ID A0A0B0KIE6_9GAMM Unreviewed; 1017 AA.
AC A0A0B0KIE6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=PJ15_3523 {ECO:0000313|EMBL:KHF77247.1};
OS Acinetobacter sp. neg1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1561068 {ECO:0000313|EMBL:KHF77247.1, ECO:0000313|Proteomes:UP000030886};
RN [1] {ECO:0000313|EMBL:KHF77247.1, ECO:0000313|Proteomes:UP000030886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=neg1 {ECO:0000313|Proteomes:UP000030886};
RA Chiara M., Horner D.S., Pesole G., Mule' G., Logrieco A., Fanelli F.;
RT "Genome Sequencing of an Acinetobacter spp capable to degrade OTA.";
RL Submitted (NOV-2014) 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:KHF77247.1}.
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DR EMBL; JSZD01000012; KHF77247.1; -; Genomic_DNA.
DR RefSeq; WP_047430147.1; NZ_JSZD01000012.1.
DR AlphaFoldDB; A0A0B0KIE6; -.
DR PATRIC; fig|1561068.3.peg.1821; -.
DR Proteomes; UP000030886; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 299..565
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 1017 AA; 116831 MW; C801B622F55F21A1 CRC64;
MDDSMKHSLL QDPTKYGISE NMLIQFSEKE PLYVHLSYLD LFTNEIDKRP DAVVEINGRA
ALYLVSENIF TIDELRQLKE ILASRADARF LGVLRAGVID IYPLGIFSEN DDQPIVKRID
LSESSINLHD FLIGNLTDKL DKKNNQRKVE QSWLENYLFR LLQTTARNLR ENICANKLTD
NQILSLVGRA LFTRFLIDRK IIVDSDVGNI SNKTSKLNNL FNSVSSISDT FAWLDKTFNG
NLLPLGNFYY NSEDYKEFFS QIGDESEHIC FELQDILLAT INRQMSLDWG RIQFQHVPAD
MLSQVYEHFA HAYQNEFARK TSIHYTPSHI AKILVDSAFD GLEIEDKSSA QILDPSAGAG
VFLVLAFKRL VLEKWKITGE RPTRNQIRGI LNRQLVGLDI NSESLKFAAL SLYLTALELD
PNPTPLSELK FDCLNTKTLI NVSFGEDLQE TLGSLSERLP VELNERFDIV VGNPPWTKQR
GRGVGEKFNE LIERIAISRG IDSKIASQFN VGCDPDIPFI WRAIEWCKPN GMIAYALHAQ
HTLFNYGNSF ILRSALFDCI ELTGIFNGSA LRQEKAIWEN NDAPFCFLIA KNRKPSPFSS
FYYLSPYVEK SLNEQGGFRM DPHMAIPVEQ SQVQANPHLL KTLFRGSWLD HEIIEKIRTN
SEVITLQEFC DKWKLICGSG FQLGSQKVDA SLFKGKYLFD SKEKNKHQYI INTSRLHYFY
HDRIYGNRNP QLFKAPLVLF LESPPPFRNQ RGALLSTEEV IYSESYVGVS TAKHSSPILL
AKYLQLISYS NLFLYYFLMT SAKFGVERDA ILTKEIFTFP LIDFGSFNEE QLTLIESLSE
KLINREEPWN EIDQFMASIY GLNKNEMQVI EDSLKMSLPY AENKKVAQNN PENETLECFQ
NELCRVINPF TKRLNLKLWT SIEDNLNGNQ SGWKFIRIGF SEPKDINNNL SHKFLSELAD
QFWVSQVKIH IDETGCELLI GQLAQNRYWT KTKARLLALD ILNTDLDRAY NYCEGIQ
//