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Database: UniProt
Entry: A0A164HDC0_9NOCA
LinkDB: A0A164HDC0_9NOCA
Original site: A0A164HDC0_9NOCA 
ID   A0A164HDC0_9NOCA        Unreviewed;       385 AA.
AC   A0A164HDC0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=AWN90_11070 {ECO:0000313|EMBL:KZM68415.1};
OS   Nocardia terpenica.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=455432 {ECO:0000313|EMBL:KZM68415.1, ECO:0000313|Proteomes:UP000076512};
RN   [1] {ECO:0000313|EMBL:KZM68415.1, ECO:0000313|Proteomes:UP000076512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 0406 {ECO:0000313|EMBL:KZM68415.1,
RC   ECO:0000313|Proteomes:UP000076512};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-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:KZM68415.1}.
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DR   EMBL; LWGR01000021; KZM68415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164HDC0; -.
DR   STRING; 455432.AWN90_11070; -.
DR   REBASE; 170385; M.Nte406ORF11070P.
DR   OrthoDB; 9813719at2; -.
DR   Proteomes; UP000076512; 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; 3.40.50.150; 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; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF59; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT1-RELATED; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}; Reference proteome {ECO:0000313|Proteomes:UP000076512};
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        73
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   385 AA;  41504 MW;  DE003948DA24FF43 CRC64;
     MTGARMVGLF AGIGGLELGL GAHGWESELL CEIEPGAQAV LSARFPGVEV HGDVTRLRAL
     PAGTELVAAG FPCQDLSQAG RTAGITGARS GLVDEVFRLV RRKRGPRWLL IENVPFMLQL
     GQGQAMRHIT AALDELGYTW AYRVVDARAF GLPQRRQRVL MLASRTEDPR PVLFGPDAGP
     RVIGNPETDP CGFYWTEGVR GLGWAVNAVP TLKGGSALGI ASPPAVRLPS GEIVTPGITD
     AERLQGFSRD WTAPALTAPG IRPGHRWKLV GNAVSVRMAE WIGGRLATPT ADTFPDDLPL
     TGTRWPTAAW GRAGTARRVP VSTWPVHEPY EDLQWFLEDA RLLSARAAAG FLRRAARGTL
     RFPPGFIVEV QNHLLRMGGM PQEAA
//
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