ID U2SC28_9BACL Unreviewed; 303 AA.
AC U2SC28;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=HMPREF1983_00215 {ECO:0000313|EMBL:ERK60302.1};
OS Gemella bergeri ATCC 700627.
OC Bacteria; Bacillota; Bacilli; Bacillales; Gemellaceae; Gemella.
OX NCBI_TaxID=1321820 {ECO:0000313|EMBL:ERK60302.1, ECO:0000313|Proteomes:UP000016637};
RN [1] {ECO:0000313|EMBL:ERK60302.1, ECO:0000313|Proteomes:UP000016637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700627 {ECO:0000313|EMBL:ERK60302.1,
RC ECO:0000313|Proteomes:UP000016637};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERK60302.1}.
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DR EMBL; AWVP01000013; ERK60302.1; -; Genomic_DNA.
DR AlphaFoldDB; U2SC28; -.
DR PATRIC; fig|1321820.3.peg.213; -.
DR eggNOG; COG0827; Bacteria.
DR HOGENOM; CLU_073534_0_0_9; -.
DR Proteomes; UP000016637; 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 CDD; cd02440; AdoMet_MTases; 1.
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 PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 56..288
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 303 AA; 35292 MW; 0B9DAD0C155AB542 CRC64;
MRKLSKLEEL FFKIDRKTEE NRSNNTYFES LINYLSLEKD EDYFEIVDNY SKETIRKAYQ
FLLLKSLKEL NDPSYSITPE IITMYVSHLI ECIFGEKSIS VSDFASGSGN FLINIAALSN
GEKILTSIDV DNNYVKLQQN IFNLLETNVN IINQDVLKPL NIKKQDIIVS DVPFGYYADI
DNSLNYKLCS NNGYSLNSLL FIEQTVNYLK DNGIGILVVP KKVLEFDNKF KKFLEKDINL
NAVITLPIEM FKTDEQVKVI ILITKKEQKL LPKQVFLAEI PSYQNKKQYS NFIEEFKNWL
KER
//
