ID A0A024H4T2_9MICC Unreviewed; 535 AA.
AC A0A024H4T2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN Name=hsdM {ECO:0000313|EMBL:CCQ47180.1};
GN ORFNames=ARTSIC4J27_3160 {ECO:0000313|EMBL:CCQ47180.1};
OS Pseudarthrobacter siccitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=861266 {ECO:0000313|EMBL:CCQ47180.1, ECO:0000313|Proteomes:UP000035722};
RN [1] {ECO:0000313|Proteomes:UP000035722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4J27 {ECO:0000313|Proteomes:UP000035722};
RX PubMed=24948757; DOI=10.1128/genomeA.00526-14;
RA Manzanera M., Santa-Cruz-Calvo L., Vilchez J.I., Garcia-Fontana C.,
RA Silva-Castro G.A., Calvo C., Gonzalez-Lopez J.;
RT "Genome Sequence of Arthrobacter siccitolerans 4J27, a Xeroprotectant-
RT Producing Desiccation-Tolerant Microorganism.";
RL Genome Announc. Announc.2:e00526-e00514(2014).
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:CCQ47180.1}.
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DR EMBL; CAQI01000048; CCQ47180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024H4T2; -.
DR STRING; 861266.ARTSIC4J27_3160; -.
DR REBASE; 89118; M1.Asi4J27ORF3159P.
DR Proteomes; UP000035722; 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; 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:SF3; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 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:0000313|EMBL:CCQ47180.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000313|EMBL:CCQ47180.1}.
FT DOMAIN 42..169
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 181..495
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 535 AA; 59696 MW; 480E543C1DB03D98 CRC64;
MTYPRHCGMN WNLVRENVTE DEAREYAGGF HLAVQPLSLS ELESYLARAA DLLRGSIDQA
DFKAYIFPLM FFKRISDVYM EEFAQALEDS GGDHEYALFA ENHRFSIPGG HLWGDIRNRT
ENIGTALQTA FREIEKANPE TLYGIFGNAS WTNRDKLPDR KLADLVEHFS TKTLSNAAVA
PDVFGNAYEY LIKRFADQSN KKAGEYYTPR SVVRLLINIL NPVDQESVYD PACGTGGMLI
EVIEHVKAAG GSPKSLWGKL YGQEKVLATS GIARMNLLLH GVEDFKIVRE DTLREPAFYS
GNHLAQFDCV VANPPFSLKN WGESEWVSDK WGRNNLGGVP PKGYADWAWV QHMLTSARTQ
NGRVAVVLPQ GALFRQGAEA RIRTHILKAD LVESVIGLAP NLFYGTGLAA CVLILRHEKR
PEKKGKVLFI NGNKLFKRGR NQNTLETEHA ERLLDAYELY QDQDGLSRVV NLAEIAGHGY
SLNIPLYVAP EDEGEELTLA DALANLEAAH TKTAETRRAL EAELAKWGVG QEILA
//