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Elongation factor 3A (EF-3) (EF-3A) (Eukaryotic elongation factor 3) (eEF3) (Translation elongation factor 3A) (Yeast elongation factor 3)

 EF3A_YEAST              Reviewed;        1044 AA.
P16521; D6VYP7; O93815; Q06558;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 4.
22-NOV-2017, entry version 196.
RecName: Full=Elongation factor 3A;
Short=EF-3;
Short=EF-3A;
AltName: Full=Eukaryotic elongation factor 3;
Short=eEF3;
AltName: Full=Translation elongation factor 3A;
AltName: Full=Yeast elongation factor 3;
Name=YEF3; Synonyms=EFC1, TEF3, YEF3A; OrderedLocusNames=YLR249W;
ORFNames=L9672.5;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2404974;
Qin S., Xie A., Bonato M.C.M., McLaughlin C.S.;
"Sequence analysis of the translational elongation factor 3 from
Saccharomyces cerevisiae.";
J. Biol. Chem. 265:1903-1912(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1976386; DOI=10.1016/0167-4781(90)90172-X;
Sandbaken M.G., Lupisella J.A., DiDomenico B., Chakraburtty K.;
"Isolation and characterization of the structural gene encoding
elongation factor 3.";
Biochim. Biophys. Acta 1050:230-234(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2203789;
Sandbaken M.G., Lupisella J.A., DiDomenico B., Chakraburtty K.;
"Protein synthesis in yeast. Structural and functional analysis of the
gene encoding elongation factor 3.";
J. Biol. Chem. 265:15838-15844(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 446-955.
STRAIN=ATCC 208279 / BJ926;
PubMed=10361693; DOI=10.1271/bbb.63.769;
Uritani M., Shoumura Y., Yamada S.;
"Detection and analysis of translation elongation factor 3 genes from
various yeasts.";
Biosci. Biotechnol. Biochem. 63:769-772(1999).
[7]
PROTEIN SEQUENCE OF 959-967.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733; DOI=10.1002/elps.11501501210;
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein
database.";
Electrophoresis 15:1466-1486(1994).
[8]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=6456269;
Dasmahapatra B., Chakraburtty K.;
"Protein synthesis in yeast. I. Purification and properties of
elongation factor 3 from Saccharomyces cerevisiae.";
J. Biol. Chem. 256:9999-10004(1981).
[9]
FUNCTION.
PubMed=7657623; DOI=10.1074/jbc.270.35.20473;
Triana-Alonso F.J., Chakraburtty K., Nierhaus K.H.;
"The elongation factor 3 unique in higher fungi and essential for
protein biosynthesis is an E site factor.";
J. Biol. Chem. 270:20473-20478(1995).
[10]
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=7957240; DOI=10.1111/j.1432-1033.1994.tb20034.x;
Kovalchuke O., Chakraburtty K.;
"Comparative analysis of ribosome-associated adenosinetriphosphatase
(ATPase) from pig liver and the ATPase of elongation factor 3 from
Saccharomyces cerevisiae.";
Eur. J. Biochem. 226:133-140(1994).
[11]
ACETYLATION AT SER-2.
PubMed=9298649; DOI=10.1002/elps.1150180810;
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
Kobayashi R., Schwender B., Volpe T., Anderson D.S.,
Mesquita-Fuentes R., Payne W.E.;
"Proteome studies of Saccharomyces cerevisiae: identification and
characterization of abundant proteins.";
Electrophoresis 18:1347-1360(1997).
[12]
INTERACTION WITH EEF1A.
PubMed=9990316; DOI=10.1046/j.1432-1327.1998.2580986.x;
Kovalchuke O., Kambampati R., Pladies E., Chakraburtty K.;
"Competition and cooperation amongst yeast elongation factors.";
Eur. J. Biochem. 258:986-993(1998).
[13]
CHARACTERIZATION.
PubMed=9544245;
DOI=10.1002/(SICI)1097-0061(199802)14:3<239::AID-YEA219>3.0.CO;2-B;
Sarthy A.V., McGonigal T., Capobianco J.O., Schmidt M., Green S.R.,
Moehle C.M., Goldman R.C.;
"Identification and kinetic analysis of a functional homolog of
elongation factor 3, YEF3 in Saccharomyces cerevisiae.";
Yeast 14:239-253(1998).
[14]
INTERACTION WITH 18S RRNA.
