ID J9R2L5_RIEAN Unreviewed; 313 AA.
AC J9R2L5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=B739_0013 {ECO:0000313|EMBL:AFR34623.1};
OS Riemerella anatipestifer RA-CH-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=1228997 {ECO:0000313|EMBL:AFR34623.1, ECO:0000313|Proteomes:UP000006276};
RN [1] {ECO:0000313|EMBL:AFR34623.1, ECO:0000313|Proteomes:UP000006276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA-CH-1 {ECO:0000313|EMBL:AFR34623.1,
RC ECO:0000313|Proteomes:UP000006276};
RA Chun C.A., Shu W.M., Kang Z.D., Jia W.X.;
RT "Riemerella anatipestifer vaccine strains.";
RL Submitted (SEP-2012) 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; CP003787; AFR34623.1; -; Genomic_DNA.
DR AlphaFoldDB; J9R2L5; -.
DR REBASE; 52812; M2.Ran1ORF11P.
DR KEGG; rag:B739_0013; -.
DR PATRIC; fig|1228997.3.peg.13; -.
DR HOGENOM; CLU_063430_0_0_10; -.
DR Proteomes; UP000006276; Chromosome.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00571; dam; 1.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AFR34623.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006276};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT BINDING 22
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT BINDING 208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ SEQUENCE 313 AA; 36600 MW; 0B744D9DEECD667B CRC64;
MNKNEMTKYK IAKPFLKWAG GKTQLISDIE RTLPTNITQK NFTYIEPFVG SGAVLFWVLN
NFANLKKAVI NDINEDLINT YKTIADRPKE LISILQIMQN EFHTLEGNEE KKKLYYYQKR
ELYNSRKEEQ SGQAALFIFL NRTCFNGLYR VNRKNEYNVP MGGYKKPTIC DKENILAVSD
ALQKVEILCG DFEQTLDFAE QNTLFYFDPP YKPLSETSSF NSYAKDEFND SEQIRLRDFC
NKLDILNHIW ILSNSDVKGK DENDNFFDNL YSDFNIQRVD ARRSINANPE KRGKLTELLI
TNQVNNEEYV RAI
//
