DPH3_YEAST
ID DPH3_YEAST Reviewed; 82 AA.
AC Q3E840; D6VPT1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Diphthamide biosynthesis protein 3;
DE AltName: Full=Kluyveromyces lactis toxin-insensitive protein 11 {ECO:0000303|PubMed:12940988};
GN Name=KTI11 {ECO:0000303|PubMed:12940988, ECO:0000312|SGD:S000007587};
GN Synonyms=DPH3; OrderedLocusNames=YBL071W-A;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 INTERACTION WITH DPH1; DPH2; ELP1; ELP2; ELP3; ELONGATION FACTOR 2; RPS7
RP AND RPS19.
RX PubMed=12940988; DOI=10.1046/j.1365-2958.2003.03632.x;
RA Fichtner L., Jablonowski D., Schierhorn A., Kitamoto H.K., Stark M.J.R.,
RA Schaffrath R.;
RT "Elongator's toxin-target (TOT) function is nuclear localization sequence
RT dependent and suppressed by post-translational modification.";
RL Mol. Microbiol. 49:1297-1307(2003).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=15485916; DOI=10.1128/mcb.24.21.9487-9497.2004;
RA Liu S., Milne G.T., Kuremsky J.G., Fink G.R., Leppla S.H.;
RT "Identification of the proteins required for biosynthesis of diphthamide,
RT the target of bacterial ADP-ribosylating toxins on translation elongation
RT factor 2.";
RL Mol. Cell. Biol. 24:9487-9497(2004).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE
RP SYNTHASE COMPLEX, INTERACTION WITH DPH1; DPH2; ELP2; ELP5 AND ATS1,
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-56 AND
RP 66-TYR--ALA-82.
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 [8]
RP INTERACTION WITH THE ELONGATOR COMPLEX.
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 [9]
RP INTERACTION WITH DPH1.
RX PubMed=23645155; DOI=10.3390/toxins5050958;
RA Abdel-Fattah W., Scheidt V., Uthman S., Stark M.J., Schaffrath R.;
RT "Insights into diphthamide, key diphtheria toxin effector.";
RL Toxins 5:958-968(2013).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN DPH-TYPE MB.
RX PubMed=24422557; DOI=10.1021/ja4118957;
RA Dong M., Su X., Dzikovski B., Dando E.E., Zhu X., Du J., Freed J.H.,
RA Lin H.;
RT "Dph3 is an electron donor for Dph1-Dph2 in the first step of eukaryotic
RT diphthamide biosynthesis.";
RL J. Am. Chem. Soc. 136:1754-1757(2014).
RN [11]
RP FUNCTION, INTERACTION WITH ELP1; ELP2; ELP3; DPH1; DPH2; ATS1 AND CBR1, AND
RP DISRUPTION 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 [12]
RP FUNCTION.
RX PubMed=31463593; DOI=10.1007/s00775-019-01702-0;
RA Dong M., Dando E.E., Kotliar I., Su X., Dzikovski B., Freed J.H., Lin H.;
RT "The asymmetric function of Dph1-Dph2 heterodimer in diphthamide
RT biosynthesis.";
RL J. Biol. Inorg. Chem. 24:777-782(2019).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=34154323; DOI=10.1021/jacs.1c03956;
RA Zhang Y., Su D., Dzikovski B., Majer S.H., Coleman R., Chandrasekaran S.,
RA Fenwick M.K., Crane B.R., Lancaster K.M., Freed J.H., Lin H.;
RT "Dph3 Enables Aerobic Diphthamide Biosynthesis by Donating One Iron Atom to
RT Transform a [3Fe-4S] to a [4Fe-4S] Cluster in Dph1-Dph2.";
RL J. Am. Chem. Soc. 143:9314-9319(2021).
RN [14] {ECO:0007744|PDB:1YOP}
RP STRUCTURE BY NMR, AND ZINC-BINDING.
RX PubMed=15952786; DOI=10.1021/bi0504714;
RA Sun J., Zhang J., Wu F., Xu C., Li S., Zhao W., Wu Z., Wu J., Zhou C.-Z.,
RA Shi Y.;
RT "Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel
RT zinc-binding module.";
RL Biochemistry 44:8801-8809(2005).
