ID   A0A2C9CUP0_9RHOB        Unreviewed;       469 AA.
AC   A0A2C9CUP0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   ORFNames=SAMN06273572_108105 {ECO:0000313|EMBL:SOH95231.1};
OS   Monaibacterium marinum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Monaibacterium.
OX   NCBI_TaxID=1690039 {ECO:0000313|EMBL:SOH95231.1, ECO:0000313|Proteomes:UP000220034};
RN   [1] {ECO:0000313|EMBL:SOH95231.1, ECO:0000313|Proteomes:UP000220034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 {ECO:0000313|EMBL:SOH95231.1,
RC   ECO:0000313|Proteomes:UP000220034};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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; OCTN01000008; SOH95231.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9CUP0; -.
DR   REBASE; 259266; M.MmaC7VORF108105P.
DR   OrthoDB; 9806213at2; -.
DR   Proteomes; UP000220034; Unassembled WGS sequence.
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; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF07669; Eco57I; 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   Methyltransferase {ECO:0000313|EMBL:SOH95231.1};
KW   Transferase {ECO:0000313|EMBL:SOH95231.1}.
FT   DOMAIN          140..231
FT                   /note="Type II methyltransferase M.TaqI-like"
FT                   /evidence="ECO:0000259|Pfam:PF07669"
SQ   SEQUENCE   469 AA;  52094 MW;  CF1A41017BB2296F CRC64;
     MLLEFIDQTR LEVSPTLDPK RRSKLGQFMT PARIASFMAG MFGDLPAHIR LLDAGAGMGA
     LTAAFVAESL GRETCPTSID VTCYEVDDQL ASILDGTLAV CADQCAGAGV AFTSRVVRDD
     YILQSLEPLL RDQRTYNYAI LNPPYGKINQ TSEWRLGLRS LGIETVNLYT AFVAVALQQI
     EVDGEIVAIT PRSFCNGSYY EPFRRLLLDG SAISNLHVFE SRRSSFKDDD VLQENMIFRV
     RKGVTQEDVT LSTDESEARA VSFSDIVRPS DRHAFIRLPV SGNDLADSVQ ALPCVLADLG
     IKVSTGRVVD FRTRDNLLKE SGDDTVPLIY PQHFHEGGIR WPLPDFRKHN ALADNEDTVK
     LIIPAGIYVL TKRFTAKEEK RRLVASIYDG GRAGFENHLN YFHENGEGLP LDLAKGLAAF
     LNSEGVDQYF RIFSGHTQVN ATDLRNLHYP SRDQLEAFGR GETSIADLF
//