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Database: UniProt
Entry: E1L7N0_9FIRM
LinkDB: E1L7N0_9FIRM
Original site: E1L7N0_9FIRM 
ID   E1L7N0_9FIRM            Unreviewed;       175 AA.
AC   E1L7N0;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=HMPREF9321_1710 {ECO:0000313|EMBL:EFL55716.1};
OS   Veillonella atypica ACS-049-V-Sch6.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=866776 {ECO:0000313|EMBL:EFL55716.1, ECO:0000313|Proteomes:UP000004211};
RN   [1] {ECO:0000313|EMBL:EFL55716.1, ECO:0000313|Proteomes:UP000004211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-049-V-Sch6 {ECO:0000313|EMBL:EFL55716.1,
RC   ECO:0000313|Proteomes:UP000004211};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) 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}.
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:EFL55716.1}.
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DR   EMBL; AEDR01000043; EFL55716.1; -; Genomic_DNA.
DR   RefSeq; WP_005378197.1; NZ_AEDR01000043.1.
DR   AlphaFoldDB; E1L7N0; -.
DR   eggNOG; COG0286; Bacteria.
DR   eggNOG; COG3206; Bacteria.
DR   Proteomes; UP000004211; Unassembled WGS sequence.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; 2.
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   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000313|EMBL:EFL55716.1};
KW   Hydrolase {ECO:0000313|EMBL:EFL55716.1};
KW   Nuclease {ECO:0000313|EMBL:EFL55716.1}.
FT   DOMAIN          1..93
FT                   /note="Type II methyltransferase M.TaqI-like"
FT                   /evidence="ECO:0000259|Pfam:PF07669"
SQ   SEQUENCE   175 AA;  20400 MW;  B2CFE8D25113D65D CRC64;
     MKFDVVIGNP PYQEDIDNNR PKLIYHLFID EAYKIAKKAI LITPARFLFK AGQTPKWVVE
     KMVNDLESEN PGIFEDDTKT FVDLYMKSGL YITEIVKRLF NNPVMKTKYP DDAQRLRHIL
     EKQVYGFAPS EIIYRIATNF IFGPVDDTVE QSHFVQVDTI PYAKEGRIQE LVDTY
//
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