ID EF3A_YEAST Reviewed; 1044 AA. AC P16521; D6VYP7; O93815; Q06558; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 4. DT 27-MAR-2024, entry version 234. DE RecName: Full=Elongation factor 3A; DE Short=EF-3; DE Short=EF-3A; DE EC=3.6.4.- {ECO:0000269|PubMed:29300771, ECO:0000269|PubMed:6456269, ECO:0000269|PubMed:7657623, ECO:0000269|PubMed:7957240}; DE AltName: Full=Eukaryotic elongation factor 3; DE Short=eEF3; DE AltName: Full=Translation elongation factor 3A; DE AltName: Full=Yeast elongation factor 3; GN Name=YEF3; Synonyms=EFC1, TEF3, YEF3A; OrderedLocusNames=YLR249W; GN ORFNames=L9672.5; 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]. RX PubMed=2404974; DOI=10.1016/s0021-9258(19)39916-8; RA Qin S., Xie A., Bonato M.C.M., McLaughlin C.S.; RT "Sequence analysis of the translational elongation factor 3 from RT Saccharomyces cerevisiae."; RL J. Biol. Chem. 265:1903-1912(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1976386; DOI=10.1016/0167-4781(90)90172-x; RA Sandbaken M.G., Lupisella J.A., DiDomenico B., Chakraburtty K.; RT "Isolation and characterization of the structural gene encoding elongation RT factor 3."; RL Biochim. Biophys. Acta 1050:230-234(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2203789; DOI=10.1016/s0021-9258(18)55474-0; RA Sandbaken M.G., Lupisella J.A., DiDomenico B., Chakraburtty K.; RT "Protein synthesis in yeast. Structural and functional analysis of the gene RT encoding elongation factor 3."; RL J. Biol. Chem. 265:15838-15844(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 446-955. RC STRAIN=ATCC 208279 / BJ926; RX PubMed=10361693; DOI=10.1271/bbb.63.769; RA Uritani M., Shoumura Y., Yamada S.; RT "Detection and analysis of translation elongation factor 3 genes from RT various yeasts."; RL Biosci. Biotechnol. Biochem. 63:769-772(1999). RN [7] RP PROTEIN SEQUENCE OF 959-967. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7895733; DOI=10.1002/elps.11501501210; RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., RA Volpe T., Warner J.R., McLaughlin C.S.; RT "Protein identifications for a Saccharomyces cerevisiae protein database."; RL Electrophoresis 15:1466-1486(1994). RN [8] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=6456269; DOI=10.1016/s0021-9258(19)68730-2; RA Dasmahapatra B., Chakraburtty K.; RT "Protein synthesis in yeast. I. Purification and properties of elongation RT factor 3 from Saccharomyces cerevisiae."; RL J. Biol. Chem. 256:9999-10004(1981). RN [9] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=7657623; DOI=10.1074/jbc.270.35.20473; RA Triana-Alonso F.J., Chakraburtty K., Nierhaus K.H.; RT "The elongation factor 3 unique in higher fungi and essential for protein RT biosynthesis is an E site factor."; RL J. Biol. Chem. 270:20473-20478(1995). RN [10] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION. RX PubMed=7957240; DOI=10.1111/j.1432-1033.1994.tb20034.x; RA Kovalchuke O., Chakraburtty K.; RT "Comparative analysis of ribosome-associated adenosinetriphosphatase RT (ATPase) from pig liver and the ATPase of elongation factor 3 from RT Saccharomyces cerevisiae."; RL Eur. J. Biochem. 226:133-140(1994). RN [11] RP ACETYLATION AT SER-2. RX PubMed=9298649; DOI=10.1002/elps.1150180810; RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., RA Payne W.E.; RT "Proteome studies of Saccharomyces cerevisiae: identification and RT characterization of abundant proteins."; RL Electrophoresis 18:1347-1360(1997). RN [12] RP INTERACTION WITH EEF1A. 