EFM6_YEAST
ID EFM6_YEAST Reviewed; 246 AA.
AC P53970; D6W1F5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein-lysine N-methyltransferase EFM6 {ECO:0000255|HAMAP-Rule:MF_03198, ECO:0000305|PubMed:26115316};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03198, ECO:0000305|PubMed:26115316};
DE AltName: Full=Elongation factor methyltransferase 6 {ECO:0000255|HAMAP-Rule:MF_03198, ECO:0000303|PubMed:26115316};
GN Name=EFM6 {ECO:0000255|HAMAP-Rule:MF_03198, ECO:0000303|PubMed:26115316};
GN OrderedLocusNames=YNL024C {ECO:0000312|SGD:S000004969}; ORFNames=N2809;
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=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 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=26115316; DOI=10.1371/journal.pone.0131426;
RA Jakobsson M.E., Davydova E., Malecki J., Moen A., Falnes P.O.;
RT "Saccharomyces cerevisiae eukaryotic elongation factor 1A (eEF1A) is
RT methylated at Lys-390 by a METTL21-like methyltransferase.";
RL PLoS ONE 10:E0131426-E0131426(2015).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that methylates elongation factor 1-alpha (TEF1 and
CC TEF2) at 'Lys-390'. {ECO:0000269|PubMed:26115316}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03198,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1760 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. METTL21 family. EFM6 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03198, ECO:0000305}.
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DR EMBL; Z71300; CAA95886.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10521.1; -; Genomic_DNA.
DR PIR; S62936; S62936.
DR RefSeq; NP_014374.1; NM_001182863.1.
DR AlphaFoldDB; P53970; -.
DR SMR; P53970; -.
DR BioGRID; 35802; 58.
DR DIP; DIP-4380N; -.
DR IntAct; P53970; 1.
DR MINT; P53970; -.
DR STRING; 4932.YNL024C; -.
DR PaxDb; P53970; -.
DR PRIDE; P53970; -.
DR EnsemblFungi; YNL024C_mRNA; YNL024C; YNL024C.
DR GeneID; 855707; -.
DR KEGG; sce:YNL024C; -.
DR SGD; S000004969; EFM6.
DR VEuPathDB; FungiDB:YNL024C; -.
DR eggNOG; KOG2793; Eukaryota.
DR HOGENOM; CLU_055721_2_1_1; -.
DR InParanoid; P53970; -.
DR OMA; RFMKMAK; -.
DR BioCyc; YEAST:G3O-33062-MON; -.
DR Reactome; R-SCE-8876725; Protein methylation.
DR PRO; PR:P53970; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53970; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:SGD.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03198; Methyltr_EFM6; 1.
DR InterPro; IPR033684; EFM6.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..246
FT /note="Protein-lysine N-methyltransferase EFM6"
FT /id="PRO_0000203460"
FT BINDING 51
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867, ECO:0000255|HAMAP-
FT Rule:MF_03198"
FT BINDING 87..89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867, ECO:0000255|HAMAP-
FT Rule:MF_03198"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867, ECO:0000255|HAMAP-
FT Rule:MF_03198"
FT BINDING 143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867, ECO:0000255|HAMAP-
FT Rule:MF_03198"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867, ECO:0000255|HAMAP-
FT Rule:MF_03198"
SQ SEQUENCE 246 AA; 27738 MW; EBE1601027A37410 CRC64;
MESIFGGFGD LVVPRPKEHL GQTDLSFGGK LLPALKICED GGESGCGGKV WIAGELLCEY
ILEKSVDHLL SKTVNGTKQF KKVLELGSGT GLVGLCVGLL EKNTFHDGTK VYVTDIDKLI
PLLKRNIELD EVQYEVLARE LWWGEPLSAD FSPQEGAMQA NNVDLVLAAD CVYLEEAFPL
LEKTLLDLTH CINPPVILMA YKKRRKADKH FFNKIKRNFD VLEITDFSKF EHYLKERTHL
FQLIRK