RN [15] {ECO:0007744|PDB:4X33}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-57 IN COMPLEX WITH IRON AND
RP ATS1, AND INTERACTION WITH ATS1.
RX PubMed=25604895; DOI=10.1111/febs.13199;
RA Kolaj-Robin O., McEwen A.G., Cavarelli J., Seraphin B.;
RT "Structure of the Elongator cofactor complex Kti11/Kti13 provides insight
RT into the role of Kti13 in Elongator-dependent tRNA modification.";
RL FEBS J. 282:819-833(2015).
RN [16] {ECO:0007744|PDB:4D4O, ECO:0007744|PDB:4D4P}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH IRON AND ATS1,
RP FUNCTION, INTERACTION WITH ATS1, AND MUTAGENESIS OF TYR-4; ASP-5 AND GLU-8.
RX PubMed=25543256; DOI=10.1016/j.str.2014.11.008;
RA Glatt S., Zabel R., Vonkova I., Kumar A., Netz D.J., Pierik A.J., Rybin V.,
RA Lill R., Gavin A.C., Balbach J., Breunig K.D., Muller C.W.;
RT "Structure of the Kti11/Kti13 heterodimer and its double role in
RT modifications of tRNA and eukaryotic elongation factor 2.";
RL Structure 23:149-160(2015).
RN [17] {ECO:0007744|PDB:5AX2}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-78.
RX PubMed=30608169; DOI=10.1021/acs.jpcb.8b11019;
RA Klamt A., Nagarathinam K., Tanabe M., Kumar A., Balbach J.;
RT "Hyperbolic Pressure-Temperature Phase Diagram of the Zinc-Finger Protein
RT apoKti11 Detected by NMR Spectroscopy.";
RL J. Phys. Chem. B 123:792-801(2019).
CC -!- FUNCTION: Required for the first step of diphthamide biosynthesis, a
CC post-translational modification of histidine which occurs in elongation
CC factor 2 (PubMed:15485916, PubMed:18627462, PubMed:24422557,
CC PubMed:27694803, PubMed:31463593, PubMed:34154323, PubMed:25543256).
CC DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-
CC adenosyl-L-methionine (SAM) to a histidine residue, the reaction is
CC assisted by a reduction system comprising KTI11/DPH3 and a NADH-
CC dependent reductase, predominantly CBR1 (PubMed:24422557,
CC PubMed:27694803, PubMed:31463593, PubMed:34154323). Acts as an electron
CC donor to reduce the Fe-S cluster in DPH1-DPH2 keeping the [4Fe-4S]
CC clusters in the active and reduced state (PubMed:34154323). Restores
CC iron to DPH1-DPH2 iron-sulfur clusters which have degraded from [4Fe-
CC 4S] to [3Fe-4S] by donating an iron atom to reform [4Fe-4S] clusters,
CC in a manner dependent on the presence of elongation factor 2 and SAM
CC (PubMed:34154323). Together with ATS1; associates with the elongator
CC complex and is required for tRNA Wobble base modifications mediated by
CC the elongator complex (PubMed:25543256, PubMed:27694803,
CC PubMed:18627462). The elongator complex is required for multiple tRNA
CC modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s
CC 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-
CC carbamoylmethyl uridine) (PubMed:25543256).
CC {ECO:0000269|PubMed:15485916, ECO:0000269|PubMed:18627462,
CC ECO:0000269|PubMed:24422557, ECO:0000269|PubMed:25543256,
CC ECO:0000269|PubMed:27694803, ECO:0000269|PubMed:31463593,
CC ECO:0000269|PubMed:34154323}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[3Fe-4S](1+)-[protein] + Fe(2+)-[Dph3] = [3Fe-4S](0)-[protein]
CC + Fe(3+)-[Dph3]; Xref=Rhea:RHEA:71235, Rhea:RHEA-COMP:17996,
CC Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:18002, Rhea:RHEA-COMP:18003,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33751,
CC ChEBI:CHEBI:47402, ChEBI:CHEBI:83228;
CC Evidence={ECO:0000269|PubMed:24422557};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [3Fe-4S](0)-[protein] + 2 Fe(2+)-[Dph3] + NADH = 2 [4Fe-
CC 4S](1+)-[protein] + 2 [Dph3] + H(+) + NAD(+); Xref=Rhea:RHEA:71239,
CC Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:17998, Rhea:RHEA-COMP:18001,
CC Rhea:RHEA-COMP:18002, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:33723, ChEBI:CHEBI:47402, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC Evidence={ECO:0000269|PubMed:34154323};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000269|PubMed:15485916}.