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 [13] RP CHARACTERIZATION. RX PubMed=9544245; RX DOI=10.1002/(sici)1097-0061(199802)14:3<239::aid-yea219>3.0.co;2-b; RA Sarthy A.V., McGonigal T., Capobianco J.O., Schmidt M., Green S.R., RA Moehle C.M., Goldman R.C.; RT "Identification and kinetic analysis of a functional homolog of elongation RT factor 3, YEF3 in Saccharomyces cerevisiae."; RL Yeast 14:239-253(1998). RN [14] RP INTERACTION WITH 18S RRNA. RX PubMed=9553076; DOI=10.1074/jbc.273.17.10249; RA Gontarek R.R., Li H., Nurse K., Prescott C.D.; RT "The N-terminus of eukaryotic translation elongation factor 3 interacts RT with 18 S rRNA and 80 S ribosomes."; RL J. Biol. Chem. 273:10249-10252(1998). RN [15] RP PHOSPHORYLATION. RX PubMed=10523624; DOI=10.1128/mcb.19.11.7357; RA Futcher B., Latter G.I., Monardo P., McLaughlin C.S., Garrels J.I.; RT "A sampling of the yeast proteome."; RL Mol. Cell. Biol. 19:7357-7368(1999). RN [16] RP MUTAGENESIS OF PHE-650, AND INTERACTION WITH EEF1A. RX PubMed=12493761; DOI=10.1074/jbc.m209224200; RA Anand M., Chakraburtty K., Marton M.J., Hinnebusch A.G., Kinzy T.G.; RT "Functional interactions between yeast translation eukaryotic elongation RT factor (eEF) 1A and eEF3."; RL J. Biol. Chem. 278:6985-6991(2003). RN [17] 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 [18] 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039 AND SER-1040, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-972; SER-1039 AND SER-1040, RP AND 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; THR-972; SER-974; RP SER-1039 AND SER-1040, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [22] RP FUNCTION, ASSOCIATION WITH RIBOSOMES, AND DOMAIN. RX PubMed=22888004; DOI=10.1074/jbc.m112.368266; RA Visweswaraiah J., Lee S.J., Hinnebusch A.G., Sattlegger E.; RT "Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 RT protein activation."; RL J. Biol. Chem. 287:37757-37768(2012). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [24] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-350 AND LYS-636, AND RP IDENTIFICATION BY MASS SPECTROMETRY [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 [25] RP METHYLATION AT LYS-187; LYS-196 AND LYS-789. 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 [26] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=29300771; DOI=10.1371/journal.pone.0190524; RA Mateyak M.K., Pupek J.K., Garino A.E., Knapp M.C., Colmer S.F., Kinzy T.G., RA Dunaway S.; RT "Demonstration of translation elongation factor 3 activity from a non- RT fungal species, Phytophthora infestans."; RL PLoS ONE 13:e0190524-e0190524(2018). RN [27] RP INDUCTION. RX PubMed=33260587; DOI=10.3390/genes11121432; RA Goscinska K., Shahmoradi Ghahe S., Domogala S., Topf U.; RT "Eukaryotic Elongation Factor 3 Protects Saccharomyces cerevisiae Yeast RT from Oxidative Stress."; RL Genes (Basel) 11:E1432-E1432(2020). CC -!- FUNCTION: Ribosome-dependent ATPase that functions in cytoplasmic CC translation elongation (PubMed:7657623, PubMed:6456269, CC PubMed:29300771). Required for the ATP-dependent release of deacylated CC tRNA from the ribosomal E-site during protein biosynthesis CC (PubMed:7657623). Stimulates the eEF1A-dependent binding of aminoacyl- CC tRNA to the ribosomal A-site, which has reduced affinity for tRNA as CC long as the E-site is occupied (PubMed:7657623). Plays a role as a CC negative regulator of the GCN2 kinase activity; impairs GCN1-mediated CC GCN2 activation on ribosomes by reducing GCN1-ribosome affinity, and CC hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved CC or repleted cells (PubMed:22888004). {ECO:0000269|PubMed:22888004, CC ECO:0000269|PubMed:29300771, ECO:0000269|PubMed:6456269, CC ECO:0000269|PubMed:7657623}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:29300771, ECO:0000269|PubMed:6456269, CC ECO:0000269|PubMed:7657623, ECO:0000269|PubMed:7957240}; CC -!- ACTIVITY REGULATION: Inhibited by the translational inhibitors neomycin CC and alpha-sarcin, which suppress the ATPase activity. CC {ECO:0000269|PubMed:7957240}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.126 mM for ATP {ECO:0000269|PubMed:7957240}; CC KM=0.125 mM for GTP {ECO:0000269|PubMed:7957240}; CC Vmax=15.2 umol/min/mg enzyme with ATP as substrate CC {ECO:0000269|PubMed:7957240}; CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC {ECO:0000305}. CC -!- SUBUNIT: Monomer. Interacts with elongation factor 1A (eEF1A). CC Interacts through its N-terminus with 18S rRNA. Associates with CC ribosomes (PubMed:22888004). {ECO:0000269|PubMed:12493761, CC ECO:0000269|PubMed:22888004, ECO:0000269|PubMed:9553076, CC ECO:0000269|PubMed:9990316}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC -!