ID A6DQ84_9BACT Unreviewed; 494 AA.
AC A6DQ84;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=LNTAR_16348 {ECO:0000313|EMBL:EDM26135.1};
OS Lentisphaera araneosa HTCC2155.
OC Bacteria; Lentisphaerota; Lentisphaeria; Lentisphaerales; Lentisphaeraceae;
OC Lentisphaera.
OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM26135.1, ECO:0000313|Proteomes:UP000004947};
RN [1] {ECO:0000313|EMBL:EDM26135.1, ECO:0000313|Proteomes:UP000004947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM26135.1,
RC ECO:0000313|Proteomes:UP000004947};
RX PubMed=20363947; DOI=10.1128/JB.00208-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.;
RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species of
RT the order Lentisphaerales in the phylum Lentisphaerae.";
RL J. Bacteriol. 192:2938-2939(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};
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:EDM26135.1}.
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DR EMBL; ABCK01000019; EDM26135.1; -; Genomic_DNA.
DR RefSeq; WP_007280013.1; NZ_ABCK01000019.1.
DR AlphaFoldDB; A6DQ84; -.
DR STRING; 313628.LNTAR_16348; -.
DR REBASE; 26131; M.LarORF16348P.
DR eggNOG; COG0286; Bacteria.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000004947; 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:EDM26135.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004947};
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:EDM26135.1}.
FT DOMAIN 6..136
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 144..455
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 494 AA; 56048 MW; D54931EDE22D2042 CRC64;
MITGEIKNKI DRIWDVFWEG GLSNPLTVVE QLTYLLFIKG LDELQSTKEA TASMLDLPVD
APVYSDDQRE LRWSAFKELE AQQMFSLFTR VDDSNPGIFQ FIKNLHGDND SAFSRYMTDA
LFQVQSPKML QRVVEMLDEI PMQDRDTKGD IYEYLLSKIA TSGTLGQFRT PRHIIDLMVD
LMRPTPQDTI IDPASGSCGF LVSANNYLRN NHKEIFTDGA LNHHFNNEMF YGHDMDSTML
RIGAMNMMLH GVENPNIDRR DSLGEENKDE NSYSLILANP PFKGALDFEA CSKSLLAMCK
TKKTELLFLA LMIRSLKLGG RCAVIVPDGV LFGSSKAHKQ IREQLVEKQN LEGVISMPSG
VFKPYAGVST AILLFTKTDE GGTDKVWFYD MKNDGFSLDD KRAPIEGSDL PDIIKSFHER
NNGQDGQSRT AQSFFVPKEE IIENGYDLSI NRYKEIVYEE VQYDEPEIIL DRIDSLEKDI
VAGVSELREM VKNK
//