ID Q3SKA1_THIDA Unreviewed; 577 AA.
AC Q3SKA1;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Adenine specific DNA methylase MOD {ECO:0000313|EMBL:AAZ96889.1};
GN OrderedLocusNames=Tbd_0936 {ECO:0000313|EMBL:AAZ96889.1};
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ96889.1, ECO:0000313|Proteomes:UP000008291};
RN [1] {ECO:0000313|EMBL:AAZ96889.1, ECO:0000313|Proteomes:UP000008291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ96889.1,
RC ECO:0000313|Proteomes:UP000008291};
RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; CP000116; AAZ96889.1; -; Genomic_DNA.
DR RefSeq; WP_011311448.1; NC_007404.1.
DR AlphaFoldDB; Q3SKA1; -.
DR STRING; 292415.Tbd_0936; -.
DR REBASE; 11302; M.TdeDORF936P.
DR KEGG; tbd:Tbd_0936; -.
DR eggNOG; COG2189; Bacteria.
DR HOGENOM; CLU_020164_1_1_4; -.
DR OrthoDB; 9816288at2; -.
DR Proteomes; UP000008291; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-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; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR PANTHER; PTHR13370:SF16; TYPE III RESTRICTION-MODIFICATION ENZYME STYLTI MOD SUBUNIT; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1.
DR PRINTS; PR00506; D21N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AAZ96889.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008291};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 68..372
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
FT REGION 542..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 65349 MW; 1FF2DD8ADEA3EB6E CRC64;
MSKQKLELTW IGKEKRPKLE PRILLEDPEK SYHAKHRVSD NDIFDNRLIF GDNLLALKAL
EQEFSGKVKC VFIDPPYNTG SAFAQYDDGL EHSIWLGLVR DRLEIIRRLL SDDGSLWISI
DDNEAHYLKV LCDEIFGRKC FVTSFIWKKV DSPNDNKGAL SPDHEYILCY VKNPDSIYFR
PKQDESILNA YRQPDAESDR PYRDRLLKKN GKNSLRIDRP SMYFPIKGPD GVDVYPIHDD
GQEARWAMGK KGVDELIAKG ELVWKQRESG GVLRWVPYTR EYAPDAPTRP WPTIWSDLHT
TRQTKAHQRS VLEGVQAFET PKPEDLVSRI LSISTNPGDW VLDSFAGSGT TGAAAHKMGR
RWIMVELEET CHTHIIPRLR KVIDGEDKGG VTEALSWHGG GGFRYYRLAP SLIVNDRWGN
PVINPEYNAA QLAEALAKLE GFNYAPSETH WWQHGHSSER DFIYVTTQNL SAEQLQALAD
EVGPERSLLV CCAAFHGVTA AKAAERWPNL TLKKIPKMVL ARCHWGRDDY SLNVTNLPMA
EIEKSEPAPP GNSFKNTKSR KAALANAGQG GLFGENE
//
