ID U1Y014_9BURK Unreviewed; 528 AA.
AC U1Y014;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=N879_04440 {ECO:0000313|EMBL:ERI34779.1};
OS Alcaligenes sp. EGD-AK7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=1386079 {ECO:0000313|EMBL:ERI34779.1, ECO:0000313|Proteomes:UP000016497};
RN [1] {ECO:0000313|EMBL:ERI34779.1, ECO:0000313|Proteomes:UP000016497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGD-AK7 {ECO:0000313|EMBL:ERI34779.1};
RX PubMed=24407646;
RA Sagarkar S., Bhardwaj P., Yadav T.C., Qureshi A., Khardenavis A.,
RA Purohit H.J., Kapley A.;
RT "Draft genome sequence of atrazine-utilizing bacteria isolated from Indian
RT agricultural soil.";
RL Genome Announc. 2:e01149-13(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|ARBA:ARBA00000743};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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:ERI34779.1}.
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DR EMBL; AVOG02000001; ERI34779.1; -; Genomic_DNA.
DR RefSeq; WP_009458984.1; NZ_AVOG02000001.1.
DR AlphaFoldDB; U1Y014; -.
DR REBASE; 78247; M.AspAK7ORF4440P.
DR PATRIC; fig|1386079.3.peg.849; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000016497; 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:UP000016497};
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 88
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 528 AA; 57952 MW; EDE3A37781C07B80 CRC64;
MTTKQFLLPI ASEITVDLFA GGGGASTGLE QALGRHVDIA VNHDPEAIAL HTINHPQTEH
YVSDVFEINP HVATRGRPVG LLWASPDCKH FSKAKGGKPV SKRIRGLAWV VVKWAKAVRP
RVIILENVEE FQTWGPLTDD GMPCPERKGQ TFQLWKEQLR ALGYRLEYKE LRACDYGAPT
IRKRFFMVAR CDGLPIVWPQ QTHFAKPAKG QLAWRPASDI IDWSIPCPSI FERKRPLADA
TCRRIAKGVM RYVIEAENPF IVPGGVSFIT KFRSGSVGTG LDEPLHTVTA GGETKRMSTG
NVMGMVTAFL AKHYTGVVGS DLQDPIGTVT SVDHHSLITA NLIHMGHGEG KAGGKRFSHG
IRDVEQPLNT VTASGCPAGL VTSHLVKLRN NQFGQGHDEP MPTLTAGGGH VGEVRSFLVK
YYGNEQDGVS LHEPLHTIPT RDRFGLVTVH GVDYQIVDIG LRMLTPRELY RAQGFPDSYI
IDQKPDGSPL TKTAQVRMCG NSVCPPLAHA LVRANYSDQQ ISPREKVA
//