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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//