ID A0A098LNM8_9FLAO Unreviewed; 412 AA.
AC A0A098LNM8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=JCM19538_2320 {ECO:0000313|EMBL:GAL87957.1};
OS Jejuia pallidilutea.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Jejuia.
OX NCBI_TaxID=504487 {ECO:0000313|EMBL:GAL87957.1, ECO:0000313|Proteomes:UP000030184};
RN [1] {ECO:0000313|EMBL:GAL87957.1, ECO:0000313|Proteomes:UP000030184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19538 {ECO:0000313|EMBL:GAL87957.1,
RC ECO:0000313|Proteomes:UP000030184};
RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA Sawabe T., Sawabe T.;
RT "Draft Genome Sequence of Marine Flavobacterium Jejuia pallidilutea Strain
RT 11shimoA1 and Pigmentation Mutants.";
RL Genome Announc. 2:e01236-14(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAL87957.1}.
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DR EMBL; BBNY01000001; GAL87957.1; -; Genomic_DNA.
DR RefSeq; WP_045370944.1; NZ_BBNY01000001.1.
DR AlphaFoldDB; A0A098LNM8; -.
DR REBASE; 99791; M.Jpa19538ORF2320P.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000030184; 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 73
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 412 AA; 48133 MW; CC31C16A7CF1B5A5 CRC64;
MRFIDLFAGL GGFHKALHEL GHNCVFASEL DTNLRQLYKQ NWNIEAHGDI KKIVEKEIEI
IPEHDILCAG FPCQPFSKAG KQLGRIDDRG NLFDEIIKIL DFRKPTYFIL ENVPFIAKHD
NEETWSVMKT ELENLGYEVN HEVYSPQDFG IPQHRQRIFI VGSLNGLEHF SFKTIDNKKV
DSIKIEKYID KNSKTAKALP QVNIDCLNIW QEFLENIPEE IKIPGFPIWS MEFGANYPFE
DNYPEKMTVR ELSKYKGNFG VSLEGMSRKE IRANLPSYAR VTKKFPEWKK RYIRENRKFY
EENKKHIENV VKKISTLPSQ SWQKLEWNVG DSERNIYNYF LQFRASGIRI KLPNFFPSLV
CTNTQKPIIG WEKRYISQKE ALRLQSLEGL KLPDNDNAAF KALGNFKLKI AA
//
