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Database: UniProt
Entry: A0A1S2Q049_9ACTN
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ID   A0A1S2Q049_9ACTN        Unreviewed;       351 AA.
AC   A0A1S2Q049;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=BIV23_28210 {ECO:0000313|EMBL:OIJ99471.1};
OS   Streptomyces monashensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1678012 {ECO:0000313|EMBL:OIJ99471.1, ECO:0000313|Proteomes:UP000179642};
RN   [1] {ECO:0000313|EMBL:OIJ99471.1, ECO:0000313|Proteomes:UP000179642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 1 {ECO:0000313|EMBL:OIJ99471.1,
RC   ECO:0000313|Proteomes:UP000179642};
RA   Lee L.-H., Ser H.-L., Law J.W.-F.;
RT   "Genome sequence of Streptomyces sp. MUSC 1.";
RL   Submitted (OCT-2016) 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}.
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:OIJ99471.1}.
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DR   EMBL; MLYO01000051; OIJ99471.1; -; Genomic_DNA.
DR   RefSeq; WP_071383795.1; NZ_MLYO01000051.1.
DR   AlphaFoldDB; A0A1S2Q049; -.
DR   OrthoDB; 9813719at2; -.
DR   Proteomes; UP000179642; 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:UP000179642};
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        90
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   351 AA;  38428 MW;  7F09D656958BBFC9 CRC64;
     MTRTKKRKYT SVEICAGAGG QAVGLHNAGF KHVALIEIDR DACQTLRSNT SANPEWEGCR
     VIEADLKDFQ ADALGLEPGE LDLLAGGVPC PPFSAAGKQL GRDDDRDLFP TMLRLVDDLE
     PKAVMIENVR GLLDPKFDEY RQDIIKQLES MGYEECYWDI LEAKDYGVPQ LRPRAILVAM
     KPEYARHFEH HKPTKTKVIT VGDALHDSMR ARYDAVADDP RAENAFKRWY ERALDGVAPT
     VVGGSKKHGG ADLGPTRAKK AWAELGVCGM GVANEPDEMK DSERDLFAPA GPKLTVTQAA
     LIQGFPEGWK FSGRKTAAYR QVGNAFPPPV AQAVGDQIYA AFEAAAQAEK G
//
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