ID B5JV81_9GAMM Unreviewed; 580 AA.
AC B5JV81;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 51.
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_2 {ECO:0000313|EMBL:EDY86459.1};
GN ORFNames=GP5015_377 {ECO:0000313|EMBL:EDY86459.1};
OS gamma proteobacterium HTCC5015.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=391615 {ECO:0000313|EMBL:EDY86459.1, ECO:0000313|Proteomes:UP000004692};
RN [1] {ECO:0000313|Proteomes:UP000004692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC5015 {ECO:0000313|Proteomes:UP000004692};
RX PubMed=20472792; DOI=10.1128/JB.00510-10;
RA Thrash J.C., Stingl U., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequence of the novel marine member of the Gammaproteobacteria
RT strain HTCC5015.";
RL J. Bacteriol. 192:3838-3839(2010).
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; DS990603; EDY86459.1; -; Genomic_DNA.
DR AlphaFoldDB; B5JV81; -.
DR STRING; 391615.GP5015_377; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_4_2_6; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000004692; Unassembled WGS sequence.
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:InterPro.
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; 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; 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.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EDY86459.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004692};
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:EDY86459.1}.
FT DOMAIN 10..145
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 158..464
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 580 AA; 65721 MW; 2656C48651037C5A CRC64;
MSQTITLQQL ESFLWEAADI LRGNMDASEY KDYIFGMMFL KRLSDAFEEA QESVVQYYMG
KGKSEDQARE LADDEDEYDK TFYIPPVARW GAIKDLKHDI GAELNKATEA IEEHNGSLEG
VLVSIDFNIK NKLSDKKLQD LLSHFSRHRL RNEDFERPDL LGTAYEYLIK MFADSAGKKG
GEFYTPSEVV QLLVSLLKPH AGMRIYDPTA GSGGMLVQTR NHLATHGENP SNLSLYGQEM
NLNTWAICKM NMFLHGVYSA DIRKGDTLRD PQHTQGGSLM TFDRVIANPP FSLKKWGKEE
AENDPYGRFP YGTPPKDAGD LAFVQHMIAS LNAEGMMGVV MPHGVLFRGA SEKAIRKGIL
EDDLLEAVVG LPAALFYGTG IPACLLIINK NKPQERKGKV LFINSELEYE EGKNQNKLRQ
QDIEKIVNTF ENFADIKRYS KVVPLEEIEE NDFNLNIRRY ADTSPPPEIY DVRAILHGGI
PVREVENEYI REEILEGFDV SVVFVKRDEE PSADEGYYDF KPEIDSKEAI RDAVGEVDAK
VIAQLERWWD KYRVSLSELD AKVAEAESVM KGYLQELGYV
//
