ID A0A1D7QMZ1_9SPHI Unreviewed; 412 AA.
AC A0A1D7QMZ1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=BFS30_24410 {ECO:0000313|EMBL:AOM80026.1};
OS Pedobacter steynii.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=430522 {ECO:0000313|EMBL:AOM80026.1, ECO:0000313|Proteomes:UP000094313};
RN [1] {ECO:0000313|EMBL:AOM80026.1, ECO:0000313|Proteomes:UP000094313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DX4 {ECO:0000313|EMBL:AOM80026.1,
RC ECO:0000313|Proteomes:UP000094313};
RA Seilhamer J.J.;
RL Submitted (AUG-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|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; CP017141; AOM80026.1; -; Genomic_DNA.
DR RefSeq; WP_069381688.1; NZ_CP017141.1.
DR AlphaFoldDB; A0A1D7QMZ1; -.
DR REBASE; 159726; M.PstDX4ORF24410P.
DR KEGG; psty:BFS30_24410; -.
DR Proteomes; UP000094313; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
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; PS00095; C5_MTASE_2; 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:UP000094313};
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 REGION 190..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 412 AA; 46287 MW; E607C5EAF399D00D CRC64;
MERQKKVRHG SLFSGIGGFD LAAEWMGWTN VFHCEFDLFC QNVLKYYYPK SRSYGDIKKT
DFRAHRGGID ILSGGFPCQP YSIAGKRLGT ADERHLWPDM LRAIREIRPM WVVGENVRGI
ISWNDGLVFE QVQADLEAEG YQVQAYVLPA AGINAPHRRE RVWFIAYRDS DGCNRGNSPN
EFLADERGQH AFSDPKQGPG HGPFTYTDCI RSKTRNSQAT DDQRRKDTEP LPERNAIRHR
DTPAGRTGAT TDPAMLGCND RRDNWQERSL QSDKGAAAQD QSERQIRKCR PGSAGAAAAD
TGGPGLEGQT GERVSPGREN RAERENKEPA GYGRIPGWRD FPQTEPTICR GNDGIPGKLD
FDALFELYPS TIMPLTFPKW RTESIKALGN AIVPQLALQI FKAIEQTMRK LK
//
