EF1A_YEAST
ID EF1A_YEAST Reviewed; 458 AA.
AC P02994; D6VQB6; Q7Z7U8; Q7Z8Q8; Q7Z8Q9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 237.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
DE AltName: Full=Eukaryotic elongation factor 1A;
DE Short=eEF1A;
DE AltName: Full=Translation elongation factor 1A;
GN Name=TEF1; OrderedLocusNames=YPR080W; ORFNames=P9513.7;
GN and
GN Name=TEF2; OrderedLocusNames=YBR118W; ORFNames=YBR0913;
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 [GENOMIC DNA] (TEF1).
RX PubMed=6383821; DOI=10.1002/j.1460-2075.1984.tb02053.x;
RA Nagata S., Nagashima K., Tsunetsugu-Yokota Y., Fujimura K., Miyazaki M.,
RA Kaziro Y.;
RT "Polypeptide chain elongation factor 1 alpha (EF-1 alpha) from yeast:
RT nucleotide sequence of one of the two genes for EF-1 alpha from
RT Saccharomyces cerevisiae.";
RL EMBO J. 3:1825-1830(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF2).
RX PubMed=6396088; DOI=10.1002/j.1460-2075.1984.tb02295.x;
RA Schirmaier F., Philippsen P.;
RT "Identification of two genes coding for the translation elongation factor
RT EF-1 alpha of S. cerevisiae.";
RL EMBO J. 3:3311-3315(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1).
RX PubMed=2982849; DOI=10.1016/s0021-9258(18)89477-7;
RA Cottrelle P., Thiele D., Price V.L., Memet S., Micouin J.-Y., Marck C.,
RA Buhler J.-M., Sentenac A., Fromageot P.;
RT "Cloning, nucleotide sequence, and expression of one of two genes coding
RT for yeast elongation factor 1 alpha.";
RL J. Biol. Chem. 260:3090-3096(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1 AND TEF2).
RX PubMed=3026912; DOI=10.1016/0378-1119(86)90024-7;
RA Nagashima K., Kasai M., Nagata S., Kaziro Y.;
RT "Structure of the two genes coding for polypeptide chain elongation factor
RT 1 alpha (EF-1 alpha) from Saccharomyces cerevisiae.";
RL Gene 45:265-273(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF2).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF2).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF1).
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., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., 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., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [8]
RP GENOME REANNOTATION (TEF1 AND TEF2).
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-237 (TEF1).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7916691; DOI=10.1111/j.1432-1033.1993.tb18268.x;
RA Schaaff-Gerstenschlaeger I., Mannhaupt G., Vetter I., Zimmermann F.K.,
RA Feldmann H.;
RT "TKL2, a second transketolase gene of Saccharomyces cerevisiae. Cloning,
RT sequence and deletion analysis of the gene.";
RL Eur. J. Biochem. 217:487-492(1993).
RN [11]
RP PARTIAL PROTEIN SEQUENCE, AND METHYLATION AT LYS-30; LYS-79; LYS-316 AND
RP LYS-390.
RX PubMed=8476932; DOI=10.1016/0167-4838(93)90281-u;
RA Cavallius J., Zoll W., Chakraburtty K., Merrick W.C.;
RT "Characterization of yeast EF-1 alpha: non-conservation of post-
RT translational modifications.";
RL Biochim. Biophys. Acta 1163:75-80(1993).
RN [12]
RP PROTEIN SEQUENCE OF 6-20, AND INTERACTION WITH SRV2.
RX PubMed=9125210; DOI=10.1006/bbrc.1997.6326;
RA Yanagihara C., Shinkai M., Kariya K., Yamawaki-Kataoka Y., Hu C.-D.,
RA Masuda T., Kataoka T.;
RT "Association of elongation factor 1 alpha and ribosomal protein L3 with the
RT proline-rich region of yeast adenylyl cyclase-associated protein CAP.";
RL Biochem. Biophys. Res. Commun. 232:503-507(1997).
RN [13]
RP PROTEIN SEQUENCE OF 56-61 AND 265-280.
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=9509572;
RX DOI=10.1002/(sici)1097-0061(199712)13:16<1519::aid-yea211>3.0.co;2-u;
RA Norbeck J., Blomberg A.;
RT "Two-dimensional electrophoretic separation of yeast proteins using a non-
RT linear wide range (pH 3-10) immobilized pH gradient in the first dimension;
RT reproducibility and evidence for isoelectric focusing of alkaline (pI > 7)
RT proteins.";
RL Yeast 13:1519-1534(1997).
