ID B3H2F7_ACTP7 Unreviewed; 489 AA.
AC B3H2F7;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN Name=hsdM {ECO:0000313|EMBL:ACE62182.1};
GN OrderedLocusNames=APP7_1530 {ECO:0000313|EMBL:ACE62182.1};
OS Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=537457 {ECO:0000313|EMBL:ACE62182.1, ECO:0000313|Proteomes:UP000001226};
RN [1] {ECO:0000313|Proteomes:UP000001226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP76 {ECO:0000313|Proteomes:UP000001226};
RA Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA Tegetmeyer H., Singh M., Gerlach G.F.;
RT "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL Submitted (JUN-2008) 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}.
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DR EMBL; CP001091; ACE62182.1; -; Genomic_DNA.
DR RefSeq; WP_005617884.1; NC_010939.1.
DR AlphaFoldDB; B3H2F7; -.
DR REBASE; 18418; M.AplAORF1530P.
DR KEGG; apa:APP7_1530; -.
DR HOGENOM; CLU_018284_4_0_6; -.
DR Proteomes; UP000001226; Chromosome.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 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 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ACE62182.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACE62182.1}.
FT DOMAIN 3..133
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 143..443
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 489 AA; 56477 MW; A0E3117720F0C6F7 CRC64;
MSLNNLVKRL QDVMRNDAGI NGDAQRIEQI VWILFLKIYD AKEQEWEQID DNYHSILPDF
LRWQNWAKDN KDGKAMTGDE LLNFVNNELF PALKNLPISA ETPMNQKIIR AAFEDNNNYM
KNGILLRQVI NIIDEINFEQ YQERHAFGDI YENILKSLQS AGNAGEFYTP RAVTDFMAKM
IKPRLGEKIA DFACGTGGFL TSALKELDKQ NDSINDKNLL SNSVYGIEKK ALPHLLCITN
LLLHDIDNPN VHHDNTLEKP VKDYTENDKF DVILMNPPYG GSEIEQIKTN FPSALRSSET
ADLFMSVIMY RLKKNGRVAI VLPDGFLFGT DNAKMAIKQK LMSEMNLHTV IRLPHSVFAP
YTSITTNILF FDNTEPTKET WFYRLDMPQG YKNFSKTKPM KLEHFNEVME WWHNRQAIEI
DGFDKARCYS YQEIADRQFN IDLCGFPHEE EEILPPDELI ANYQQKRTAL NADIDRILGE
ITQILGIKL
//
