ID Q8RJ67_CAMJU Unreviewed; 509 AA.
AC Q8RJ67;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 103.
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:AAL93191.1};
OS Campylobacter jejuni.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=197 {ECO:0000313|EMBL:AAL93191.1};
RN [1] {ECO:0000313|EMBL:AAL93191.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=30 {ECO:0000313|EMBL:AAL93191.1};
RA Millar W.G., Pearson B.M., Wells J.M., Mandrell R.E.;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAL93191.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=30 {ECO:0000313|EMBL:AAL93191.1}, and RM1516
RC {ECO:0000313|EMBL:AAM00901.1};
RX PubMed=15699185; DOI=10.1099/mic.0.27327-0;
RA Miller W.G., Pearson B.M., Wells J.M., Parker C.T., Kapitonov V.V.,
RA Mandrell R.E.;
RT "Diversity within the Campylobacter jejuni type I restriction-modification
RT loci.";
RL Microbiology 151:337-351(2005).
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};
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DR EMBL; AF486635; AAL93191.1; -; Genomic_DNA.
DR EMBL; AF486570; AAM00901.1; -; Genomic_DNA.
DR RefSeq; WP_004306557.1; NZ_SYTO01000001.1.
DR REBASE; 6084; M.Cje33560ORFAP.
DR REBASE; 6089; M.Cje30ORFAP.
DR PATRIC; fig|197.5249.peg.1618; -.
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 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 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 10..156
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 167..476
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 509 AA; 58255 MW; 80DF64A0FD174963 CRC64;
MKSVVEREEL HKTIWKIAND LRGSVDGWDF KSYVLGFLFY YFICENLKNY VLKSFEQDYE
NLSDEMAENG RDTIINAKGF FIKPSHLFSN IFKNAKLENL NEKLSVVFKE IESSANGSES
EKSFKGLFDD LDLYSNKLGA DNKERNKKIL KIMETISELD LHYNENEIDA FGDAYEFLMT
MYASNAGKSG GEFFTPQEVS KLLVEITLYN NAKPNKVYDP ACGSGSLLLQ YKKSLKSDPK
KGYFGQEINI TTYNLARMNM FLHDVNYTRF DIAHGDTLIN PSENHKELEP FDAIVSNPPY
STKWEGKDNA LLINDERFNK AGVLAPTSKA DLAFVMHSLS WLSEKGSAAI VCFPGVMYRG
GAERDIRKYM IEENFVDCVI SLAPNLFFGT SIAVCILVLR KNKTDKNTLF INANEEFIKV
TNKNMLSKEN LENILKLYKD RKEVPHLTKL VSIEEIAKND YNLSVSSYVE AKDTREIIDI
KALNKEIEEI VKRQSVLRNR IDSLVRELE
//
