ELP1_YEAST
ID ELP1_YEAST Reviewed; 1349 AA.
AC Q06706; D6VZ19; O00036;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Elongator complex protein 1;
DE AltName: Full=Gamma-toxin target 1;
DE AltName: Full=Protein IKI3;
GN Name=IKI3; Synonyms=ELP1, TOT1; OrderedLocusNames=YLR384C;
GN ORFNames=L3502.7;
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=9145530; DOI=10.1271/bbb.61.704;
RA Yajima H., Tokunaga M., Nakayama-Murayama A., Hishinuma F.;
RT "Characterization of IKI1 and IKI3 genes conferring pGKL killer sensitivity
RT on Saccharomyces cerevisiae.";
RL Biosci. Biotechnol. Biochem. 61:704-709(1997).
RN [2]
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 [3]
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10024884; DOI=10.1016/s1097-2765(00)80179-3;
RA Otero G., Fellows J., Li Y., de Bizemont T., Dirac A.M., Gustafsson C.M.,
RA Erdjument-Bromage H., Tempst P., Svejstrup J.Q.;
RT "Elongator, a multisubunit component of a novel RNA polymerase II
RT holoenzyme for transcriptional elongation.";
RL Mol. Cell 3:109-118(1999).
RN [5]
RP FUNCTION OF THE ELONGATOR COMPLEX IN ZYMOCIN SENSITIVITY.
RX PubMed=11296232; DOI=10.1093/emboj/20.8.1993;
RA Frohloff F., Fichtner L., Jablonowski D., Breunig K.D., Schaffrath R.;
RT "Saccharomyces cerevisiae Elongator mutations confer resistance to the
RT Kluyveromyces lactis zymocin.";
RL EMBO J. 20:1993-2003(2001).
RN [6]
RP IDENTIFICATION IN THE ELONGATOR COMPLEX.
RX PubMed=11435442; DOI=10.1074/jbc.m105303200;
RA Winkler G.S., Petrakis T.G., Ethelberg S., Tokunaga M.,
RA Erdjument-Bromage H., Tempst P., Svejstrup J.Q.;
RT "RNA polymerase II elongator holoenzyme is composed of two discrete
RT subcomplexes.";
RL J. Biol. Chem. 276:32743-32749(2001).
RN [7]
RP IDENTIFICATION IN THE ELONGATOR COMPLEX.
RX PubMed=11689709; DOI=10.1128/mcb.21.23.8203-8212.2001;
RA Krogan N.J., Greenblatt J.F.;
RT "Characterization of a six-subunit holo-elongator complex required for the
RT regulated expression of a group of genes in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 21:8203-8212(2001).
RN [8]
RP INTERACTION WITH ELP2.
RX PubMed=12139626; DOI=10.1046/j.1365-2958.2002.03055.x;
RA Fichtner L., Frohloff F., Jablonowski D., Stark M.J.R., Schaffrath R.;
RT "Protein interactions within Saccharomyces cerevisiae Elongator, a complex
RT essential for Kluyveromyces lactis zymocicity.";
RL Mol. Microbiol. 45:817-826(2002).
RN [9]
RP DISPUTED FUNCTION IN HISTONE ACETYLATION.
RX PubMed=11904415; DOI=10.1073/pnas.022042899;
RA Winkler G.S., Kristjuhan A., Erdjument-Bromage H., Tempst P.,
RA Svejstrup J.Q.;
RT "Elongator is a histone H3 and H4 acetyltransferase important for normal
RT histone acetylation levels in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3517-3522(2002).
RN [10]
RP FUNCTION.
RX PubMed=12424236; DOI=10.1074/jbc.m210060200;
RA Frohloff F., Jablonowski D., Fichtner L., Schaffrath R.;
RT "Subunit communications crucial for the functional integrity of the yeast
RT RNA polymerase II elongator (gamma-toxin target (TOT)) complex.";
RL J. Biol. Chem. 278:956-961(2003).