RN [14]
RP PROTEIN SEQUENCE OF 70-77 AND 80-87.
RX PubMed=3882705; DOI=10.1016/s0021-9258(18)89476-5;
RA Thiele D., Cottrelle P., Iborra F., Buhler J.-M., Sentenac A.,
RA Fromageot P.;
RT "Elongation factor 1 alpha from Saccharomyces cerevisiae. Rapid large-scale
RT purification and molecular characterization.";
RL J. Biol. Chem. 260:3084-3089(1985).
RN [15]
RP PROTEIN SEQUENCE OF 211-214 AND 289-308, INTERACTION WITH BNI1, AND
RP IDENTIFICATION IN A COMPLEX WITH BNI1 AND PROFILIN.
RX PubMed=9591785; DOI=10.1038/sj.onc.1201724;
RA Umikawa M., Tanaka K., Kamei T., Shimizu K., Imamura H., Sasaki T.,
RA Takai Y.;
RT "Interaction of Rho1p target Bni1p with F-actin-binding elongation factor
RT 1alpha: implication in Rho1p-regulated reorganization of the actin
RT cytoskeleton in Saccharomyces cerevisiae.";
RL Oncogene 16:2011-2016(1998).
RN [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-397.
RC STRAIN=ATCC 13507 / CBS 459 / NRRL Y-12649,
RC ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632,
RC ATCC 24702 / NRRL Y-2034,
RC Diastaticus / ATCC 13007 / CBS 1782 / IFO 1046 / NRRL Y-2416, and
RC NRRL YB-210;
RX PubMed=12748053; DOI=10.1016/s1567-1356(03)00012-6;
RA Kurtzman C.P., Robnett C.J.;
RT "Phylogenetic relationships among yeasts of the 'Saccharomyces complex'
RT determined from multigene sequence analyses.";
RL FEMS Yeast Res. 3:417-432(2003).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF GLU-286 AND GLU-317.
RX PubMed=3066688; DOI=10.1093/genetics/120.4.923;
RA Sandbaken M.G., Culbertson M.R.;
RT "Mutations in elongation factor EF-1 alpha affect the frequency of
RT frameshifting and amino acid misincorporation in Saccharomyces
RT cerevisiae.";
RL Genetics 120:923-934(1988).
RN [18]
RP INTERACTION WITH YEF3, AND MUTAGENESIS OF GLU-122.
RX PubMed=9990316; DOI=10.1046/j.1432-1327.1998.2580986.x;
RA Kovalchuke O., Kambampati R., Pladies E., Chakraburtty K.;
RT "Competition and cooperation amongst yeast elongation factors.";
RL Eur. J. Biochem. 258:986-993(1998).
RN [19]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASN-153 AND ASP-156.
RX PubMed=9786872; DOI=10.1074/jbc.273.44.28752;
RA Cavallius J., Merrick W.C.;
RT "Site-directed mutagenesis of yeast eEF1A. Viable mutants with altered
RT nucleotide specificity.";
RL J. Biol. Chem. 273:28752-28758(1998).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH ZPR1.
RX PubMed=9852145; DOI=10.1083/jcb.143.6.1471;
RA Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.;
RT "Interaction of ZPR1 with translation elongation factor-1alpha in
RT proliferating cells.";
RL J. Cell Biol. 143:1471-1484(1998).
RN [21]
RP MUTAGENESIS OF ASN-153 AND ASP-156.
RX PubMed=10514524; DOI=10.1074/jbc.274.42.30297;
RA Carr-Schmid A., Durko N., Cavallius J., Merrick W.C., Kinzy T.G.;
RT "Mutations in a GTP-binding motif of eukaryotic elongation factor 1A reduce
RT both translational fidelity and the requirement for nucleotide exchange.";
RL J. Biol. Chem. 274:30297-30302(1999).
RN [22]
RP FUNCTION IN NUCLEAR EXPORT OF AMINOACYL-TRNAS.
RX PubMed=10766739;
RA Grosshans H., Hurt E.C., Simos G.;
RT "An aminoacylation-dependent nuclear tRNA export pathway in yeast.";
RL Genes Dev. 14:830-840(2000).
RN [23]
RP METHYLATION AT LYS-458.
RX PubMed=10973948; DOI=10.1074/jbc.m001005200;
RA Zobel-Thropp P., Yang M.C., Machado L., Clarke S.;
RT "A novel post-translational modification of yeast elongation factor 1A.
