ID A0A0E0ET37_9ORYZ Unreviewed; 922 AA.
AC A0A0E0ET37;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
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:OMERI09G10520.3};
RN [1] {ECO:0000313|EnsemblPlants:OMERI09G10520.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI09G10520.3};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI09G10520.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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; A0A0E0ET37; -.
DR STRING; 40149.A0A0E0ET37; -.
DR EnsemblPlants; OMERI09G10520.3; OMERI09G10520.3; OMERI09G10520.
DR Gramene; OMERI09G10520.3; OMERI09G10520.3; OMERI09G10520.
DR Proteomes; UP000008021; Chromosome 9.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 80..527
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 198..204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 291
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 922 AA; 103295 MW; 77AC0D7FB27F28F6 CRC64;
MGGGRKRGRT QRRHFKQGRE NVWKHNPQRP PAAGGEGAEG GAAEGREGNP SWQPFATENP
AFEDYYKAQQ IIPEGEWDDF MNMLRKPLPA TFRINASCQF YQDICSQLEN DFRKSLETEV
SDEHEEDAIR PLPWYPGNLA WHLNFSRMQL RRNQALEGFH EFLKRENEVG NITRQEAVSM
VPPLFLNVQP DHHILDMCAA PGSKTFQLLE MIHQSTKPGM LPNALVVAND VDVQRCNLLI
HQTKRMCTAN LIVTNHEAQN FPGCNLAKFS SEICTDESKL QRLEFDRVLC DVPCSGDGTV
RKAPDMWRKW NAGMGNGLHR LQVEIAMRGI GLLKVGGRIV YSTCSMNPVE NEAVVAEILR
RCGGSVELLD VSNELPELVR RPGLSTWKVR DRGSWFGTHE DVPRYRKNVI SPSMFPSGKG
TMDSHVAIGS VEINTDVIDA DMKDSTNMVE GEQQTKTASD DANNGGDPNT EETSKLESNE
VPNDSDKKSN STSIRTEHSN FPLHRCMRIV PHDQNSGAFF IAVLQKLSPI NENQEAELTK
GEHSISKDRA EKLEKGLRSD KVPHKENTVQ QQGVDDGNVM DEQQNGDVDN ETSNGKSSEE
AKVVNEAEND QAGPRDRRRK PQNQGRWRGV DPVIFFKDEA TIRSIVSFYC IKDTFPLEGH
LVTRNPDASH VKRIYYVSKS VQEVLELNVK VGERLKITSL GLKIFERQSS KDGSPCTFRL
SSEGLPLLLP YITKQILYAS AIDFQHLLQY RTIKFPDFVD AKFGEEASAL LPGCCVVVLR
EGHQNIDSIA MDPSAIAIVC WKGKTNLCVM VSPLDGKELL ERICLRYGLK IPKADDVKPS
MKIDGSDEQP DLSTEAVDPE AVPESKTSDM EIADAKEVEI MSSRSQLGNC GHNFYNVSNY
GMHTRQGCLR QSLYPNNNSN AI
//
