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Database: UniProt
Entry: A0A4U6U5C9_SETVI
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Original site: A0A4U6U5C9_SETVI 
ID   A0A4U6U5C9_SETVI        Unreviewed;       751 AA.
AC   A0A4U6U5C9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=SEVIR_6G195000v2 {ECO:0000313|EMBL:TKW10850.1};
OS   Setaria viridis (Green bristlegrass) (Setaria italica subsp. viridis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4556 {ECO:0000313|EMBL:TKW10850.1, ECO:0000313|Proteomes:UP000298652};
RN   [1] {ECO:0000313|EMBL:TKW10850.1, ECO:0000313|Proteomes:UP000298652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. A10 {ECO:0000313|Proteomes:UP000298652};
RA   Huang P., Jenkins J., Grimwood J., Barry K., Healey A., Mamidi S.,
RA   Sreedasyam A., Shu S., Feldman M., Wu J., Yu Y., Chen C., Johnson J.,
RA   Rokhsar D., Baxter I., Schmutz J., Brutnell T., Kellogg E.;
RT   "WGS assembly of Setaria viridis.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CM016557; TKW10850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U6U5C9; -.
DR   EnsemblPlants; TKW10850; TKW10850; SEVIR_6G195000v2.
DR   Gramene; TKW10850; TKW10850; SEVIR_6G195000v2.
DR   OMA; YRTVNFA; -.
DR   Proteomes; UP000298652; Chromosome 6.
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:SF14; OS08G0484400 PROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000298652};
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          1..425
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        264
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         118..124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         150
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         211
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   751 AA;  85159 MW;  79D7C6B11F65505D CRC64;
     MSFLRKPLPA TFRINASCQF YKDICSKLEN DFRQSLESEV SNEYGEDAIR PLPWYPGNLA
     WHLNFSRKEL RKNLALESFH EFLKHESEVG NITRQEAVSM VPPLFLNVHP DHHILDMCAA
     PGSKTFQLLE MIHQSKEPGL LPGALVMAND LNVQRCDLLI HNTKRMCTAN LIVTNHEAQN
     FPNCSLAKDY SEAYKDNCKS QRLEFDRVLC DVPCSGDGTI RKGHDMWRKW NSGMGNQLHL
     LQVNIAMRGI ALLKVGGRMV YSTCSMNPVE NEAVIAELLR RNGNSVELLD VSSELPELVR
     RPGLSTWKVQ DRGSWFQTHD DVPHDRKNVV LPSMFPSSNI TEESHAVCGY VEINTDNRGS
     FSRNCDIEET SNINHDMDGV STDPTSNLDC TSNVVNSKFP LHRCMRIVPH DQNSGAFFIA
     VLHKLSPLNG SQIQGTKVQH TLGKGRIKQL HKEPEPETRP CETILTCQQN NVLEVDDAEL
     LGRRQNLSAD NQTSKDKNST EVEMVFNDVK SGREESGDIM KLQKQSRWKG VDPVLFFKDE
     LVIKSIKSFF GIKESFPLEG YLVTRSTDNA RRMYYISKSV KEIVELNEEV GEQLKIASLG
     VKMFERHRSK DGCSCAYRLS YEGLSLLLPY ISTRILYASP LDFHRLLQYR TINFAHFVDS
     RFGEEAASMM PGCCVVVLLE GHENADSILK DPTTIAIVCW RGKGTMNVMV SPPDRTDLLE
     RMAYRFGIKA SAEEDEKLMD LTREDGNIMR I
//
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