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Database: UniProt
Entry: M0P7X3_9EURY
LinkDB: M0P7X3_9EURY
Original site: M0P7X3_9EURY 
ID   M0P7X3_9EURY            Unreviewed;       323 AA.
AC   M0P7X3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=16S ribosomal RNA methyltransferase KsgA/Dim1 family protein {ECO:0000313|EMBL:EMA65644.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:EMA65644.1};
GN   Name=ksgA {ECO:0000313|EMBL:EMA65644.1};
GN   ORFNames=C468_06668 {ECO:0000313|EMBL:EMA65644.1};
OS   Halorubrum kocurii JCM 14978.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halorubrum.
OX   NCBI_TaxID=1230456 {ECO:0000313|EMBL:EMA65644.1, ECO:0000313|Proteomes:UP000011546};
RN   [1] {ECO:0000313|EMBL:EMA65644.1, ECO:0000313|Proteomes:UP000011546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14978 {ECO:0000313|EMBL:EMA65644.1,
RC   ECO:0000313|Proteomes:UP000011546};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(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:EMA65644.1}.
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DR   EMBL; AOJH01000043; EMA65644.1; -; Genomic_DNA.
DR   RefSeq; WP_008848067.1; NZ_AOJH01000043.1.
DR   AlphaFoldDB; M0P7X3; -.
DR   STRING; 1230456.C468_06668; -.
DR   PATRIC; fig|1230456.3.peg.1307; -.
DR   OrthoDB; 9883at2157; -.
DR   Proteomes; UP000011546; 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};
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          42..241
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         35
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         37
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         63
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         144
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         159
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   323 AA;  34412 MW;  09D73D450DD3E371 CRC64;
     MTDSSTGAGA AYGGRDPDAL ARRAGERANP DRDQHFLVDD RVLDRIPAYL PDDADASHLL
     EIGGGAGALT DRLLAVAARR GSDADAAPVD ADAAPVDADA APADADTAPG RLSVIERDGV
     FADFLREEFA TAVDDGLLDV IEGDALDVDL PPFTACVANL PYGVSSEIAF RLLPEGKPLV
     LMFQVEFAER MVASAGESEY GRLSVSAQHY AAVEIVERVP KEAFDPQPAV ESAVVLCTPR
     DPEYEVGDEA FFLRFVKALF TQRRKTVRNA IRNTGHISGL DDPEAVVDAA DEDLLRRRPG
     DLDPSAFAAL AELARERGSP AEV
//
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