ID A0A1H4F4D8_9GAMM Unreviewed; 144 AA.
AC A0A1H4F4D8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=DNA-methyltransferase (Dcm) {ECO:0000313|EMBL:SEA92194.1};
GN ORFNames=SAMN05660964_02839 {ECO:0000313|EMBL:SEA92194.1};
OS Thiothrix caldifontis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiothrix.
OX NCBI_TaxID=525918 {ECO:0000313|EMBL:SEA92194.1, ECO:0000313|Proteomes:UP000199397};
RN [1] {ECO:0000313|EMBL:SEA92194.1, ECO:0000313|Proteomes:UP000199397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21228 {ECO:0000313|EMBL:SEA92194.1,
RC ECO:0000313|Proteomes:UP000199397};
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|ARBA:ARBA00000743};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; FNQP01000018; SEA92194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4F4D8; -.
DR STRING; 525918.SAMN05660964_02839; -.
DR Proteomes; UP000199397; Unassembled WGS sequence.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF13384; HTH_23; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:UP000199397};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01016}.
FT ACT_SITE 141
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 144 AA; 15922 MW; 22BA51D6CC1B701C CRC64;
MYEVRASTVL QCLEEAAHYY NHSEIAEKLG VNPSTVGRWL KRETEPKHGI LYGLQQMLMP
FGKPADSADF TFIDLFAGIG GIRKAFELNG GRCVFTSEWD AYAQRTYHAN FADGQPIAGD
ITAIPEANIP AHDVLLAGFP CQPF
//