ID   RKM5_YEASA              Reviewed;         367 AA.
AC   E7KFK5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
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=AWRI796_3230;
OS   Saccharomyces cerevisiae (strain AWRI796) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI796;
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}.
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DR   EMBL; ADVS01000038; EGA73971.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7KFK5; -.
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_0000411050"
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;  41356 MW;  8F962B2B33969097 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 IIEYDLTVYD IVDQVIQESR
     FNFYLIT