ID A0A1Z5H7W1_9GAMM Unreviewed; 434 AA.
AC A0A1Z5H7W1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=bplSymb_SCF00602P017 {ECO:0000313|EMBL:GAW85365.1};
OS Bathymodiolus platifrons methanotrophic gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=113268 {ECO:0000313|EMBL:GAW85365.1, ECO:0000313|Proteomes:UP000196430};
RN [1] {ECO:0000313|EMBL:GAW85365.1, ECO:0000313|Proteomes:UP000196430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPD1508-B01-01 {ECO:0000313|EMBL:GAW85365.1,
RC ECO:0000313|Proteomes:UP000196430};
RX PubMed=28453654; DOI=10.1093/gbe/evx082;
RA Takishita K., Takaki Y., Chikaraishi Y., Ikuta T., Ozawa G., Yoshida T.,
RA Ohkouchi N., Fujikura K.;
RT "Genomic Evidence that Methanotrophic Endosymbionts Likely Provide Deep-Sea
RT Bathymodiolus Mussels with a Sterol Intermediate in Cholesterol
RT Biosynthesis.";
RL Genome Biol. Evol. 9:1148-1160(2017).
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:GAW85365.1}.
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DR EMBL; BDMN01000050; GAW85365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5H7W1; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000196430; 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: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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_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 ECO:0000313|EMBL:GAW85365.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196430};
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:GAW85365.1}.
FT DOMAIN 6..138
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 145..426
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 434 AA; 49177 MW; A4321DF3F3ECA6CF CRC64;
MITGELKNQV DKIWEAFWTG GISNPLTVIE QFTFLLFLRR LDERQLLEEK KANMIGSTVE
NPIYLEAHQK FRWHTFKNLD PESLFTLFTQ AQTDSDNLTT FEHMKQLGSG AGVFAQFMKG
ATFMIPTPKL LEQVVQMIDK IKMDDRDTKG DLYEYLLSKI ATAGTNGQFR TPRHIMKMMV
DIMQPTQEDT VCDPACGSAG FLVATGEYIH DNHPDWFHEQ DFRTHYNNSM FTGIEFDSTM
LRIGAMNLQL HGIDSPQLIG RDALSEANAE TRDQYSLILA NPPFKGSLDY DSVESSLLKT
VKTKKTELLF LALILRMLNI GGRCAVIIPD GVLFGSSKAH KQLRETLLSK HKLDAVISMP
SGVFKPYAGV STAILVFTKT NNGGTDNVWF YDMQADGYSL DDKCSPIADN DSADIVKRFK
QREQEHKRKR TEQI
//
