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Database: UniProt
Entry: F3NG59_9ACTN
LinkDB: F3NG59_9ACTN
Original site: F3NG59_9ACTN 
ID   F3NG59_9ACTN            Unreviewed;       663 AA.
AC   F3NG59;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=SGM_2123 {ECO:0000313|EMBL:EGG47494.1};
OS   Streptomyces griseoaurantiacus M045.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG47494.1, ECO:0000313|Proteomes:UP000003022};
RN   [1] {ECO:0000313|EMBL:EGG47494.1, ECO:0000313|Proteomes:UP000003022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M045 {ECO:0000313|EMBL:EGG47494.1,
RC   ECO:0000313|Proteomes:UP000003022};
RX   PubMed=21551298; DOI=10.1128/JB.05053-11;
RA   Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT   "Draft genome sequence of the marine bacterium Streptomyces
RT   griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT   with a pABA core component.";
RL   J. Bacteriol. 193:3417-3418(2011).
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:EGG47494.1}.
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DR   EMBL; AEYX01000031; EGG47494.1; -; Genomic_DNA.
DR   RefSeq; WP_006139778.1; NZ_AEYX01000031.1.
DR   AlphaFoldDB; F3NG59; -.
DR   STRING; 996637.SGM_2123; -.
DR   REBASE; 37164; M2.Sgr45ORF2120P.
DR   eggNOG; COG0286; Bacteria.
DR   Proteomes; UP000003022; 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:EGG47494.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003022};
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:EGG47494.1}.
FT   DOMAIN          9..141
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          153..458
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   663 AA;  73816 MW;  1C78BA5956BABA5E CRC64;
     MNSSKHTELA NHAWSVADLL RGDYKQSDYG KVILPFTVLR RLECVLEPTR DAVTETVERF
     AGQDINADKF LRKAAGHAFY NTSSLTLKKI AADPGSAAKN LQVYVASFSD NARGVLDRFE
     FAQQVKRLDS AGLLYKIIGK FTDLDLRPEV VSNHNMGYIF EELIRRFSEQ SNETAGEHFT
     PREVIQLMVR LLVAPDGDAL QLPGVVRTVM DPACGTGGML SATDDLIKEL NPDATVEVYG
     QELNPESWAI CRSDLMIKGQ NPENIAFGNS FNDDGHARRT FDYLLANPPF GVEWKKVKED
     VEEEHEKLGS AGRFGAGLPR INDGSLLFLQ HMISKMKPVD VNGGGGSRIA IVFNGSPLFT
     GAAGSGESEI RRWILENDWL EGIVALPDQL FYNTGISTYF WILTNRKSPD HKGKVVLLDA
     RDQWQKMRKS LGDKRKELGK DHIATVVKLY GEALSAAQDA EHPLHAKVKV FDNTAFGYQR
     ITVERPLKLR FEVTEETLAA LEASKAIQKL PQASVMLEAF ASLKGSGWSK KTDAWLALKD
     AVVQAGSTWP TGAPFNKALR EAIGVRDPEG EVQLVKGKPE ADAELRDYEN VPLGEDVEEY
     LEREVHPHVP DAWIDHSKTK IGYEIPFTRH FYVYKPPRPL AEIDAELKLL EAEIQGLLGE
     VTE
//
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