ID W2BYZ1_9FIRM Unreviewed; 341 AA.
AC W2BYZ1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN ORFNames=HMPREF0378_0533 {ECO:0000313|EMBL:ETJ99466.1};
OS Eubacterium nodatum ATCC 33099.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis.
OX NCBI_TaxID=1161902 {ECO:0000313|EMBL:ETJ99466.1, ECO:0000313|Proteomes:UP000018868};
RN [1] {ECO:0000313|EMBL:ETJ99466.1, ECO:0000313|Proteomes:UP000018868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33099 {ECO:0000313|EMBL:ETJ99466.1,
RC ECO:0000313|Proteomes:UP000018868};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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:ETJ99466.1}.
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DR EMBL; AZKM01000019; ETJ99466.1; -; Genomic_DNA.
DR AlphaFoldDB; W2BYZ1; -.
DR STRING; 1161902.HMPREF0378_0533; -.
DR PATRIC; fig|1161902.3.peg.1062; -.
DR eggNOG; COG0863; Bacteria.
DR OrthoDB; 9773571at2; -.
DR Proteomes; UP000018868; Unassembled WGS sequence.
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: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 ECO:0000313|EMBL:ETJ99466.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018868};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..320
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 341 AA; 39570 MW; 61B197D2A231DF65 CRC64;
MSVDRSKEAF IKENENKIIC GDALETLKNF PDESISCCIT SPPYYGLRDY YKKGQIGREK
TVEEYLDRLV AVFREVRRVL KKDGTCFVVI GDSYAGSGGG KGQYMDPKYS KGRNGQNPSI
TQKVLGYKAK DLMGIPWRLA LLLREDGWYL RSDIIWHKEN AMPEACRDRP TRSYEHVFLL
SKSLRYYYDY EQMAEPMKEV SKKRYVRGRS EDNKYLREDA GIKVQKINEA RRYGEYKGDN
IPQFRNKRDI WTINTTSFRG NHYAAFPPKL AEICMIAGCP KDGIILDPFI GSGTVGFVAL
MQDRKYIGIE LNEEYCKLAR KRISEEVEKI DKEKEYEVCK E
//