PubMed=9553076; DOI=10.1074/jbc.273.17.10249;
Gontarek R.R., Li H., Nurse K., Prescott C.D.;
"The N-terminus of eukaryotic translation elongation factor 3
interacts with 18 S rRNA and 80 S ribosomes.";
J. Biol. Chem. 273:10249-10252(1998).
[15]
PHOSPHORYLATION.
PubMed=10523624; DOI=10.1128/MCB.19.11.7357;
Futcher B., Latter G.I., Monardo P., McLaughlin C.S., Garrels J.I.;
"A sampling of the yeast proteome.";
Mol. Cell. Biol. 19:7357-7368(1999).
[16]
MUTAGENESIS OF PHE-650, AND INTERACTION WITH EEF1A.
PubMed=12493761; DOI=10.1074/jbc.M209224200;
Anand M., Chakraburtty K., Marton M.J., Hinnebusch A.G., Kinzy T.G.;
"Functional interactions between yeast translation eukaryotic
elongation factor (eEF) 1A and eEF3.";
J. Biol. Chem. 278:6985-6991(2003).
[17]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[18]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039 AND SER-1040, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-972; SER-1039 AND
SER-1040, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; THR-972; SER-974;
SER-1039 AND SER-1040, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[22]
FUNCTION, ASSOCIATION WITH RIBOSOMES, AND DOMAIN.
PubMed=22888004; DOI=10.1074/jbc.M112.368266;
Visweswaraiah J., Lee S.J., Hinnebusch A.G., Sattlegger E.;
"Overexpression of eukaryotic translation elongation factor 3 impairs
Gcn2 protein activation.";
J. Biol. Chem. 287:37757-37768(2012).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-350 AND LYS-636, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[25]
METHYLATION AT LYS-187; LYS-196 AND LYS-789.
PubMed=22522802; DOI=10.1002/pmic.201100570;
Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
"Methylation of translation-associated proteins in Saccharomyces
cerevisiae: Identification of methylated lysines and their
methyltransferases.";
Proteomics 12:960-972(2012).
-!- FUNCTION: Required for the ATP-dependent release of deacylated
tRNA from the ribosomal E-site during protein biosynthesis.
Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the
ribosomal A-site, which has reduced affinity for tRNA as long as
the E-site is occupied. Plays a role as a negative regulator of
the GCN2 kinase activity; impairs GCN1-mediated GCN2 activation on
ribosomes by reducing GCN1-ribosome affinity, and hence GCN2-
mediated eIF-2-alpha phosphorylation in amino acid-starved or
repleted cells (PubMed:22888004). {ECO:0000269|PubMed:22888004,
ECO:0000269|PubMed:6456269, ECO:0000269|PubMed:7657623}.
-!- ENZYME REGULATION: Inhibited by the translational inhibitors
neomycin and alpha-sarcin, which suppress the ATPase activity.
{ECO:0000269|PubMed:7957240}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.126 mM for ATP {ECO:0000269|PubMed:7957240};
KM=0.125 mM for GTP {ECO:0000269|PubMed:7957240};
Vmax=15.2 umol/min/mg enzyme with ATP as substrate
{ECO:0000269|PubMed:7957240};
-!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
-!- SUBUNIT: Monomer. Interacts with elongation factor 1A (eEF1A).
Interacts through its N-terminus with 18S rRNA. Associates with
ribosomes (PubMed:22888004). {ECO:0000269|PubMed:12493761,
ECO:0000269|PubMed:22888004, ECO:0000269|PubMed:9553076,
ECO:0000269|PubMed:9990316}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
-!- DOMAIN: The heat repeats and the C-terminal domain are necessary
for impairing GCN1 function on ribosomes, and hence preventing
GCN2 kinase activity in amino acid-starved or repleted cells
(PubMed:22888004). {ECO:0000269|PubMed:22888004}.
-!- MISCELLANEOUS: Present with 870578 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF
family. EF3 subfamily. {ECO:0000305}.
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EMBL; J05197; AAA35232.1; -; Genomic_DNA.
EMBL; J05583; AAA35233.1; -; Genomic_DNA.
EMBL; U20865; AAB67391.1; -; Genomic_DNA.
EMBL; AB018539; BAA33897.1; -; Genomic_DNA.
EMBL; BK006945; DAA09563.1; -; Genomic_DNA.
PIR; S59395; DVBYE3.
RefSeq; NP_013350.1; NM_001182136.1.
PDB; 2IW3; X-ray; 2.40 A; A/B=2-981.
