ID A0A366D5N9_9NOCA Unreviewed; 668 AA.
AC A0A366D5N9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=DFR74_115124 {ECO:0000313|EMBL:RBO85276.1};
OS Nocardia puris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=208602 {ECO:0000313|EMBL:RBO85276.1, ECO:0000313|Proteomes:UP000252586};
RN [1] {ECO:0000313|EMBL:RBO85276.1, ECO:0000313|Proteomes:UP000252586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44599 {ECO:0000313|EMBL:RBO85276.1,
RC ECO:0000313|Proteomes:UP000252586};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-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:RBO85276.1}.
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DR EMBL; QNRE01000015; RBO85276.1; -; Genomic_DNA.
DR RefSeq; WP_067509191.1; NZ_QNRE01000015.1.
DR AlphaFoldDB; A0A366D5N9; -.
DR STRING; 1210090.GCA_001613185_03072; -.
DR Proteomes; UP000252586; 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; 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 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:UP000252586};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..140
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 153..454
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 668 AA; 74491 MW; 83EDD124F7676966 CRC64;
MSVLSSFVWS VADTLRGPYA EAEYGSVILP FTVLRRLECV MAPHRDVMAE IVAQYPGEQQ
RRTHLKRKTR TADSAGLSFW TTSDFTLQKA LQDPNNLAAN LIDYVGGFSA NLDVFKSFDF
ENVIRTLDTR ERLAQVTRHF EKLDLSPDAV SNADMGDLFE NLIYRFAESA NDGAGQFYTP
RDVVRLLVDL LYAEDTEALR GRGTVRSIYD PTVGTGGMLT IADEHLRGLN PDASTALFGQ
EINPRTYAIC KADLLITGQD ASNVRQGDTL VVDRFEDRRF DYVLSNPPFG TDWKAVESDV
KNEHARGGQG RFAPGLPAVG DAAMLFLLHV ASKMRDVDES GRGGKAGIVL NGSPLFTGGA
GSGPSDIRGH LLENDLIEAI VALPNDMFYN TGIATYLWIL SNAKPADRKG RVQLIDATGL
GSKLRKSIGS KRVEIADKHR TAIVRAFTET QSVDDEITVP TKVFSNRDFA YWTVTVERPL
QLRFECTPDT IEAVTEHKKL GQIAGLRQAL ESFGDQPYLN REKFNRELGK HLGDHGLTLT
TAQRKTLWQT IGIHDEAADI CRYTSGTSKG EPEPDPALRD TENVPFGWGG HPKTHEARDE
TVQDYFDAEV KPHVDNAWID WDKTKTGYEI PFTRHFYTYE PPRPLAEIDR DLERVVGEIM
ELLREVEA
//