RN [11]
RP FUNCTION OF THE ELONGATOR COMPLEX IN PICHIA INOSITOVORA TOXIN SENSITIVITY.
RX PubMed=13680368; DOI=10.1007/s00438-003-0920-5;
RA Klassen R., Meinhardt F.;
RT "Structural and functional analysis of the killer element pPin1-3 from
RT Pichia inositovora.";
RL Mol. Genet. Genomics 270:190-199(2003).
RN [12]
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 [13]
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 [14]
RP FUNCTION IN EXOCYTOSIS REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=15780940; DOI=10.1016/j.molcel.2005.02.018;
RA Rahl P.B., Chen C.Z., Collins R.N.;
RT "Elp1p, the yeast homolog of the FD disease syndrome protein, negatively
RT regulates exocytosis independently of transcriptional elongation.";
RL Mol. Cell 17:841-853(2005).
RN [15]
RP FUNCTION IN TRNA MODIFICATION.
RX PubMed=15769872; DOI=10.1261/rna.7247705;
RA Huang B., Johansson M.J.O., Bystroem A.S.;
RT "An early step in wobble uridine tRNA modification requires the Elongator
RT complex.";
RL RNA 11:424-436(2005).
RN [16]
RP FUNCTION.
RX PubMed=18755837; DOI=10.1261/rna.1184108;
RA Huang B., Lu J., Bystroem A.S.;
RT "A genome-wide screen identifies genes required for formation of the wobble
RT nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces
RT cerevisiae.";
RL RNA 14:2183-2194(2008).
RN [17]
RP SUBUNIT.
RX PubMed=22343726; DOI=10.1038/nsmb.2234;
RA Glatt S., Letoquart J., Faux C., Taylor N.M., Seraphin B., Muller C.W.;
RT "The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase.";
RL Nat. Struct. Mol. Biol. 19:314-320(2012).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1228-ARG--ARG-1235;
RP 1228-ARG--LYS-1246 AND 1240-LYS--LYS-1245.
RX PubMed=24750273; DOI=10.1111/mmi.12624;
RA Di Santo R., Bandau S., Stark M.J.;
RT "A conserved and essential basic region mediates tRNA binding to the Elp1
RT subunit of the Saccharomyces cerevisiae Elongator complex.";
RL Mol. Microbiol. 92:1227-1242(2014).
RN [19]
RP FUNCTION, INTERACTION WITH HRR25 AND KTI12, DISRUPTION PHENOTYPE,
RP PHOSPHORYLATION AT SER-529; SER-539; SER-551; SER-636; SER-828; SER-1198;
RP SER-1202; SER-1205 AND SER-1209, MUTAGENESIS OF SER-529; SER-539; SER-551;
RP SER-636; SER-828; SER-1198; SER-1202; SER-1205 AND SER-1209, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25569479; DOI=10.1371/journal.pgen.1004931;
RA Abdel-Fattah W., Jablonowski D., Di Santo R., Thuering K.L., Scheidt V.,
RA Hammermeister A., Ten Have S., Helm M., Schaffrath R., Stark M.J.;
RT "Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA
RT modification in yeast.";
RL PLoS Genet. 11:e1004931-e1004931(2015).
RN [20]
RP IDENTIFICATION IN THE ELONGATOR ELP123 SUBCOMPLEX.
RX PubMed=25960406; DOI=10.1016/j.str.2015.03.018;
RA Dong C., Lin Z., Diao W., Li D., Chu X., Wang Z., Zhou H., Xie Z., Shen Y.,
RA Long J.;
RT "The Elp2 subunit is essential for elongator complex assembly and
RT functional regulation.";
RL Structure 23:1078-1086(2015).
