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Database: UniProt
Entry: W5C5B1_WHEAT
LinkDB: W5C5B1_WHEAT
Original site: W5C5B1_WHEAT 
ID   W5C5B1_WHEAT            Unreviewed;       352 AA.
AC   W5C5B1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN   ORFNames=CAMPLR22A2D_LOCUS2167 {ECO:0000313|EMBL:SPT17557.1},
GN   CFC21_029367 {ECO:0000313|EMBL:KAF7015541.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS2D02G231300.1};
RN   [1] {ECO:0000313|EMBL:KAF7015541.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7015541.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS2D02G231300.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS2D02G231300.1};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [3] {ECO:0000313|EMBL:SPT17557.1, ECO:0000313|Proteomes:UP000280104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Thind KAUR A.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblPlants:TraesCS2D02G231300.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [5] {ECO:0000313|EMBL:KAF7015541.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7015541.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) 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, ECO:0000256|RuleBase:RU362106}.
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DR   EMBL; CM022216; KAF7015541.1; -; Genomic_DNA.
DR   EMBL; LS480641; SPT17557.1; -; Genomic_DNA.
DR   SMR; W5C5B1; -.
DR   STRING; 4565.W5C5B1; -.
DR   PaxDb; 4565-Traes_2DS_5C8A4D416-1; -.
DR   EnsemblPlants; TraesCS2D02G231300.1; TraesCS2D02G231300.1; TraesCS2D02G231300.
DR   Gramene; TraesCAD_scaffold_015599_01G000200.1; TraesCAD_scaffold_015599_01G000200.1; TraesCAD_scaffold_015599_01G000200.
DR   Gramene; TraesCLE_scaffold_114533_01G000200.1; TraesCLE_scaffold_114533_01G000200.1; TraesCLE_scaffold_114533_01G000200.
DR   Gramene; TraesCS2D02G231300.1; TraesCS2D02G231300.1; TraesCS2D02G231300.
DR   Gramene; TraesCS2D03G0489000.1; TraesCS2D03G0489000.1.CDS; TraesCS2D03G0489000.
DR   Gramene; TraesKAR2D01G0150530.1; cds.TraesKAR2D01G0150530.1; TraesKAR2D01G0150530.
DR   Gramene; TraesPAR_scaffold_081620_01G000200.1; TraesPAR_scaffold_081620_01G000200.1; TraesPAR_scaffold_081620_01G000200.
DR   Gramene; TraesRN2D0100521400.1; TraesRN2D0100521400.1; TraesRN2D0100521400.
DR   Gramene; TraesROB_scaffold_017435_01G000300.1; TraesROB_scaffold_017435_01G000300.1; TraesROB_scaffold_017435_01G000300.
DR   Gramene; TraesWEE_scaffold_015146_01G000300.1; TraesWEE_scaffold_015146_01G000300.1; TraesWEE_scaffold_015146_01G000300.
DR   eggNOG; KOG0820; Eukaryota.
DR   HOGENOM; CLU_041220_2_0_1; -.
DR   OMA; DFVPCPK; -.
DR   OrthoDB; 21458at2759; -.
DR   Proteomes; UP000019116; Chromosome 2D.
DR   Proteomes; UP000280104; Chromosome ii.
DR   Proteomes; UP000815260; Chromosome 2D.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; 1.10.8.480; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001737; KsgA/Erm.
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:SF12; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE, MITOCHONDRIAL; 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:UP000019116};
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          46..216
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   REGION          282..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         41
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         88
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         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   352 AA;  38515 MW;  5902FE2A117DD84A CRC64;
     MNRAVSNSRA RLAAFSASSS LASEAWDGRF RLHKPRGQHL LTNPRVLDAI ARHAALRPGD
     AVLEVGPGTG NLTARLLASP ADRVTAVEID PRMVDAVTAR FGALDLAHKL TVIQGDAMET
     EFPKFDVCVA NIPYGISSPL IAKLLFGTYH FRTATLLLQK EFARRLVAMP GDSEYNRLAA
     NVRMVADVKL LMDVSKRDFV PMPRVDSSLV EIQPRGAPPE VDLAEWLGFT RECFGQKNKT
     LGAIFKQKRK ILDLLKRSQR SERCTSDAPG TGSGIILGVL DDDGNDEACS DEDGDSGDRA
     AGFSTEEVGA FKERIAGALE STDLAGKRPS KMSNDELLYL LRLFNERGIW FQ
//
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