PDB; 2IWH; X-ray; 3.00 A; A/B=2-981.
PDB; 2IX3; X-ray; 2.70 A; A/B=2-981.
PDB; 2IX8; EM; 6.00 A; A=2-977.
PDBsum; 2IW3; -.
PDBsum; 2IWH; -.
PDBsum; 2IX3; -.
PDBsum; 2IX8; -.
ProteinModelPortal; P16521; -.
SMR; P16521; -.
BioGrid; 31517; 149.
DIP; DIP-2249N; -.
IntAct; P16521; 83.
MINT; MINT-8285353; -.
STRING; 4932.YLR249W; -.
iPTMnet; P16521; -.
MaxQB; P16521; -.
PRIDE; P16521; -.
EnsemblFungi; YLR249W; YLR249W; YLR249W.
GeneID; 850951; -.
KEGG; sce:YLR249W; -.
EuPathDB; FungiDB:YLR249W; -.
SGD; S000004239; YEF3.
GeneTree; ENSGT00550000075671; -.
HOGENOM; HOG000180957; -.
InParanoid; P16521; -.
KO; K03235; -.
OMA; EEDQYDA; -.
OrthoDB; EOG092C22OB; -.
BioCyc; YEAST:G3O-32354-MONOMER; -.
UniPathway; UPA00345; -.
EvolutionaryTrace; P16521; -.
PRO; PR:P16521; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
GO; GO:0022626; C:cytosolic ribosome; IDA:SGD.
GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
GO; GO:0005840; C:ribosome; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IMP:SGD.
GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
GO; GO:0003746; F:translation elongation factor activity; IDA:SGD.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0006414; P:translational elongation; IMP:SGD.
GO; GO:0006415; P:translational termination; IDA:SGD.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR015688; Elongation_fac_3.
InterPro; IPR021133; HEAT_type_2.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR19211:SF5; PTHR19211:SF5; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF48371; SSF48371; 6.
SUPFAM; SSF52540; SSF52540; 3.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PROSITE; PS50077; HEAT_REPEAT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Elongation factor; Isopeptide bond;
Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
Reference proteome; Repeat; RNA-binding; rRNA-binding;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:9298649}.
CHAIN 2 1044 Elongation factor 3A.
/FTId=PRO_0000093458.
REPEAT 5 42 HEAT 1.
REPEAT 86 123 HEAT 2.
REPEAT 125 162 HEAT 3.
REPEAT 166 203 HEAT 4.
REPEAT 205 241 HEAT 5.
REPEAT 242 279 HEAT 6.
REPEAT 285 323 HEAT 7.
DOMAIN 426 641 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 667 993 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 463 470 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 701 708 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
COMPBIAS 1009 1031 Lys-rich (basic).
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:9298649}.
MOD_RES 187 187 N6,N6,N6-trimethyllysine.
{ECO:0000269|PubMed:22522802}.
MOD_RES 196 196 N6,N6,N6-trimethyllysine.
{ECO:0000269|PubMed:22522802}.
MOD_RES 642 642 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 789 789 N6,N6,N6-trimethyllysine.
{ECO:0000269|PubMed:22522802}.
MOD_RES 972 972 Phosphothreonine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 974 974 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1039 1039 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 1040 1040 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
CROSSLNK 350 350 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 636 636 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 650 650 F->S: Reduces ATPase activity and
interaction with eEF1A. Required for
growth at 37 degrees Celsius and causes a
50% reduction of total protein synthesis
at permissive temperatures.
{ECO:0000269|PubMed:12493761}.
CONFLICT 153 153 I -> F (in Ref. 1; AAA35232, 2; no
nucleotide entry and 3; AAA35233).
{ECO:0000305}.
CONFLICT 332 332 V -> L (in Ref. 1; AAA35232, 2; no
nucleotide entry and 3; AAA35233).
{ECO:0000305}.
HELIX 3 18 {ECO:0000244|PDB:2IW3}.
TURN 23 25 {ECO:0000244|PDB:2IW3}.
HELIX 26 37 {ECO:0000244|PDB:2IW3}.
STRAND 42 45 {ECO:0000244|PDB:2IW3}.
HELIX 48 58 {ECO:0000244|PDB:2IW3}.
HELIX 61 74 {ECO:0000244|PDB:2IW3}.
TURN 77 79 {ECO:0000244|PDB:2IW3}.
TURN 82 84 {ECO:0000244|PDB:2IW3}.