RN [21]
RP INTERACTION WITH KTI11, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27694803; DOI=10.1038/nchembio.2190;
RA Lin Z., Dong M., Zhang Y., Lee E.A., Lin H.;
RT "Cbr1 is a Dph3 reductase required for the tRNA wobble uridine
RT modification.";
RL Nat. Chem. Biol. 12:995-997(2016).
RN [22]
RP REVIEW.
RX PubMed=29332244; DOI=10.1007/s00018-018-2747-6;
RA Dalwadi U., Yip C.K.;
RT "Structural insights into the function of Elongator.";
RL Cell. Mol. Life Sci. 75:1613-1622(2018).
RN [23] {ECO:0007744|PDB:5CQS}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 919-1349, SUBUNIT, IDENTIFICATION
RP IN THE ELONGATOR COMPLEX, DIMERIZATION REGION, AND MUTAGENESIS OF ARG-1063;
RP ARG-1282 AND ARG-1286.
RX PubMed=26261306; DOI=10.1073/pnas.1502597112;
RA Xu H., Lin Z., Li F., Diao W., Dong C., Zhou H., Xie X., Wang Z., Shen Y.,
RA Long J.;
RT "Dimerization of elongator protein 1 is essential for Elongator complex
RT assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:10697-10702(2015).
RN [24]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.3 ANGSTROMS), AND IDENTIFICATION IN THE
RP ELONGATOR COMPLEX.
RX PubMed=27974378; DOI=10.15252/embr.201643353;
RA Dauden M.I., Kosinski J., Kolaj-Robin O., Desfosses A., Ori A., Faux C.,
RA Hoffmann N.A., Onuma O.F., Breunig K.D., Beck M., Sachse C., Seraphin B.,
RA Glatt S., Mueller C.W.;
RT "Architecture of the yeast Elongator complex.";
RL EMBO Rep. 18:264-279(2017).
RN [25]
RP STRUCTURE BY ELECTRON MICROSCOPY, AND IDENTIFICATION IN THE ELONGATOR
RP COMPLEX.
RX PubMed=27872205; DOI=10.15252/embr.201642548;
RA Setiaputra D.T., Cheng D.T., Lu S., Hansen J.M., Dalwadi U., Lam C.H.,
RA To J.L., Dong M.Q., Yip C.K.;
RT "Molecular architecture of the yeast Elongator complex reveals an
RT unexpected asymmetric subunit arrangement.";
RL EMBO Rep. 18:280-291(2017).
RN [26] {ECO:0007744|PDB:6QK7}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF THE ELONGATOR ELP123
RP SUBCOMPLEX, AND FUNCTION.
RX PubMed=31309145; DOI=10.1126/sciadv.aaw2326;
RA Dauden M.I., Jaciuk M., Weis F., Lin T.Y., Kleindienst C., Abbassi N.E.H.,
RA Khatter H., Krutyholowa R., Breunig K.D., Kosinski J., Mueller C.W.,
RA Glatt S.;
RT "Molecular basis of tRNA recognition by the Elongator complex.";
RL Sci. Adv. 5:eaaw2326-eaaw2326(2019).
CC -!- FUNCTION: Component of the elongator complex which is required for
CC multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC (5-carbamoylmethyl uridine) (PubMed:15769872, PubMed:18755837,
CC PubMed:31309145, PubMed:25569479). The elongator complex catalyzes
CC formation of carboxymethyluridine in the wobble base at position 34 in
CC tRNAs (PubMed:29332244). Functions as a gamma-toxin target (TOT);
CC disruption of the complex confers resistance to Kluyveromyces lactis
CC toxin zymocin (pGKL1 killer toxin) (PubMed:12424236). May also be
CC involved in sensitivity to Pichia inositovora toxin (PubMed:13680368).
