RKM5_YEAS8
ID RKM5_YEAS8 Reviewed; 367 AA.
AC C8ZDA6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Ribosomal lysine N-methyltransferase 5 {ECO:0000250|UniProtKB:Q12367};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q12367};
GN Name=RKM5; ORFNames=EC1118_1L10_2223g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that monomethylates 60S ribosomal protein L1 (RPL1A
CC and RPL1B) at 'Lys-46'. {ECO:0000250|UniProtKB:Q12367}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RKM5 family. {ECO:0000305}.
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DR EMBL; FN393078; CAY81372.1; -; Genomic_DNA.
DR AlphaFoldDB; C8ZDA6; -.
DR EnsemblFungi; CAY81372; CAY81372; EC1118_1L10_2223g.
DR HOGENOM; CLU_051532_0_0_1; -.
DR Proteomes; UP000000286; Chromosome XII, Scaffold EC1118_1L10.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006479; P:protein methylation; IEA:UniProt.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
PE 3: Inferred from homology;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..367
FT /note="Ribosomal lysine N-methyltransferase 5"
FT /id="PRO_0000411049"
FT REGION 55..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 170..172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 192
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 288
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
SQ SEQUENCE 367 AA; 41390 MW; 8F962B2B339BFDF7 CRC64;
MAFKLWLLDE ETIYEHVFER YTQLEGQSGK LAQDLGIQDR RGGVLEITFE PSGLEGGRKK
KRVRRRNKAS SVEEDQNVAV DSYHVSVGQS ISSLHSSRDN GNSTTGYVLW STTPFFINWL
LYSTSAAPFR LGSQVEVTCG SSCEGHMLEL PRLIDLTGAD RGKRGILELG AGISGILPVI
LGNFVDTYVS TDQKGILNKL KDNIMENLSQ LTRKRCISRS LRLELPTVEP VGDADITAAS
LPSKSTLHLE VAALDWEKIN LQDKKTHSLH PELSLIGETC SSVYVIAMDV IYNEYLIDPF
LKTLKQLKHW LQTTYNLQFH VLVGIHLRSQ EVTTLFLEKA IIEYDFTVYD IVDQVIQESR
FNFYLIT