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Database: UniProt
Entry: L0RUQ0_MYCC1
LinkDB: L0RUQ0_MYCC1
Original site: L0RUQ0_MYCC1 
ID   L0RUQ0_MYCC1            Unreviewed;       549 AA.
AC   L0RUQ0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=MCYN0531 {ECO:0000313|EMBL:CCP24263.1};
GN   OrderedLocusNames=MCYN_0531 {ECO:0000313|EMBL:CCP24263.1};
OS   Mycoplasmopsis cynos (strain C142) (Mycoplasma cynos).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC   Mycoplasmopsis.
OX   NCBI_TaxID=1246955 {ECO:0000313|EMBL:CCP24263.1, ECO:0000313|Proteomes:UP000010466};
RN   [1] {ECO:0000313|Proteomes:UP000010466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C142 {ECO:0000313|Proteomes:UP000010466};
RX   PubMed=23409256; DOI=10.1128/genomeA.00196-12;
RA   Walker C.A., Mannering S.A., Shields S., Blake D.P., Brownlie J.;
RT   "Complete genome sequence of Mycoplasma cynos strain C142.";
RL   Genome Announc. 1:E00196-E00196(2013).
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; HF559394; CCP24263.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0RUQ0; -.
DR   STRING; 1246955.MCYN_0531; -.
DR   KEGG; mcy:MCYN_0531; -.
DR   PATRIC; fig|1246955.3.peg.481; -.
DR   eggNOG; COG0286; Bacteria.
DR   eggNOG; COG0732; Bacteria.
DR   HOGENOM; CLU_021520_0_0_14; -.
DR   Proteomes; UP000010466; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.220.20; DNA methylase specificity domains; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010466};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          143..426
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   549 AA;  62877 MW;  957A15B9193DF859 CRC64;
     MQKRISGETI SDEELIRVIK DLNKKFNLNN RVRSTDRSLF FSGLIIALTN NNFRQTFEAI
     EAPSEEEVAK IDATILEAYN LNEAILTAIE KQISIKINNL SKEYVWKDKF SFIRNIDYSL
     KEYKEIIKTI RDKVYIPFKN EEKQDILGKA YKLFLARGGK AEDKNIILTP DHIKELMVKL
     ARLTVDDVVL DTCMGSGGFL MEAMEVITHM LKDDVQKINN VYDKQLIGFE IDSVLFALAC
     SNMYLHGDGR SNLLYRSSLL HSDSNGTIVN NKDQVLYKYI KDLKPTKCII NPPYELDSPI
     KFTEQALKYI EDNGKLIIIM PTPTLNKHKS DLTKNILEMA KLDFVIKMPY NLFNEQGRTV
     NTSIFGFTKT PHQPDDEVLF VNLKEDGFES IQHKGRVDVN NKWNDIENKI LDIINNSKEE
     NGLSTKKKIY RKKKDTVDEL ELYPTGIPTK KTGKDLVKLG DLFDFDKEEL FADETSKLQS
     SKNDESGKYD FITAADDWKK HTEYSHDVEA LVYAVSAGGS LGKSQYVNGK FICSNLCTIL
     TKKRVLIVR
//
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