ID X0SRE5_9BACI Unreviewed; 286 AA. AC X0SRE5; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 28-FEB-2018, entry version 24. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN ORFNames=BTS2_3301 {ECO:0000313|EMBL:GAF66400.1}; OS Bacillus sp. TS-2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1450694 {ECO:0000313|EMBL:GAF66400.1, ECO:0000313|Proteomes:UP000019504}; RN [1] {ECO:0000313|EMBL:GAF66400.1, ECO:0000313|Proteomes:UP000019504} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TS-2 {ECO:0000313|EMBL:GAF66400.1, RC ECO:0000313|Proteomes:UP000019504}; RA Fujinami S., Takeda K., Onodera T., Satoh K., Sano M., Narumi I., RA Ito M.; RT "Draft Genome Sequence of Potassium-Dependent Alkaliphilic Bacillus RT sp. Strain TS-2, Isolated from a Jumping Spider."; RL Genome Announc. 2:e00458-14(2014). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L- CC homocysteine + DNA containing 5-methylcytosine. CC {ECO:0000256|RuleBase:RU000417}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. C5-methyltransferase family. CC {ECO:0000256|RuleBase:RU000416}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAF66400.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BAWL01000025; GAF66400.1; -; Genomic_DNA. DR RefSeq; WP_045487356.1; NZ_BAWL01000025.1. DR EnsemblBacteria; GAF66400; GAF66400; BTS2_3301. DR Proteomes; UP000019504; 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 InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR031303; C5_meth_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR PRINTS; PR00105; C5METTRFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00675; dcm; 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 Complete proteome {ECO:0000313|Proteomes:UP000019504}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:GAF66400.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000019504}; KW Restriction system {ECO:0000256|SAAS:SAAS00783597}; KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01016}; KW Transferase {ECO:0000256|RuleBase:RU000417}. FT ACT_SITE 72 72 {ECO:0000256|PROSITE-ProRule:PRU01016}. SQ SEQUENCE 286 AA; 32774 MW; 70D3ED7A1A670922 CRC64; MITAKSYFSG AGGMDLGMKE AGIDIIESYE IDSVACQTLR MNFNHNINEC DLTKTKVLDQ KEADVFIGTF PCKNYSRIAD IHGTRTGDDL FLHFFRHVAL AKPEVYIVEN VPGMRKFQVV MECLTKLPDY YVRVECQVNA NIWLPQERKR LIVIGTKKPF HNFRYPENVE RIKMKDVIEI GSEVYTPNYV KSRLEGAYRD KPIITDLEGI APTCVAHYSK DRSTRLINDG KTIRPYSVLE YGRLQGFPDW FKFAGSDNDA YKQIGNAVPP VMGRWIGNEI KRYFAA //