ID ELP3_YEAST Reviewed; 557 AA. AC Q02908; D6W3T1; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 182. DE RecName: Full=Elongator complex protein 3 {ECO:0000305}; DE EC=2.3.1.- {ECO:0000250|UniProtKB:D5VRB9}; DE AltName: Full=Gamma-toxin target 3; DE AltName: Full=tRNA uridine(34) acetyltransferase {ECO:0000305}; GN Name=ELP3 {ECO:0000303|PubMed:15138274, ECO:0000312|SGD:S000006007}; GN Synonyms=HPA1, TOT3; OrderedLocusNames=YPL086C; 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=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 [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP SUBCELLULAR LOCATION. 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 [4] 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 [5] RP IDENTIFICATION IN THE ELONGATOR COMPLEX. RX PubMed=10445034; DOI=10.1016/s1097-2765(00)80194-x; RA Wittschieben B.O., Otero G., de Bizemont T., Fellows J., RA Erdjument-Bromage H., Ohba R., Li Y., Allis C.D., Tempst P., RA Svejstrup J.Q.; RT "A novel histone acetyltransferase is an integral subunit of elongating RNA RT polymerase II holoenzyme."; RL Mol. Cell 4:123-128(1999). 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 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 [9] 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 [10] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-453, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC STRAIN=SUB592; RX PubMed=12872131; DOI=10.1038/nbt849; RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., RA Roelofs J., Finley D., Gygi S.P.; RT "A proteomics approach to understanding protein ubiquitination."; RL Nat. Biotechnol. 21:921-926(2003). RN [11] 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 [12] 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 [13] RP DISPUTED FUNCTION IN HISTONE ACETYLATION. RX PubMed=15138274; DOI=10.1074/jbc.m403361200; RA Petrakis T.G., Wittschieben B.O., Svejstrup J.Q.; RT "Molecular architecture, structure-function relationship, and importance of RT the Elp3 subunit for the RNA binding of holo-elongator."; RL J. Biol. Chem. 279:32087-32092(2004). RN [14] RP INTERACTION WITH KTI12. RX PubMed=15772087; DOI=10.1074/jbc.m413373200; RA Petrakis T.G., Soegaard T.M.M., Erdjument-Bromage H., Tempst P., RA Svejstrup J.Q.; RT "Physical and functional interaction between Elongator and the chromatin- RT associated Kti12 protein."; RL J. Biol. Chem. 280:19454-19460(2005). RN [15] 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 [16] 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 [17] RP FUNCTION, AND PATHWAY. RX PubMed=17018299; DOI=10.1016/j.molcel.2006.07.031; RA Esberg A., Huang B., Johansson M.J., Bystroem A.S.; RT "Elevated levels of two tRNA species bypass the requirement for elongator RT complex in transcription and exocytosis."; RL Mol. Cell 24:139-148(2006). RN [18] RP COFACTOR, S-ADENOSYLMETHIONINE-BINDING, PRESENCE OF IRON-SULFUR (4FE-4S) RP CLUSTER, AND MUTAGENESIS OF CYS-108; CYS-118 AND CYS-121. RX PubMed=16420352; DOI=10.1111/j.1365-2958.2005.04989.x; RA Paraskevopoulou C., Fairhurst S.A., Lowe D.J., Brick P., Onesti S.; RT "The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S- RT adenosylmethionine."; RL Mol. Microbiol. 59:795-806(2006). RN [19] RP DISRUPTION PHENOTYPE. RX PubMed=18627462; DOI=10.1111/j.1365-2958.2008.06350.x; RA Baer C., Zabel R., Liu S., Stark M.J., Schaffrath R.; RT "A versatile partner of eukaryotic protein complexes that is involved in RT multiple biological processes: Kti11/Dph3."; RL Mol. Microbiol. 69:1221-1233(2008). RN [20] 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 [21] RP COFACTOR, IDENTIFICATION IN THE ELONGATOR COMPLEX, INTERACTION WITH KTI11 RP AND KTI12, AND MUTAGENESIS OF CYS-103; CYS-108; CYS-118; CYS-121 AND RP TYR-540. RX PubMed=18986986; DOI=10.1074/jbc.m805312200; RA Greenwood C., Selth L.A., Dirac-Svejstrup A.B., Svejstrup J.Q.; RT "An iron-sulfur cluster domain in Elp3 important for the structural RT integrity of elongator."; RL J. Biol. Chem. 284:141-149(2009). RN [22] RP FUNCTION, PATHWAY, AND MUTAGENESIS OF CYS-103 AND GLY-168. RX PubMed=21912530; DOI=10.1371/journal.pgen.1002258; RA Chen C., Huang B., Eliasson M., Ryden P., Bystroem A.S.; RT "Elongator complex influences telomeric gene silencing and DNA damage RT response by its role in wobble uridine tRNA modification."; RL PLoS Genet. 