ID A0A0A2DY94_9PORP Unreviewed; 681 AA.
AC A0A0A2DY94;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=HQ37_01515 {ECO:0000313|EMBL:KGN71571.1};
OS Porphyromonas sp. COT-239 OH1446.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1515613 {ECO:0000313|EMBL:KGN71571.1, ECO:0000313|Proteomes:UP000030150};
RN [1] {ECO:0000313|EMBL:KGN71571.1, ECO:0000313|Proteomes:UP000030150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-239 OH1446 {ECO:0000313|Proteomes:UP000030150};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. COT-239_OH1446 Genome sequencing.";
RL Submitted (AUG-2014) 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:KGN71571.1}.
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DR EMBL; JRAO01000008; KGN71571.1; -; Genomic_DNA.
DR RefSeq; WP_036879393.1; NZ_JRAO01000008.1.
DR AlphaFoldDB; A0A0A2DY94; -.
DR STRING; 1515613.HQ37_01515; -.
DR eggNOG; COG0286; Bacteria.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000030150; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 Endonuclease {ECO:0000313|EMBL:KGN71571.1};
KW Hydrolase {ECO:0000313|EMBL:KGN71571.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:KGN71571.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030150};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 356..605
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 681 AA; 76689 MW; B57F91006F0ECBDA CRC64;
MAKGIQSVEP NIADLVNGWL RSYKLDYKLE QQSLNAEIDK ALNEYFTKNG GSGANRPDAK
LLLRDKQLNY YPILIEYKGY KDKLVKLDAQ GIVDNKKAKN EPNFKHINSY AVNGAIHYAN
AILHHTGYTD IISIGVTGYR DERGELQYEI GVYYVSKGNL GVGQEVGKYE DLSFLKAENF
DSFIERVNKL SLTPEELQRL KEQREQEINI SLAKLNNDIY QSEKGLGEND RVYLVAASII
ATLGIPGKVR PLEKAELLSL QEAGSTDGEI IMRKIRAFLK EKAIPTEKKD LILRTLQNTL
TTENINRVEN GETQLKRVFC KIVDDLGIYY KIGLTTDFTG KLFNEMYSWL GFTQDKLNDV
VLTPSYVAQL LVRLARVNKD SYVWDFATGS AGLLVAAMNE MLNDARRTIN SPDKLARKEA
LIKAEQLLGL ELLSSVYMLA ILNMILMGDG SSNILNKNSL TDFDGRYGFG KDNTPFPADA
FVLNPPYSAD GNGMNFVERA LSMMSKGYAA VIIQNSAGSG KAREINKRIL QRNTLVASIK
MPIDLFLGKS SVQTNIYVFK VAEKHDPKHI VKFIDFSNDG YTRTNRKKAS VNLRDTDQAK
ERYDELVNLV LYGKQYLKIF TEKEYYEATI DPQNGSDWNK STPVDTHPTL ADFKKTVADY
LAWEVSNLLK QQTDGENSLG K
//