ID L2F6Z0_9GAMM Unreviewed; 412 AA.
AC L2F6Z0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=MOMA_06616 {ECO:0000313|EMBL:ELA08213.1};
OS Moraxella macacae 0408225.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=1230338 {ECO:0000313|EMBL:ELA08213.1, ECO:0000313|Proteomes:UP000023795};
RN [1] {ECO:0000313|EMBL:ELA08213.1, ECO:0000313|Proteomes:UP000023795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0408225 {ECO:0000313|EMBL:ELA08213.1,
RC ECO:0000313|Proteomes:UP000023795};
RX PubMed=23409273;
RA Ladner J.T., Whitehouse C.A., Koroleva G.I., Palacios G.F.;
RT "Genome Sequence of Moraxella macacae 0408225, a Novel Bacterial Species
RT Isolated from a Cynomolgus Macaque with Epistaxis.";
RL Genome Announc. 1:E00188-12(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELA08213.1}.
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DR EMBL; ANIN01000002; ELA08213.1; -; Genomic_DNA.
DR AlphaFoldDB; L2F6Z0; -.
DR STRING; 1230338.MOMA_06616; -.
DR REBASE; 62234; M.Mma225ORF6616P.
DR PATRIC; fig|1230338.3.peg.1413; -.
DR eggNOG; COG2189; Bacteria.
DR Proteomes; UP000023795; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR PANTHER; PTHR13370:SF16; TYPE III RESTRICTION-MODIFICATION ENZYME STYLTI MOD SUBUNIT; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00506; D21N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ELA08213.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023795};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELA08213.1}.
FT DOMAIN 15..341
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 412 AA; 47456 MW; 2D10A59B4B01FE35 CRC64;
MDADNCLKHL ANNSVQMVYI DPPYNTQSTS FEYHDNLADW DDFMGQKLTK TRDLLKDTGF
VFISIDDNKL AELLALCYQI FAKKNFLGVF ITRQATRSNA KHINTTHEYI VAFAKNKQLA
PKFAIKRLAL PFYQKKLNPL INKIKKIYQH EGIDKANIAL KQALKEFEPL DEFSWLKNYN
IVDEQGEICF ATDLSTPGEP NCLHIPEINL TLQPLKTRAW SSKEKIIKLF YANKLIFKNG
RPYEKHLLKN ATDSAMSLLN FYSRQGKHDL AKLNMEALFS TAKPVEMIKY LLRIATPNPD
DIVLDYFAGS GTTAQAVLEC NHEDNTHKQF ILCQIDEPIK QNAFAINYLI KHHYPPSIAS
ITQLRLERLK QHFNFSYETV TMNTVTMNTV TTTLITTTNL QKEQLWQNTS PF
//
