ID Q50FR5_CAMJU Unreviewed; 314 AA.
AC Q50FR5;
DT 07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
DE Flags: Fragment;
OS Campylobacter jejuni.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=197 {ECO:0000313|EMBL:AAW56179.1};
RN [1] {ECO:0000313|EMBL:AAW56179.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=81-176 {ECO:0000313|EMBL:AAW56179.1};
RX PubMed=15872262; DOI=10.1128/JCM.43.5.2330-2338.2005;
RA Poly F., Threadgill D., Stintzi A.;
RT "Genomic diversity in Campylobacter jejuni: identification of C. jejuni 81-
RT 176-specific genes.";
RL J. Clin. Microbiol. 43:2330-2338(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; AY681287; AAW56179.1; -; Genomic_DNA.
DR AlphaFoldDB; Q50FR5; -.
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; 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 PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII 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 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..144
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 173..314
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT NON_TER 314
FT /evidence="ECO:0000313|EMBL:AAW56179.1"
SQ SEQUENCE 314 AA; 36353 MW; D4615A8C954F433C CRC64;
MEQSQFQPIV NFIWSVADDL LRDVYVKGKY RDVILPMTII RRIDAVLEPT KDKVLKTYNT
YKDEFENLES LLGGKQGNKL GFFNYSRFNL QTLLNDPKNI RINFENYLDC FSENIKDIIL
KFKFKNQLDT LEESNILFGV IERFCSPKVN FGIEDILDEK GNVIHKGLSN LGMGYVFEEL
IRKFNEENNE EAGEHFTPRE IIELMTHLVF LPVKEQIKQG TWLIYDNACG SGGMLTESKE
FITDPEGLIQ SKANIYLYGQ EINPETYAIC KADMLIKGED PDHIKFGSTL SNDQQNLQFD
FMLSNPPYGK SWEN
//