- INDUCTION: Increases in strong (1 mM) hydrogen peroxide stress, and CC decreases in milder (0.5 mM) hydrogen peroxide stress. CC {ECO:0000269|PubMed:33260587}. CC -!- DOMAIN: The heat repeats and the C-terminal domain are necessary for CC impairing GCN1 function on ribosomes, and hence preventing GCN2 kinase CC activity in amino acid-starved or repleted cells (PubMed:22888004). CC {ECO:0000269|PubMed:22888004}. CC -!- MISCELLANEOUS: Present with 870578 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. CC EF3 subfamily. {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; J05197; AAA35232.1; -; Genomic_DNA. DR EMBL; J05583; AAA35233.1; -; Genomic_DNA. DR EMBL; U20865; AAB67391.1; -; Genomic_DNA. DR EMBL; AB018539; BAA33897.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09563.1; -; Genomic_DNA. DR PIR; S59395; DVBYE3. DR RefSeq; NP_013350.1; NM_001182136.1. DR PDB; 2IW3; X-ray; 2.40 A; A/B=2-981. DR PDB; 2IWH; X-ray; 3.00 A; A/B=2-981. DR PDB; 2IX3; X-ray; 2.70 A; A/B=2-981. DR PDB; 2IX8; EM; 6.00 A; A=2-977. DR PDB; 7B7D; EM; 3.30 A; EF=1-1044. DR PDBsum; 2IW3; -. DR PDBsum; 2IWH; -. DR PDBsum; 2IX3; -. DR PDBsum; 2IX8; -. DR PDBsum; 7B7D; -. DR AlphaFoldDB; P16521; -. DR EMDB; EMD-12081; -. DR EMDB; EMD-1233; -. DR SMR; P16521; -. DR BioGRID; 31517; 239. DR DIP; DIP-2249N; -. DR IntAct; P16521; 83. DR MINT; P16521; -. DR STRING; 4932.YLR249W; -. DR CarbonylDB; P16521; -. DR iPTMnet; P16521; -. DR MaxQB; P16521; -. DR PaxDb; 4932-YLR249W; -. DR PeptideAtlas; P16521; -. DR EnsemblFungi; YLR249W_mRNA; YLR249W; YLR249W. DR GeneID; 850951; -. DR KEGG; sce:YLR249W; -. DR AGR; SGD:S000004239; -. DR SGD; S000004239; YEF3. DR VEuPathDB; FungiDB:YLR249W; -. DR eggNOG; KOG0062; Eukaryota. DR eggNOG; KOG1242; Eukaryota. DR GeneTree; ENSGT00940000176346; -. DR HOGENOM; CLU_002848_0_0_1; -. DR InParanoid; P16521; -. DR OMA; VLSEAMW; -. DR OrthoDB; 49929at2759; -. DR BioCyc; YEAST:G3O-32354-MONOMER; -. DR SABIO-RK; P16521; -. DR UniPathway; UPA00345; -. DR BioGRID-ORCS; 850951; 6 hits in 10 CRISPR screens. DR EvolutionaryTrace; P16521; -. DR PRO; PR:P16521; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; P16521; Protein. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD. DR GO; GO:0022626; C:cytosolic ribosome; IDA:SGD. DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB. DR GO; GO:0005840; C:ribosome; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:SGD. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003746; F:translation elongation factor activity; IDA:SGD. 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:0006414; P:translational elongation; IMP:SGD. DR GO; GO:0006415; P:translational termination; IDA:SGD. DR CDD; cd03221; ABCF_EF-3; 1. DR CDD; cd18626; CD_eEF3; 1. DR Gene3D; 1.20.1390.20; -; 1. DR Gene3D; 2.40.50.990; -; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR015688; eEF3_ABC2_chromodomain-like. DR InterPro; IPR047038; eEF3_chromodomain-like_sf. DR InterPro; IPR040533; EF3_4HB. DR InterPro; IPR047036; EF3_4HB_sf. DR InterPro; IPR021133; HEAT_type_2. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1. DR PANTHER; PTHR19211:SF5; ELONGATION FACTOR 3A-RELATED; 1. DR Pfam; PF17947; 4HB; 1. DR Pfam; PF00005; ABC_tran; 3. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR PROSITE; PS50077; HEAT_REPEAT; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; KW Direct protein sequencing; Elongation factor; Hydrolase; Isopeptide bond; KW Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; KW Reference proteome; Repeat; RNA-binding; rRNA-binding; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9298649, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..1044 FT /note="Elongation factor 3A" FT /id="PRO_0000093458" FT REPEAT 5..42 FT /note="HEAT 1" FT REPEAT 86..123 FT /note="HEAT 2" FT REPEAT 125..162 FT /note="HEAT 3" FT REPEAT 166..203 FT /note="HEAT 4" FT REPEAT 205..241 FT /note="HEAT 5" FT REPEAT 242..279 FT /note="HEAT 6" FT REPEAT 285..323 FT /note="HEAT 7" FT DOMAIN 426..641 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 