ELP2_YEAST
ID ELP2_YEAST Reviewed; 788 AA.
AC P42935; D6VUY2; E9P8V1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Elongator complex protein 2;
DE AltName: Full=Gamma-toxin target 2;
GN Name=ELP2; Synonyms=TOT2; OrderedLocusNames=YGR200C; ORFNames=G7725;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8904340;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<273::aid-yea898>3.0.co;2-1;
RA Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A.,
RA Rodrigues-Pousada C.;
RT "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII
RT reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the
RT yeast PMT and EF1G genes, of the human and bacterial electron-transferring
RT flavoproteins (beta-chain) and of the Escherichia coli phosphoserine
RT phosphohydrolase, and five new ORFs.";
RL Yeast 12:273-280(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP INTERACTION WITH IKI3.
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 [10]
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 [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.
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 [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 INTERACTION WITH KTI11.
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 [18]
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 [19]
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 [20]
RP PHOSPHORYLATION AT SER-492.
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 [21]
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 [22] {ECO:0007744|PDB:4XFV}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), FUNCTION, IDENTIFICATION IN THE
RP ELONGATOR ELP123 SUBCOMPLEX, DOMAIN, AND MUTAGENESIS OF 1-MET--ALA-14;
RP ARG-626; ARG-628; ARG-654 AND ARG-675.
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 [23]
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 [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 X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS), STRUCTURE BY ELECTRON MICROSCOPY,
RP AND IDENTIFICATION IN THE ELONGATOR 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, a multiprotein complex
CC which is required for multiple tRNA modifications, including mcm5U (5-
CC methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-
CC thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872,
CC PubMed:18755837, PubMed:31309145). The elongator complex catalyzes
CC formation of carboxymethyluridine in the wobble base at position 34 in
CC tRNAs (PubMed:29332244). It 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 ELP2 binds to microtubules (PubMed:25960406). Independently, ELP2 may
CC be involved in polarized exocytosis (PubMed:15138274, PubMed:15780940).
CC {ECO:0000269|PubMed:11296232, ECO:0000269|PubMed:13680368,
CC ECO:0000269|PubMed:15138274, ECO:0000269|PubMed:15769872,
CC ECO:0000269|PubMed:15780940, ECO:0000269|PubMed:18755837,
CC ECO:0000269|PubMed:25960406, ECO:0000269|PubMed:31309145,
CC 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: Component of the elongator complex which consists of
CC ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:11435442,
CC PubMed:11689709, PubMed:27974378, PubMed:27872205). The elongator
CC complex is composed of two copies of the Elp123 subcomplex (composed of
CC ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex
CC (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:27974378,
CC PubMed:27872205, PubMed:25960406). The Elp123 subcomplex forms a two-
CC lobed scaffold, which binds the Elp456 subcomplex asymmetrically
CC (PubMed:27974378, PubMed:27872205). In the complex, ELP2 interacts with
CC ELP1/IKI3 (PubMed:12139626). In each lobe, ELP2 is tightly sandwiched
CC between ELP1/IKI3 and ELP3 (PubMed:31309145). The Elp123 subcomplex
CC binds tRNA through ELP1/IKI3 and ELP3 and can bind 2 tRNAs
CC simultaneously (PubMed:31309145). tRNA-binding induces conformational
CC rearrangements which precisely position the targeted anticodon base in
CC the active site (PubMed:31309145). The Elp456 subcomplex binds tRNA and
CC has ATPase activity (PubMed:22343726). Interacts with KTI11/DPH3
CC (PubMed:27694803, PubMed:18627462). {ECO:0000269|PubMed:11435442,
CC ECO:0000269|PubMed:11689709, ECO:0000269|PubMed:12139626,
CC ECO:0000269|PubMed:22343726, ECO:0000269|PubMed:25960406,
CC ECO:0000269|PubMed:27694803, ECO:0000269|PubMed:27872205,
CC ECO:0000269|PubMed:27974378, ECO:0000269|PubMed:31309145}.
