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Database: UniProt
Entry: A0A1N7L379_9RHOB
LinkDB: A0A1N7L379_9RHOB
Original site: A0A1N7L379_9RHOB 
ID   A0A1N7L379_9RHOB        Unreviewed;       517 AA.
AC   A0A1N7L379;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SAMN05421774_101876 {ECO:0000313|EMBL:SIS68283.1};
OS   Gemmobacter megaterium.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Gemmobacter.
OX   NCBI_TaxID=1086013 {ECO:0000313|EMBL:SIS68283.1, ECO:0000313|Proteomes:UP000186141};
RN   [1] {ECO:0000313|EMBL:SIS68283.1, ECO:0000313|Proteomes:UP000186141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26375 {ECO:0000313|EMBL:SIS68283.1,
RC   ECO:0000313|Proteomes:UP000186141};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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};
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DR   EMBL; FTOT01000001; SIS68283.1; -; Genomic_DNA.
DR   RefSeq; WP_076529006.1; NZ_FTOT01000001.1.
DR   AlphaFoldDB; A0A1N7L379; -.
DR   STRING; 1086013.SAMN05421774_101876; -.
DR   OrthoDB; 9806213at2; -.
DR   Proteomes; UP000186141; 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:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 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:UP000186141};
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..165
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          176..477
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   517 AA;  57861 MW;  6A09133C32ED3B73 CRC64;
     MTDEQKRKLE QKLWDIANTL RGKMGADEFR DYILGFIFYK YLSERMHGYA DRILGDDGMA
     YTDIPEGTPQ GEEFLSAVRD ASLEALGYFL RPSELFTAIA RRGAEGAFIL GDLKTILNNI
     ERSTMGTESE EDFDHLFEDL DLSSTKLGRT EDAKNELIAK VLTHLDAIDF ALDDADSDVL
     GDAYEYLIGQ FASGAGKKAG EFYTPQEVST ILARIVTTGK TRLRSVYDPT CGSGSLLLRV
     AREVSQVDDF YGQEMNRTTY NLARMNMILH GVSYRNFNLR QEDTLEHPQH EGQLFEAIVA
     NPPFSAKWSA RPLFLTDDRF AQYGRLAPAS KADFAFVQHM LAHLDDNGAM AVVLPHGALF
     RGGAEGAIRE FIIREKNWLD AVIGLPANIF YGTGIPTCIM VFKKCRETED VLFVDASGCF
     EKAKNQNYLR PADIDRIVTA FRTRSEDPRF AHKASREEIA GNGWNLNIPR YVESFEAEPE
     IDLASVVADI RRIDAAMVGI DARIRAFCAE LGLEAPV
//
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