ID   HBS1_YEAST              Reviewed;         611 AA.
AC   P32769; D6VXE4;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Elongation factor 1 alpha-like protein {ECO:0000305};
DE            EC=3.6.5.- {ECO:0000269|PubMed:20947765};
GN   Name=HBS1 {ECO:0000303|PubMed:8203164, ECO:0000312|SGD:S000001792};
GN   OrderedLocusNames=YKR084C; ORFNames=YKR404;
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].
RX   PubMed=8203164; DOI=10.1002/yea.320100210;
RA   Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G.,
RA   Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.;
RT   "The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae
RT   chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open
RT   reading frames.";
RL   Yeast 10:231-245(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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] OF 92-611.
RX   PubMed=1394434; DOI=10.1016/0092-8674(92)90269-i;
RA   Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., Craig E.A.;
RT   "The translation machinery and 70 kd heat shock protein cooperate in
RT   protein synthesis.";
RL   Cell 71:97-105(1992).
RN   [5]
RP   INTERACTION WITH DOM34, AND MUTAGENESIS OF VAL-176 AND HIS-255.
RX   PubMed=11909951; DOI=10.1128/mcb.22.8.2564-2574.2002;
RA   Carr-Schmid A., Pfund C., Craig E.A., Kinzy T.G.;
RT   "Novel G-protein complex whose requirement is linked to the translational
RT   status of the cell.";
RL   Mol. Cell. Biol. 22:2564-2574(2002).
RN   [6]
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   [7]
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   [8]
RP   FUNCTION.
RX   PubMed=16554824; DOI=10.1038/nature04530;
RA   Doma M.K., Parker R.;
RT   "Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation
RT   elongation.";
RL   Nature 440:561-564(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE DOM34-HBS1 COMPLEX.
RX   PubMed=20947765; DOI=10.1126/science.1192430;
RA   Shoemaker C.J., Eyler D.E., Green R.;
RT   "Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to
RT   initiate no-go decay.";
RL   Science 330:369-372(2010).
RN   [13] {ECO:0007744|PDB:3P26, ECO:0007744|PDB:3P27}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 135-611 IN COMPLEX WITH GDP,
RP   FUNCTION, IDENTIFICATION IN THE DOM34-HBS1 COMPLEX, AND MUTAGENESIS OF
RP   VAL-176; LYS-180; HIS-255; ARG-517; LEU-520 AND 557-ARG-HIS-558.
RX   PubMed=21102444; DOI=10.1038/nsmb.1963;
RA   van den Elzen A.M., Henri J., Lazar N., Gas M.E., Durand D., Lacroute F.,
RA   Nicaise M., van Tilbeurgh H., Seraphin B., Graille M.;
RT   "Dissection of Dom34-Hbs1 reveals independent functions in two RNA quality
RT   control pathways.";
RL   Nat. Struct. Mol. Biol. 17:1446-1452(2010).
RN   [14] {ECO:0007744|PDB:3IZQ}
RP   STRUCTURE BY ELECTRON MICROSCOPY (9.50 ANGSTROMS) IN COMPLEX WITH DOM34,
RP   AND IDENTIFICATION IN THE DOM34-HBS1 COMPLEX.
RX   PubMed=21623367; DOI=10.1038/nsmb.2057;
RA   Becker T., Armache J.P., Jarasch A., Anger A.M., Villa E., Sieber H.,
RA   Motaal B.A., Mielke T., Berninghausen O., Beckmann R.;
RT   "Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled
RT   80S ribosome.";
RL   Nat. Struct. Mol. Biol. 18:715-720(2011).
RN   [15] {ECO:0007744|PDB:5M1J}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) IN COMPLEX WITH DOM34 AND
RP   RIBOSOME, AND IDENTIFICATION IN THE DOM34-HBS1 COMPLEX.
RX   PubMed=27995908; DOI=10.1038/ncomms13521;
RA   Hilal T., Yamamoto H., Loerke J., Buerger J., Mielke T., Spahn C.M.;
RT   "Structural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic
RT   resolution.";
RL   Nat. Commun. 7:13521-13521(2016).
CC   -!- FUNCTION: GTPase component of the Dom34-Hbs1 complex, a complex that
CC       recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway
CC       (PubMed:16554824, PubMed:20947765, PubMed:21102444). The Dom34-Hbs1
CC       complex recognizes ribosomes stalled at the 3' end of an mRNA and
CC       engages stalled ribosomes by destabilizing mRNA in the mRNA channel
CC       (PubMed:16554824, PubMed:20947765). Following ribosome-binding, the
CC       Pelota-HBS1L complex promotes the disassembly of stalled ribosomes,
CC       followed by degradation of damaged mRNAs as part of the NGD pathway
CC       (PubMed:16554824, PubMed:20947765). The Dom34-Hbs1 complex is also
CC       involved in non-functional rRNA decay (PubMed:21102444).
