ID I6ZYS8_MELRP Unreviewed; 322 AA.
AC I6ZYS8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN OrderedLocusNames=MROS_0937 {ECO:0000313|EMBL:AFN74178.1};
OS Melioribacter roseus (strain JCM 17771 / P3M-2).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Melioribacteraceae; Melioribacter.
OX NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN74178.1, ECO:0000313|Proteomes:UP000009011};
RN [1] {ECO:0000313|EMBL:AFN74178.1, ECO:0000313|Proteomes:UP000009011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17771 / P3M-2 {ECO:0000313|Proteomes:UP000009011};
RX PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT organotrophic bacterium representing a novel deep lineage within
RT Bacteriodetes/Chlorobi group.";
RL PLoS ONE 8:E53047-E53047(2013).
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; CP003557; AFN74178.1; -; Genomic_DNA.
DR RefSeq; WP_014855614.1; NC_018178.1.
DR AlphaFoldDB; I6ZYS8; -.
DR STRING; 1191523.MROS_0937; -.
DR REBASE; 51257; M.Mro3ORF937P.
DR GeneID; 78565930; -.
DR KEGG; mro:MROS_0937; -.
DR PATRIC; fig|1191523.3.peg.990; -.
DR eggNOG; COG0270; Bacteria.
DR HOGENOM; CLU_006958_0_1_10; -.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000009011; Chromosome.
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 CDD; cd00315; Cyt_C5_DNA_methylase; 1.
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:UP000009011};
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 78
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 322 AA; 37259 MW; 89FD661FEB91F091 CRC64;
MEIKYIDLFC GIGGFRYAAE QAFKEYSIKP KCVFSSDIDK YAREAYFANF GEYPAGDITK
IDENDIPDHD VLFAGFPCQP FSIIGQKKGF EDTRGTLFFD IARILSAKRP KAFVLENVKM
LVGHDKGRTL KTILRVLREL GYYVDYKVLN ALDYGLPQKR ERVIIIGYYK FILFSWPPPY
PKRRSLEEIL EKNVDEKYYV SERIREKRLN SHKSEYKVSI WHENKAGHIS SYDYSCALRA
GASHNYLLVN GVRRLTPREM LRLQGFPESF KIVVSEAQTR KQAGNAVPVN MIKAVLEAFL
PHWIEDFAYE ESKQKSEIAI QG
//
