ID A0A0T6A2P5_9BACT Unreviewed; 660 AA.
AC A0A0T6A2P5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=XU15_C0011G0025 {ECO:0000313|EMBL:KRT69343.1};
OS candidate division NC10 bacterium CSP1-5.
OC Bacteria; candidate division NC10.
OX NCBI_TaxID=1640516 {ECO:0000313|EMBL:KRT69343.1, ECO:0000313|Proteomes:UP000051123};
RN [1] {ECO:0000313|EMBL:KRT69343.1, ECO:0000313|Proteomes:UP000051123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-5 {ECO:0000313|EMBL:KRT69343.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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:KRT69343.1}.
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DR EMBL; LDXR01000011; KRT69343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6A2P5; -.
DR STRING; 1640516.XU15_C0011G0025; -.
DR Proteomes; UP000051123; 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; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF50; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT3; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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}; 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 108
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 660 AA; 73100 MW; 62D840B4D25CBEB2 CRC64;
MPEFVPVDLN TATPYWWKVF EPSASRAFEA ADLYCGCGGG TQAIIESVMR RGGHIRKMIA
VNHWDAAIQV HSANYPQVAH FLNSVENVEP KLAVPNGHLD ILTAGIKCTH HSRAAGGVPR
SEQERMDAFQ VLRWLHDLDV SRLVIENVPE FLEWGPLNQE GRPIERLKGK LFVQWIGMLE
ALNYKVQWKV LTACWYGDPT SRERFWLIAK KGNRKVFFPE ATHRDPNQPA TVDMFRPELP
PWPVARDIID FELPTRSIFG SDLVPNTLSR ILAGLHRFAG IRLKVAELPG CPEFKARKTG
KGEKIRVSPY AVDAHRLHYL NLAIRAAQDH PIAVKNRRYV TKVNPKAVDM VRRLQQAGPP
NEETAAAYMI KMYGESHSAS IDEALPTVVG GSHLGFVLVN RGGQDGYDRN HSLDETMPTL
TTENPIGVVD FLLQQQSGGV ARSVEQPVPA LATDGAVRLV NVIMPSEGYY RGNGARPDDQ
PLPSLTRRGA GLVSYLVSGH HYNGRDRIAS SEVAMPTLTT RPDWSVINTF LAIQHGTNSG
NDRTASVDKA LPTIDTTNRY MAAFLALAYG TERDGQGVDE ALRTVTGKDR FMLVLPGLGF
LDIRYRMLAL KELAKAHSVP AGFTFEGVTN EAGKKMIGNM WPIRMGTAVV DAALTERGEK
//
