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Database: UniProt
Entry: C7M3R8_CAPOD
LinkDB: C7M3R8_CAPOD
Original site: C7M3R8_CAPOD 
ID   C7M3R8_CAPOD            Unreviewed;       307 AA.
AC   C7M3R8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=Coch_2150 {ECO:0000313|EMBL:ACU93694.1};
OS   Capnocytophaga ochracea (strain ATCC 27872 / DSM 7271 / JCM 12966 / NCTC
OS   12371 / VPI 2845) (Bacteroides ochraceus).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=521097 {ECO:0000313|EMBL:ACU93694.1, ECO:0000313|Proteomes:UP000006650};
RN   [1] {ECO:0000313|EMBL:ACU93694.1, ECO:0000313|Proteomes:UP000006650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845
RC   {ECO:0000313|Proteomes:UP000006650};
RX   PubMed=21304645; DOI=10.4056/sigs.15195;
RA   Mavrommatis K., Gronow S., Saunders E., Land M., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Bruce D., Goodwin L., Pitluck S., Pati A., Ivanova N., Chen A.,
RA   Palaniappan K., Chain P., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA   Detter J.C., Han C., Bristow J., Goker M., Rohde M., Eisen J.A.,
RA   Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT   "Complete genome sequence of Capnocytophaga ochracea type strain (VPI
RT   2845).";
RL   Stand. Genomic Sci. 1:101-109(2009).
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; CP001632; ACU93694.1; -; Genomic_DNA.
DR   RefSeq; WP_015783106.1; NC_013162.1.
DR   AlphaFoldDB; C7M3R8; -.
DR   STRING; 521097.Coch_2150; -.
DR   REBASE; 22061; M.CocORF2150P.
DR   GeneID; 29675540; -.
DR   KEGG; coc:Coch_2150; -.
DR   eggNOG; COG0338; Bacteria.
DR   HOGENOM; CLU_063430_0_0_10; -.
DR   Proteomes; UP000006650; Chromosome.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
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; 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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:ACU93694.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006650};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACU93694.1}.
FT   BINDING         15
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         19
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         205
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ   SEQUENCE   307 AA;  35996 MW;  FBA484A3905BEBA7 CRC64;
     MRKNTNHIAK PFLKWAGGKT QLIEQIKNNL PIFVHNENFT YIEPFVGSGA VLFWLLSEFP
     NMKKAVINDI NKELIDTYRA IAENPEQLIA ILNSLQIEYH ALEEQQEAKK AYYYQKRALF
     NSKCEEKVMQ SALFIFLNRT CFNGLYRVNS KNEFNVPIGS YKRPMICDKE NILAVSKALQ
     KVEIICGDFE QTIHYTKENT LFYFDPPYKP LSETSNFNAY AKDSFDDSEQ IRLRDFCYKL
     NNLNHYWILS NSDVKGKDEN NHFFDELYAN FEIKRVLAKR SINANPKKRG ILNELLINNY
     TNNFLTI
//
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