ID E0TJ17_ZINIC Unreviewed; 254 AA.
AC E0TJ17;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative dimethyladenosine transferase {ECO:0000313|EMBL:ADM89794.1};
GN Name=ksgA {ECO:0000313|EMBL:ADM89794.1};
GN OrderedLocusNames=ZICARI_190 {ECO:0000313|EMBL:ADM89794.1};
OS Zinderia insecticola (strain CARI).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Zinderia.
OX NCBI_TaxID=871271 {ECO:0000313|EMBL:ADM89794.1, ECO:0000313|Proteomes:UP000001303};
RN [1] {ECO:0000313|EMBL:ADM89794.1, ECO:0000313|Proteomes:UP000001303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CARI {ECO:0000313|EMBL:ADM89794.1,
RC ECO:0000313|Proteomes:UP000001303};
RX PubMed=20829280; DOI=10.1093/gbe/evq055;
RA McCutcheon J.P., Moran N.A.;
RT "Functional convergence in reduced genomes of bacterial symbionts spanning
RT 200 My of evolution.";
RL Genome Biol. Evol. 2:708-718(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CARI;
RA McCutcheon J.P., Moran N.A.;
RT "Functional convergence in reduced genomes of bacterial symbionts spanning
RT 200 million years of evolution.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01026}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01026}.
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DR EMBL; CP002161; ADM89794.1; -; Genomic_DNA.
DR AlphaFoldDB; E0TJ17; -.
DR STRING; 871271.ZICARI_190; -.
DR KEGG; zin:ZICARI_190; -.
DR HOGENOM; CLU_041220_0_2_4; -.
DR Proteomes; UP000001303; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR011530; rRNA_adenine_dimethylase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00755; ksgA; 1.
DR PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR PANTHER; PTHR11727:SF7; DIMETHYLADENOSINE TRANSFERASE-RELATED; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Reference proteome {ECO:0000313|Proteomes:UP000001303};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01026};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01026}.
FT DOMAIN 18..185
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT BINDING 13
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 254 AA; 30676 MW; D8623CBD31ECF47E CRC64;
MKIKKNKFSQ IFLINNNLIK KIIKKINIKN NDFILEIGFG NGNLTKYLIK YKIFLFAIEI
DKKLYKNLKI KYKNKINLFN YNILKFNIKI FNKKFRIIGN LPYNISKKII LYFIKFYKNI
KDIYVMLQKE FVKKINANYG NKKFSKISIL TQIKFNIIIL LNISKKNFYP IPKVNSYFIK
MIPKKYIYYN KSILNLILKI SFFKKKKIIK NSMKKIFNLN NFNFLNINFN FKAKDLSIKN
YLKLTNLLEK KLNL
//