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Database: UniProt
Entry: A0A077MA84_9MICO
LinkDB: A0A077MA84_9MICO
Original site: A0A077MA84_9MICO 
ID   A0A077MA84_9MICO        Unreviewed;       364 AA.
AC   A0A077MA84;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE            EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN   Name=hgiDIIM {ECO:0000313|EMBL:CCI52755.1};
GN   ORFNames=BN13_200015 {ECO:0000313|EMBL:CCI52755.1};
OS   Tetrasphaera jenkinsii Ben 74.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI52755.1, ECO:0000313|Proteomes:UP000035720};
RN   [1] {ECO:0000313|EMBL:CCI52755.1, ECO:0000313|Proteomes:UP000035720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ben 74 {ECO:0000313|EMBL:CCI52755.1,
RC   ECO:0000313|Proteomes:UP000035720};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCI52755.1}.
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DR   EMBL; CAJC01000113; CCI52755.1; -; Genomic_DNA.
DR   RefSeq; WP_048544993.1; NZ_HF571038.1.
DR   AlphaFoldDB; A0A077MA84; -.
DR   STRING; 1193518.BN13_200015; -.
DR   OrthoDB; 9813719at2; -.
DR   Proteomes; UP000035720; 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   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; 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; 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:UP000035720};
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        84
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   364 AA;  39728 MW;  1754CEBC89BED21A CRC64;
     MTSQRLSISA VDLFSGAGGL THGLAKAGVN VRVGVDVDPA CEYPYTANNK AKFLLKSVGD
     LEPGDLTSFF LPGSVRLLAG CAPCQTFSSY NQKASTEDDR WWLLRHFSRL AKEMLPELVT
     MENVPGLLDH AVFDEFVASL EESGYKVSKQ VVNCQDYGVP QHRNRLVLLA SRIGPISLLT
     PEQFKTKPRS VRDVIGEGKV PALAAGTADP KDRLHQCSGL SSLNLRRVKA SKPGGTWRDW
     PEELVAECHK KESGKTYPGV YGRMTWDDAA PTMTTQFYGF GNGRFGHPSQ DRAISLREGA
     ILQSFPPSYQ FVAPDAPVHM KTIGRLIGNA VPVALGELIG KSIKAHVKDH RETLLSLRAE
     GQLA
//
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