ELP4_YEAST
ID ELP4_YEAST Reviewed; 456 AA.
AC Q02884; D6W3R5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Elongator complex protein 4 {ECO:0000303|PubMed:11435442};
DE AltName: Full=Gamma-toxin target 7 {ECO:0000303|PubMed:11296232};
DE AltName: Full=HAT-associated protein 1;
GN Name=ELP4 {ECO:0000303|PubMed:11435442};
GN Synonyms=HAP1, TOT7 {ECO:0000303|PubMed:11296232};
GN OrderedLocusNames=YPL101W;
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=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 [6]
RP IDENTIFICATION IN THE ELONGATOR COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11390369; DOI=10.1074/jbc.c100274200;
RA Li Y., Takagi Y., Jiang Y., Tokunaga M., Erdjument-Bromage H., Tempst P.,
RA Kornberg R.D.;
RT "A multiprotein complex that interacts with RNA polymerase II elongator.";
RL J. Biol. Chem. 276:29628-29631(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 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 [11]
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 [12]
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 [13]
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [16]
RP FUNCTION.
RX PubMed=18755837; DOI=10.1261/rna.1184108;
RA Huang B., Lu J., Bystroem A.S.;
RT "A genome-wide screen identifies genes required for formation of the wobble
RT nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces
RT cerevisiae.";
RL RNA 14:2183-2194(2008).
RN [17]
RP PHOSPHORYLATION AT SER-222.
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 [18]
RP METHYLATION AT ARG-13.
RX PubMed=26046779; DOI=10.1002/pmic.201500032;
RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA Pears C., Schofield C.J., Kessler B.M.;
RT "Expanding the yeast protein arginine methylome.";
RL Proteomics 15:3232-3243(2015).
RN [19]
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 [20]
RP SUBUNIT.
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).
RN [21] {ECO:0007744|PDB:4EJS}
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 67-438.
RX PubMed=22556426; DOI=10.1074/jbc.m112.341560;
RA Lin Z., Zhao W., Diao W., Xie X., Wang Z., Zhang J., Shen Y., Long J.;
RT "Crystal structure of elongator subcomplex Elp4-6.";
RL J. Biol. Chem. 287:21501-21508(2012).
RN [22] {ECO:0007744|PDB:4A8J}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 66-426, AND 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 [23]
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 [24]
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).
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). The elongator complex catalyzes formation of
CC carboxymethyluridine in the wobble base at position 34 in tRNAs
CC (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 {ECO:0000269|PubMed:11296232, ECO:0000269|PubMed:13680368,
CC ECO:0000269|PubMed:15769872, ECO:0000269|PubMed:18755837,
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:11390369, PubMed:11689709, PubMed:27974378, PubMed:27872205).
CC The elongator complex is composed of two copies of the Elp123
CC subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two copies of the
CC 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). In each lobe, ELP2 is tightly
CC sandwiched between ELP1/IKI3 and ELP3 (PubMed:31309145). The Elp123
CC subcomplex binds tRNA through ELP1/IKI3 and ELP3 and can bind 2 tRNAs
CC simultaneously (PubMed:31309145). tRNA-binding by the Elp123 subcomplex
CC induces conformational rearrangements which precisely position the
CC targeted anticodon base in the active site (PubMed:31309145). The
CC Elp456 subcomplex binds tRNA and has ATPase activity (PubMed:22556426,
CC PubMed:22343726). ELP4 interacts with KTI12 (PubMed:15772087).
CC {ECO:0000269|PubMed:11390369, ECO:0000269|PubMed:11435442,
CC ECO:0000269|PubMed:11689709, ECO:0000269|PubMed:15772087,
CC ECO:0000269|PubMed:22343726, ECO:0000269|PubMed:22556426,
CC ECO:0000269|PubMed:27872205, ECO:0000269|PubMed:27974378,
CC ECO:0000269|PubMed:31309145}.
CC -!- INTERACTION:
CC Q02884; P42935: ELP2; NbExp=6; IntAct=EBI-35277, EBI-23459;
CC Q02884; Q02884: ELP4; NbExp=2; IntAct=EBI-35277, EBI-35277;
CC Q02884; Q04868: ELP6; NbExp=14; IntAct=EBI-35277, EBI-27653;
CC Q02884; P38874: IKI1; NbExp=13; IntAct=EBI-35277, EBI-9061;
CC Q02884; Q06706: IKI3; NbExp=12; IntAct=EBI-35277, EBI-9068;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ELP4 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}.