CC -!- INTERACTION:
CC P42935; Q02908: ELP3; NbExp=7; IntAct=EBI-23459, EBI-33957;
CC P42935; Q02884: ELP4; NbExp=6; IntAct=EBI-23459, EBI-35277;
CC P42935; Q04868: ELP6; NbExp=2; IntAct=EBI-23459, EBI-27653;
CC P42935; P38874: IKI1; NbExp=5; IntAct=EBI-23459, EBI-9061;
CC P42935; Q06706: IKI3; NbExp=11; IntAct=EBI-23459, EBI-9068;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DOMAIN: Folds into a two seven-bladed beta-propeller structure which is
CC required for elongator complex assembly and association with
CC microtubules. {ECO:0000269|PubMed:25960406}.
CC -!- MISCELLANEOUS: Present with 6090 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat ELP2 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:15138274, ECO:0000305|PubMed:29332244}.
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DR EMBL; Z49133; CAA88993.1; -; Genomic_DNA.
DR EMBL; Z72985; CAA97227.1; -; Genomic_DNA.
DR EMBL; AY558100; AAS56426.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08293.1; -; Genomic_DNA.
DR PIR; S53923; S53923.
DR RefSeq; NP_011716.3; NM_001181329.3.
DR PDB; 4XFV; X-ray; 3.20 A; A=1-788.
DR PDB; 5M2N; X-ray; 2.81 A; A=1-788.
DR PDB; 6QK7; EM; 3.30 A; B=1-788.
DR PDBsum; 4XFV; -.
DR PDBsum; 5M2N; -.
DR PDBsum; 6QK7; -.
DR AlphaFoldDB; P42935; -.
DR SMR; P42935; -.
DR BioGRID; 33453; 531.
DR ComplexPortal; CPX-779; Elongator holoenzyme complex.
DR DIP; DIP-2386N; -.
DR IntAct; P42935; 19.
DR MINT; P42935; -.
DR STRING; 4932.YGR200C; -.
DR iPTMnet; P42935; -.
DR MaxQB; P42935; -.
DR PaxDb; P42935; -.
DR PRIDE; P42935; -.
DR DNASU; 853114; -.
DR EnsemblFungi; YGR200C_mRNA; YGR200C; YGR200C.
DR GeneID; 853114; -.
DR KEGG; sce:YGR200C; -.
DR SGD; S000003432; ELP2.
DR VEuPathDB; FungiDB:YGR200C; -.
DR eggNOG; KOG1063; Eukaryota.
DR GeneTree; ENSGT00390000000916; -.
DR HOGENOM; CLU_006430_0_0_1; -.
DR InParanoid; P42935; -.
DR OMA; EHTKRVN; -.
DR BioCyc; YEAST:G3O-30885-MON; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:P42935; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P42935; 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:0008017; F:microtubule binding; IDA:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032447; P:protein urmylation; IMP:SGD.
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:0002098; P:tRNA wobble uridine modification; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 4.
DR InterPro; IPR037289; Elp2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44111; PTHR44111; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; tRNA processing; WD repeat.
FT CHAIN 1..788
FT /note="Elongator complex protein 2"
FT /id="PRO_0000051474"
FT REPEAT 13..51
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 57..96
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 102..139
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 200..243
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 279..318
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 336..377
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 383..422
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 437..475
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REPEAT 556..600
FT /note="WD 9"
FT /evidence="ECO:0000255"
FT REPEAT 604..643
FT /note="WD 10"
FT /evidence="ECO:0000255"
FT REPEAT 651..692
FT /note="WD 11"
FT /evidence="ECO:0000255"
FT REPEAT 699..742
FT /note="WD 12"
FT /evidence="ECO:0000255"
FT REPEAT 750..788
FT /note="WD 13"
FT /evidence="ECO:0000255"
FT REGION 490..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25569479"
FT MUTAGEN 1..14
FT /note="Missing: Abolishes interaction with ELP1/IKI3 and
FT ELP3."
FT /evidence="ECO:0000269|PubMed:25960406"
FT MUTAGEN 626
FT /note="R->A: Dramatically reduced interaction with
FT microtubules but no effect on interaction with ELP1/IKI3 or
FT ELP3; when associated with A-628, A-654 and A-675."
