GenomeNet

Database: UniProt
Entry: P38732
LinkDB: P38732
Original site: P38732 
ID   EFM1_YEAST              Reviewed;         585 AA.
AC   P38732; D3DKT0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   10-APR-2019, entry version 126.
DE   RecName: Full=Protein-lysine N-methyltransferase EFM1 {ECO:0000305|PubMed:20510667};
DE            EC=2.1.1.- {ECO:0000269|PubMed:20510667, ECO:0000269|PubMed:22522802};
DE   AltName: Full=Elongation factor methyltransferase 1 {ECO:0000303|PubMed:20510667};
GN   Name=EFM1 {ECO:0000303|PubMed:20510667};
GN   OrderedLocusNames=YHL039W {ECO:0000312|SGD:S000001031};
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
RA   Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA   Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA   Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA   Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA   Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA   Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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.
RX   PubMed=20510667; DOI=10.1016/j.abb.2010.05.023;
RA   Lipson R.S., Webb K.J., Clarke S.G.;
RT   "Two novel methyltransferases acting upon eukaryotic elongation factor
RT   1A in Saccharomyces cerevisiae.";
RL   Arch. Biochem. Biophys. 500:137-143(2010).
RN   [6]
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 elongation factor 1-alpha
CC       (TEF1/TEF2) at 'Lys-30'. {ECO:0000269|PubMed:20510667,
CC       ECO:0000269|PubMed:22522802}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 5170 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; U11583; AAB65051.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06647.1; -; Genomic_DNA.
DR   PIR; S48929; S48929.
DR   RefSeq; NP_011824.1; NM_001179119.1.
DR   ProteinModelPortal; P38732; -.
DR   BioGrid; 36384; 55.
DR   DIP; DIP-6582N; -.
DR   IntAct; P38732; 2.
DR   MINT; P38732; -.
DR   STRING; 4932.YHL039W; -.
DR   iPTMnet; P38732; -.
DR   MaxQB; P38732; -.
DR   PaxDb; P38732; -.
DR   PRIDE; P38732; -.
DR   EnsemblFungi; YHL039W_mRNA; YHL039W_mRNA; YHL039W.
DR   GeneID; 856346; -.
DR   KEGG; sce:YHL039W; -.
DR   EuPathDB; FungiDB:YHL039W; -.
DR   SGD; S000001031; EFM1.
DR   GeneTree; ENSGT00940000153577; -.
DR   HOGENOM; HOG000141878; -.
DR   InParanoid; P38732; -.
DR   OMA; WGIRQFI; -.
DR   BioCyc; YEAST:G3O-31057-MONOMER; -.
DR   PRO; PR:P38732; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:SGD.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IEA:InterPro.
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   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF037136; Ribosomal_Lys-mtfrase-1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    585       Protein-lysine N-methyltransferase EFM1.
FT                                /FTId=PRO_0000202879.
FT   DOMAIN       23    281       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   BINDING     280    280       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   585 AA;  67452 MW;  84BC2D3A204D9D29 CRC64;
     MITQTELDNC LQWAQNNGAF IDPKISFRIT EDAGVSAFVN EKFSPKPDQA LIRVPETLLI
     TSQQALSEFS QAANERSLLN SVTQLYLSKL KFGTDAVHLK SFYKPYLDVL PLHLPQPYFW
     STDEVMNLHG TDVYLTMRDT LNKLVKEWRM LFQALSIEHS SQDKQFLSLF QENKDSAVVP
     LEQFCAHING CKLEDSEWNS FVAYLWSYCI FNSRAFPRVI LGRAGTDRTN LNEGFLYPIV
     DLLNHKNDVP VRWEMNEQNE LCFMSQTTTF SAQDELFNNY GNISNEKCLL NYGFWDSSNK
     FDFSRLTLKL PSTLVSGLPV DFNKSGNFVT DDGETTILQF SLKISEPLPP VLLALFAYLS
     KLKSEETPTV RSVLEGIDQL TSVVSQRLLF YKNFKIKTSS TQKLRPHVIK LIKLYYQDNK
     KILNATTEKL SVLQKKIYSN NKEFSLSFKT IFKNDKIFAN SLLLVFGAIN YEDLITKDCL
     NDALLLWIVK LINDKSNNQG GFIKQTFKEV SDSIVIEKED VMEFLPFYKK YFPNLSERIP
     EIYSVGDWGI RQFIVADTAI DRLVWIRKSN KEPIFLMKKA YDLQI
//
DBGET integrated database retrieval system