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Database: UniProt
Entry: A0A0E0CE42_9ORYZ
LinkDB: A0A0E0CE42_9ORYZ
Original site: A0A0E0CE42_9ORYZ 
ID   A0A0E0CE42_9ORYZ        Unreviewed;       701 AA.
AC   A0A0E0CE42;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI02G01100.2};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI02G01100.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI02G01100.2};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI02G01100.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0CE42; -.
DR   STRING; 40149.A0A0E0CE42; -.
DR   EnsemblPlants; OMERI02G01100.2; OMERI02G01100.2; OMERI02G01100.
DR   Gramene; OMERI02G01100.2; OMERI02G01100.2; OMERI02G01100.
DR   HOGENOM; CLU_408482_0_0_1; -.
DR   Proteomes; UP000008021; Chromosome 2.
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   CDD; cd12234; RRM1_AtRSp31_like; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR   PANTHER; PTHR11727:SF27; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50102; RRM; 2.
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:UP000008021};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01026};
KW   rRNA processing {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          423..495
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          516..587
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..701
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         79
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         81
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         106
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         156
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         186
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   701 AA;  78311 MW;  CB77898661718824 CRC64;
     MVALPSLSPP PPRPSPSPAT PRRRPPPPPP HATSSPPRVR SRLATVVSAA SGVTDGYHST
     IRSLNSRGRH VPRKSLGQNY MLNSKVNEEL VAAAGVEEGD VVLEIGPGTG SLTAALLDAG
     ATVFAVEKDK HMATLVNDRL GSTEQLKNTM QIIEEDITKF SVRSHFLPFL EENSHHTRKY
     AKVVSNLPFN VSTEVVKLLL PMGDVFSVMV LLLQDETALR FADASIQTPE YRPINVFVNF
     YSEPEYKFKV ERTNFFPQPK VDGAVISFKL KNSGDYPPVN SAFNGKRKML RKSLQHLCSS
     SEIEAALANI GLPVTPLAVL FLPSVTAGGP TSIQHQGKYL PPSNSSIPTL STSSSIKTLT
     AATDQSPLSP PLRFSIRRRR PNQSPRGGGD LGFPRRRLPP RCRPLLPSSI TGGLRRVACP
     KMRPVFCGNL DYDARQSEIE RLFSKYGRVE RVDMKSGFAF VYMEDERDAD EAIHRLDRIE
     FGRKGRRLRV EWTKEDRSGG RRGNSKRSPN NTRPTKTLFV INFDPINTRT RDLERHFDQY
     GKISNVRIRR NFAFVQYELQ EDATKALEGT NGSTLMDRVI SVEYALRDDD EKRNGYSPER
     RGRDRSPDKR EYRGRSASPY GRGRERGSPD YGRGRERGSP DYGRGGDRGS PDYRRGASPQ
     GGNKGDERGS PPNNYDRERC EASPGYDRPR SRSPAARYDR E
//
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