7:E1002258-E1002258(2011). RN [23] 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 [24] 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 [25] RP INTERACTION WITH KTI11, IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION RP PHENOTYPE. 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 [26] RP FUNCTION, AND MUTAGENESIS OF LYS-53; LYS-56; LYS-57; LYS-59; LYS-61; RP ARG-65; LYS-78; LYS-79; 86-LYS--LYS-88; ARG-91; HIS-110; 118-CYS--CYS-121; RP 119-VAL-TYR-120; TYR-136; ARG-232; ARG-251; ARG-269; HIS-271; LYS-289; RP LYS-325; TRP-341; ARG-373; ARG-376 AND ARG-411. RX PubMed=27455459; DOI=10.1038/nsmb.3265; RA Glatt S., Zabel R., Kolaj-Robin O., Onuma O.F., Baudin F., Graziadei A., RA Taverniti V., Lin T.Y., Baymann F., Seraphin B., Breunig K.D., RA Mueller C.W.; RT "Structural basis for tRNA modification by Elp3 from Dehalococcoides RT mccartyi."; RL Nat. Struct. Mol. Biol. 23:794-802(2016). RN [27] 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 [28] 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 [29] {ECO:0007744|PDB:6QK7} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF THE ELONGATOR ELP123 RP SUBCOMPLEX, FUNCTION, COFACTOR, AND MUTAGENESIS OF CYS-118; CYS-121; RP TYR-327; ARG-376 AND TYR-540. 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: Catalytic tRNA acetyltransferase subunit of the elongator CC complex which is required for multiple tRNA modifications, including CC mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5- CC methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl CC uridine) (PubMed:15769872, PubMed:17018299, PubMed:18755837, CC PubMed:21912530, PubMed:31309145). In the elongator complex, acts as a CC tRNA uridine(34) acetyltransferase, which mediates formation of CC carboxymethyluridine in the wobble base at position 34 in tRNAs (By CC similarity). The complex functions as a gamma-toxin target (TOT); CC disruption of the complex confers resistance to Kluyveromyces lactis CC toxin zymocin (pGKL1 killer toxin) (PubMed:11296232). May also be CC involved in sensitivity to Pichia inositovora toxin (PubMed:13680368). CC Independently, ELP3 may be involved in polarized exocytosis CC (PubMed:15780940). {ECO:0000250|UniProtKB:D5VRB9, CC ECO:0000269|PubMed:11296232, ECO:0000269|PubMed:13680368, CC ECO:0000269|PubMed:15769872, ECO:0000269|PubMed:15780940, CC ECO:0000269|PubMed:17018299, ECO:0000269|PubMed:18755837, CC ECO:0000269|PubMed:21912530}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in CC tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA CC + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407, CC Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, CC ChEBI:CHEBI:74882; Evidence={ECO:0000250|UniProtKB:D5VRB9}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021; CC Evidence={ECO:0000250|UniProtKB:D5VRB9}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:16420352, ECO:0000269|PubMed:18986986, CC ECO:0000269|PubMed:31309145}; CC Note=Binds 1 [4Fe-4S] cluster (PubMed:16420352). The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (PubMed:16420352). The cluster is required for structural CC integrity of the elongator complex, while it is not required for CC catalytic activity (PubMed:18986986). {ECO:0000269|PubMed:16420352, CC ECO:0000269|PubMed:18986986}; CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA CC biosynthesis. {ECO:0000269|PubMed:15769872, CC ECO:0000269|PubMed:17018299, ECO:0000269|PubMed:21912530}. CC -!- SUBUNIT: Component of the elongator complex which consists of CC ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:10445034, CC PubMed:11435442, PubMed:11689709, PubMed:18986986, PubMed:27974378, CC PubMed:27872205). The elongator complex is composed of two copies of CC the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two CC copies of the Elp456 subcomplex (composed of ELP4, ELP5/IKI1 and ELP6) CC (PubMed:27974378, PubMed:27872205). The Elp123 subcomplex forms a two- CC lobed scaffold, which binds the Elp456 subcomplex asymmetrically CC (PubMed:27974378, PubMed:27872205, PubMed:25960406). In each lobe, ELP2 CC is tightly sandwiched between ELP1/IKI3 and ELP3 (PubMed:31309145). The