ID   RKM5_YEAS7              Reviewed;         367 AA.
AC   A7A136;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 46.
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=SCY_3710;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000167; EDN59677.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7A136; -.
DR   EnsemblFungi; EDN59677; EDN59677; SCY_3710.
DR   HOGENOM; CLU_051532_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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_0000411048"
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;  41392 MW;  4ACAB9FA00DAB9F5 CRC64;
     MAFKLWLLDE ETIYEHVFER YTQLEGQSGK LAQDLGIQDR RGGVLEITFE PSGLEGGRKK
     KRVRRRNKAS SVEEDQNVAV DSYHVSVGQS ISSLRSSRDN GNSTTGYVLW STTPFFINWL
     LYSTSAAPFR LGSQVEVTCG SSCEGHKLEL PRLVDLTGAD RGKRGILELG AGISGILPVI
     LGNFVDTYVS TDQKGILNKL KDNIMENLSQ LTRKRCISRS LRLELPTVEP VGDADITAAS
     LPSKSTLHLE VAALDWEKIN LQDKKTHSLH PELSLIGETC SSVYVIAMDV IYNEYLIDPF
     LKTLKQLKHW LQTTYNLQFH VLVGIHLRSQ EVTTLFLEKA IIEYDFTVYD IVDQVIQESR
     FNFYLIT