RT Methylesterification at the C-terminus.";
RL J. Biol. Chem. 275:37150-37158(2000).
RN [24]
RP INTERACTION WITH ACTIN.
RX PubMed=11290701; DOI=10.1093/genetics/157.4.1425;
RA Munshi R., Kandl K.A., Carr-Schmid A., Whitacre J.L., Adams A.E.M.,
RA Kinzy T.G.;
RT "Overexpression of translation elongation factor 1A affects the
RT organization and function of the actin cytoskeleton in yeast.";
RL Genetics 157:1425-1436(2001).
RN [25]
RP S-THIOLATION.
RX PubMed=12755685; DOI=10.1042/bj20030414;
RA Shenton D., Grant C.M.;
RT "Protein S-thiolation targets glycolysis and protein synthesis in response
RT to oxidative stress in the yeast Saccharomyces cerevisiae.";
RL Biochem. J. 374:513-519(2003).
RN [26]
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 [27]
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 [28]
RP FUNCTION, MUTAGENESIS OF ASP-156, AND INTERACTION WITH RPT1.
RX PubMed=15601860; DOI=10.1128/mcb.25.1.403-413.2005;
RA Chuang S.-M., Chen L., Lambertson D., Anand M., Kinzy T.G., Madura K.;
RT "Proteasome-mediated degradation of cotranslationally damaged proteins
RT involves translation elongation factor 1A.";
RL Mol. Cell. Biol. 25:403-413(2005).
RN [29]
RP INTERACTION WITH CEX1.
RX PubMed=17203074; DOI=10.1038/sj.emboj.7601493;
RA McGuire A.T., Mangroo D.;
RT "Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae
RT nuclear tRNA export machinery.";
RL EMBO J. 26:288-300(2007).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-72; THR-82; SER-163
RP AND THR-430, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [31]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-259 AND SER-414, AND
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [34]
RP METHYLATION.
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 [35]
RP FUNCTION, INTERACTION WITH GCN2, AND ASSOCIATION WITH RIBOSOMES.
RX PubMed=21849502; DOI=10.1074/jbc.m111.248898;
RA Visweswaraiah J., Lageix S., Castilho B.A., Izotova L., Kinzy T.G.,
RA Hinnebusch A.G., Sattlegger E.;
RT "Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds
RT the Gcn2 protein C terminus and inhibits Gcn2 activity.";
RL J. Biol. Chem. 286:36568-36579(2011).
RN [36]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-224; LYS-242; LYS-253;
RP LYS-271; LYS-393 AND LYS-437, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [37]
RP METHYLATION AT LYS-30 BY EFM1, METHYLATION AT LYS-316 BY SEE1, AND
RP METHYLATION AT LYS-79 AND LYS-390.
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).
RN [38]
RP METHYLATION AT LYS-79 BY EFM5.
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).
RN [39]
RP METHYLATION AT LYS-30; LYS-79 AND LYS-390, AND METHYLATION AT LYS-316 BY
RP SEE1.
RX PubMed=24517342; DOI=10.1021/pr401251k;
RA Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P., Wilkins M.R.;
RT "Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights
RT into non-histone protein lysine methyltransferase activity.";
RL J. Proteome Res. 13:1744-1756(2014).
RN [40]
RP METHYLATION AT LYS-390 BY EFM6.
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).
RN [41]
RP METHYLATION AT GLY-2 AND LYS-3 BY NNT1.
RX PubMed=26545399; DOI=10.1074/mcp.m115.052449;
RA Hamey J.J., Winter D.L., Yagoub D., Overall C.M., Hart-Smith G.,
RA Wilkins M.R.;
RT "Novel N-terminal and lysine methyltransferases that target translation
RT elongation factor 1A in yeast and human.";
RL Mol. Cell. Proteomics 15:164-176(2016).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH EFB1.
RX PubMed=11106763; DOI=10.1016/s1097-2765(00)00122-2;
RA Andersen G.R., Pedersen L., Valente L., Chatterjee I., Kinzy T.G.,
RA Kjeldgaard M., Nyborg J.;
RT "Structural basis for nucleotide exchange and competition with tRNA in the
RT yeast elongation factor complex eEF1A:eEF1Balpha.";
RL Mol. Cell 6:1261-1266(2000).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH EFB1.
