ID A0A1G5G2N9_9FIRM Unreviewed; 481 AA.
AC A0A1G5G2N9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=SAMN05660668_02711 {ECO:0000313|EMBL:SCY45833.1};
OS Pseudobutyrivibrio sp. AR14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520804 {ECO:0000313|EMBL:SCY45833.1, ECO:0000313|Proteomes:UP000198746};
RN [1] {ECO:0000313|EMBL:SCY45833.1, ECO:0000313|Proteomes:UP000198746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR14 {ECO:0000313|EMBL:SCY45833.1,
RC ECO:0000313|Proteomes:UP000198746};
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; FMUY01000022; SCY45833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5G2N9; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000198746; 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}; 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 96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 481 AA; 54877 MW; A61E74D8499AA563 CRC64;
MEKTVCELFA GVGGFRCGLN NINTLEDTNK DEKWKTVWFS QWEPADKKTQ WAHSCYVNRF
GDCPDNNGEY TTNDDINTVD KSSVPDHSLL VGGFPCQDYS VASSLATSKG LDGKKGILWW
DIRDMLEAKE SKFVLLENVD RLLKSPAKQR GRDFGIILAC FRDLDYTVEW RVINAAEYGF
QQRRRRTFIF AYKNTTSYAA NAKHAVKYNN MFGEEMKRKS MVHLIEEEGF FAKSFPVDVT
DGKKIKSAEL PKGIGELSDS FSFNFENSGV MKDGIVYTLK TFPKYNGKQI TLGDILEDGE
VDKSFFISES KLYYTSPDIH HSDETKMPLE PEQRKTWQYI KGAKKINRKA ANGHEYVFSE
GPVPMIDEYD KPARTMLTSE GGFSRTTHIV RDKMTGKIRL LTPVEMERIQ GFPSDWTKDC
LIDGEQVPMP LNKRRFMMGN ALVVDLIKQM EPVLDEIISG EPEIEVQFNI AEGLEIVKES
L
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