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Database: UniProt
Entry: A0A160KPG2_9MICO
LinkDB: A0A160KPG2_9MICO
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ID   A0A160KPG2_9MICO        Unreviewed;       319 AA.
AC   A0A160KPG2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=A6122_0175 {ECO:0000313|EMBL:AND15340.1}, C5C18_14585
GN   {ECO:0000313|EMBL:PPG03657.1};
OS   Rathayibacter tritici.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=33888 {ECO:0000313|EMBL:AND15340.1, ECO:0000313|Proteomes:UP000077071};
RN   [1] {ECO:0000313|EMBL:AND15340.1, ECO:0000313|Proteomes:UP000077071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND15340.1,
RC   ECO:0000313|Proteomes:UP000077071};
RA   Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT   "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PPG03657.1, ECO:0000313|Proteomes:UP000239776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSPB 2748 {ECO:0000313|EMBL:PPG03657.1,
RC   ECO:0000313|Proteomes:UP000239776};
RA   Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA   Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA   Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA   Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT   "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT   US Biological Select Agent, Rathayibacter toxicus.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000256|RuleBase:RU000417};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01016, ECO:0000256|RuleBase:RU000416}.
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DR   EMBL; CP015515; AND15340.1; -; Genomic_DNA.
DR   EMBL; PSUO01000043; PPG03657.1; -; Genomic_DNA.
DR   RefSeq; WP_068250475.1; NZ_PSWT01000015.1.
DR   AlphaFoldDB; A0A160KPG2; -.
DR   STRING; 33888.A6122_0175; -.
DR   REBASE; 145457; M.Rtr1953IV.
DR   KEGG; rtn:A6122_0175; -.
DR   PATRIC; fig|33888.3.peg.207; -.
DR   OrthoDB; 9813719at2; -.
DR   Proteomes; UP000077071; Chromosome.
DR   Proteomes; UP000239776; Unassembled WGS sequence.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}; Reference proteome {ECO:0000313|Proteomes:UP000077071};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01016};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}.
FT   ACT_SITE        76
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   319 AA;  34478 MW;  956BA8A33A6052E4 CRC64;
     MNADLTSIEI CTGAGGQALG LEQAGFAHEA LVELEHAACQ TLKLNRPEWN VMEKDLLTWS
     GADYKGVDLL AGGVPCPPFS KAGKQLGAED ERNLFPKAIE LVDEIRPKAV MFENVRGLLD
     AVFDMYRLDV EGQLKKMGYT GGWRLINASD YGVSQLRPRV IFTGVRNEYA DDFHWPTPQE
     ATPLTVGELL HDLMAANGWE GAGEWARNAS TIAPTLVGGS KKHGGPDLGP TRARAAWAML
     GVNGKSLADE APESGFEGMP RLTVRMAARL QGFPDEWKLF GRKTAAYRQV GNAFPPPVAA
     AVGNQISAAL TKRRLHAVA
//
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