CC ELP1/IKI3 binds to tRNA, mediating interaction of the elongator complex
CC with tRNA (PubMed:24750273). Independently, may be involved in
CC polarized exocytosis (PubMed:15780940). {ECO:0000269|PubMed:12424236,
CC ECO:0000269|PubMed:13680368, ECO:0000269|PubMed:15769872,
CC ECO:0000269|PubMed:15780940, ECO:0000269|PubMed:18755837,
CC ECO:0000269|PubMed:24750273, ECO:0000303|PubMed:29332244}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000269|PubMed:15769872,
CC ECO:0000269|PubMed:18755837}.
CC -!- SUBUNIT: Homodimer; dimerization promotes ELP1/IKI3 stability and
CC elongator complex formation (PubMed:26261306). Component of the
CC elongator complex which consists of ELP1/IKI3, ELP2, ELP3, ELP4,
CC ELP5/IKI1 and ELP6 (PubMed:11435442, PubMed:11689709, PubMed:27974378,
CC PubMed:27872205, PubMed:26261306). The elongator complex is composed of
CC two copies of the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and
CC ELP3) and two copies of the Elp456 subcomplex (composed of ELP4,
CC ELP5/IKI1 and ELP6) (PubMed:27974378, PubMed:27872205,
CC PubMed:25960406). The Elp123 subcomplex forms a two-lobed scaffold,
CC which binds the Elp456 subcomplex asymmetrically (PubMed:27974378,
CC PubMed:27872205). In the complex, ELP1/IKI3 interacts with ELP2
CC (PubMed:12139626). In each lobe, ELP2 is tightly sandwiched between
CC ELP1/IKI3 and ELP3 (PubMed:31309145). The Elp123 subcomplex binds tRNA
CC through ELP1/IKI3 and ELP3 and can bind 2 tRNAs simultaneously
CC (PubMed:31309145). tRNA-binding induces conformational rearrangements
CC which precisely position the targeted anticodon base in the active site
CC (PubMed:31309145). The Elp456 subcomplex binds tRNA and has ATPase
CC activity (PubMed:22343726). ELP1/IKI3 interacts with HRR25 and KTI12
CC (PubMed:25569479). Interacts with KTI11/DPH3 (PubMed:27694803).
CC {ECO:0000269|PubMed:11435442, ECO:0000269|PubMed:11689709,
CC ECO:0000269|PubMed:12139626, ECO:0000269|PubMed:22343726,
CC ECO:0000269|PubMed:25569479, ECO:0000269|PubMed:26261306,
CC ECO:0000269|PubMed:27694803, ECO:0000269|PubMed:27872205,
CC ECO:0000269|PubMed:27974378, ECO:0000269|PubMed:31309145}.
CC -!- INTERACTION:
CC Q06706; P42935: ELP2; NbExp=11; IntAct=EBI-9068, EBI-23459;
CC Q06706; Q02884: ELP4; NbExp=12; IntAct=EBI-9068, EBI-35277;
CC Q06706; Q04868: ELP6; NbExp=7; IntAct=EBI-9068, EBI-27653;
CC Q06706; P38874: IKI1; NbExp=10; IntAct=EBI-9068, EBI-9061;
CC Q06706; Q06706: IKI3; NbExp=3; IntAct=EBI-9068, EBI-9068;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15780940,
CC ECO:0000269|PubMed:24750273}. Nucleus {ECO:0000269|PubMed:10024884,
CC ECO:0000269|PubMed:24750273}. Note=Predominantly cytoplasmic.
CC {ECO:0000269|PubMed:24750273}.
CC -!- PTM: Phosphorylation promotes the tRNA modification function of the
CC elongator complex. {ECO:0000269|PubMed:25569479}.
CC -!- DISRUPTION PHENOTYPE: Loss of mcm5U (5-methoxycarbonylmethyl uridine)
CC and ncm5U (5-carbamoylmethyl uridine) from tRNA.
CC {ECO:0000269|PubMed:25569479}.
CC -!- MISCELLANEOUS: Present with 10500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ELP1/IKA1 family. {ECO:0000305}.
