RKM5_YEAST
ID RKM5_YEAST Reviewed; 367 AA.
AC Q12367; D6VYD2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ribosomal lysine N-methyltransferase 5 {ECO:0000303|PubMed:21460220};
DE EC=2.1.1.- {ECO:0000269|PubMed:21460220};
GN Name=RKM5 {ECO:0000303|PubMed:21460220};
GN OrderedLocusNames=YLR137W {ECO:0000312|SGD:S000004127}; ORFNames=L3146;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PREDICTION OF FUNCTION.
RX PubMed=9873020; DOI=10.1074/jbc.274.2.814;
RA Niewmierzycka A., Clarke S.;
RT "S-adenosylmethionine-dependent methylation in Saccharomyces cerevisiae.
RT Identification of a novel protein arginine methyltransferase.";
RL J. Biol. Chem. 274:814-824(1999).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PREDICTION OF FUNCTION.
RX PubMed=19351663; DOI=10.1074/mcp.m900025-mcp200;
RA Petrossian T.C., Clarke S.G.;
RT "Multiple motif scanning to identify methyltransferases from the yeast
RT proteome.";
RL Mol. Cell. Proteomics 8:1516-1526(2009).
RN [6]
RP FUNCTION.
RX PubMed=21460220; DOI=10.1074/jbc.m110.200410;
RA Webb K.J., Al-Hadid Q., Zurita-Lopez C.I., Young B.D., Lipson R.S.,
RA Clarke S.G.;
RT "The ribosomal L1 protuberance in yeast is methylated on a lysine residue
RT catalyzed by a seven beta-strand methyltransferase.";
RL J. Biol. Chem. 286:18405-18413(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:0000269|PubMed:21460220}.
CC -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RKM5 family. {ECO:0000305}.
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DR EMBL; U53881; AAB82393.1; -; Genomic_DNA.
DR EMBL; X91258; CAA62652.1; -; Genomic_DNA.
DR EMBL; Z73309; CAA97708.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09448.1; -; Genomic_DNA.
DR PIR; S59329; S59329.
DR RefSeq; NP_013238.1; NM_001182024.1.
DR AlphaFoldDB; Q12367; -.
DR BioGRID; 31406; 37.
DR DIP; DIP-4967N; -.
DR IntAct; Q12367; 1.
DR STRING; 4932.YLR137W; -.
DR MaxQB; Q12367; -.
DR PaxDb; Q12367; -.
DR PRIDE; Q12367; -.
DR EnsemblFungi; YLR137W_mRNA; YLR137W; YLR137W.
DR GeneID; 850828; -.
DR KEGG; sce:YLR137W; -.
DR SGD; S000004127; RKM5.
DR VEuPathDB; FungiDB:YLR137W; -.
DR eggNOG; KOG1018; Eukaryota.
DR HOGENOM; CLU_051532_0_0_1; -.
DR InParanoid; Q12367; -.
DR OMA; ACDTIYN; -.
DR BioCyc; YEAST:G3O-32277-MON; -.
DR Reactome; R-SCE-8876725; Protein methylation.
DR PRO; PR:Q12367; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12367; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:SGD.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IBA:GO_Central.
DR GO; GO:0006479; P:protein methylation; IDA:SGD.
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 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..367
FT /note="Ribosomal lysine N-methyltransferase 5"
FT /id="PRO_0000262873"
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
