ID Q8EVR5_MALP2 Unreviewed; 395 AA. AC Q8EVR5; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 130. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN OrderedLocusNames=MYPE4940 {ECO:0000313|EMBL:BAC44284.1}; OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Malacoplasma. OX NCBI_TaxID=272633 {ECO:0000313|EMBL:BAC44284.1, ECO:0000313|Proteomes:UP000002522}; RN [1] {ECO:0000313|EMBL:BAC44284.1, ECO:0000313|Proteomes:UP000002522} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HF-2 {ECO:0000313|EMBL:BAC44284.1, RC ECO:0000313|Proteomes:UP000002522}; RX PubMed=12466555; DOI=10.1093/nar/gkf667; RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K., RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.; RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular RT bacterial pathogen in humans."; RL Nucleic Acids Res. 30:5293-5300(2002). RN [2] {ECO:0007829|PDB:4DKJ} RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-HOMOCYSTEINE. RX PubMed=23248272; DOI=10.1073/pnas.1207986110; RA Wojciechowski M., Czapinska H., Bochtler M.; RT "CpG underrepresentation and the bacterial CpG-specific DNA RT methyltransferase M.MpeI."; RL Proc. Natl. Acad. Sci. U.S.A. 110:105-110(2013). 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}. 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; BA000026; BAC44284.1; -; Genomic_DNA. DR RefSeq; WP_011077318.1; NC_004432.1. DR PDB; 4DKJ; X-ray; 2.15 A; A=1-395. DR PDBsum; 4DKJ; -. DR AlphaFoldDB; Q8EVR5; -. DR SMR; Q8EVR5; -. DR STRING; 272633.gene:10731611; -. DR REBASE; 6754; M.MpeI. DR KEGG; mpe:MYPE4940; -. DR eggNOG; COG0270; Bacteria. DR HOGENOM; CLU_006958_0_6_14; -. DR InParanoid; Q8EVR5; -. DR BRENDA; 2.1.1.37; 10550. DR Proteomes; UP000002522; Chromosome. 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 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; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00675; dcm; 1. DR PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1. DR PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 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; PS51679; SAM_MT_C5; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4DKJ}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE- KW ProRule:PRU01016}; Reference proteome {ECO:0000313|Proteomes:UP000002522}; 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 135 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016" FT BINDING 20 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0007829|PDB:4DKJ" FT BINDING 22 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0007829|PDB:4DKJ" FT BINDING 45 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0007829|PDB:4DKJ" FT BINDING 46 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0007829|PDB:4DKJ" FT BINDING 113 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0007829|PDB:4DKJ" FT BINDING 114 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0007829|PDB:4DKJ" FT BINDING 154 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0007829|PDB:4DKJ" FT BINDING 375 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0007829|PDB:4DKJ" SQ SEQUENCE 395 AA; 46106 MW; CB06EB0EF415132E CRC64; MNSNKDKIKV IKVFEAFAGI GSQFKALKNI ARSKNWEIQH SGMVEWFVDA IVSYVAIHSK NFNPKIEQLD KDILSISNDS KMPISEYGIK KINNTIKASY LNYAKKHFNN LFDIKKVNKD NFPKNIDIFT YSFPCQDLSV QGLQKGIDKE LNTRSGLLWE IERILEEIKN SFSKEEMPKY LLMENVKNLL SHKNKKNYNT WLKQLEKFGY KSKTYLLNSK NFDNCQNRER VFCLSIRDDY LEKTGFKFKE LEKVKNPPKK IKDILVDSSN YKYLNLNKYE TTTFRETKSN IISRSLKNYT TFNSENYVYN INGIGPTLTA SGANSRIKIE TQQGVRYLTP LECFKYMQFD VNDFKKVQST NLISENKMIY IAGNSIPVKI LEAIFNTLEF VNNEE //