CC -!- CAUTION: The elongator complex was originally thought to play a role in
CC transcription elongation. However, it is no longer thought to play a
CC direct role in this process and its primary function is thought to be
CC in tRNA modification. {ECO:0000305|PubMed:10024884,
CC ECO:0000305|PubMed:11689709, ECO:0000305|PubMed:11904415,
CC ECO:0000305|PubMed:29332244}.
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DR EMBL; D87841; BAA20120.1; -; Genomic_DNA.
DR EMBL; U19104; AAB67278.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09685.1; -; Genomic_DNA.
DR PIR; S51471; S51471.
DR RefSeq; NP_013488.3; NM_001182273.3.
DR PDB; 5CQS; X-ray; 2.70 A; A/B/C/D=919-1349.
DR PDB; 6QK7; EM; 3.30 A; A/D=1-1349.
DR PDBsum; 5CQS; -.
DR PDBsum; 6QK7; -.
DR AlphaFoldDB; Q06706; -.
DR SMR; Q06706; -.
DR BioGRID; 31643; 520.
DR ComplexPortal; CPX-779; Elongator holoenzyme complex.
DR DIP; DIP-2384N; -.
DR IntAct; Q06706; 20.
DR MINT; Q06706; -.
DR STRING; 4932.YLR384C; -.
DR iPTMnet; Q06706; -.
DR MaxQB; Q06706; -.
DR PaxDb; Q06706; -.
DR PRIDE; Q06706; -.
DR DNASU; 851100; -.
DR EnsemblFungi; YLR384C_mRNA; YLR384C; YLR384C.
DR GeneID; 851100; -.
DR KEGG; sce:YLR384C; -.
DR SGD; S000004376; IKI3.
DR VEuPathDB; FungiDB:YLR384C; -.
DR eggNOG; KOG1920; Eukaryota.
DR GeneTree; ENSGT00390000013344; -.
DR HOGENOM; CLU_001477_0_1_1; -.
DR InParanoid; Q06706; -.
DR OMA; DMNILHD; -.
DR BioCyc; YEAST:G3O-32450-MON; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q06706; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06706; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006417; P:regulation of translation; IC:ComplexPortal.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.
DR IDEAL; IID50289; -.
DR InterPro; IPR006849; Elp1.
DR PANTHER; PTHR12747; PTHR12747; 1.
DR Pfam; PF04762; IKI3; 1.
DR PIRSF; PIRSF017233; IKAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; tRNA processing.
FT CHAIN 1..1349
FT /note="Elongator complex protein 1"
FT /id="PRO_0000084179"
FT REGION 919..1349
FT /note="Mediates dimerization"
FT /evidence="ECO:0000269|PubMed:26261306"
FT REGION 1214..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1246
FT /note="Required for binding to tRNA"
FT /evidence="ECO:0000269|PubMed:24750273"
FT COMPBIAS 1228..1242
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25569479"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25569479"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25569479"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25569479"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25569479"
FT MOD_RES 1198
FT /note="Phosphoserine; by HRR25"
FT /evidence="ECO:0000269|PubMed:25569479"
FT MOD_RES 1202
FT /note="Phosphoserine; by HRR25"
FT /evidence="ECO:0000269|PubMed:25569479"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25569479"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 529
FT /note="S->A: Does not affect elongator complex activity."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 539
FT /note="S->A: Does not affect elongator complex activity."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 551
FT /note="S->A: Does not affect elongator complex activity."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 636
FT /note="S->A: Does not affect elongator complex activity."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 828
FT /note="S->A: Does not affect elongator complex activity."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 1063
FT /note="R->A: Disrupts dimer formation and elongator complex
FT formation but does not affect binding to tRNA; when
FT associated with A-1282 and A-1286."
FT /evidence="ECO:0000269|PubMed:26261306"
FT MUTAGEN 1198
FT /note="S->A: Does not affect elongator complex activity.
