EFM1_YEAST
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 03-AUG-2022, entry version 139.
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; 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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., 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 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 1A
RT 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 medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. RKM1 family. {ECO:0000255|PROSITE-ProRule:PRU00190,
CC 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; 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 AlphaFoldDB; P38732; -.
DR SMR; P38732; -.
DR BioGRID; 36384; 60.
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; YHL039W.
DR GeneID; 856346; -.
DR KEGG; sce:YHL039W; -.
DR SGD; S000001031; EFM1.
DR VEuPathDB; FungiDB:YHL039W; -.
DR eggNOG; KOG1337; Eukaryota.
DR GeneTree; ENSGT00940000153577; -.
DR HOGENOM; CLU_030667_1_0_1; -.
DR InParanoid; P38732; -.
DR OMA; WGIRQFI; -.
DR BioCyc; YEAST:G3O-31057-MON; -.
DR PRO; PR:P38732; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38732; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 CDD; cd19180; SET_SpSET10-like; 1.
DR InterPro; IPR017119; Efm1/Rkm1.
DR InterPro; IPR044432; Set10/Efm1_SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PIRSF; PIRSF037136; Ribosomal_Lys-mtfrase-1; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..585
FT /note="Protein-lysine N-methyltransferase EFM1"
FT /id="PRO_0000202879"
FT DOMAIN 23..281
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="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
