ID Q12C71_POLSJ Unreviewed; 535 AA.
AC Q12C71;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 24-JAN-2024, entry version 91.
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=Bpro_1940 {ECO:0000313|EMBL:ABE43871.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE43871.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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};
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DR EMBL; CP000316; ABE43871.1; -; Genomic_DNA.
DR RefSeq; WP_011482870.1; NC_007948.1.
DR AlphaFoldDB; Q12C71; -.
DR STRING; 296591.Bpro_1940; -.
DR REBASE; 12115; M.PspJORF1940P.
DR KEGG; pol:Bpro_1940; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_4_1_4; -.
DR OMA; NSADWAW; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
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; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 1.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:ABE43871.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW Transferase {ECO:0000313|EMBL:ABE43871.1}.
FT DOMAIN 5..148
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 161..494
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 535 AA; 59042 MW; 6A64E3C20F270BDA CRC64;
MLDDIKKTLW ATADKLRANM DAAEYKHLVL GLIFVKYISD TFAARRSEVA TRLADPKDEY
FFEGATPKTL AVELEDRDYY KSVNVFWVPE AARWESLRAA AKQPDIGKRI DEALTLVEVE
NPKLKGILDK RYARAQLPDG KLGELVDLIS TVGFGDNPSV ARDILGQVYE YFLGMFASAE
GKRGGQFYTP ASIVKTLVAV LNPHSGKVYD PCCGSGGMFV QSEKFIEAHG GKLGDASIYG
QEANPTTWRL AAMNLAIRGI DFNLGREPAD TFVRNQHPDL RADFILANPP FNISDWWHAS
LTGDARWQYG DPPTGNANYA WLQHMLHHLK PTGRAGIVLA NGSMSSSQNS EGQIRAAMVE
ADVVEVMIAL PGQLFFNTQI PACLWFLVKK KTRRQGEVLF IDARKLATMI SRVQSEFTDE
VIARIANTVA AWRGESLPLP LGLGEGEGEG EGSPAPAPYA DIPGFCRSVK LKEIAQHGHV
LTPGRYVGAE EVEDNDEDFA TKMQQLTEKL GEQMAKGAEL DQLIRQKLGG LGYEF
//