CC Elp123 subcomplex binds tRNA through ELP1/IKI3 and ELP3 and can bind 2 CC tRNAs simultaneously (PubMed:31309145). tRNA-binding induces CC conformational rearrangements which precisely position the targeted CC anticodon base in the active site (PubMed:31309145). ELP3 interacts CC with KTI11/DPH3 (PubMed:18986986, PubMed:27694803). ELP3 interacts with CC KTI12 (PubMed:15772087). The Elp456 subcomplex binds tRNA and has CC ATPase activity (PubMed:22343726). {ECO:0000269|PubMed:10445034, CC ECO:0000269|PubMed:11435442, ECO:0000269|PubMed:11689709, CC ECO:0000269|PubMed:15772087, ECO:0000269|PubMed:18986986, CC ECO:0000269|PubMed:22343726, ECO:0000269|PubMed:27694803, CC ECO:0000269|PubMed:27872205, ECO:0000269|PubMed:27974378, CC ECO:0000269|PubMed:31309145}. CC -!- INTERACTION: CC Q02908; P42935: ELP2; NbExp=7; IntAct=EBI-33957, EBI-23459; CC Q02908; Q04868: ELP6; NbExp=4; IntAct=EBI-33957, EBI-27653; CC Q02908; P38874: IKI1; NbExp=6; IntAct=EBI-33957, EBI-9061; CC Q02908; Q3E840: KTI11; NbExp=2; IntAct=EBI-33957, EBI-2055307; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:15780940}. Nucleus {ECO:0000269|PubMed:10024884}. CC -!- DISRUPTION PHENOTYPE: Sensitive to caffeine and thermal stress CC (PubMed:18627462). Resistance to zymocin (PubMed:27694803, CC PubMed:18627462). {ECO:0000269|PubMed:18627462, CC ECO:0000269|PubMed:27694803}. CC -!- MISCELLANEOUS: Present with 4760 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the ELP3 family. {ECO:0000305}. CC -!- CAUTION: The elongator complex was originally thought to play a role in CC transcription elongation. Was reported to display histone CC acetyltransferase activity and to acetylate histone H3 preferentially CC at 'Lys-14', and H4 preferentially at 'Lys-8' (PubMed:10445034, CC PubMed:11904415, PubMed:15138274). However, it was later shown that the CC effect on histone acetylation and chromatin regulation is indirect and CC that the elongator complex is primarily involved in tRNA modification CC (PubMed:17018299, PubMed:18986986, PubMed:21912530). CC {ECO:0000269|PubMed:10445034, ECO:0000269|PubMed:11904415, CC ECO:0000269|PubMed:17018299, ECO:0000269|PubMed:18986986, CC ECO:0000269|PubMed:21912530, ECO:0000305|PubMed:10024884, CC ECO:0000305|PubMed:11689709, ECO:0000305|PubMed:15138274}. 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; U43281; AAB68213.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11347.1; -; Genomic_DNA. DR PIR; S61980; S61980. DR RefSeq; NP_015239.1; NM_001183900.1. DR PDB; 6QK7; EM; 3.30 A; C=1-557. DR PDB; 8ASV; EM; 4.35 A; C=1-557. DR PDB; 8ASW; EM; 3.96 A; C=1-557. DR PDBsum; 6QK7; -. DR PDBsum; 8ASV; -. DR PDBsum; 8ASW; -. DR AlphaFoldDB; Q02908; -. DR EMDB; EMD-4571; -. DR SMR; Q02908; -. DR BioGRID; 36095; 589. DR ComplexPortal; CPX-779; Elongator holoenzyme complex. DR DIP; DIP-2385N; -. DR IntAct; Q02908; 18. DR MINT; Q02908; -. DR STRING; 4932.YPL086C; -. DR iPTMnet; Q02908; -. DR MaxQB; Q02908; -. DR PaxDb; 4932-YPL086C; -. DR PeptideAtlas; Q02908; -. DR DNASU; 856019; -. DR EnsemblFungi; YPL086C_mRNA; YPL086C; YPL086C. DR GeneID; 856019; -. DR KEGG; sce:YPL086C; -. DR AGR; SGD:S000006007; -. DR SGD; S000006007; ELP3. DR VEuPathDB; FungiDB:YPL086C; -. DR eggNOG; KOG2535; Eukaryota. DR GeneTree; ENSGT00390000013141; -. DR HOGENOM; CLU_025983_2_1_1; -. DR InParanoid; Q02908; -. DR OMA; TFETRPD; -. DR OrthoDB; 46095at2759; -. DR BioCyc; MetaCyc:G3O-33992-MONOMER; -. DR BioCyc; YEAST:G3O-33992-MONOMER; -. DR UniPathway; UPA00988; -. DR BioGRID-ORCS; 856019; 8 hits in 10 CRISPR screens. DR PRO; PR:Q02908; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; Q02908; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. 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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0106261; F:tRNA uridine(34) acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0006417; P:regulation of translation; NAS:ComplexPortal. DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IDA:UniProtKB. DR GO; GO:0002098; P:tRNA wobble uridine modification; IDA:UniProtKB. DR CDD; cd01335; Radical_SAM; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR039661; ELP3. DR InterPro; IPR034687; ELP3-like. