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Database: UniProt
Entry: A0A1I2E5I1_9FIRM
LinkDB: A0A1I2E5I1_9FIRM
Original site: A0A1I2E5I1_9FIRM 
ID   A0A1I2E5I1_9FIRM        Unreviewed;       405 AA.
AC   A0A1I2E5I1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=SAMN05216245_12912 {ECO:0000313|EMBL:SFE88214.1};
OS   Succiniclasticum ruminis DSM 9236.
OC   Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC   Succiniclasticum.
OX   NCBI_TaxID=1123323 {ECO:0000313|EMBL:SFE88214.1, ECO:0000313|Proteomes:UP000198896};
RN   [1] {ECO:0000313|EMBL:SFE88214.1, ECO:0000313|Proteomes:UP000198896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9236 {ECO:0000313|EMBL:SFE88214.1,
RC   ECO:0000313|Proteomes:UP000198896};
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; FONL01000029; SFE88214.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2E5I1; -.
DR   STRING; 1123323.SAMN05216245_12912; -.
DR   OrthoDB; 9813719at2; -.
DR   Proteomes; UP000198896; 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; 1.
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:UP000198896};
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        87
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   405 AA;  45630 MW;  EDA44AC19A1AFD99 CRC64;
     MEKTICELFA GVGGFRLGFD RLGTGWKTTW FSQWEPGART QWAHKCYVAH FNDSPDMNGE
     YHTAEDIAAV SKEAIPDHSV LVGGFPCQDY SVAHSLSSAK GIEGKKGVLW WQIRDTIIAK
     KPPFCLLENV DRLLKSPASQ RGRDFGVMLA CLDQLGYIVE WRVINAAVYG AAQRRRRTFI
     FAYKKDTAYA QRMSACLPVD IISQQGFFAT GFPIETIEKT CDTSFPADLV EISDTFEFRF
     ENAGFMKNGK VYTAPVKEIE ETPTLLGSVL QANVDENYYL TTEDMAKWAY MKGAKKIPRK
     SSNGHEYVFS EGPIAFPDPW DRPSRTMLTS ESTKNRSTHV VSDPGTGRLR LITPVEAERL
     QGFDDNWTDT GMPPRMRYFC MGNALVVPMI TRMGKVLDRI INEEP
//
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