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Database: UniProt
Entry: A0A1I1TVS2_9ACTN
LinkDB: A0A1I1TVS2_9ACTN
Original site: A0A1I1TVS2_9ACTN 
ID   A0A1I1TVS2_9ACTN        Unreviewed;       435 AA.
AC   A0A1I1TVS2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=SAMN05421773_12158 {ECO:0000313|EMBL:SFD62629.1};
OS   Streptomyces aidingensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=910347 {ECO:0000313|EMBL:SFD62629.1, ECO:0000313|Proteomes:UP000199207};
RN   [1] {ECO:0000313|EMBL:SFD62629.1, ECO:0000313|Proteomes:UP000199207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5739 {ECO:0000313|EMBL:SFD62629.1,
RC   ECO:0000313|Proteomes:UP000199207};
RA   de Groot N.N.;
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}.
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DR   EMBL; FOLM01000021; SFD62629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1TVS2; -.
DR   STRING; 910347.SAMN05421773_12158; -.
DR   OrthoDB; 9813719at2; -.
DR   Proteomes; UP000199207; 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; 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:UP000199207};
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        98
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   435 AA;  49056 MW;  D5DF29F537F1CB1C CRC64;
     MTPAPQSEPI KIADLFAGCG GFTQGFYSFR PEGQEDRPEP FFRSVLAIEN NHSAAATYAA
     NFASEPGAGA HVHNEDIEKW EPAHDEIEAD VVLGGPPCQG FSGLGPGKPD DPRNKLWRHY
     VEIVSKIIEP KVFVIENVDR FLRSLEFHQL VEETKPGGML EKYRLIDPPG GSVDEKMPRE
     KRYRRYLLNA ANYGVRQKRR RAIVIGVHKD IPEVADLQYP EPTHADPRKL ASEPEDTLFA
     SNRILPWRTV DDVFKQSAHM QLKDDLEMGP DGCCLTTELH IRRHPEELSL ARYAAIPEGG
     NRKHLVGRSY KVDRFGVIRL SGEPGYASIK GTERYLSTES WDNHNNGSGD VMGRLRMNEP
     AVTIRTEFFK PEKGRYLHPS EPRPITHFEA ARLQGFPETF KWCGSKTEIA RQIGNAVPVE
     LGQQIARAIY RALRG
//
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