ID A0A1G9MYF7_9GAMM Unreviewed; 568 AA.
AC A0A1G9MYF7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=SAMN05661010_02559 {ECO:0000313|EMBL:SDL78917.1};
OS Halomonas muralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=119000 {ECO:0000313|EMBL:SDL78917.1, ECO:0000313|Proteomes:UP000198654};
RN [1] {ECO:0000313|EMBL:SDL78917.1, ECO:0000313|Proteomes:UP000198654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14789 {ECO:0000313|EMBL:SDL78917.1,
RC ECO:0000313|Proteomes:UP000198654};
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; FNGI01000007; SDL78917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9MYF7; -.
DR STRING; 119000.SAMN05661010_02559; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000198654; 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; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF50; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT3; 1.
DR Pfam; PF00145; DNA_methylase; 2.
DR PRINTS; PR00105; C5METTRFRASE.
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:UP000198654};
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 84
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 568 AA; 60947 MW; 8DE5E34B24C90C6B CRC64;
MNLNLFGHEL VVDNFAGGGG ASEGIEQALG RPVDLAINHD ATAIAVHTAN HPGSEHSVAD
VWDVDPEQAT RGMPVGLAWF SPDCRHHSKA KGGRPVSKSV RGLAWVAARW AAKVKPRVII
LENVEEFQDW GPLIKDDQAR IVPDPARKGQ TFRGFVGNLR RHGYQVDWRL LRACDYGTPT
IRRRLFLIAR RDGLPICWPK PTHAAPEAPA VRRGKMQPHR TAAECIDWSI PCPSIFSRNR
PLAENTMKRI AKGVMRYVVE AEQPFIVTCN HGGEGFRGQS LLEPMKTVTA AHDAHGLVVP
HITKFRSGAI GHACDEPMHT ITANSNVEGT GTNPGGAAPF GLVAATMVQT GYGERPGQAP
RAIGLQKPLG TVVAGGQKHA LVSAFLAKHF TGVVGDDLRN PVPTVTATDH NALVAANLVN
LKGADRGGRD LREPMPTVCA GGTHAAAVAA FLAPYYGSGS GETGRDLRAP APTVTTKDRF
QLITVLIDGE RYVITDIGMR MLQPHELAAA QGFPDGYKFA EVNGRPVPKY VQVRLIGNSV
CPPLARAIVA ANFTHEKQFM PAPAAAVA
//