667..993 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT REGION 974..1044 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 986..1006 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1007..1028 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 463..470 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 701..708 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:9298649, FT ECO:0007744|PubMed:22814378" FT MOD_RES 187 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:22522802" FT MOD_RES 196 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:22522802" FT MOD_RES 642 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 789 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:22522802" FT MOD_RES 972 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 974 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 1039 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 1040 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT CROSSLNK 350 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 636 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 650 FT /note="F->S: Reduces ATPase activity and interaction with FT eEF1A. Required for growth at 37 degrees Celsius and causes FT a 50% reduction of total protein synthesis at permissive FT temperatures." FT /evidence="ECO:0000269|PubMed:12493761" FT CONFLICT 153 FT /note="I -> F (in Ref. 1; AAA35232, 2; no nucleotide entry FT and 3; AAA35233)" FT /evidence="ECO:0000305" FT CONFLICT 332 FT /note="V -> L (in Ref. 1; AAA35232, 2; no nucleotide entry FT and 3; AAA35233)" FT /evidence="ECO:0000305" FT HELIX 3..18 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 23..25 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 26..37 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 48..58 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 61..74 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 77..79 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 85..89 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 92..98 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 104..120 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 126..139 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 143..159 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 161..178 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 184..197 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 204..206 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 210..218 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 222..230 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 241..255 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 257..259 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 260..274 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 284..289 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 291..297 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 298..300 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 304..321 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 325..327 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 338..348 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 349..351 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 359..374 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 380..386 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 388..391 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 397..413 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 426..428 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 430..440 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 443..454 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 458..462 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 469..478 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 487..489 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 492..494 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 508..513 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 514..516 FT /evidence="ECO:0007829|PDB:2IX3" FT HELIX 520..529 