ID EFM5_YEAST Reviewed; 248 AA.
AC P53200; D6VUD8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 27-MAR-2024, entry version 160.
DE RecName: Full=Protein-lysine N-methyltransferase EFM5 {ECO:0000255|HAMAP-Rule:MF_03187, ECO:0000305|PubMed:25446118};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03187, ECO:0000305|PubMed:25446118};
DE AltName: Full=Elongation factor methyltransferase 5 {ECO:0000255|HAMAP-Rule:MF_03187, ECO:0000303|PubMed:25446118};
DE AltName: Full=N(6)-adenine-specific DNA methyltransferase-like 1 {ECO:0000305|PubMed:15225602};
GN Name=EFM5 {ECO:0000255|HAMAP-Rule:MF_03187, ECO:0000303|PubMed:25446118};
GN Synonyms=AML1 {ECO:0000303|PubMed:21858014};
GN OrderedLocusNames=YGR001C {ECO:0000312|SGD:S000003233};
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 REVISION OF GENE MODEL.
RX PubMed=10734188; DOI=10.1093/nar/28.8.1700;
RA Davis C.A., Grate L., Spingola M., Ares M. Jr.;
RT "Test of intron predictions reveals novel splice sites, alternatively
RT spliced mRNAs and new introns in meiotically regulated genes of yeast.";
RL Nucleic Acids Res. 28:1700-1706(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=14671320; DOI=10.1073/pnas.2536857100;
RA Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M.,
RA Ahlquist P.;
RT "Systematic, genome-wide identification of host genes affecting replication
RT of a positive-strand RNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003).
RN [7]
RP SIMILARITY TO METHYLTRANSFERASES.
RX PubMed=15225602; DOI=10.1016/j.febslet.2004.03.126;
RA Albrecht M., Lengauer T.;
RT "Novel Sm-like proteins with long C-terminal tails and associated
RT methyltransferases.";
RL FEBS Lett. 569:18-26(2004).
RN [8]
RP FUNCTION PREDICTION.
RX PubMed=20582239; DOI=10.2217/epi.09.3;
RA Petrossian T., Clarke S.;
RT "Bioinformatic identification of novel methyltransferases.";
RL Epigenomics 1:163-175(2009).
RN [9]
RP GENE NAME.
RX PubMed=21858014; DOI=10.1371/journal.pone.0023168;
RA Wlodarski T., Kutner J., Towpik J., Knizewski L., Rychlewski L.,
RA Kudlicki A., Rowicka M., Dziembowski A., Ginalski K.;
RT "Comprehensive structural and substrate specificity classification of the
RT Saccharomyces cerevisiae methyltransferome.";
RL PLoS ONE 6:E23168-E23168(2011).
RN [10]
RP FUNCTION.
RX PubMed=25446118; DOI=10.1016/j.bbrc.2014.11.022;
RA Dzialo M.C., Travaglini K.J., Shen S., Loo J.A., Clarke S.G.;
RT "A new type of protein lysine methyltransferase trimethylates Lys-79 of
RT elongation factor 1A.";
RL Biochem. Biophys. Res. Commun. 455:382-389(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that trimethylates elongation factor 1-alpha (TEF1
CC and TEF2) at 'Lys-79' (PubMed:25446118). Required for replication of
CC Brome mosaic virus (BMV) (PubMed:14671320). {ECO:0000255|HAMAP-
CC Rule:MF_03187, ECO:0000269|PubMed:14671320,
CC ECO:0000269|PubMed:25446118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03187,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3060 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. EFM5 family. {ECO:0000255|HAMAP-Rule:MF_03187,
CC ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an N(6)-adenine-specific DNA
CC methyltransferase based on primary sequence and predicted secondary
CC structure. {ECO:0000305|PubMed:20582239}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA96984.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z72786; CAA96984.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006941; DAA08099.1; -; Genomic_DNA.
DR PIR; S64290; S64290.
DR RefSeq; NP_011515.4; NM_001181130.3.
DR AlphaFoldDB; P53200; -.
DR BioGRID; 33245; 77.
DR IntAct; P53200; 1.
DR MINT; P53200; -.
DR STRING; 4932.YGR001C; -.
DR iPTMnet; P53200; -.
DR MaxQB; P53200; -.
DR PaxDb; 4932-YGR001C; -.
DR PeptideAtlas; P53200; -.
DR EnsemblFungi; YGR001C_mRNA; YGR001C; YGR001C.
DR GeneID; 852884; -.
DR KEGG; sce:YGR001C; -.
DR AGR; SGD:S000003233; -.
DR SGD; S000003233; EFM5.
DR VEuPathDB; FungiDB:YGR001C; -.
DR eggNOG; KOG3350; Eukaryota.
DR GeneTree; ENSGT00390000016366; -.
DR HOGENOM; CLU_074410_1_0_1; -.
DR InParanoid; P53200; -.
DR OMA; CNFRPEH; -.
DR OrthoDB; 6014at2759; -.
DR BioCyc; YEAST:G3O-30732-MONOMER; -.
DR BRENDA; 2.1.1.244; 984.
DR Reactome; R-SCE-8876725; Protein methylation.
DR BioGRID-ORCS; 852884; 0 hits in 10 CRISPR screens.
DR PRO; PR:P53200; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53200; Protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:SGD.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA:SGD.
DR HAMAP; MF_03187; Methyltr_EFM5; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR019369; Efm5/EEF1AKMT1.
DR InterPro; IPR041370; Mlase_EEF1AKMT1/ZCCHC4.
DR PANTHER; PTHR13200:SF0; EEF1A LYSINE METHYLTRANSFERASE 1; 1.
DR PANTHER; PTHR13200; UNCHARACTERIZED; 1.
DR Pfam; PF10237; N6-adenineMlase; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; Transferase.
FT CHAIN 1..248
FT /note="Protein-lysine N-methyltransferase EFM5"
FT /id="PRO_0000202778"
SQ SEQUENCE 248 AA; 28582 MW; CA7D4148E3767FF7 CRC64;
MSDSDSDSDY ELTLSANALA ALEEFKREEQ QHQEAFQKLY DETDEDFQKK KKEEGMKLFK
EDWQLSQFWY SDDTAAILAD AILEGADENT VIAIVSAPSV YAAIQKKPTN EIPTEHIYLF
EFDKRFELLA GRDHFFFYDY NKPLDFSDEI KGKVDRLLID PPFLNEDCQT KSSITAKCLL
APNDNSKTKK GVFKHRLISC TGERMSEVIS KVYSDTRITT FLPEHSNGLS NEFRCYANFE
CSSWKFAS
//
