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Database: UniProt
Entry: W7KX76_9CREN
LinkDB: W7KX76_9CREN
Original site: W7KX76_9CREN 
ID   W7KX76_9CREN            Unreviewed;       221 AA.
AC   W7KX76;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=16S ribosomal RNA methyltransferase KsgA/Dim1 family protein {ECO:0000313|EMBL:EWG07282.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:EWG07282.1};
GN   Name=ksgA {ECO:0000313|EMBL:EWG07282.1};
GN   ORFNames=ASUL_04796 {ECO:0000313|EMBL:EWG07282.1};
OS   Candidatus Aramenus sulfurataquae.
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Aramenus.
OX   NCBI_TaxID=1326980 {ECO:0000313|EMBL:EWG07282.1, ECO:0000313|Proteomes:UP000054284};
RN   [1] {ECO:0000313|EMBL:EWG07282.1, ECO:0000313|Proteomes:UP000054284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ1-illumnia {ECO:0000313|EMBL:EWG07282.1};
RX   PubMed=24604657;
RA   Servin-Garciduenas L.E., Martinez-Romero E.;
RT   "Draft Genome Sequence of the Sulfolobales Archaeon AZ1, Obtained through
RT   Metagenomic Analysis of a Mexican Hot Spring.";
RL   Genome Announc. 2:e00164-14(2014).
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: 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:EWG07282.1}.
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DR   EMBL; ASRH01000004; EWG07282.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7KX76; -.
DR   PATRIC; fig|1326980.6.peg.953; -.
DR   Proteomes; UP000054284; Unassembled WGS sequence.
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   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; IPR029063; SAM-dependent_MTases_sf.
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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}; Reference proteome {ECO:0000313|Proteomes:UP000054284};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01026};
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          14..163
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   BINDING         7
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         9
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         35
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         52
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         70
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   221 AA;  25818 MW;  6AC558020297713D CRC64;
     MSKLSQNFLH DKSFVDKFVY YVFSMGLTRP LIEVGCGKGI ITAKVNPDVC IEIDVNLLQY
     LRSFSPVVSD ARFLPVFRGS IVSSLPYSIT RDFFIEVSEL NDVNKMLLIL QKDFVDKILE
     YPSYISFLLN YYYLIRPMDV IPPDAFSPKP KVYSQIVYFV RKRRYDDRVS QVIECVSRFR
     NKKVKKAAEL CNIKSDNERR VRDYKPWEIL ELLSSMDISS V
//
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