RX PubMed=11373622; DOI=10.1038/88598;
RA Andersen G.R., Valente L., Pedersen L., Kinzy T.G., Nyborg J.;
RT "Crystal structures of nucleotide exchange intermediates in the eEF1A-
RT eEF1Balpha complex.";
RL Nat. Struct. Biol. 8:531-534(2001).
CC -!- FUNCTION: GTP-binding component of the eukaryotic elongation factor 1
CC complex (eEF1). In its active GTP-bound form, binds to and delivers
CC aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
CC In the presence of a correct codon-anticodon match between the
CC aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the
CC ribosome acts as a GTPase activator and the GTP is hydrolyzed. The
CC inactive GDP-bound form leaves the ribosome and must be recycled by its
CC guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before
CC binding another molecule of aminoacyl-tRNA. Required for nuclear export
CC of aminoacyl-tRNAs. May also be involved in translational quality
CC control by targeting cotranslationally damaged proteins to the
CC proteasome. Also exhibits actin filament-binding and -bundling
CC activities and is involved in cytoskeleton organization. Plays a role
CC as a negative regulator of GCN2 kinase activity by inhibiting GCN2-
CC mediated eIF-2-alpha phosphorylation in amino acid-repleted cells
CC (PubMed:21849502). {ECO:0000269|PubMed:10766739,
CC ECO:0000269|PubMed:15601860, ECO:0000269|PubMed:21849502,
CC ECO:0000269|PubMed:3066688}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for GTP {ECO:0000269|PubMed:9786872};
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC -!- SUBUNIT: The eukaryotic elongation factor 1 complex (eEF1) is probably
CC a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1
CC or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably
CC dimerized via the eF1Bgamma subunits. eEF1A interacts directly with
CC eEF1Balpha. Interacts with elongation factor 3 (YEF3 or HEF3), BNI1,
CC SRV2 and ZPR1. Binds to actin and forms a ternary complex with BNI1 and
CC profilin. Interacts with the proteasome, probably via RPT1. Interacts
CC with CEX1 and NAP1. Interacts with GCN2 (via C-terminus); this
CC interaction is direct, occurs in amino acid-repleted cells, may be
CC stabilzed in a ribosome-dependent manner, reduces GCN2-mediated eIF-2-
CC alpha phosphorylation and is lost in amino acid-starved cells and by
CC uncharged tRNAs (PubMed:21849502). Associates with ribosomes
CC (PubMed:21849502). {ECO:0000269|PubMed:11106763,
CC ECO:0000269|PubMed:11290701, ECO:0000269|PubMed:11373622,
CC ECO:0000269|PubMed:15601860, ECO:0000269|PubMed:17203074,
CC ECO:0000269|PubMed:18086883, ECO:0000269|PubMed:21849502,
CC ECO:0000269|PubMed:9125210, ECO:0000269|PubMed:9591785,
CC ECO:0000269|PubMed:9852145, ECO:0000269|PubMed:9990316}.
CC -!- INTERACTION:
CC P02994; P43573: BUD27; NbExp=2; IntAct=EBI-6314, EBI-22787;
CC P02994; P32471: EFB1; NbExp=2; IntAct=EBI-6314, EBI-6319;
CC P02994; Q05040: FAR8; NbExp=2; IntAct=EBI-6314, EBI-28053;
CC P02994; P17555: SRV2; NbExp=3; IntAct=EBI-6314, EBI-4024;
CC P02994; Q62384: Zpr1; Xeno; NbExp=2; IntAct=EBI-6314, EBI-11566629;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095}.
CC -!- PTM: S-thiolated in response to oxidative stress, probably inhibiting
CC the protein and causing a reduction in protein synthesis.
CC {ECO:0000269|PubMed:12755685}.
CC -!- MISCELLANEOUS: Present with 827 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are two genes for eEF1A in yeast.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; X00779; CAA25356.1; -; Genomic_DNA.
DR EMBL; X01638; CAA25798.1; -; Genomic_DNA.
DR EMBL; M10992; AAA34585.1; -; Genomic_DNA.
DR EMBL; M15666; AAA34584.1; -; Genomic_DNA.
DR EMBL; M15667; AAA34586.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55620.1; -; Genomic_DNA.
DR EMBL; Z35987; CAA85075.1; -; Genomic_DNA.
DR EMBL; U51033; AAB68129.1; -; Genomic_DNA.
DR EMBL; AY692927; AAT92946.1; -; Genomic_DNA.
DR EMBL; X73532; CAA51936.1; -; Genomic_DNA.
