ID Q0B0X4_SYNWW Unreviewed; 481 AA.
AC Q0B0X4;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN OrderedLocusNames=Swol_0021 {ECO:0000313|EMBL:ABI67380.1};
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI67380.1, ECO:0000313|Proteomes:UP000001968};
RN [1] {ECO:0000313|Proteomes:UP000001968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
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}.
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DR EMBL; CP000448; ABI67380.1; -; Genomic_DNA.
DR RefSeq; WP_011639491.1; NC_008346.1.
DR AlphaFoldDB; Q0B0X4; -.
DR STRING; 335541.Swol_0021; -.
DR REBASE; 12331; M.SwoGORF21P.
DR KEGG; swo:Swol_0021; -.
DR eggNOG; COG0863; Bacteria.
DR HOGENOM; CLU_567334_0_0_9; -.
DR OrthoDB; 9773571at2; -.
DR Proteomes; UP000001968; Chromosome.
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; 2.
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; 2.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ABI67380.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001968};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 228..299
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 55364 MW; F95EE617213BF426 CRC64;
MIDTETSNNN LTKKRSGPPN RMNDLIYRDW MKFQKSFFRF KDYQNLIEEC VCFFTKAIWP
DNRPSQTLII GFEDINKEMI PKPRQIEYKS VKSIGEIVKI LKQKEEYYDF VLIDLTNIDS
EEKLADFLNN DADLLFYSLR RSMVTFRYCG VVSKLPRTNG SGFPIPWSIA FSSRNHLRLR
DEKVGLVEAT GQILYCLFMQ AEDDSELAKK VFPNELSIFN GNIEIPSWTI PKSPPRSSIE
VLHPAKFPET LVEEFIKLFT KPGDNVFDPM AGTGSTLIAA LRNERNAIGV ELSPEWASIG
QNRLNYELQP TLFGEPLQKA KMLQGDATNL DAIGQLNGVY FDYVVTSPPY WSMLTNPGSE
NQRNRRNKNL PLTYSKDQND LGNIQDYNDF LDKLVNVYDD VVKKLNSGGV ITIVVKNVKR
NHILYCLAWD LTIRLCQKDK LLEYAGTTLW CQDDVGLKPF AVGTHWVSNI LHQYCLHFRK
K
//