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Database: UniProt
Entry: I2IZF6_9STRE
LinkDB: I2IZF6_9STRE
Original site: I2IZF6_9STRE 
ID   I2IZF6_9STRE            Unreviewed;       104 AA.
AC   I2IZF6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=HMPREF1117_1501 {ECO:0000313|EMBL:EIF36108.1};
OS   Streptococcus sp. SK643.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1095727 {ECO:0000313|EMBL:EIF36108.1, ECO:0000313|Proteomes:UP000006010};
RN   [1] {ECO:0000313|EMBL:EIF36108.1, ECO:0000313|Proteomes:UP000006010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK643 {ECO:0000313|EMBL:EIF36108.1,
RC   ECO:0000313|Proteomes:UP000006010};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (APR-2012) 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   -!- 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:EIF36108.1}.
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DR   EMBL; AJMM01000029; EIF36108.1; -; Genomic_DNA.
DR   AlphaFoldDB; I2IZF6; -.
DR   STRING; 1095727.HMPREF1117_1501; -.
DR   PATRIC; fig|1095727.3.peg.1617; -.
DR   eggNOG; COG0286; Bacteria.
DR   Proteomes; UP000006010; 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:0006306; P:DNA methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EIF36108.1};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..50
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          55..82
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   104 AA;  11915 MW;  18254AF1BB8EDD76 CRC64;
     MTEDHIAKIL ETYQKRENVE KFAHLASFEE IVENDYNLNI PRYVDTFEEE PVVPLADLAA
     QLAEIDKEIG EVEARLAHMR SQLVGTTPEA QAELTAYLEK LKEI
//
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