ID Q0EWP7_9PROT Unreviewed; 572 AA.
AC Q0EWP7;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=SPV1_06369 {ECO:0000313|EMBL:EAU53742.1};
OS Mariprofundus ferrooxydans PV-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU53742.1, ECO:0000313|Proteomes:UP000005297};
RN [1] {ECO:0000313|EMBL:EAU53742.1, ECO:0000313|Proteomes:UP000005297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV-1 {ECO:0000313|EMBL:EAU53742.1,
RC ECO:0000313|Proteomes:UP000005297};
RA Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-2006) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU53742.1}.
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DR EMBL; AATS01000018; EAU53742.1; -; Genomic_DNA.
DR RefSeq; WP_009851567.1; NZ_DS022295.1.
DR AlphaFoldDB; Q0EWP7; -.
DR SMR; Q0EWP7; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_4_2_0; -.
DR InParanoid; Q0EWP7; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000005297; 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 Reference proteome {ECO:0000313|Proteomes:UP000005297};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..143
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 156..463
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 572 AA; 65425 MW; 6653563774330001 CRC64;
MSKITLQQLE SFLWETADIL RGNMDASEFK DYIFGMLFLK RLSDAFEEEQ EKVVAHYLSV
GKTQAQAEEL AQDEDEYDNT FFVPERARWS YLKDLHHDIG AELNKATEAI EEANTTLEGV
LVSIDFNIKN KLSDKKLRDL ISHYSKYRLR NEDFEKPDLL GTAYEYLIKM FADSAGKKGG
EFYTPSEVVR LLVSLLKPEA GMRVYDPTVG SGGMLIQTRN YLASHGENPR DLALYGQEMN
LNTWAICKMN MFLHGVFNAD IRKGDTLRDP AHIQHGELMH FDRVIANPPF SLKKWGKDEA
DNDAYGRFPY GTPPKDAGDL AFVQHMIASL NAEGKMGVVM PHGVLFRGSS EKAIRKGILQ
DDLLEAVIGL PSGLFYGTGI PACLLIINKQ KADERKGKVL FINAELEYEE GKNQNKLRDE
DIAKITATFE NYEEIKRYSH IATLSEIEEN DFNLNIRRYA DTSPPPEIYD VRAILHGGIP
VREVEDEYIQ EEILDGFDVS VVFNRRDDDY YEFKPEIESK ESIREFVGLD DQKVIAQIER
WWDKYKVSLK ELDAEVDEAE SVMKGYLQEL GY
//