HELIX 85 89 {ECO:0000244|PDB:2IW3}.
HELIX 92 98 {ECO:0000244|PDB:2IW3}.
HELIX 104 120 {ECO:0000244|PDB:2IW3}.
HELIX 123 125 {ECO:0000244|PDB:2IW3}.
HELIX 126 139 {ECO:0000244|PDB:2IW3}.
HELIX 143 159 {ECO:0000244|PDB:2IW3}.
HELIX 161 178 {ECO:0000244|PDB:2IW3}.
HELIX 184 197 {ECO:0000244|PDB:2IW3}.
HELIX 198 200 {ECO:0000244|PDB:2IW3}.
TURN 204 206 {ECO:0000244|PDB:2IW3}.
HELIX 207 209 {ECO:0000244|PDB:2IW3}.
HELIX 210 218 {ECO:0000244|PDB:2IW3}.
HELIX 222 230 {ECO:0000244|PDB:2IW3}.
HELIX 241 255 {ECO:0000244|PDB:2IW3}.
STRAND 257 259 {ECO:0000244|PDB:2IW3}.
HELIX 260 274 {ECO:0000244|PDB:2IW3}.
HELIX 280 283 {ECO:0000244|PDB:2IW3}.
HELIX 284 289 {ECO:0000244|PDB:2IW3}.
HELIX 291 297 {ECO:0000244|PDB:2IW3}.
TURN 298 300 {ECO:0000244|PDB:2IW3}.
HELIX 304 321 {ECO:0000244|PDB:2IW3}.
TURN 325 327 {ECO:0000244|PDB:2IW3}.
HELIX 338 348 {ECO:0000244|PDB:2IW3}.
TURN 349 351 {ECO:0000244|PDB:2IW3}.
HELIX 356 358 {ECO:0000244|PDB:2IW3}.
HELIX 359 374 {ECO:0000244|PDB:2IW3}.
HELIX 380 386 {ECO:0000244|PDB:2IW3}.
HELIX 388 391 {ECO:0000244|PDB:2IW3}.
TURN 392 394 {ECO:0000244|PDB:2IW3}.
HELIX 397 413 {ECO:0000244|PDB:2IW3}.
STRAND 426 428 {ECO:0000244|PDB:2IW3}.
STRAND 430 440 {ECO:0000244|PDB:2IW3}.
STRAND 443 454 {ECO:0000244|PDB:2IW3}.
STRAND 458 462 {ECO:0000244|PDB:2IW3}.
HELIX 469 478 {ECO:0000244|PDB:2IW3}.
TURN 487 489 {ECO:0000244|PDB:2IW3}.
STRAND 492 494 {ECO:0000244|PDB:2IW3}.
HELIX 508 513 {ECO:0000244|PDB:2IW3}.
TURN 514 516 {ECO:0000244|PDB:2IX3}.
HELIX 520 529 {ECO:0000244|PDB:2IW3}.
HELIX 534 538 {ECO:0000244|PDB:2IW3}.
HELIX 541 543 {ECO:0000244|PDB:2IW3}.
HELIX 546 559 {ECO:0000244|PDB:2IW3}.
STRAND 563 569 {ECO:0000244|PDB:2IW3}.
TURN 570 573 {ECO:0000244|PDB:2IW3}.
HELIX 576 588 {ECO:0000244|PDB:2IW3}.
STRAND 591 596 {ECO:0000244|PDB:2IW3}.
HELIX 600 606 {ECO:0000244|PDB:2IW3}.
STRAND 608 614 {ECO:0000244|PDB:2IW3}.
STRAND 617 623 {ECO:0000244|PDB:2IW3}.
HELIX 625 631 {ECO:0000244|PDB:2IW3}.
HELIX 633 637 {ECO:0000244|PDB:2IW3}.
STRAND 638 640 {ECO:0000244|PDB:2IW3}.
TURN 641 643 {ECO:0000244|PDB:2IW3}.
STRAND 664 674 {ECO:0000244|PDB:2IW3}.
STRAND 679 681 {ECO:0000244|PDB:2IX3}.
STRAND 683 692 {ECO:0000244|PDB:2IW3}.
STRAND 696 699 {ECO:0000244|PDB:2IW3}.
HELIX 705 714 {ECO:0000244|PDB:2IW3}.
STRAND 721 727 {ECO:0000244|PDB:2IW3}.
STRAND 733 736 {ECO:0000244|PDB:2IW3}.
