ID A0A068YTD0_9BURK Unreviewed; 450 AA.
AC A0A068YTD0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
OS Polaromonas sp. CG9_12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1504672 {ECO:0000313|EMBL:CDS53211.1, ECO:0000313|Proteomes:UP000043372};
RN [1] {ECO:0000313|EMBL:CDS53211.1, ECO:0000313|Proteomes:UP000043372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Smith H.J., Foreman C.M., Ramaraj T.;
RT "Draft Genome Sequence of a Metabolically Diverse Antarctic Supraglacial
RT Stream Organism, Polaromonas sp. Strain CG9_12, Determined Using Pacific
RT Biosciences Single-Molecule Real-Time Sequencing Technology.";
RL Genome Announc. 2:1-2(2014).
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; CCJP01000005; CDS53211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068YTD0; -.
DR SMR; A0A068YTD0; -.
DR STRING; 1504672.gene:199032445; -.
DR REBASE; 100478; M.PspCG912ORFDP.
DR eggNOG; COG0286; Bacteria.
DR Proteomes; UP000043372; Unassembled WGS sequence.
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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CDS53211.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000043372};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDS53211.1}.
FT DOMAIN 55..314
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 394..421
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 450 AA; 49722 MW; 15E9E140EAE9497D CRC64;
MGWLNPAASP KQRVIGRIMS AVERVRVDSE TNLCDILDKV NDIHTDHIDD QHFFTLSQVY
EDLLLKMGEK NSDGGQFFTP REVVRAMVRI VDPQPCETVY DPCCGTGGFL AQAYEQMAHA
LGDTVSSTEL ERLKHDTFFG REKENLVFPI ALANLVLHGI DQPNLWHGNT LSGAPTYEAL
FEQAPATFDV ILTNPPFGGK EGSEAQKNYS FETSSTQVLF MQHILDDLKP ALDGKPGGRC
AVVLDEGLLF RTNESAFVET KRKLLDECDL WCIVSLPGGV FSTAGAGVKT NLLFMTKGKK
TERIWYYDLS HVKVGKKTPM TLSQFGWGPQ FEVLDDAALP ATLVGDWPAQ DGHANPPFPT
LARLLAQRGT PEADSDFSWT VDFSARRAKA REDMAPHLAE VERLKNQAVA LKEEIGALKK
GADEARLAAC RAVGGHRKGR TRCARQSRCD
//
