ID A0A136JLD8_9BACT Unreviewed; 254 AA.
AC A0A136JLD8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN Name=yhdJ_2 {ECO:0000313|EMBL:KXJ97947.1};
GN ORFNames=UZ19_OD1000850 {ECO:0000313|EMBL:KXJ97947.1};
OS Parcubacteria bacterium OLB19.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1617425 {ECO:0000313|EMBL:KXJ97947.1, ECO:0000313|Proteomes:UP000070365};
RN [1] {ECO:0000313|EMBL:KXJ97947.1, ECO:0000313|Proteomes:UP000070365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB19 {ECO:0000313|EMBL:KXJ97947.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (MAR-2015) 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:KXJ97947.1}.
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DR EMBL; JZEL01000028; KXJ97947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136JLD8; -.
DR STRING; 1617425.UZ19_OD1000850; -.
DR PATRIC; fig|1617425.3.peg.864; -.
DR Proteomes; UP000070365; 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 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 PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR PANTHER; PTHR13370:SF33; TYPE II METHYLTRANSFERASE M.MJAV; 1.
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:KXJ97947.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXJ97947.1}.
FT DOMAIN 31..239
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 254 AA; 28936 MW; 3DD72A6DAA0E615F CRC64;
MSKADFETKF LNKIICGNTV DVMKEMPDSS VDLIITSPPY NLKNSTGNGM KDGRGGKWAN
AALQKGYSHY DDNMPHDEYV KWQRDCLTEM YRLIPEDGAI FYNHKWRVQG GLLQDRQDIV
TGFPVRQILI WRRKGGLNFN PGYFLPTYEV IYLIAKPKFR LVDKANAYGD IWEFTQEMKN
GHPAPFPVAL IDRIVGSTKA KIVLDPFMGS GTTAISAINH SRHYIGIDIS PDYCEMAEKR
IKEHTVQDKL ALNI
//
