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Database: UniProt
Entry: A0A0C4WT42_9GAMM
LinkDB: A0A0C4WT42_9GAMM
Original site: A0A0C4WT42_9GAMM 
ID   A0A0C4WT42_9GAMM        Unreviewed;       583 AA.
AC   A0A0C4WT42;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE            EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN   ORFNames=Achr_20160 {ECO:0000313|EMBL:AJE21467.1};
OS   Azotobacter chroococcum NCIMB 8003.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE21467.1, ECO:0000313|Proteomes:UP000068210};
RN   [1] {ECO:0000313|EMBL:AJE21467.1, ECO:0000313|Proteomes:UP000068210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE21467.1,
RC   ECO:0000313|Proteomes:UP000068210};
RX   PubMed=26061173;
RA   Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.;
RT   "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003
RT   (ATCC 4412).";
RL   PLoS ONE 10:E0127997-E0127997(2015).
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};
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DR   EMBL; CP010415; AJE21467.1; -; Genomic_DNA.
DR   RefSeq; WP_039804023.1; NZ_CP010415.1.
DR   AlphaFoldDB; A0A0C4WT42; -.
DR   STRING; 1328314.Achr_20160; -.
DR   REBASE; 101849; M.Ach8003ORF20160P.
DR   KEGG; acx:Achr_20160; -.
DR   HOGENOM; CLU_014695_0_0_6; -.
DR   Proteomes; UP000068210; 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; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AJE21467.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068210};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   583 AA;  63018 MW;  4623F9E47AB0097E CRC64;
     MTAFHTQFGL NFTGEIIVDL FAGGGGASTG IEQALGRPVD VAINHDPDAV SMHTLNHSHA
     KHYLSDVYEV CPLEATAGRP VGLLHASPDC THHSQARAGQ PRSRKIRALA WVVIKWAGTL
     SRHGRAPRVI TLENVEQMLQ WGPLVAKRCA KTGRVVKVDG SVADPGKRVP VAEQYLVPCT
     KRRGRNWAHF VSALRGLGYA VQWRAYAACL HGAATLRKRL YLAARRDDVP IRWPEPSHAA
     KPKRGQRKLS TAAEHIDWSI PCPSIFLDAQ EGKALGVRRP LAEKTLVRLA KGIQKFVIDN
     PDPFIAPDGA VGSLAAMAQN VTGIDPREPL PTVLAGAARF AAVKCEVAPL ITEHANGSSQ
     RNMPASEPLR TICSEVKGGH FALAVAYLAQ QNGGFNETPG HPLTKPMTTI TNTGSQQQLV
     TASLMTLRKN CVGRELTEPV PVITAGAEHH ALVACTLSSE VEAGALRVAA FLTKYYGQGD
     GQDLRDPLHT ITTKDRLALV TVTVRGTPYV IVDIGMRMLT PAELYAAQGF PKGYVFDRGH
     DGRIFSKKTQ VRFVGNSVSP PPMCALVSAL FAEELRISQR MLA
//
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