ID   D0T030_ACILW            Unreviewed;       640 AA.
AC   D0T030;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
GN   Name=dam {ECO:0000313|EMBL:EEY88494.1};
GN   ORFNames=HMPREF0017_02904 {ECO:0000313|EMBL:EEY88494.1};
OS   Acinetobacter lwoffii SH145.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY88494.1, ECO:0000313|Proteomes:UP000018425};
RN   [1] {ECO:0000313|Proteomes:UP000018425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH145 {ECO:0000313|Proteomes:UP000018425};
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
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         ECO:0000256|RuleBase:RU361257};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU361257}.
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DR   EMBL; GG705071; EEY88494.1; -; Genomic_DNA.
DR   RefSeq; WP_004282035.1; NZ_GG705071.1.
DR   AlphaFoldDB; D0T030; -.
DR   HOGENOM; CLU_439881_0_0_6; -.
DR   Proteomes; UP000018425; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro.
DR   Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 3.
DR   InterPro; IPR012186; Ade-mod_methylase_MStsI.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00571; dam; 1.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   Pfam; PF02086; MethyltransfD12; 2.
DR   PIRSF; PIRSF036638; M_m6A_StsI; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU361257};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU361257};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361257}.
FT   COILED          408..435
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   640 AA;  73920 MW;  4CB4F481061349BF CRC64;
     MNKPLLADFS TDLTPTKIKC KPILKWAGGK TQMLDSILSR FPNTYGKYIE PFFGGGAVFF
     ALQPENAVIA DSNPELINLY QTVANNVDSV INELEKFINT EEMFYEVRSQ DWESLSSVEA
     AARTIYLNKT CFNGLYRVNK KGQFNVPFGK YKNPKIVDET NLRAASSLLS QAQIICGDYS
     EVLDKFSCPN DLIFLDPPYV PISEYSDFKR YTKEQFYLED HEKLAEIYKK LSNQGCHVFL
     TNSNHPVVQN LYSDFTYEVI QTKRHISCDS KSRKGEDVIV SNSSNKKDFR LDLEKISSVP
     DQVAFYPSTR YMGSKQKLLP YILSIVDQFN EPTLVDLFSG SGIVSYLFKS LGKAVITNDY
     MNMSHTFTKA MIENNHVTLS AEKAKSLLIQ KNSVDDFVQV TFKDLYFSDD ENKLIDILRS
     NIRELDNEYE RAIARSALIR ACMKKRPRGI FTYTGHRYDD GRKDLVLTLE EQFLNAVESI
     NNSIFDNKQS NISWRKNALD IDLDDNCLVY MDPPYYSTCS DNEYVRRYHF VEGLSLDWKD
     IEIQENTKTK KFKSYPTPFS SRKDVYVAFE KLFEKFKKNI LVISYSSNSL PNMDEMLEML
     KKYKKNVEVI PIDYKYSFGN QANKVGDNRN SVQEYLFVAY
//