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Database: UniProt
Entry: D8GQ55_CLOLD
LinkDB: D8GQ55_CLOLD
Original site: D8GQ55_CLOLD 
ID   D8GQ55_CLOLD            Unreviewed;       156 AA.
AC   D8GQ55;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=CLJU_c30980 {ECO:0000313|EMBL:ADK16146.1};
OS   Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK16146.1, ECO:0000313|Proteomes:UP000001656};
RN   [1] {ECO:0000313|EMBL:ADK16146.1, ECO:0000313|Proteomes:UP000001656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55383 / DSM 13528 / PETC
RC   {ECO:0000313|Proteomes:UP000001656};
RX   PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA   Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA   Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT   "Clostridium ljungdahlii represents a microbial production platform based
RT   on syngas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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DR   EMBL; CP001666; ADK16146.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8GQ55; -.
DR   STRING; 748727.CLJU_c30980; -.
DR   REBASE; 27007; M.CljORF30980P.
DR   KEGG; clj:CLJU_c30980; -.
DR   PATRIC; fig|748727.19.peg.2560; -.
DR   eggNOG; COG0338; Bacteria.
DR   HOGENOM; CLU_063430_10_0_9; -.
DR   Proteomes; UP000001656; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
SQ   SEQUENCE   156 AA;  18709 MW;  2C9CEEFEEC002BAB CRC64;
     MQHGLYFQKT NRPTWKFKTS YGSDHKLYGC VKKDINVATK YLTDIQERLS GVVIENKDFE
     DLLKVYDKED ALVYLDPPYY GTERYYQNKF SKGDHIRLSD YLKNVKGKFI LSYNDCEFIR
     DLYKNFNIDE VQRNHNLVGK YSGRNHKYSE LIIRNY
//
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