ID A0A0D9YLI8_9ORYZ Unreviewed; 730 AA.
AC A0A0D9YLI8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 28-JUN-2023, entry version 40.
DE RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G01640.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G01640.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM02G01640.1}
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; A0A0D9YLI8; -.
DR EnsemblPlants; OGLUM02G01640.1; OGLUM02G01640.1; OGLUM02G01640.
DR Gramene; OGLUM02G01640.1; OGLUM02G01640.1; OGLUM02G01640.
DR Proteomes; UP000026961; 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 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:UP000026961};
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 453..525
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 546..617
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..730
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 152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 730 AA; 82257 MW; 7C20B17C4F6200E8 CRC64;
MVALPSLSPP PPRPSPSPAT PRRRPPPPPP PHATPSHRVR SRPATVVSAA SGVTDGYHST
IRSLNSRGRH VPRKSLGQNY MLNSKVNEEL VAAAGVEEGD VVLEIGPGTG SLTAALLDAG
ATVFAVEKDK HMATLVNDRF GSTEQLKIIE EDITKFNVRS HFLPFLEEKS HHRRKYAKVV
SNLPFNVSTE VVKLLLPMGD VFSVTVLLLQ DETALRFADA SIQTPEYRPI NVFVNFYSEP
EYKFKVERTN FFPQPKVDGA VISFKLKNSG DYPPVNSAFN GKRKMLRKSL QHLCSSSEIE
AALANIGLPV TCSPDFLQSL HGLQASVATI VVMHPIPIKK TVPISLTITC HHHSWAHIHP
APGKISTPIQ LIHPHLVHVV AYKNPRYAAT DQSPLSPPLR FSIRRRRPNQ SPRGGGDLGF
PRPRRRRLPP RHRPLLPSSI PGGLRRVACP KMRPVFCGNL DYDARQSEIE RLFSKYGRVE
RVDMKSGFAF VYMEDERDAD EAIHRLDRIE FGRKGRRLRV EWTKEDRSGG RRGNSKRSPN
NTRPTKTLFV INFDPINTRT RDLERHFDQY GKISNVRIRR NFAFVQYELQ EDATKALEGT
NGSTLMDRVI SVEYALRDDD EKRNGYSPER RGRDRSPDRR DYRGRSASPY GRGRERGSPD
YGRGRERGSP DYGRGGDRGS PDYRRGASPQ GGNKGDERGS PPNNYDRERR EASPGYDRPR
SRSPARYERE
//
