ID D8L800_SORBI Unreviewed; 343 AA.
AC D8L800;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN ORFNames=Sb24P17cg_040 {ECO:0000313|EMBL:CAZ96033.1},
GN SORBI_3004G020800 {ECO:0000313|EMBL:KXG29333.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:CAZ96033.1};
RN [1] {ECO:0000313|EMBL:KXG29333.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|EMBL:CAZ96033.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21039564; DOI=10.1111/j.1469-8137.2010.03497.x;
RA Garsmeur O., Charron C., Bocs S., Jouffe V., Samain S., Couloux A.,
RA Droc G., Zini C., Glaszmann J.C., Van Sluys M.A., D'Hont A.;
RT "High homologous gene conservation despite extreme autopolyploid redundancy
RT in sugarcane.";
RL New Phytol. 189:629-642(2011).
RN [3] {ECO:0000313|EMBL:KXG29333.1}
RP NUCLEOTIDE SEQUENCE.
RA Paterson A., Mullet J., Bowers J., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A., Chapman J., Feltus F.,
RA Gowik U., Grigoriev I., Lyons E., Maher C., Martis M., Narechania A.,
RA Otillar R., Penning B., Salamov A., Wang Y., Zhang L., Carpita N.,
RA Freeling M., Gingle A., Hash C., Keller B., Klein P., Kresovich S.,
RA Mccann M., Ming R., Peterson D., Rahman M., Ware D., Westhoff P., Mayer K.,
RA Messing J., Sims D., Jenkins J., Shu S., Rokhsar D.;
RT "WGS assembly of Sorghum bicolor.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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, ECO:0000256|RuleBase:RU362106}.
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DR EMBL; FN431662; CAZ96033.1; -; Genomic_DNA.
DR EMBL; CM000763; KXG29333.1; -; Genomic_DNA.
DR EMBL; CM000763; KXG29334.1; -; Genomic_DNA.
DR AlphaFoldDB; D8L800; -.
DR STRING; 4558.D8L800; -.
DR EnsemblPlants; KXG29333; KXG29333; SORBI_3004G020800.
DR EnsemblPlants; KXG29334; KXG29334; SORBI_3004G020800.
DR Gramene; KXG29333; KXG29333; SORBI_3004G020800.
DR Gramene; KXG29334; KXG29334; SORBI_3004G020800.
DR eggNOG; KOG0820; Eukaryota.
DR InParanoid; D8L800; -.
DR OrthoDB; 316496at2759; -.
DR Proteomes; UP000000768; Chromosome 4.
DR ExpressionAtlas; D8L800; baseline and differential.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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; IPR020596; rRNA_Ade_Mease_Trfase_CS.
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:SF27; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01131; RRNA_A_DIMETH; 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:UP000000768};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01026};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW ECO:0000256|RuleBase:RU362106};
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 87..269
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 343 AA; 37955 MW; 8B967469A85C82CD CRC64;
MVALTSLSPG PPRPSPSPAT PRRRPPAPKP HVYASSRRRG RILRAATAAA ATPGADDYHS
TIRSLNSRGR HVPRKSLGQN YMLNSKVNEE LVAAAGVEEG DVVLEIGPGT GSLTAALLQA
GATVFAVEKD KHMATLVKDR FGSTEQLKVI EEDITKFHIR SHFLPFMKEK YHATKKLAKV
VSNLPFNVSS EVVKLLLPMG DVFSVVVLML QDETAVRLAD ASIQIPEYRP INVFVNFYSK
PEYKFRVDRE NFFPRPKVNG AVISFKLKNA EEYPPVSSPK SFFSMVNSAF MGKRKMLRKS
LQHLCSSSEI EAALDNIGLP VTARPSDLIL DDFVRLHNHL TKV
//