HELIX 738 743 {ECO:0000244|PDB:2IW3}.
HELIX 744 746 {ECO:0000244|PDB:2IW3}.
HELIX 752 759 {ECO:0000244|PDB:2IW3}.
TURN 760 762 {ECO:0000244|PDB:2IW3}.
TURN 766 772 {ECO:0000244|PDB:2IW3}.
HELIX 783 785 {ECO:0000244|PDB:2IW3}.
STRAND 788 790 {ECO:0000244|PDB:2IW3}.
STRAND 793 806 {ECO:0000244|PDB:2IW3}.
STRAND 809 821 {ECO:0000244|PDB:2IW3}.
STRAND 828 831 {ECO:0000244|PDB:2IW3}.
HELIX 834 836 {ECO:0000244|PDB:2IW3}.
STRAND 838 841 {ECO:0000244|PDB:2IW3}.
HELIX 842 844 {ECO:0000244|PDB:2IW3}.
HELIX 846 863 {ECO:0000244|PDB:2IW3}.
HELIX 872 881 {ECO:0000244|PDB:2IW3}.
HELIX 886 891 {ECO:0000244|PDB:2IW3}.
HELIX 894 896 {ECO:0000244|PDB:2IW3}.
HELIX 899 911 {ECO:0000244|PDB:2IW3}.
STRAND 916 921 {ECO:0000244|PDB:2IW3}.
HELIX 923 925 {ECO:0000244|PDB:2IW3}.
HELIX 929 940 {ECO:0000244|PDB:2IW3}.
STRAND 943 949 {ECO:0000244|PDB:2IW3}.
HELIX 953 956 {ECO:0000244|PDB:2IW3}.
TURN 957 959 {ECO:0000244|PDB:2IW3}.
STRAND 962 964 {ECO:0000244|PDB:2IW3}.
SEQUENCE 1044 AA; 115945 MW; 41E40B8BDD7A4C33 CRC64;
MSDSQQSIKV LEELFQKLSV ATADNRHEIA SEVASFLNGN IIEHDVPEHF FGELAKGIKD
KKTAANAMQA VAHIANQSNL SPSVEPYIVQ LVPAICTNAG NKDKEIQSVA SETLISIVNA
VNPVAIKALL PHLTNAIVET NKWQEKIAIL AAISAMVDAA KDQVALRMPE LIPVLSETMW
DTKKEVKAAA TAAMTKATET VDNKDIERFI PSLIQCIADP TEVPETVHLL GATTFVAEVT
PATLSIMVPL LSRGLNERET GIKRKSAVII DNMCKLVEDP QVIAPFLGKL LPGLKSNFAT
IADPEAREVT LRALKTLRRV GNVGEDDAIP EVSHAGDVST TLQVVNELLK DETVAPRFKI
VVEYIAAIGA DLIDERIIDQ QAWFTHITPY MTIFLHEKKA KDILDEFRKR AVDNIPVGPN
FDDEEDEGED LCNCEFSLAY GAKILLNKTQ LRLKRARRYG ICGPNGCGKS TLMRAIANGQ
VDGFPTQEEC RTVYVEHDID GTHSDTSVLD FVFESGVGTK EAIKDKLIEF GFTDEMIAMP
ISALSGGWKM KLALARAVLR NADILLLDEP TNHLDTVNVA WLVNYLNTCG ITSITISHDS
VFLDNVCEYI INYEGLKLRK YKGNFTEFVK KCPAAKAYEE LSNTDLEFKF PEPGYLEGVK
TKQKAIVKVT NMEFQYPGTS KPQITDINFQ CSLSSRIAVI GPNGAGKSTL INVLTGELLP
TSGEVYTHEN CRIAYIKQHA FAHIESHLDK TPSEYIQWRF QTGEDRETMD RANRQINEND
AEAMNKIFKI EGTPRRIAGI HSRRKFKNTY EYECSFLLGE NIGMKSERWV PMMSVDNAWI
PRGELVESHS KMVAEVDMKE ALASGQFRPL TRKEIEEHCS MLGLDPEIVS HSRIRGLSGG
QKVKLVLAAG TWQRPHLIVL DEPTNYLDRD SLGALSKALK EFEGGVIIIT HSAEFTKNLT
EEVWAVKDGR MTPSGHNWVS GQGAGPRIEK KEDEEDKFDA MGNKIAGGKK KKKLSSAELR
KKKKERMKKK KELGDAYVSS DEEF


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