CC -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase
CC complex composed of DPH1, DPH2, KTI11/DPH3 and a NADH-dependent
CC reductase, predominantly CBR1 (PubMed:12940988, PubMed:27694803,
CC PubMed:18627462, PubMed:23645155). Interacts with DPH1
CC (PubMed:12940988, PubMed:27694803, PubMed:18627462, PubMed:23645155).
CC Interacts with DPH2 (PubMed:12940988, PubMed:27694803,
CC PubMed:18627462). Interacts with CBR1 (PubMed:27694803). Interacts with
CC elongation factor 2 (PubMed:12940988). Interacts with ATS1/KTI13; the
CC interaction is direct (PubMed:25604895, PubMed:25543256,
CC PubMed:18627462). Interacts with the 40S ribosomal protein RPS7A
CC (PubMed:12940988). Interacts with the 40S ribosomal protein RPS19A
CC (PubMed:12940988). Interacts with the elongator complex subunit
CC IKI3/ELP1 (PubMed:12940988, PubMed:18986986, PubMed:27694803).
CC Interacts with the elongator complex subunit ELP2 (PubMed:12940988,
CC PubMed:18986986, PubMed:27694803, PubMed:18627462). Interacts with the
CC elongator complex subunit ELP3 (PubMed:12940988, PubMed:18986986,
CC PubMed:27694803). Interacts with the elongator complex subunit ELP5
CC (PubMed:18627462). {ECO:0000269|PubMed:12940988,
CC ECO:0000269|PubMed:18627462, ECO:0000269|PubMed:18986986,
CC ECO:0000269|PubMed:23645155, ECO:0000269|PubMed:25543256,
CC ECO:0000269|PubMed:25604895, ECO:0000269|PubMed:27694803}.
CC -!- INTERACTION:
CC Q3E840; P31386: ATS1; NbExp=9; IntAct=EBI-2055307, EBI-2046012;
CC Q3E840; Q02908: ELP3; NbExp=2; IntAct=EBI-2055307, EBI-33957;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:18627462}. Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:18627462}.
CC -!- DOMAIN: The DPH-type metal-binding (MB) domain can also bind zinc.
CC However, iron is the physiological binding partner as zinc binding
CC impairs the protein electron donor function.
CC {ECO:0000269|PubMed:24422557}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to caffeine, paromycin, and thermal
CC stress (PubMed:18627462). Resistance to diphtheria toxin, sordarin and
CC zymocin (PubMed:27694803, PubMed:18627462).
CC {ECO:0000269|PubMed:18627462, ECO:0000269|PubMed:27694803}.
CC -!- MISCELLANEOUS: Present with 8400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DPH3 family. {ECO:0000305}.
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DR EMBL; Z35832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006936; DAA07051.1; -; Genomic_DNA.
DR RefSeq; NP_660100.1; NM_001184454.1.
DR PDB; 1YOP; NMR; -; A=1-82.
DR PDB; 1YWS; NMR; -; A=1-82.
DR PDB; 4D4O; X-ray; 2.90 A; A/B/C=1-82.
DR PDB; 4D4P; X-ray; 3.00 A; A/B/C/E/G/H=1-82.
DR PDB; 4X33; X-ray; 1.45 A; A=1-57.
DR PDB; 5AX2; X-ray; 2.40 A; A=2-78.
DR PDBsum; 1YOP; -.
DR PDBsum; 1YWS; -.
DR PDBsum; 4D4O; -.
DR PDBsum; 4D4P; -.
DR PDBsum; 4X33; -.
DR PDBsum; 5AX2; -.
DR AlphaFoldDB; Q3E840; -.
DR SMR; Q3E840; -.
DR BioGRID; 32630; 143.
DR DIP; DIP-52225N; -.
DR IntAct; Q3E840; 5.
DR MINT; Q3E840; -.
DR STRING; 4932.YBL071W-A; -.
DR MaxQB; Q3E840; -.