FT Loss of elongator complex activity, reduced levels of mcm5U
FT and ncm5U on tRNA and reduced interaction with HRR25 but no
FT effect on elongator complex assembly; when associated with
FT A-1202."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 1198
FT /note="S->E: Slightly reduced levels of mcm5U and ncm5U on
FT tRNA; when associated with E-1202."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 1202
FT /note="S->A: Does not affect elongator complex activity.
FT Loss of elongator complex activity, reduced levels of mcm5U
FT and ncm5U on tRNA and reduced interaction with HRR25 but no
FT effect on elongator complex assembly; when associated with
FT A-1198."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 1202
FT /note="S->E: Slightly reduced levels of mcm5U and ncm5U on
FT tRNA; when associated with E-1198."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 1205
FT /note="S->A: Does not affect elongator complex activity."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 1209
FT /note="S->A: Loss of phosphorylation at this site. Loss of
FT elongator complex activity. Almost complete loss of mcm5U
FT and ncm5U on tRNA. Does not affect elongator complex
FT assembly. Enhances interaction with HRR25 and KTI12."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 1209
FT /note="S->D: Phosphomimetic mutant. Does not affect
FT elongator complex activity."
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 1228..1245
FT /note="RRTAKNKRREERKRARGK->AATAANAAREERAAAAGA: Loss of
FT elongator complex activity. Abolishes binding to tRNA. Does
FT not disrupt elongator complex assembly but decreases
FT association of ELP1 with ELP5 and KTI12. Does not affect
FT ELP1 self-association or association with ELP3. Does not
FT affect the predominantly cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:24750273"
FT MUTAGEN 1228..1235
FT /note="RRTAKNKR->AATAANAA: Some loss of elongator complex
FT activity."
FT /evidence="ECO:0000269|PubMed:24750273"
FT MUTAGEN 1240..1245
FT /note="KRARGK->AAAAGA: Does not affect elongator complex
FT activity."
FT /evidence="ECO:0000269|PubMed:24750273"
FT MUTAGEN 1282
FT /note="R->A: Disrupts dimer formation and elongator complex
FT formation but does not affect binding to tRNA; when
FT associated with A-1063 and A-1286."
FT /evidence="ECO:0000269|PubMed:26261306"
FT MUTAGEN 1286
FT /note="R->A: Disrupts dimer formation and elongator complex
FT formation but does not affect binding to tRNA; when
FT associated with A-1063 and A-1282."
FT /evidence="ECO:0000269|PubMed:26261306"
FT STRAND 20..29
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:6QK7"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6QK7"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 257..269
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 281..292
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:6QK7"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 374..385
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 387..394
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 405..415
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 418..427
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:6QK7"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 492..499
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 503..507
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 529..536
FT /evidence="ECO:0007829|PDB:6QK7"
FT TURN 537..539
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 540..546
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 559..563
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 585..592
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 596..600
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 606..611
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 616..625
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 640..651
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 666..670
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 673..677
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 679..687
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 705..710
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 716..721
FT /evidence="ECO:0007829|PDB:6QK7"
FT TURN 722..725