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR032432; Radical_SAM_C. DR InterPro; IPR007197; rSAM. DR NCBIfam; TIGR01211; ELP3; 1. DR PANTHER; PTHR11135:SF0; ELONGATOR COMPLEX PROTEIN 3; 1. DR PANTHER; PTHR11135; HISTONE ACETYLTRANSFERASE-RELATED; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF16199; Radical_SAM_C; 1. DR PIRSF; PIRSF005669; Hist_AcTrfase_ELP3; 1. DR SFLD; SFLDG01086; elongater_protein-like; 1. DR SFLD; SFLDF00344; ELP3-like; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR PROSITE; PS51186; GNAT; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Acyltransferase; Cytoplasm; Iron; Iron-sulfur; KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat; KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing; KW tRNA-binding; Ubl conjugation. FT CHAIN 1..557 FT /note="Elongator complex protein 3" FT /id="PRO_0000235811" FT DOMAIN 91..381 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT DOMAIN 405..557 FT /note="N-acetyltransferase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532" FT BINDING 108 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000269|PubMed:16420352, FT ECO:0000269|PubMed:31309145, ECO:0007744|PDB:6QK7" FT BINDING 118 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000269|PubMed:16420352, FT ECO:0000269|PubMed:31309145, ECO:0007744|PDB:6QK7" FT BINDING 121 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000269|PubMed:16420352, FT ECO:0000269|PubMed:31309145, ECO:0007744|PDB:6QK7" FT BINDING 173 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7" FT BINDING 485..488 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7" FT BINDING 508..510 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7" FT BINDING 541 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7" FT CROSSLNK 453 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:12872131" FT MUTAGEN 53 FT /note="K->A: Does not affect tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 56 FT /note="K->A: Does not affect tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 57 FT /note="K->A: Does not affect tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 59 FT /note="K->A: Does not affect tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 61 FT /note="K->A: Does not affect tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 65 FT /note="R->A: Does not affect tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 78 FT /note="K->A: Does not affect tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 79 FT /note="K->A: Does not affect tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 86..88 FT /note="KAK->AAA: Decreased tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 91 FT /note="R->A: Decreased tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 103 FT /note="C->A: Impaired tRNA wobble uridine modification." FT /evidence="ECO:0000269|PubMed:18986986, FT ECO:0000269|PubMed:21912530" FT MUTAGEN 108 FT /note="C->A: Dissociation of the elongator complex FT following assembly. Abolished interaction with KTI11 and FT KTI12." FT /evidence="ECO:0000269|PubMed:18986986" FT MUTAGEN 108 FT /note="C->S: Eliminates iron contents; when associated with FT S-118 and S-121." FT /evidence="ECO:0000269|PubMed:16420352" FT MUTAGEN 110 FT /note="H->A: Decreased tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 118..121 FT /note="CVYC->SVYS: Decreased tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 118 FT /note="C->A: Dissociation of the elongator complex FT following assembly. Loss of elongator complex activity; FT when associated with A-121." FT /evidence="ECO:0000269|PubMed:18986986, FT ECO:0000269|PubMed:31309145" FT MUTAGEN 118 FT /note="C->S: Eliminates iron contents; when associated with FT S-108 and S-121." FT /evidence="ECO:0000269|PubMed:16420352" FT MUTAGEN 119..120 FT /note="VY->AA: Decreased tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 121 FT /note="C->A: Dissociation of the elongator complex FT following assembly. Loss of elongator complex activity; FT when associated with A-118." FT /evidence="ECO:0000269|PubMed:18986986, FT ECO:0000269|PubMed:31309145" FT MUTAGEN 121 FT /note="C->S: Eliminates iron contents; when associated with FT S-108 and S-118." FT /evidence="ECO:0000269|PubMed:16420352" FT MUTAGEN 136 FT /note="Y->A: Decreased tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 