggNOG; COG0827; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_002539_1_1_10; -.
DR BioCyc; PGIN242619:G1G02-804-MONOMER; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF20473; MmeI_Mtase; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:AAQ66010.1};
KW Hydrolase {ECO:0000313|EMBL:AAQ66010.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:AAQ66010.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000588};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 479..593
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT DOMAIN 692..803
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 911..1060
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 1132 AA; 130028 MW; 0CA076D80A9A84D9 CRC64;
MELKQYLQQS YQGIESFLEK IVFPIFGQEL FEDGHGVSIL EMYPDLRPAA QATGILEIKH
IGNIDMDFNP INIFDITVSS QIKMARNKVG IQNIIRRIMD TYSSAFMIFH YEDNPLWEWR
FTFCHKGRSQ SDITSSKRFT FLLGPGQHCR TAADNFQKLI DKKQRQDIEL KDIEDAFSVE
ALTKQFYKDL FEWYQWAISP EADISFPNDT STSEDDREDL ETKIIRLITR IMFVWFIKQK
ELVPQHLFDI AFLKTILKDF DPNSTTEGNY YNAILQNLFF GTLNRARQDE DGKPRRFATG
SKRDVKTLYR YAELFSISEK EVIQLFDSIP FLNGGLFECL DKTRYIDGVE RCYSLDGFSR
NDTRFANGRF KHRATIPNNL FFAPERGLVS ILSRYNFTIE ENSPEEQQVA LDPELLGKVF
ENLLGAYNPE TQETARNQSG SFYTPREVVN YMVDESLISY LGDSDLVRSL FRPDFVLQED
NKVQCEAIAS KLKAVKILDP ACGSGAFPMG LLNRMIELLE RISPQEKSYD LKLFVIENCL
YGSDIQSIAA QITKLRFFIS LICDCERDET KPNFGIPTLP NLETKFVAAN SLIAKKKMAQ
HRNLFEDPAI EETKNELIGV RHKHFSAKST SAKLRLREQD QDLRKKLAQL LAENEDFAPE
DALQLAAWNP YDQNAVSSFF DPEWMFGLAD GFDIVIGNPP YVQLQNNGGE LTKLYQGCDF
KTFARTGDVY CLFYERGWQL LKEGGHLCYI TSNKWMRAGY GEKTRLFFAS KTNPKLLVDF
AGVKVFESAT VDTNILLFAK EANAGQTQAV SLNKNVQIGG SELCEYIQQH ATASAFISSE
SWVILSPIEQ SIKRKIEAVG KPLKDWDINI YRGVLTGCNE AFIIDEDKRN EILNNCQSED
ERKRTEEIIR PILRGRDIKR YSYDWAGLYI VYIPWHFPLH LDSTITGASE KAEDAFKASY
PAVYRYLEGY KDLLTKRNQA ETGIRYEWYA LQRWGANYWE DFSKPKIMWK RIGSILRFCY
NENGALGLDS TCFAAGKGAE FLCCLLNSPM GHYLLKDSPK TGTGDLLISI QAVEPIKVPP
ITETLIRSFK ALLTNVCQIG TEEQETSINH QIFSLYNLSE EEQRYIKNNF SH
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