FT /evidence="ECO:0000269|PubMed:25960406"
FT MUTAGEN 628
FT /note="R->A: Dramatically reduced interaction with
FT microtubules but no effect on interaction with ELP1/IKI3 or
FT ELP3; when associated with A-626, A-654 and A-675."
FT /evidence="ECO:0000269|PubMed:25960406"
FT MUTAGEN 654
FT /note="R->A: Dramatically reduced interaction with
FT microtubules but no effect on interaction with ELP1/IKI3 or
FT ELP3; when associated with A-626, A-628 and A-675."
FT /evidence="ECO:0000269|PubMed:25960406"
FT MUTAGEN 675
FT /note="Missing: Dramatically reduced interaction with
FT microtubules but no effect on interaction with ELP1/IKI3 or
FT ELP3; when associated with A-626, A-628 and A-654."
FT /evidence="ECO:0000269|PubMed:25960406"
FT CONFLICT 579
FT /note="S -> P (in Ref. 4; AAS56426)"
FT /evidence="ECO:0000305"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:5M2N"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 165..185
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:4XFV"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 228..239
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 267..278
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 280..289
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:5M2N"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 364..373
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:4XFV"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:5M2N"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 429..438
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 442..457
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:5M2N"
FT HELIX 469..479
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:6QK7"
FT HELIX 539..544
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 550..555
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 572..577
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 586..591
FT /evidence="ECO:0007829|PDB:5M2N"
FT TURN 592..594
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 597..603
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 609..614
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 618..625
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:4XFV"
FT STRAND 630..636
FT /evidence="ECO:0007829|PDB:5M2N"
FT TURN 637..640
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 641..651
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 656..661
FT /evidence="ECO:0007829|PDB:5M2N"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 668..674
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 677..685
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 687..699
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 704..709
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:6QK7"
FT STRAND 717..724
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 729..735
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 738..744
FT /evidence="ECO:0007829|PDB:5M2N"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 755..760
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 768..775
FT /evidence="ECO:0007829|PDB:5M2N"
FT STRAND 780..786
FT /evidence="ECO:0007829|PDB:5M2N"
SQ SEQUENCE 788 AA; 89411 MW; 5371908FE2E6EC0D CRC64;
MVECITPEAI FIGANKQTQV SDIHKVKKIV AFGAGKTIAL WDPIEPNNKG VYATLKGHEA
EVTCVRFVPD SDFMVSASED HHVKIWKFTD YSHLQCIQTI QHYSKTIVAL SALPSLISVG
CADGTISIWR QNIQNDEFGL AHEFTIKKGF FYPLCLSLSK VEEKKYLLAI GGTNVNVFIA
SFILSDSGIE KCRVVAELEG HEDWVKSLAF RHQETPGDYL LCSGSQDRYI RLWRIRINDL
IDDSEEDSKK LTLLSNKQYK FQIDDELRVG INFEALIMGH DDWISSLQWH ESRLQLLAAT
ADTSLMVWEP DETSGIWVCS LRLGEMSSKG ASTATGSSGG FWSCLWFTHE RMDFFLTNGK
TGSWRMWATK DNIICDQRLG ISGATKDVTD IAWSPSGEYL LATSLDQTTR LFAPWIYDAS
GRKREIATWH EFSRPQIHGY DMICVETVTD TRFVSGGDEK ILRSFDLPKG VAGMLQKFVG
IQFEEKSEMP DSATVPVLGL SNKAGEDDAN EDDEEEEGGN KETPDITDPL SLLECPPMED
QLQRHLLWPE VEKLYGHGFE ITCLDISPDQ KLIASACRSN NVQNAVIRIF STENWLEIKP
ALPFHSLTIT RLKFSKDGKF LLSVCRDRKW ALWERNMEDN TFELRFKNEK PHTRIIWDAD
WAPLEFGNVF VTASRDKTVK VWRHQKEPAD DYVLEASIKH TKAVTAISIH DSMIREKILI
SVGLENGEIY LYSYTLGKFE LITQLNEDIT PADKITRLRW SHLKRNGKLF LGVGSSDLST
RIYSLAYE
