ID A0A1I5MTI1_9BACT Unreviewed; 444 AA.
AC A0A1I5MTI1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=SAMN04515674_101440 {ECO:0000313|EMBL:SFP12825.1};
OS Pseudarcicella hirudinis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Pseudarcicella.
OX NCBI_TaxID=1079859 {ECO:0000313|EMBL:SFP12825.1, ECO:0000313|Proteomes:UP000199306};
RN [1] {ECO:0000313|EMBL:SFP12825.1, ECO:0000313|Proteomes:UP000199306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E92,LMG 26720,CCM 7988 {ECO:0000313|Proteomes:UP000199306};
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; FOXH01000001; SFP12825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5MTI1; -.
DR STRING; 1079859.SAMN04515674_101440; -.
DR Proteomes; UP000199306; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199306};
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 98
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 444 AA; 50100 MW; D453A6AE9FBEA817 CRC64;
MPGIGIYKNK DMSKKISYSD FSLDDIVLLD LFAGTGGFAK GLKDAGFKFK KHYFSEIDPN
CIANYQYNFR NAEPLGSITN IRGFDLGKVD IITFGSPCQD FSLAGNRKGM GGKRSSFIKE
AIRLVDECKP QLFFWENVKG AFSSNNGEDF WSIIKAFANL GNYNIEWQLL NTTWVLPQNR
ERIFLVGHLA TSGGSFKGIF PFTETDCLRY KPETNFKKIH SNYRISLPLM ASGTQTWTGD
YIRSGTYRTH KDGNGFRQNH GDCAATIPAR ARKDGSGQGV IKIISKPHGF YKGNESEISP
TIKSNSFEHN NFVSIKPVLT PGRIVKRQNG RRIKEDGDPA FTLGCQEQHG ILLDDSEIRR
FTEIECERLQ GLPDNWTKFG LFKARNVDIK KRSDEIMIHN NEAYIVREIK PTNRYKMCGN
AVTATIVTLI GIKYLNNNID TVKP
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