ID A0A3N4ZLL7_9MICO Unreviewed; 488 AA.
AC A0A3N4ZLL7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EDD32_1116 {ECO:0000313|EMBL:RPF26668.1};
OS Georgenia muralis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Georgenia.
OX NCBI_TaxID=154117 {ECO:0000313|EMBL:RPF26668.1, ECO:0000313|Proteomes:UP000280726};
RN [1] {ECO:0000313|EMBL:RPF26668.1, ECO:0000313|Proteomes:UP000280726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14418 {ECO:0000313|EMBL:RPF26668.1,
RC ECO:0000313|Proteomes:UP000280726};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) 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:RPF26668.1}.
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DR EMBL; RKRA01000001; RPF26668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4ZLL7; -.
DR Proteomes; UP000280726; 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 Reference proteome {ECO:0000313|Proteomes:UP000280726};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..133
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 140..453
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 488 AA; 54364 MW; 2745581DA464F09D CRC64;
MVAQVITGEL KNKIDRVWDA FWSGGISNPM EVIEQITYLL FIRRLDDIQT LAEKKARITK
AGIENPVFLP GQAHLRWSQF KNTAPEVMHK TIADEVFPFL RSIGDGTTYS DHMKDARFTI
PTPALLSKVV DMLDDIPMAD RDTNGDVYEY MLSRIATAGT NGQFRTPRHI IDLMVKMTAP
QPTDEICDPA CGTAGFLVAA SEHVRDTHGD ALLDSAQRKH FHASMFHGYD FDSTMLRIGS
MNMLLHGIES PDIRYRDSLS EGAASDANKY TLILANPPFA GSLDYEATAK DLQRIVKTKK
TELLFLALFL KLLKPGGRAA VIVPDGVLFG SSTAHKALRR MLVEDQKLDA VVKLPSGVFR
PYAGVSTAIL LFTKTNSGGT NDVWFYDVRA DGFSLDDKRN PVEANDLPDV LGRWQHLTAE
KDRARTEQSF LVPKADIVSQ GYDLSLNRYR ESVSDETEHR APLDIISDIE TLEDEIIKGL
AELKSMLS
//
