ID A0A1H9B8Z7_9ACTN Unreviewed; 676 AA.
AC A0A1H9B8Z7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05216481_102257 {ECO:0000313|EMBL:SEP85500.1};
OS Streptomyces radiopugnans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=403935 {ECO:0000313|EMBL:SEP85500.1, ECO:0000313|Proteomes:UP000199055};
RN [1] {ECO:0000313|EMBL:SEP85500.1, ECO:0000313|Proteomes:UP000199055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3519 {ECO:0000313|EMBL:SEP85500.1,
RC ECO:0000313|Proteomes:UP000199055};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOET01000002; SEP85500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9B8Z7; -.
DR STRING; 403935.SAMN05216481_102257; -.
DR Proteomes; UP000199055; 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 CDD; cd02440; AdoMet_MTases; 1.
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:UP000199055};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 22..154
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 167..466
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 676 AA; 75469 MW; F639C4F4D3C30B28 CRC64;
MGSGHFGRIP GIQLNSSKHT ELANHAWSVA DLLRGDYKQS DYGKVILPFT VLRRLECVLE
PTREKVTQIA EQYKDSDIDP DRFLRRAAGH AFYNRSGLTL KKIAADPQNA AKNLAVYVGA
FSDNARGVLD RFEFAQQIKR LDGAGLLYQV IGKFTDLDLR PETVPNHNMG YIFEELIRRF
AEQSNETAGE HFTPREVIQL MVRLLVAPDG DALQLPGAVR TVLDPACGTG GMLSAMDDLI
TELNPDATVE VYGQELNPES WAICRSDLMI KGQDPENIAF GNSFSDDGHA RKTFDYMLAN
PPFGVEWKKV KEDVEAEHKT LGEAGRFGAG LPRINDGSLL FLQHMISKMK PVDVDGGGGS
RLAIVFNGSP LFTGAAGSGE SEIRRWILEN DWLEGIVALP DQLFYNTGIS TYFWILTNRK
SPDHKGKVVL LDARDQWQKM RKSLGDKRKQ LGTDHIATVV KLYGEALAVA DDADHPLHGK
VKVFRNEDFG YRRITVERPL KLRFEVTEES LAALEASKPI QRLEQAPLLA GAFKSLMGTR
WATKQEAWLA LKDAVVQAGG TWPTSAPFYK ALREVIGVRD PEGEVQLVKG QPEPDTELRD
YENVPLGEDV EEYLAREVHP HVPDAWIDHS KTKIGYEIPF TRHFYVYEPP RPLAEIDAEL
KALEAEIQGL LGEVTE
//
