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Database: UniProt
Entry: G1DUR4_9CAUD
LinkDB: G1DUR4_9CAUD
Original site: G1DUR4_9CAUD 
ID   G1DUR4_9CAUD            Unreviewed;       389 AA.
AC   G1DUR4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   Name=70 {ECO:0000313|EMBL:AEJ93254.1};
GN   ORFNames=SHILAN_70 {ECO:0000313|EMBL:AEJ93254.1};
OS   Mycobacterium phage ShiLan.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Gracegardnervirinae; Cheoctovirus; Mycobacterium virus Shilan.
OX   NCBI_TaxID=1036616 {ECO:0000313|EMBL:AEJ93254.1, ECO:0000313|Proteomes:UP000008402};
RN   [1] {ECO:0000313|EMBL:AEJ93254.1, ECO:0000313|Proteomes:UP000008402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22282335; DOI=10.1128/JVI.06870-11;
RG   the Science Education Alliance Phage Hunters Advancing Genomics and Evolutionary Science Program;
RG   the KwaZulu-Natal Research Institute for Tuberculosis and HIV Mycobacterial Genetics Course Students;
RG   the Phage Hunters Integrating Research and Education Program;
RA   Hatfull G.F.;
RT   "Complete Genome Sequences of 138 Mycobacteriophages.";
RL   J. Virol. 86:2382-2384(2012).
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; JN020143; AEJ93254.1; -; Genomic_DNA.
DR   REBASE; 682814; M.MphSLORF70P.
DR   OrthoDB; 8328at10239; -.
DR   Proteomes; UP000008402; Genome.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Inhibition of host innate immune response by virus
KW   {ECO:0000256|ARBA:ARBA00033479};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01016};
KW   Restriction-modification system evasion by virus
KW   {ECO:0000256|ARBA:ARBA00033479};
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}; Viral immunoevasion {ECO:0000256|ARBA:ARBA00033479}.
FT   REGION          160..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   389 AA;  41865 MW;  39BBEFC7F5E257B2 CRC64;
     MKIGSLFSGA GGLDMAVEHV FNSHVVWQCE YDTAAAKVLA HRYPNIPNCG DVTAINWDSL
     DRVDILCGGY PCQPFSAAGQ RKGTEDERHL WPYFAEAIRR IRPRYVVLEN VAGHRSMGFD
     TVLGDLASVG YDAQWCSVRA SDVGAPHRRE RVFVLATPSD ASDATADRQR SRTQLGQGSA
     DAADANLWSV AARIGRGELL LPTPSAADGD GGHLTRSGER GDELLLPGVA RAYGNGELLP
     TPNAQDGNGG GRYNSAGHQS TLPGTVRLLP TPRKSDGDGG PNPLHRSERM DDVETRIIRC
     AGQWGKYAPA IAHWEAVTRP APTPTEPNRN GNPRLAPAFS EWMMGWPAGW VTEVPGISRN
     DQLRIIGNGV VPQQAAAALR WLLSVEVAA
//
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