ID A0A1M5L085_9FLAO Unreviewed; 421 AA.
AC A0A1M5L085;
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 ORFNames=SAMN04488116_1856 {ECO:0000313|EMBL:SHG57833.1};
OS Allomuricauda flava.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=570519 {ECO:0000313|EMBL:SHG57833.1, ECO:0000313|Proteomes:UP000184532};
RN [1] {ECO:0000313|Proteomes:UP000184532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22638 {ECO:0000313|Proteomes:UP000184532};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQWL01000002; SHG57833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5L085; -.
DR STRING; 570519.SAMN04488116_1856; -.
DR Proteomes; UP000184532; 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; 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 91
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 421 AA; 47503 MW; 9E45944CB46BC670 CRC64;
MPKPQILFLG MQQLRVCELF AGVGGFRLGL EVSGNYKVVW SNQWEPSTKM QHASLVYEAR
FGPKNHSNQN IEEVPTSEIP DHDILVGGFP CQDYSVATSL KNSKGLLGKK GVLWWSIHRI
LSEKKNKPKY LFFENVDRML KSPSTQRGRD FAVMLSSLNE LGYAVEWRVI NAADYGMPQR
RRRVFFLGYH KSTALYQHLK KSSSSTWIEE DGVLSTSFPH KKVSPSATIF NLDKDLVRLS
ERFNPDGGLS PFLNSGLSLD GKVMTQKTLP VYGETGTVLA DVLENGSADE LLFIPQDDLP
KWEYLKGAKK EIRRTKAGFE YNYSEGGMVF PDALDQPSRT IITGEGGKSP SRFKHVVQTT
KGLRRLSPVE LERLNMFPDN HTQLEGISDA KRAFFMGNAL VVGVVERIGK TLFRKIQEFE
K
//