ID A0A1M4N6M0_9CLOT Unreviewed; 350 AA.
AC A0A1M4N6M0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN Name=haeIIIM {ECO:0000313|EMBL:SCN21871.1};
GN ORFNames=N3C_0473 {ECO:0000313|EMBL:SCN21871.1};
OS Clostridium sp. N3C.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1776758 {ECO:0000313|EMBL:SCN21871.1, ECO:0000313|Proteomes:UP000184869};
RN [1] {ECO:0000313|EMBL:SCN21871.1, ECO:0000313|Proteomes:UP000184869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N3C {ECO:0000313|EMBL:SCN21871.1};
RA Seilhamer J.J.;
RL Submitted (AUG-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; FMJL01000003; SCN21871.1; -; Genomic_DNA.
DR RefSeq; WP_074364472.1; NZ_FMJL01000003.1.
DR AlphaFoldDB; A0A1M4N6M0; -.
DR STRING; 1776758.N3C_0473; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000184869; 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; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 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:UP000184869};
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 84
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 350 AA; 39176 MW; 3B599BD2A6296799 CRC64;
MKYRLGELFC GPGGLAYGAI NARSADGKHF IVHEWANDYD KDTCETYRYN ICPDRPESVY
HEDIRKLNMD KLTPIDALAF GFPCNDFSVV GEQKGINGVF GPLYSYGVKA LKKFQPMWFL
AENVGGLRNA NDGKAFAKIL DELKETGYVI TPHLYKFEQY GIPQARHRII IVGIRNDINV
TFKVPSPAPY ANIDNTCRTA LEVPPIPADA PNNERTKQSK TVIQRLLHIK PGENAFTADL
PPELQLKVKG AKISQIYKRL DPDKPAYTVT GSGGGGTHIY HWSEPRALTN RERARLQTFP
DTFVFMGSKE SVRKQIGMAV PCQGAKIIFE AILNCFAGIE YESIEPNINE
//