DR PaxDb; Q3E840; -.
DR PRIDE; Q3E840; -.
DR EnsemblFungi; YBL071W-A_mRNA; YBL071W-A; YBL071W-A.
DR GeneID; 852207; -.
DR KEGG; sce:YBL071W-A; -.
DR SGD; S000007587; KTI11.
DR VEuPathDB; FungiDB:YBL071W-A; -.
DR eggNOG; KOG2923; Eukaryota.
DR HOGENOM; CLU_155991_4_1_1; -.
DR InParanoid; Q3E840; -.
DR OMA; LFTYPCP; -.
DR BioCyc; MetaCyc:MON-15580; -.
DR BioCyc; YEAST:MON-15580; -.
DR Reactome; R-SCE-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR EvolutionaryTrace; Q3E840; -.
DR PRO; PR:Q3E840; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; Q3E840; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR GO; GO:0034986; F:iron chaperone activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:SGD.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IDA:UniProtKB.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IMP:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.
DR DisProt; DP01653; -.
DR Gene3D; 3.10.660.10; -; 1.
DR InterPro; IPR044248; DPH3/4-like.
DR InterPro; IPR007872; DPH_MB_dom.
DR InterPro; IPR036671; DPH_MB_sf.
DR PANTHER; PTHR21454; PTHR21454; 1.
DR Pfam; PF05207; zf-CSL; 1.
DR SUPFAM; SSF144217; SSF144217; 1.
DR PROSITE; PS51074; DPH_MB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome; tRNA processing.
FT CHAIN 1..82
FT /note="Diphthamide biosynthesis protein 3"
FT /id="PRO_0000082639"
FT DOMAIN 3..59
FT /note="DPH-type MB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT REGION 66..82
FT /note="Required for interaction with the elongator complex"
FT /evidence="ECO:0000269|PubMed:18627462"
FT BINDING 25
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25543256,
FT ECO:0000269|PubMed:25604895, ECO:0007744|PDB:4D4O,
FT ECO:0007744|PDB:4D4P, ECO:0007744|PDB:4X33"
FT BINDING 27
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25543256,
FT ECO:0000269|PubMed:25604895, ECO:0007744|PDB:4D4O,
FT ECO:0007744|PDB:4D4P, ECO:0007744|PDB:4X33"
FT BINDING 47
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25543256,
FT ECO:0000269|PubMed:25604895, ECO:0007744|PDB:4D4O,
FT ECO:0007744|PDB:4D4P, ECO:0007744|PDB:4X33"
FT BINDING 50
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25543256,
FT ECO:0000269|PubMed:25604895, ECO:0007744|PDB:4D4O,
FT ECO:0007744|PDB:4D4P, ECO:0007744|PDB:4X33"
FT MUTAGEN 4
FT /note="Y->A: Impaired interaction with ATS1/KTI13."
FT /evidence="ECO:0000269|PubMed:25543256"
FT MUTAGEN 5
FT /note="D->A: Impaired interaction with ATS1/KTI13."
FT /evidence="ECO:0000269|PubMed:25543256"
FT MUTAGEN 8
FT /note="E->A: Little or no effect on interaction with
FT ATS1/KTI13."
FT /evidence="ECO:0000269|PubMed:25543256"
FT MUTAGEN 56
FT /note="V->G: Resistance to zymocin. Sensitive to thermal
FT stress, diphtheria toxin, and caffeine."
FT /evidence="ECO:0000269|PubMed:18627462"
FT MUTAGEN 66..82
FT /note="Missing: Decreases interaction with elongator
FT complex subunits ELP2 and ELP5. Resistance to zymocin.
FT Sensitive to thermal stress and caffeine. Normal
FT sensitivity to diphtheria toxin and interaction with
FT ATS1/KTI13."
FT /evidence="ECO:0000269|PubMed:18627462"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:4X33"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:4X33"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:4X33"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4D4O"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4X33"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:5AX2"
SQ SEQUENCE 82 AA; 9356 MW; 8B27A307831B0ECE CRC64;
MSTYDEIEIE DMTFEPENQM FTYPCPCGDR FQIYLDDMFE GEKVAVCPSC SLMIDVVFDK
EDLAEYYEEA GIHPPEPIAA AA
