ID G5K208_9STRE Unreviewed; 496 AA.
AC G5K208;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN Name=dcm {ECO:0000313|EMBL:EHI70131.1};
GN ORFNames=STRIC_2416 {ECO:0000313|EMBL:EHI70131.1};
OS Streptococcus ictaluri 707-05.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764299 {ECO:0000313|EMBL:EHI70131.1, ECO:0000313|Proteomes:UP000003330};
RN [1] {ECO:0000313|EMBL:EHI70131.1, ECO:0000313|Proteomes:UP000003330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=707-05 {ECO:0000313|EMBL:EHI70131.1,
RC ECO:0000313|Proteomes:UP000003330};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
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:EHI70131.1}.
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DR EMBL; AEUX02000005; EHI70131.1; -; Genomic_DNA.
DR RefSeq; WP_008088331.1; NZ_AEUX02000005.1.
DR AlphaFoldDB; G5K208; -.
DR STRING; 764299.STRIC_2416; -.
DR eggNOG; COG0270; Bacteria.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000003330; 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; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Reference proteome {ECO:0000313|Proteomes:UP000003330};
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 74
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 496 AA; 55450 MW; BE2103E8674717DB CRC64;
MSRLTLGSLF DGSGGFPLAG LQVGIEPLWA SEVEPYTILI TRKNIPSMKH LGDITKLSGY
EIEPVDIITF GSPCQDMSIA GKRDGLNGKS SSLFYEAIRI IKEMRCKTNG QYPRFIIWEN
VLGAFSSNKG EDFRCVLEEI AKVTNENLFI PKPNKWQPAG SVVGESLSIC WRVLDAQYFG
VPQRRKRIFL VADFNSNRGG KILFESKGMS WDITTCQDEK QSITRSTTSS IGEQSECLMF
ENHGQDTRYK GPLEVSNTVS STYGTGGNNQ PFVVENFDVR LTSENTKNAR ANIYKTETSR
TIDTGGNNPD RNQGGVAIVT KSYGISRTTY NQSQKGNMSF NIEEEQSATM LSTGPNAVAQ
PTYSTSKNSH HTIAVKEQAS TLVASDYKDP PIVNTVSYVV RRLTPLECGR LQGFPDYWCQ
NLAISEPTAE DIEFFREVFE MHRVINGKKK SKTDKQIIKW LQNPYSDTAE YKMWGNGVAL
PCVVYVMQSI LKFIEK
//
