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Database: UniProt
Entry: N1ZQX3_9FIRM
LinkDB: N1ZQX3_9FIRM
Original site: N1ZQX3_9FIRM 
ID   N1ZQX3_9FIRM            Unreviewed;       341 AA.
AC   N1ZQX3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN   ORFNames=C823_05485 {ECO:0000313|EMBL:EMZ19402.1};
OS   Eubacterium plexicaudatum ASF492.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ19402.1, ECO:0000313|Proteomes:UP000012589};
RN   [1] {ECO:0000313|EMBL:EMZ19402.1, ECO:0000313|Proteomes:UP000012589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF492 {ECO:0000313|EMBL:EMZ19402.1,
RC   ECO:0000313|Proteomes:UP000012589};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT   community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-e00214(2014).
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|ARBA:ARBA00001893};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000256|ARBA:ARBA00010203}.
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:EMZ19402.1}.
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DR   EMBL; AQFT01000163; EMZ19402.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1ZQX3; -.
DR   STRING; 1235802.C823_05485; -.
DR   REBASE; 86240; M.Epl492ORF5485P.
DR   PATRIC; fig|1235802.3.peg.5786; -.
DR   eggNOG; COG0863; Bacteria.
DR   HOGENOM; CLU_024927_2_0_9; -.
DR   OrthoDB; 9773571at2; -.
DR   Proteomes; UP000012589; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012589};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          44..331
FT                   /note="DNA methylase N-4/N-6"
FT                   /evidence="ECO:0000259|Pfam:PF01555"
SQ   SEQUENCE   341 AA;  37534 MW;  6B0D88E88280A252 CRC64;
     MDIGVSGNGQ IQGVAAEDIV AVRSNVIINK DCLAALKEMP DKSVDCCITS PPYYGLRDYG
     VEGQIGREAT PEQYVERLAE VFAQLYRVLS DSGTFWLNIS DSYFGTGSKG ACLDPKNPKG
     RNGQKVSLTQ NVRGCKNKDM IGIPWMVAFA LRDSGWYLRS DIIWQKGNAM PENVKDRPTR
     SYEHVFLFSK SSRYYYDASA IAEPIASGTA ARYMRGRSDS NKYSVAVPGQ GNGKVQGINR
     PRKQGEIKKD DISQYRNSRD VWLINTVAYR GAHFAAFPPN LALKCILAGC PENGIVIDPF
     FGSGTTGMVA AENGRRYIGI ELNPEYCILA AERIGGVQIE H
//
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