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Database: UniProt
Entry: Q08961
LinkDB: Q08961
Original site: Q08961 
ID   RKM1_YEAST              Reviewed;         583 AA.
AC   Q08961; D6W3G2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-APR-2019, entry version 127.
DE   RecName: Full=Ribosomal lysine N-methyltransferase 1 {ECO:0000303|PubMed:16096273};
DE            EC=2.1.1.- {ECO:0000269|PubMed:16096273, ECO:0000269|PubMed:22522802};
GN   Name=RKM1 {ECO:0000303|PubMed:16096273};
GN   OrderedLocusNames=YPL208W {ECO:0000312|SGD:S000006129};
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
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.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16096273; DOI=10.1074/jbc.M507672200;
RA   Porras-Yakushi T.R., Whitelegge J.P., Miranda T.B., Clarke S.;
RT   "A novel SET domain methyltransferase modifies ribosomal protein
RT   Rpl23ab in yeast.";
RL   J. Biol. Chem. 280:34590-34598(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=17327221; DOI=10.1074/jbc.M611896200;
RA   Porras-Yakushi T.R., Whitelegge J.P., Clarke S.;
RT   "Yeast ribosomal/cytochrome c SET domain methyltransferase subfamily:
RT   identification of Rpl23ab methylation sites and recognition motifs.";
RL   J. Biol. Chem. 282:12368-12376(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [8]
RP   FUNCTION.
RX   PubMed=22522802; DOI=10.1002/pmic.201100570;
RA   Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
RT   "Methylation of translation-associated proteins in Saccharomyces
RT   cerevisiae: Identification of methylated lysines and their
RT   methyltransferases.";
RL   Proteomics 12:960-972(2012).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that monomethylates ribosomal protein S18
CC       (RPS18A and RPS18B) at 'Lys-48' and dimethylates ribosomal protein
CC       L23 (RPL23A and RPL23B) at 'Lys-106' and 'Lys-110'.
CC       {ECO:0000269|PubMed:16096273, ECO:0000269|PubMed:22522802}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 4800 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. RKM1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190, ECO:0000305}.
DR   EMBL; Z73564; CAA97923.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11228.1; -; Genomic_DNA.
DR   PIR; S65227; S65227.
DR   RefSeq; NP_015116.1; NM_001184022.1.
DR   ProteinModelPortal; Q08961; -.
DR   BioGrid; 35977; 39.
DR   DIP; DIP-3971N; -.
DR   IntAct; Q08961; 4.
DR   MINT; Q08961; -.
DR   STRING; 4932.YPL208W; -.
DR   iPTMnet; Q08961; -.
DR   MaxQB; Q08961; -.
DR   PaxDb; Q08961; -.
DR   PRIDE; Q08961; -.
DR   EnsemblFungi; YPL208W_mRNA; YPL208W_mRNA; YPL208W.
DR   GeneID; 855893; -.
DR   KEGG; sce:YPL208W; -.
DR   EuPathDB; FungiDB:YPL208W; -.
DR   SGD; S000006129; RKM1.
DR   GeneTree; ENSGT00940000153577; -.
DR   HOGENOM; HOG000142041; -.
DR   InParanoid; Q08961; -.
DR   OMA; NMKFYYE; -.
DR   BioCyc; YEAST:G3O-34099-MONOMER; -.
DR   PRO; PR:Q08961; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:SGD.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:SGD.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; IMP:SGD.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IBA:GO_Central.
DR   InterPro; IPR017119; Efm1/Rkm1.
DR   InterPro; IPR001214; SET_dom.
DR   PIRSF; PIRSF037136; Ribosomal_Lys-mtfrase-1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Complete proteome; Cytoplasm; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    583       Ribosomal lysine N-methyltransferase 1.
FT                                /FTId=PRO_0000228984.
FT   DOMAIN       22    274       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   COILED      378    407       {ECO:0000255}.
FT   COILED      433    459       {ECO:0000255}.
FT   BINDING     273    273       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   583 AA;  67178 MW;  DB47FD895A895B31 CRC64;
     MSSDALKALL QWGASFGVIV PEELKFLYTD LKGIICVCEK DIDNPSIKIP PEIVISRNLP
     MKFFGLSEST KNINGWLKLF FAKIKFDRDN DTIVDNVRVN DKFKPYLDAL PSRLNSPLVW
     NPSELKRLSS TNIGNSIHEK FEGIFKEWFE LVSSSDMFDL ERVADDVQTF HNLDELTYEA
     LYEKILKITE LQRPTIWYSF PAFLWSHLIF ISRAFPEYVL NRNCPDNSIV LLPIVDLLNH
     DYRSKVKWYP ENGWFCYEKI GTASQSRELS NNYGGKGNEE LLSGYGFVLE DNIFDSVALK
     VKLPLDVVST ILETEPSLKL PLLSDYTTYA FENKDCVQQE KKATRSATDY INGVTYFINI
     QNEQCLEPLL DLFTYLSKAE EEDLHDLRAR LQGIQMLRNA LQSKLNSITG PPATDDSYAI
     DPYRVYCADV YTKGQKQILK EALTRLKKLE KTMLSENKHQ LLTMSKILKN DPAFAETELP
     SLFSNEDGEE VIFESTYDLL ILWILLKTKK NSYPTKYEWV GQQYTNFKQT AYISDDAKAF
     HTAYFEKQDD VDLAEVDHAI QFVVDNSFTR TSSTTEETIL VRK
//
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