168 FT /note="G->R: Impaired tRNA wobble uridine modification." FT /evidence="ECO:0000269|PubMed:21912530" FT MUTAGEN 232 FT /note="R->A: Decreased tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 251 FT /note="R->A: Abolished tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 269 FT /note="R->A: Decreased tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 271 FT /note="H->A: Decreased tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 289 FT /note="K->A: Abolished tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 325 FT /note="K->A: Abolished tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 327 FT /note="Y->A: Loss of elongator complex activity." FT /evidence="ECO:0000269|PubMed:31309145" FT MUTAGEN 341 FT /note="W->A: Decreased tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 373 FT /note="R->A: Abolished tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 376 FT /note="R->A: Abolished tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459, FT ECO:0000269|PubMed:31309145" FT MUTAGEN 411 FT /note="R->A: Abolished tRNA modification." FT /evidence="ECO:0000269|PubMed:27455459" FT MUTAGEN 540 FT /note="Y->A: Does not affect interaction with KTI11 and FT KTI12. Loss of elongator complex activity." FT /evidence="ECO:0000269|PubMed:18986986, FT ECO:0000269|PubMed:31309145" FT STRAND 97..102 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 123..129 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 141..149 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 153..163 FT /evidence="ECO:0007829|PDB:6QK7" FT TURN 164..168 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 173..181 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 188..203 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 210..216 FT /evidence="ECO:0007829|PDB:6QK7" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 221..231 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 238..247 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 251..257 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 261..266 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 273..286 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 289..294 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 305..315 FT /evidence="ECO:0007829|PDB:6QK7" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 322..326 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 338..342 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 353..361 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 362..364 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 370..375 FT /evidence="ECO:0007829|PDB:6QK7" FT TURN 380..382 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 392..399 FT /evidence="ECO:0007829|PDB:6QK7" FT TURN 400..403 FT /evidence="ECO:0007829|PDB:6QK7" FT TURN 410..412 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 430..438 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 441..450 FT /evidence="ECO:0007829|PDB:6QK7" FT TURN 451..454 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 455..464 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 473..475 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 480..488 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 508..522 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 527..531 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 538..542 FT /evidence="ECO:0007829|PDB:6QK7" FT TURN 543..545 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 547..549 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 552..556 FT /evidence="ECO:0007829|PDB:6QK7" SQ SEQUENCE 557 AA; 63657 MW; 64EF8B42D3C3102E CRC64; MARHGKGPKT NKKKLAPEKE RFIQCCADIT LELTDSLTSG TTREINLNGL ITKYSKKYKL KQQPRLTDII NSIPDQYKKY LLPKLKAKPV RTASGIAVVA VMCKPHRCPH IAYTGNICVY CPGGPDSDFE YSTQSYTGYE PTSMRAIRAR YDPYEQARGR VEQLKQLGHS IDKVEYVLMG GTFMSLPKEY REDFIVKLHN ALSGFNGNDI DEAILYSQQS LTKCVGITIE TRPDYCTQTH LDDMLKYGCT RLEIGVQSLY EDVARDTNRG HTVRSVCETF AVSKDAGYKV VSHMMPDLPN VGMERDIEQF KEYFENPDFR TDGLKIYPTL VIRGTGLYEL WKTGRYKSYS ANALVDLVAR ILALVPPWTR IYRVQRDIPM PLVTSGVDNG NLRELALARM KDLGTTCRDV RTREVGIQEV HHKVQPDQVE LIRRDYYANG GWETFLSYED PKKDILIGLL RLRKASKKYT YRKEFTSQRT SIVRELHVYG SVVPLHSRDP RKFQHQGFGT LLMEEAERIA KEEHGSEKIS VISGVGVRNY YGKLGYELDG PYMSKRI //