ID F0LL26_THEBM Unreviewed; 312 AA.
AC F0LL26;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Type II methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.113 {ECO:0000256|RuleBase:RU362026};
DE AltName: Full=N-4 cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU362026};
GN OrderedLocusNames=TERMP_01959 {ECO:0000313|EMBL:ADT84933.1};
OS Thermococcus barophilus (strain DSM 11836 / MP).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT84933.1, ECO:0000313|Proteomes:UP000007478};
RN [1] {ECO:0000313|EMBL:ADT84933.1, ECO:0000313|Proteomes:UP000007478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX PubMed=21217005; DOI=10.1128/JB.01490-10;
RA Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT "Complete genome sequence of the hyperthermophilic, piezophilic,
RT heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL J. Bacteriol. 193:1481-1482(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC Evidence={ECO:0000256|RuleBase:RU362026};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|RuleBase:RU362026}.
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DR EMBL; CP002372; ADT84933.1; -; Genomic_DNA.
DR RefSeq; WP_013468229.1; NC_014804.1.
DR AlphaFoldDB; F0LL26; -.
DR REBASE; 29889; M.TbaMPORF1959P.
DR GeneID; 10042274; -.
DR KEGG; tba:TERMP_01959; -.
DR PATRIC; fig|391623.17.peg.1957; -.
DR eggNOG; arCOG00115; Archaea.
DR HOGENOM; CLU_024927_5_1_2; -.
DR OrthoDB; 38200at2157; -.
DR Proteomes; UP000007478; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU362026};
KW Reference proteome {ECO:0000313|Proteomes:UP000007478};
KW Restriction system {ECO:0000256|RuleBase:RU362026};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU362026};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..242
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 312 AA; 36755 MW; A19989C44569D9C7 CRC64;
MIIDEIILGD CLEWIPKLKG VHLSFLDPPF NQGKEYRFFN DNLSEEEYWG WMKEVVREIY
KVTEKGGAIY FMQREKNTEW VLRILRETGW TLQNLIIWKK MASAVPQRYR FNKAYQIIAF
ATKGKKPRVF NKLRVDYPLA PWHKYPRENG IYLTDVWDDI RELTSGYFAG DEPLRDESGK
RIHLQQSPVA LLLRIILSST MPGDLVLDPF AGTGTTLVVA KQLKRHYVGI EIDPHYVEVI
KKRLSKLRKA DDISRYREYY RFTENLEKIW PMPEKPLKIP KQKTLLDVEL SKHSKHILKD
GRATGIEENQ LT
//