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 534..538 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 541..543 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 546..559 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 563..569 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 570..573 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 576..588 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 591..596 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 600..606 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 608..614 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 617..623 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 625..631 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 633..637 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 638..640 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 641..643 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 664..674 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 679..681 FT /evidence="ECO:0007829|PDB:2IX3" FT STRAND 683..692 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 696..699 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 705..714 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 721..727 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 733..736 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 738..743 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 744..746 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 752..759 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 760..762 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 766..772 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 783..785 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 788..790 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 793..806 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 809..821 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 828..831 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 834..836 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 838..841 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 842..844 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 846..863 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 872..881 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 886..891 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 894..896 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 899..911 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 916..921 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 923..925 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 929..940 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 943..949 FT /evidence="ECO:0007829|PDB:2IW3" FT HELIX 953..956 FT /evidence="ECO:0007829|PDB:2IW3" FT TURN 957..959 FT /evidence="ECO:0007829|PDB:2IW3" FT STRAND 962..964 FT /evidence="ECO:0007829|PDB:2IW3" SQ SEQUENCE 1044 AA; 115945 MW; 41E40B8BDD7A4C33 CRC64; MSDSQQSIKV LEELFQKLSV ATADNRHEIA SEVASFLNGN IIEHDVPEHF FGELAKGIKD KKTAANAMQA VAHIANQSNL SPSVEPYIVQ LVPAICTNAG NKDKEIQSVA SETLISIVNA VNPVAIKALL PHLTNAIVET NKWQEKIAIL AAISAMVDAA KDQVALRMPE LIPVLSETMW DTKKEVKAAA TAAMTKATET VDNKDIERFI PSLIQCIADP TEVPETVHLL GATTFVAEVT PATLSIMVPL LSRGLNERET GIKRKSAVII DNMCKLVEDP QVIAPFLGKL LPGLKSNFAT IADPEAREVT LRALKTLRRV GNVGEDDAIP EVSHAGDVST TLQVVNELLK DETVAPRFKI VVEYIAAIGA DLIDERIIDQ QAWFTHITPY MTIFLHEKKA KDILDEFRKR AVDNIPVGPN FDDEEDEGED LCNCEFSLAY GAKILLNKTQ LRLKRARRYG ICGPNGCGKS TLMRAIANGQ VDGFPTQEEC RTVYVEHDID GTHSDTSVLD FVFESGVGTK EAIKDKLIEF GFTDEMIAMP ISALSGGWKM KLALARAVLR NADILLLDEP TNHLDTVNVA WLVNYLNTCG ITSITISHDS VFLDNVCEYI INYEGLKLRK YKGNFTEFVK KCPAAKAYEE LSNTDLEFKF PEPGYLEGVK TKQKAIVKVT NMEFQYPGTS KPQITDINFQ CSLSSRIAVI GPNGAGKSTL INVLTGELLP TSGEVYTHEN CRIAYIKQHA FAHIESHLDK TPSEYIQWRF QTGEDRETMD RANRQINEND AEAMNKIFKI EGTPRRIAGI HSRRKFKNTY EYECSFLLGE NIGMKSERWV PMMSVDNAWI PRGELVESHS KMVAEVDMKE ALASGQFRPL TRKEIEEHCS MLGLDPEIVS HSRIRGLSGG QKVKLVLAAG TWQRPHLIVL DEPTNYLDRD SLGALSKALK EFEGGVIIIT HSAEFTKNLT EEVWAVKDGR MTPSGHNWVS GQGAGPRIEK KEDEEDKFDA MGNKIAGGKK KKKLSSAELR KKKKERMKKK KELGDAYVSS DEEF //