ID   RKM5_KLULA              Reviewed;         322 AA.
AC   Q6CQI9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Ribosomal lysine N-methyltransferase 5 {ECO:0000250|UniProtKB:Q12367};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q12367};
GN   Name=RKM5; OrderedLocusNames=KLLA0D16753g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that methylates 60S ribosomal protein L1.
CC       {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; CR382124; CAH00896.1; -; Genomic_DNA.
DR   RefSeq; XP_453800.1; XM_453800.1.
DR   AlphaFoldDB; Q6CQI9; -.
DR   STRING; 28985.XP_453800.1; -.
DR   EnsemblFungi; CAH00896; CAH00896; KLLA0_D16753g.
DR   GeneID; 2893437; -.
DR   KEGG; kla:KLLA0_D16753g; -.
DR   eggNOG; KOG1018; Eukaryota.
DR   HOGENOM; CLU_051532_0_0_1; -.
DR   InParanoid; Q6CQI9; -.
DR   OMA; ACDTIYN; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0006479; P:protein methylation; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; PTHR14614; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..322
FT                   /note="Ribosomal lysine N-methyltransferase 5"
FT                   /id="PRO_0000411042"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         141..143
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         163
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         214
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         242
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
SQ   SEQUENCE   322 AA;  37517 MW;  2FEA8C2BC4AB7A17 CRC64;
     MELVLLDEET LYEYIFERYV ELEANANDLS QDLGILSRNE SELEIDIGPH RLVTRKKKAP
     ERDEYTFSIH QNLTSLNSNR DNNNSTTGYV IWTTSTFILK WLLYNDNATI FTRGGVKDEV
     DITSIFQCQQ DDKLRYVLEL GTGTSPMFPI VFSNYVDKYV ATDQKDILPR LKDNIQENQS
     ECRRRLLKSN TIALDDLKRR TELECQIDIA LLDWELFSGS KKSRNDPVLQ CGPNFHLTII
     AMDVIYNEYL IVPFLTTLES LFVWYTEQRV TVSALIGIQL RTQDVLEMFL EEAIIERQFI
     VHAVDEKELN KSRFILLHVN LP