ELP3_YEAST
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 03-AUG-2022, entry version 174.
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 + carboxymethyluridine(34) in tRNA + CoA + 2
CC 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}.
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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 PDBsum; 6QK7; -.
DR AlphaFoldDB; Q02908; -.
DR SMR; Q02908; -.
DR BioGRID; 36095; 553.
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; Q02908; -.
DR PRIDE; Q02908; -.
DR DNASU; 856019; -.
DR EnsemblFungi; YPL086C_mRNA; YPL086C; YPL086C.
DR GeneID; 856019; -.
DR KEGG; sce:YPL086C; -.
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 BioCyc; YEAST:G3O-33992-MON; -.
DR UniPathway; UPA00988; -.
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:0004402; F:histone acetyltransferase activity; IDA:SGD.
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: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; IDA:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IDA:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR039661; ELP3.
DR InterPro; IPR034687; ELP3-like.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032432; Radical_SAM_C.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR11135; PTHR11135; 1.
DR PANTHER; PTHR11135:SF0; PTHR11135:SF0; 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; SFLDF00344; ELP3-like; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR01211; ELP3; 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