CC       {ECO:0000269|PubMed:16554824, ECO:0000269|PubMed:20947765,
CC       ECO:0000269|PubMed:21102444}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:20947765};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000269|PubMed:20947765};
CC   -!- SUBUNIT: Component of the Dom34-Hbs1 complex, also named Pelota-HBS1L
CC       complex, composed of DOM34 and HBS1. {ECO:0000269|PubMed:11909951,
CC       ECO:0000269|PubMed:20947765, ECO:0000269|PubMed:21102444,
CC       ECO:0000269|PubMed:21623367, ECO:0000269|PubMed:27995908}.
CC   -!- INTERACTION:
CC       P32769; P33309: DOM34; NbExp=8; IntAct=EBI-8194, EBI-6012;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2750 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; M98437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z27116; CAA81635.1; -; Genomic_DNA.
DR   EMBL; Z28309; CAA82163.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09234.1; -; Genomic_DNA.
DR   PIR; S38162; S38162.
DR   RefSeq; NP_013010.3; NM_001179874.3.
DR   PDB; 3IZQ; EM; -; 1=1-611.
DR   PDB; 3P26; X-ray; 2.50 A; A/B=135-611.
DR   PDB; 3P27; X-ray; 2.95 A; A/B=135-611.
DR   PDB; 5M1J; EM; 3.30 A; A6=1-611.
DR   PDBsum; 3IZQ; -.
DR   PDBsum; 3P26; -.
DR   PDBsum; 3P27; -.
DR   PDBsum; 5M1J; -.
DR   AlphaFoldDB; P32769; -.
DR   SMR; P32769; -.
DR   BioGRID; 34215; 158.
DR   ComplexPortal; CPX-465; DOM34-HBS1 ribosome dissociation complex.
DR   DIP; DIP-762N; -.
DR   IntAct; P32769; 1.
DR   STRING; 4932.YKR084C; -.
DR   iPTMnet; P32769; -.
DR   MaxQB; P32769; -.
DR   PaxDb; 4932-YKR084C; -.
DR   PeptideAtlas; P32769; -.
DR   EnsemblFungi; YKR084C_mRNA; YKR084C; YKR084C.
DR   GeneID; 853959; -.
DR   KEGG; sce:YKR084C; -.
DR   AGR; SGD:S000001792; -.
DR   SGD; S000001792; HBS1.
DR   VEuPathDB; FungiDB:YKR084C; -.
DR   eggNOG; KOG0458; Eukaryota.
DR   GeneTree; ENSGT00940000156274; -.
DR   HOGENOM; CLU_007265_3_8_1; -.
DR   InParanoid; P32769; -.
DR   OMA; DYQGWDN; -.
DR   OrthoDB; 5477300at2759; -.
DR   BioCyc; YEAST:G3O-32047-MONOMER; -.
DR   Reactome; R-SCE-429958; mRNA decay by 3' to 5' exoribonuclease.
DR   BioGRID-ORCS; 853959; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P32769; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P32769; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:1990533; C:Dom34-Hbs1 complex; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0070651; P:nonfunctional rRNA decay; IDA:UniProtKB.
DR   GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IDA:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:SGD.
DR   GO; GO:0045948; P:positive regulation of translational initiation; IDA:ComplexPortal.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IDA:ComplexPortal.
DR   GO; GO:0032790; P:ribosome disassembly; IDA:SGD.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd04093; HBS1_C_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR015033; HBS1-like_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   PANTHER; PTHR23115:SF303; ELONGATION FACTOR 1 ALPHA-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF08938; HBS1_N; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Elongation factor; GTP-binding; Hydrolase;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; Translation regulation.
FT   CHAIN           1..611
FT                   /note="Elongation factor 1 alpha-like protein"
FT                   /id="PRO_0000091490"
FT   DOMAIN          165..390
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..181
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          230..234
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          251..254
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          313..316
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          352..354
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         174..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000305|PubMed:21102444,
FT                   ECO:0007744|PDB:3P27"
FT   BINDING         313..316
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000305|PubMed:21102444,
FT                   ECO:0007744|PDB:3P27"
FT   BINDING         352..354
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000305|PubMed:21102444,
FT                   ECO:0007744|PDB:3P27"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MUTAGEN         176
FT                   /note="V->G: Loss of function. Abolished GTP-binding and
FT                   ability to trigger the No-Go Decay (NGD) pathway and
FT                   promote degradation of non-functional rRNAs."