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; AAB68198.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11331.1; -; Genomic_DNA.
DR PIR; S61965; S61965.
DR RefSeq; NP_015224.1; NM_001183915.1.
DR PDB; 4A8J; X-ray; 2.10 A; A/D=66-426.
DR PDB; 4EJS; X-ray; 2.61 A; A=67-438.
DR PDBsum; 4A8J; -.
DR PDBsum; 4EJS; -.
DR AlphaFoldDB; Q02884; -.
DR SMR; Q02884; -.
DR BioGRID; 36079; 431.
DR ComplexPortal; CPX-779; Elongator holoenzyme complex.
DR DIP; DIP-6718N; -.
DR IntAct; Q02884; 7.
DR MINT; Q02884; -.
DR STRING; 4932.YPL101W; -.
DR iPTMnet; Q02884; -.
DR MaxQB; Q02884; -.
DR PaxDb; Q02884; -.
DR PRIDE; Q02884; -.
DR DNASU; 856002; -.
DR EnsemblFungi; YPL101W_mRNA; YPL101W; YPL101W.
DR GeneID; 856002; -.
DR KEGG; sce:YPL101W; -.
DR SGD; S000006022; ELP4.
DR VEuPathDB; FungiDB:YPL101W; -.
DR eggNOG; KOG3949; Eukaryota.
DR GeneTree; ENSGT00390000001443; -.
DR HOGENOM; CLU_040685_0_0_1; -.
DR InParanoid; Q02884; -.
DR OMA; CHTFDLT; -.
DR BioCyc; YEAST:G3O-34004-MON; -.
DR UniPathway; UPA00988; -.
DR ChiTaRS; HAP1; yeast.
DR PRO; PR:Q02884; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02884; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; 3.40.50.300; -; 1.
DR InterPro; IPR008728; Elongator_complex_protein_4.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12896; PTHR12896; 1.
DR Pfam; PF05625; PAXNEB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; tRNA processing.
FT CHAIN 1..456
FT /note="Elongator complex protein 4"
FT /id="PRO_0000235812"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25569479,
FT ECO:0007744|PubMed:17330950"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4A8J"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4A8J"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:4A8J"
FT HELIX 119..135
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:4A8J"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4EJS"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:4EJS"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4EJS"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:4A8J"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:4A8J"
FT TURN 289..292
FT /evidence="ECO:0007829|PDB:4A8J"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:4A8J"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:4A8J"
FT HELIX 304..320
FT /evidence="ECO:0007829|PDB:4A8J"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:4A8J"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4EJS"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:4A8J"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:4A8J"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:4A8J"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:4A8J"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 398..406
FT /evidence="ECO:0007829|PDB:4A8J"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:4A8J"
SQ SEQUENCE 456 AA; 51156 MW; 276F0D1538EAA8FA CRC64;
MSFRKRGEIL NDRGSGLRGP LLRGPPRTSS TPLRTGNRRA PGNVPLSDTT ARLKKLNIAD
ESKTKMGLDS SHVGVRPSPA TSQPTTSTGS ADLDSILGHM GLPLGNSVLV EEQSTTEFHS
ILGKLFAAQG IVHNRISDSS ADKTRNGDTH VIVLSLNQMF AKELPGIYKG SRKQMKKNLI
SEEESKVTVQ NLNETQRSTP SRYKDLKIAW KYKLADEKRL GSPDRDDIQQ NSEYKDYNHQ
FDITTRLMPA PIASELTFIA PTQPVSTILS QIEQTIKRND KKLIRIVIPS LLHPAMYPPK
MFESSEIIGL MHGVRSLVKK YYERVVLFAS ISIDIITPPL LVLLRNMFDS VINLEPFNQE
MTEFLERVYK SQPGKIQHGL VHILKLPVFT DRGEMRVLKS EWAFKNGRKK FEIEQWGIPV
DDAEGSAASE QSHSHSHSDE ISHNIPAKKT KISLDY
