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Database: UniProt
Entry: A6ELT0_9BACT
LinkDB: A6ELT0_9BACT
Original site: A6ELT0_9BACT 
ID   A6ELT0_9BACT            Unreviewed;       421 AA.
AC   A6ELT0;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   13-SEP-2023, entry version 68.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=SCB49_06972 {ECO:0000313|EMBL:EDM45530.1};
OS   unidentified eubacterium SCB49.
OC   Bacteria; Bacteroidota; environmental samples.
OX   NCBI_TaxID=50743 {ECO:0000313|EMBL:EDM45530.1, ECO:0000313|Proteomes:UP000003659};
RN   [1] {ECO:0000313|EMBL:EDM45530.1, ECO:0000313|Proteomes:UP000003659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCB49 {ECO:0000313|EMBL:EDM45530.1,
RC   ECO:0000313|Proteomes:UP000003659};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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}.
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:EDM45530.1}.
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DR   EMBL; ABCO01000001; EDM45530.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ELT0; -.
DR   STRING; 50743.SCB49_06972; -.
DR   REBASE; 23585; M.UbaSCBORF6972P.
DR   Proteomes; UP000003659; 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   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.90.120.30; -; 1.
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; 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; 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:UP000003659};
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        168
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   421 AA;  47968 MW;  5D86C7855230964A CRC64;
     MKLEKINIEN IDGQLFEIKV VEPDNSMPAS FTHYLHNHKN GVSKFYKKDA LKFVKEILTK
     EYPENNITNK VAEEALQLLI FDVNKSVPFP APEKPKFKFI DLFAGIGGFR MALQNLEGKC
     VFTSEWDKYS KQTYKANFGE IPFGDITRPQ TKSYIPDNFD VLCAGFPCQA FSIAGKRGGF
     EDTRGTLFFD VAEIIKRKKP KAIFLENVKG LRNHDKGKTL ATILNVLRED LNYYVPEPQI
     LNAKKFGVPQ NRERIFIVGF RKDLGINNFK YPEPTDTEAI LENILEAEEV SVKYYLSEVY
     LQTLRNHRAR HESKGNGFGY EIIPNNGTAN AVVCGGMGRE RNLVYDDRLT NFKPVTHIKG
     NVNREGIRKM TPREWARLQG FPDNFKIVVS DAQAYKQFGN SVAVPAIQAT AEKIIAKLNY
     K
//
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