FT                   /evidence="ECO:0000269|PubMed:11909951,
FT                   ECO:0000269|PubMed:21102444"
FT   MUTAGEN         180
FT                   /note="K->A: Abolished GTP-binding and ability to trigger
FT                   the No-Go Decay (NGD) pathway and promote degradation of
FT                   non-functional rRNAs."
FT                   /evidence="ECO:0000269|PubMed:21102444"
FT   MUTAGEN         255
FT                   /note="H->E: Loss of function. Abolished GTP-binding and
FT                   ability to trigger the No-Go Decay (NGD) pathway and
FT                   promote degradation of non-functional rRNAs."
FT                   /evidence="ECO:0000269|PubMed:11909951,
FT                   ECO:0000269|PubMed:21102444"
FT   MUTAGEN         517
FT                   /note="R->E: Abolished ability to trigger the No-Go Decay
FT                   (NGD) pathway, without affecting the ability to promote
FT                   degradation of non-functional rRNAs."
FT                   /evidence="ECO:0000269|PubMed:21102444"
FT   MUTAGEN         520
FT                   /note="L->R: Abolished ability to trigger the No-Go Decay
FT                   (NGD) pathway, without affecting the ability to promote
FT                   degradation of non-functional rRNAs."
FT                   /evidence="ECO:0000269|PubMed:21102444"
FT   MUTAGEN         557..558
FT                   /note="RH->AA: Abolished ability to trigger the No-Go Decay
FT                   (NGD) pathway, without affecting the ability to promote
FT                   degradation of non-functional rRNAs."
FT                   /evidence="ECO:0000269|PubMed:21102444"
FT   CONFLICT        92..94
FT                   /note="NGS -> MGV (in Ref. 4; M98437)"
FT                   /evidence="ECO:0000305"
FT   HELIX           157..163
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          167..174
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           180..190
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           196..202
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           219..222
FT                   /evidence="ECO:0007829|PDB:3P27"
FT   STRAND          237..241
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          246..250
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           256..258
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           259..266
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          270..277
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           291..302
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          308..313
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           315..318
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           322..339
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           343..345
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          346..350
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          353..355
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          359..362
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           366..371
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           377..392
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          397..399
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          402..409
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          419..430
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          435..439
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   TURN            440..442
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          443..452
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   TURN            453..455
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          464..466
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          473..480
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   HELIX           483..485
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          491..493
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          504..512
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          524..529
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          532..547
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          564..571
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   TURN            583..585
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   TURN            587..590
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          591..596
FT                   /evidence="ECO:0007829|PDB:3P26"
FT   STRAND          599..609
FT                   /evidence="ECO:0007829|PDB:3P26"
SQ   SEQUENCE   611 AA;  68730 MW;  11EC2CB6936396EE CRC64;
     MAYSDYSDGA DDMPDFHDEG EFDDYLNDDE YDLMNEVFPT LKAQLQDYQG WDNLSLKLAL
     FDNNFDLEST LAELKKTLKK KKTPKKPIAA ANGSANVTQK LANISISQQR PNDRLPDWLD
     EEESEGERNG EEANDEKTVQ RYYKTTVPTK PKKPHDISAF VKSALPHLSF VVLGHVDAGK
     STLMGRLLYD LNIVNQSQLR KLQRESETMG KSSFKFAWIM DQTNEERERG VTVSICTSHF
     STHRANFTIV DAPGHRDFVP NAIMGISQAD MAILCVDCST NAFESGFDLD GQTKEHMLLA
     SSLGIHNLII AMNKMDNVDW SQQRFEEIKS KLLPYLVDIG FFEDNINWVP ISGFSGEGVY
     KIEYTDEVRQ WYNGPNLMST LENAAFKISK ENEGINKDDP FLFSVLEIIP SKKTSNDLAL
     VSGKLESGSI QPGESLTIYP SEQSCIVDKI QVGSQQGQST NHEETDVAIK GDFVTLKLRK
     AYPEDIQNGD LAASVDYSSI HSAQCFVLEL TTFDMNRPLL PGTPFILFIG VKEQPARIKR
     LISFIDKGNT ASKKKIRHLG SKQRAFVEIE LIEVKRWIPL LTAHENDRLG RVVLRKDGRT
     IAAGKISEIT Q
//