DR EMBL; AF402004; AAP86465.1; -; Genomic_DNA.
DR EMBL; AY130810; AAM83111.1; -; Genomic_DNA.
DR EMBL; AY130811; AAM83112.1; -; Genomic_DNA.
DR EMBL; AY130812; AAM83113.1; -; Genomic_DNA.
DR EMBL; AY130813; AAM83114.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07236.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11498.1; -; Genomic_DNA.
DR PIR; A03522; EFBY1A.
DR RefSeq; NP_009676.1; NM_001178466.1.
DR RefSeq; NP_015405.1; NM_001184177.1.
DR PDB; 1F60; X-ray; 1.67 A; A=1-458.
DR PDB; 1G7C; X-ray; 2.05 A; A=1-458.
DR PDB; 1IJE; X-ray; 2.40 A; A=1-458.
DR PDB; 1IJF; X-ray; 3.00 A; A=1-458.
DR PDB; 2B7B; X-ray; 2.60 A; A=1-458.
DR PDB; 2B7C; X-ray; 1.80 A; A=1-458.
DR PDB; 5O8W; X-ray; 1.67 A; A=1-458.
DR PDBsum; 1F60; -.
DR PDBsum; 1G7C; -.
DR PDBsum; 1IJE; -.
DR PDBsum; 1IJF; -.
DR PDBsum; 2B7B; -.
DR PDBsum; 2B7C; -.
DR PDBsum; 5O8W; -.
DR AlphaFoldDB; P02994; -.
DR SMR; P02994; -.
DR BioGRID; 32820; 355.
DR BioGRID; 36251; 258.
DR ComplexPortal; CPX-2854; Elongation Factor eEF1 complex, variant CAM1.
DR ComplexPortal; CPX-425; Elongation Factor eEF1 complex, variant TEF4.
DR DIP; DIP-2250N; -.
DR IntAct; P02994; 808.
DR MINT; P02994; -.
DR STRING; 4932.YBR118W; -.
DR CarbonylDB; P02994; -.
DR iPTMnet; P02994; -.
DR MaxQB; P02994; -.
DR PaxDb; P02994; -.
DR PRIDE; P02994; -.
DR TopDownProteomics; P02994; -.
DR EnsemblFungi; YBR118W_mRNA; YBR118W; YBR118W.
DR EnsemblFungi; YPR080W_mRNA; YPR080W; YPR080W.
DR GeneID; 852415; -.
DR GeneID; 856195; -.
DR KEGG; sce:YBR118W; -.
DR KEGG; sce:YPR080W; -.
DR SGD; S000006284; TEF1.
DR SGD; S000000322; TEF2.
DR VEuPathDB; FungiDB:YBR118W; -.
DR VEuPathDB; FungiDB:YPR080W; -.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00940000164334; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P02994; -.
DR OMA; AIRDMGM; -.
DR BioCyc; YEAST:G3O-34224-MON; -.
DR Reactome; R-SCE-156842; Eukaryotic Translation Elongation.
DR Reactome; R-SCE-3371511; HSF1 activation.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8876725; Protein methylation.
DR UniPathway; UPA00345; -.
DR EvolutionaryTrace; P02994; -.
DR PRO; PR:P02994; -.
DR Proteomes; UP000002311; Chromosome II.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P02994; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IC:ComplexPortal.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IPI:SGD.
DR GO; GO:0005840; C:ribosome; IDA:ComplexPortal.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0019003; F:GDP binding; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IDA:SGD.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:1904408; F:melatonin binding; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:SGD.
