ID A0A0M2V239_9BACT Unreviewed; 414 AA.
AC A0A0M2V239;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN Name=dcm_1 {ECO:0000313|EMBL:KKO21186.1};
GN ORFNames=BROFUL_00068 {ECO:0000313|EMBL:KKO21186.1};
OS Candidatus Brocadia fulgida.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Brocadia.
OX NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO21186.1, ECO:0000313|Proteomes:UP000034954};
RN [1] {ECO:0000313|EMBL:KKO21186.1, ECO:0000313|Proteomes:UP000034954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KKO21186.1};
RX PubMed=24267221; DOI=10.1186/1471-2180-13-265;
RA Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W.,
RA Keltjens J.T., Jetten M.S.;
RT "Identification of the type II cytochrome c maturation pathway in anammox
RT bacteria by comparative genomics.";
RL BMC Microbiol. 13:265-265(2013).
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:KKO21186.1}.
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DR EMBL; LAQJ01000008; KKO21186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2V239; -.
DR PATRIC; fig|380242.3.peg.85; -.
DR Proteomes; UP000034954; 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; 2.
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:UP000034954};
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 116
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 414 AA; 48075 MW; 1A42F11903F4331B CRC64;
MRYIDLFAGA GGFSEGFKRA GFEPVAHVEI DPAACFTLKT RLSYHYLNEN KKLDIYIKYL
KGEISRNLLY SVIPSHILGS VINLSIGDEN NFKIFQMVEK LAGRKKIDII VGGPPCQAYS
LVGRARDRNG MRDDPRNHLY VQYGRFLKKY SPKLFIFENV LGLLSAEKGK YFKNIQADFK
SFGYIVEPFI VNANEFGVLQ NRKRVIIIGW KKDINFSFDQ LKCQSRVEYK VGNIFNDLPK
LSDGKGKDKY YEYAEGINDY LSFTRIRNGL DVLTQHITRP HTEQDKEIYR IAVRKWKRSK
ERLDYNDLPE RLKTHKNRYA FLDRFKVVAD DVPYSQTVVA HIAKDGHYYI HPDIEQNRSI
SVREAARLQS FPDDYYFEGV KEGKNRTAAF RQIGNAVPPL MIEKIAKLLI EYLK
//
