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Database: UniProt
Entry: A0A193GFV0_9BORD
LinkDB: A0A193GFV0_9BORD
Original site: A0A193GFV0_9BORD 
ID   A0A193GFV0_9BORD        Unreviewed;       635 AA.
AC   A0A193GFV0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE            EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN   ORFNames=BAU07_19040 {ECO:0000313|EMBL:ANN78937.1};
OS   Bordetella flabilis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463014 {ECO:0000313|EMBL:ANN78937.1, ECO:0000313|Proteomes:UP000091926};
RN   [1] {ECO:0000313|EMBL:ANN78937.1, ECO:0000313|Proteomes:UP000091926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU10664 {ECO:0000313|EMBL:ANN78937.1,
RC   ECO:0000313|Proteomes:UP000091926};
RA   LiPuma J.J., Spilker T.;
RT   "Complete genome sequences of Bordetella bronchialis and Bordetella
RT   flabilis.";
RL   Submitted (JUN-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; CP016172; ANN78937.1; -; Genomic_DNA.
DR   RefSeq; WP_066660933.1; NZ_CP016172.1.
DR   AlphaFoldDB; A0A193GFV0; -.
DR   STRING; 463014.BAU07_19040; -.
DR   REBASE; 154093; M2.Bfl10664ORF19035P.
DR   KEGG; bfz:BAU07_19040; -.
DR   OrthoDB; 9813719at2; -.
DR   Proteomes; UP000091926; 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; 3.90.120.10; 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}; 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   635 AA;  68519 MW;  BA3EEA776718A8CD CRC64;
     MIRNQFVLDV HPEILVDNFA GGGGASTGIE MALGRCVDIA INHDPEAVAM HEINHPQTRH
     YCESVWDVDP VEATQGRPVG LAWFSPDCKH FSKAKGGKPR DKRIRGLAWI VLRWAALVRP
     RVIMLENVEE FRTWGPLLES GQPCPARKGQ TFRSFIHQLQ EKGYAVEHRE LRACDYGAPT
     IRKRLFLIAR CDGQPIVWPE PTHGAPTSPE VQAGQRKPWR TAADCIDWSI PCPSIFERQR
     PLAEATLRRI ARGIRRYVID AAQPFIVGAG GPVYSGKPVP ANRPFGALTT ENHRHVVVPH
     ITKFRTGSTG AALGEPMPTI TAGPKENPAG APHAVGIVAP SLVKVNHGGD DFRGRPLDAP
     IATLTGKHGT GIVAPTLVQA GFGERPGQAP RCLDLHKPLG TVTAQGRKHA LVSAFLAKHY
     GGNYDGPGLP LGGPMHTATT VDHHAVVAAQ LVGCGGRAGQ SRPRDAGEPA QTLTAKADTC
     VVTSHLAKLR NNQFGQATDE PMPTLTAGGG HVADVRAFLV KYYSEGGQDQ DCRDPMHTIP
     TKDRIGLVTV AGQEYVIADI GMRMLEPHEL YAAQGFPGDY IIAPTINGRR LPKHAQVRMC
     GNSVCPPLAA ALVRANVSDL SAWTPREAKE KRVAA
//
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