DR GO; GO:0003746; F:translation elongation factor activity; IMP:SGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:SGD.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IDA:ComplexPortal.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Elongation factor; GTP-binding; Isopeptide bond;
KW Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:26545399"
FT CHAIN 2..458
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090973"
FT DOMAIN 5..240
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 192..194
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT SITE 298
FT /note="Not modified"
FT SITE 372
FT /note="Not modified"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine; by EFM7"
FT /evidence="ECO:0000269|PubMed:26545399"
FT MOD_RES 3
FT /note="N6,N6-dimethyllysine; by EFM7; alternate"
FT /evidence="ECO:0000269|PubMed:26545399"
FT MOD_RES 3
FT /note="N6-methyllysine; by EFM7; alternate"
FT /evidence="ECO:0000269|PubMed:26545399"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 30
FT /note="N6-methyllysine; by EFM1"
FT /evidence="ECO:0000269|PubMed:22522802,
FT ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:8476932"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine; by EFM5"
FT /evidence="ECO:0000269|PubMed:22522802,
FT ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25446118,
FT ECO:0000269|PubMed:8476932"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 316
FT /note="N6,N6-dimethyllysine; by EFM4; alternate"
FT /evidence="ECO:0000269|PubMed:22522802,
FT ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:8476932"
FT MOD_RES 316
FT /note="N6-methyllysine; by EFM4; alternate"
FT /evidence="ECO:0000269|PubMed:24517342"
FT MOD_RES 390
FT /note="N6-methyllysine; by EFM6"
FT /evidence="ECO:0000269|PubMed:22522802,
FT ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:26115316,
FT ECO:0000269|PubMed:8476932"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 458
FT /note="Lysine methyl ester"
FT /evidence="ECO:0000269|PubMed:10973948"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 242
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 393
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 437
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 122
FT /note="E->K: Reduces interaction with YEF3."
FT /evidence="ECO:0000269|PubMed:9990316"
FT MUTAGEN 153
FT /note="N->D: Increases KM for GTP to 2.7 mM."
FT /evidence="ECO:0000269|PubMed:10514524,
FT ECO:0000269|PubMed:9786872"
FT MUTAGEN 153
FT /note="N->T: Increases KM for GTP to 6.0 mM and reduces
FT translation fidelity. Increases Km for GTP to 10.3 mM and
FT reduces translation fidelity; when associated with E-156."
FT /evidence="ECO:0000269|PubMed:10514524,
FT ECO:0000269|PubMed:9786872"
FT MUTAGEN 156
FT /note="D->E: Increases KM for GTP to 10.3 mM and reduces
FT translation fidelity; when associated with T-152."
FT /evidence="ECO:0000269|PubMed:10514524,
FT ECO:0000269|PubMed:15601860, ECO:0000269|PubMed:9786872"
FT MUTAGEN 156
FT /note="D->N: Increases KM for GTP to 13.1 mM and reduces
FT translation fidelity. Confers hyperresistance to
FT canavanine."
FT /evidence="ECO:0000269|PubMed:10514524,
FT ECO:0000269|PubMed:15601860, ECO:0000269|PubMed:9786872"
FT MUTAGEN 156
FT /note="D->W: Increases KM for GTP to 4.2 mM. Preferres XTP
FT over GTP as substrate."
FT /evidence="ECO:0000269|PubMed:10514524,
FT ECO:0000269|PubMed:15601860, ECO:0000269|PubMed:9786872"
FT MUTAGEN 286
FT /note="E->K: In TEF2-1; strongly reduces translation
FT fidelity by increasing the frequency of frameshifting and
FT amino acid misincorporation."
FT /evidence="ECO:0000269|PubMed:3066688"
FT MUTAGEN 317
FT /note="E->K: In TEF2-2; strongly reduces translation
FT fidelity by increasing the frequency of frameshifting and
FT amino acid misincorporation."
FT /evidence="ECO:0000269|PubMed:3066688"
FT CONFLICT 86
FT /note="Q -> E (in Ref. 14; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 162..179
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1F60"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1F60"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:2B7C"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:1F60"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1F60"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 283..292
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:2B7C"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:1F60"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 336..344
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 364..377
FT /evidence="ECO:0007829|PDB:1F60"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 397..406
FT /evidence="ECO:0007829|PDB:1F60"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 420..426
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 429..440
FT /evidence="ECO:0007829|PDB:1F60"
SQ SEQUENCE 458 AA; 50033 MW; 411C66D830716576 CRC64;
MGKEKSHINV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETPKYQVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGV
GEFEAGISKD GQTREHALLA FTLGVRQLIV AVNKMDSVKW DESRFQEIVK ETSNFIKKVG
YNPKTVPFVP ISGWNGDNMI EATTNAPWYK GWEKETKAGV VKGKTLLEAI DAIEQPSRPT
DKPLRLPLQD VYKIGGIGTV PVGRVETGVI KPGMVVTFAP AGVTTEVKSV EMHHEQLEQG
VPGDNVGFNV KNVSVKEIRR GNVCGDAKND PPKGCASFNA TVIVLNHPGQ ISAGYSPVLD
CHTAHIACRF DELLEKNDRR SGKKLEDHPK FLKSGDAALV KFVPSKPMCV EAFSEYPPLG
RFAVRDMRQT VAVGVIKSVD KTEKAAKVTK AAQKAAKK
