ID U1SDR0_9PAST Unreviewed; 514 AA.
AC U1SDR0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=HMPREF9065_00315 {ECO:0000313|EMBL:ERH28807.1};
OS Aggregatibacter sp. oral taxon 458 str. W10330.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=1321772 {ECO:0000313|EMBL:ERH28807.1, ECO:0000313|Proteomes:UP000016531};
RN [1] {ECO:0000313|EMBL:ERH28807.1, ECO:0000313|Proteomes:UP000016531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W10330 {ECO:0000313|EMBL:ERH28807.1,
RC ECO:0000313|Proteomes:UP000016531};
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:ERH28807.1}.
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DR EMBL; AWSH01000013; ERH28807.1; -; Genomic_DNA.
DR RefSeq; WP_021615410.1; NZ_KE952596.1.
DR AlphaFoldDB; U1SDR0; -.
DR STRING; 1321772.HMPREF9065_00315; -.
DR PATRIC; fig|1321772.3.peg.291; -.
DR HOGENOM; CLU_013049_0_1_6; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000016531; 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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004546; Restrct_endonuc_T1M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR NCBIfam; TIGR00497; hsdM; 1.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 11..158
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 172..480
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 484..511
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 514 AA; 57492 MW; D32E12B1B21A8632 CRC64;
MATAIQQREE LQRRIWQIAN DVRGAVDGWD FKQYVLGTLF YRFISENFIN YMKNGDESIN
YAGLADNIIT PAIKEEAVKS KGYFIYPSQL FKNVVANANT NPNLNTELKQ IFNDIENSAI
GYPSEQDIKG LFADFDTTSN RLGNTVADKN SRLAAVLKGV AELDFGDFED NHIDLFGDAY
EFLISNYAAN AGKSGGEFFT PQCVSKLIAR LALYGQDKVN KIYDPAAGSG SLLLQAKKPF
DEHIIEEGFF GQEINHTTYN LARMNMFLHN INYDKFDIAL GNTLMNPQFG DDKPFDAIVS
NPPYSVKWIG SDDPTLINDE RFAPAGVLAP KSKADFAFIL HTLSYLSAKG RAAIVSFPGI
FYRGGAEQKI RQYLVDNNYV ETVIALAPNL FFGTSIAVNI LVLSKHKPDT QTQFIDASGL
FKSATNNNIL EPEHIEQILK LFADKEDVPH LAKSVSFEDI VNNEYNLAVS SYVEQKDTRE
VIDIDELNAE IKQTVAKIDR LRAEINKIVA EIDQ
//
