ID   RKM5_YEASV              Reviewed;         367 AA.
AC   E7LXI9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 31.
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=VIN13_3206;
OS   Saccharomyces cerevisiae (strain VIN 13) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VIN 13;
RX   PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "Whole-genome comparison reveals novel genetic elements that characterize
RT   the genome of industrial strains of Saccharomyces cerevisiae.";
RL   PLoS Genet. 7:E1001287-E1001287(2011).
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}.
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   EMBL; ADXC01000055; EGA77926.1; -; Genomic_DNA.
DR   EnsemblFungi; EGA77926; EGA77926; VIN13_3206.
DR   HOGENOM; CLU_051532_0_0_1; -.
DR   OMA; ACDTIYN; -.
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_0000411051"
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;  41368 MW;  A9FD4D9D5DAE2B29 CRC64;
     MAFKLWLLDE ETIYEHVFER YTQLEGQSGK LAQDLGIQDR RGGVLEITFE PSGLEGGRKK
     KRVRRRNKAS SVEEDQNVAV DSYHVSVGQS ISSLHSSRDN GNSTTGYVLW STTPFFINWL
     LYSTSAAPFR LGSQVEVTCG SSCEGHXLEL PRLXDLTGAD RGKRGILELG AGISGILPVI
     LGNFVDTYVS TDQKGILNKL KDNIMENLSQ LTRKRCISRS LRLELPTVEP VGDADITAAS
     LPSKSTLHLE VAALDWEKIN LQDKKTHSLH PELSLIGETC SSVYVIAMDV IYNEYLIDPF
     LKTLKQLKHW LQTTYNLQFH VLVGIHLRSQ EVTTLFLEKA IIEYDFTVYD IVDQVIQESR
     FNFYLIT