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 736..739
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 742..754
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 760..767
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 774..777
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 780..785
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 787..793
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 797..805
FT /evidence="ECO:0007829|PDB:6QK7"
FT TURN 813..816
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 838..842
FT /evidence="ECO:0007829|PDB:6QK7"
FT TURN 843..846
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 854..865
FT /evidence="ECO:0007829|PDB:6QK7"
FT TURN 866..868
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 872..875
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 877..884
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 887..889
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 892..898
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 904..906
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 907..915
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 923..930
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 934..943
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 948..950
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 952..959
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 963..974
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 977..984
FT /evidence="ECO:0007829|PDB:5CQS"
FT STRAND 990..992
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 995..1004
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1007..1013
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1014..1016
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1018..1032
FT /evidence="ECO:0007829|PDB:5CQS"
FT TURN 1033..1036
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1038..1047
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1051..1060
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1064..1073
FT /evidence="ECO:0007829|PDB:5CQS"
FT TURN 1076..1078
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1079..1092
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1096..1107
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1110..1119
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1123..1132
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1138..1141
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1143..1170
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1253..1282
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1286..1308
FT /evidence="ECO:0007829|PDB:5CQS"
FT HELIX 1345..1347
FT /evidence="ECO:0007829|PDB:5CQS"
SQ SEQUENCE 1349 AA; 152990 MW; 7AEB1C0BA99282F6 CRC64;
MVEHDKSGSK RQELRSNMRN LITLNKGKFK PTASTAEGDE DDLSFTLLDS VFDTLSDSIT
CVLGSTDIGA IEVQQFMKDG SRNVLASFNI QTFDDKLLSF VHFADINQLV FVFEQGDIIT
ATYDPVSLDP AETLIEIMGT IDNGIAAAQW SYDEETLAMV TKDRNVVVLS KLFEPISEYH
LEVDDLKISK HVTVGWGKKE TQFRGKGARA MEREALASLK ASGLVGNQLR DPTMPYMVDT
GDVTALDSHE ITISWRGDCD YFAVSSVEEV PDEDDETKSI KRRAFRVFSR EGQLDSASEP
VTGMEHQLSW KPQGSLIASI QRKTDLGEED SVDVIFFERN GLRHGEFDTR LPLDEKVESV
CWNSNSEALA VVLANRIQLW TSKNYHWYLK QELYASDISY VKWHPEKDFT LMFSDAGFIN
IVDFAYKMAQ GPTLEPFDNG TSLVVDGRTV NITPLALANV PPPMYYRDFE TPGNVLDVAC
SFSNEIYAAI NKDVLIFAAV PSIEEMKKGK HPSIVCEFPK SEFTSEVDSL RQVAFINDSI
VGVLLDTDNL SRIALLDIQD ITQPTLITIV EVYDKIVLLR SDFDYNHLVY ETRDGTVCQL
DAEGQLMEIT KFPQLVRDFR VKRVHNTSAE DDDNWSAESS ELVAFGITNN GKLFANQVLL
ASAVTSLEIT DSFLLFTTAQ HNLQFVHLNS TDFKPLPLVE EGVEDERVRA IERGSILVSV
IPSKSSVVLQ ATRGNLETIY PRIMVLAEVR KNIMAKRYKE AFIVCRTHRI NLDILHDYAP
ELFIENLEVF INQIGRVDYL NLFISCLSED DVTKTKYKET LYSGISKSFG MEPAPLTEMQ
IYMKKKMFDP KTSKVNKICD AVLNVLLSNP EYKKKYLQTI ITAYASQNPQ NLSAALKLIS
ELENSEEKDS CVTYLCFLQD VNVVYKSALS LYDVSLALLV AQKSQMDPRE YLPFLQELQD
NEPLRRKFLI DDYLGNYEKA LEHLSEIDKD GNVSEEVIDY VESHDLYKHG LALYRYDSEK
QNVIYNIYAK HLSSNQMYTD AAVAYEMLGK LKEAMGAYQS AKRWREAMSI AVQKFPEEVE
SVAEELISSL TFEHRYVDAA DIQLEYLDNV KEAVALYCKA YRYDIASLVA IKAKKDELLE
EVVDPGLGEG FGIIAELLAD CKGQINSQLR RLRELRAKKE ENPYAFYGQE TEQADDVSVA
PSETSTQESF FTRYTGKTGG TAKTGASRRT AKNKRREERK RARGKKGTIY EEEYLVQSVG
RLIERLNQTK PDAVRVVEGL CRRNMREQAH QIQKNFVEVL DLLKANVKEI YSISEKDRER
VNENGEVYYI PEIPVPEIHD FPKSHIVDF
