IPYR_YEAST
ID IPYR_YEAST Reviewed; 287 AA.
AC P00817; D6VQ12;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 4.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Inorganic pyrophosphatase;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
GN Name=IPP1; Synonyms=PPA, PPA1; OrderedLocusNames=YBR011C; ORFNames=YBR0202;
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 26109 / X2180;
RX PubMed=2849749; DOI=10.1093/nar/16.22.10441;
RA Kolakowski L.F. Jr., Schloesser M., Cooperman B.S.;
RT "Cloning, molecular characterization and chromosome localization of the
RT inorganic pyrophosphatase (PPA) gene from S. cerevisiae.";
RL Nucleic Acids Res. 16:10441-10452(1988).
RN [2]
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 [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 PROTEIN SEQUENCE OF 2-287.
RX PubMed=340461; DOI=10.1016/s0021-9258(17)38188-7;
RA Cohen S.A., Sterner R., Keim P.S., Heinrikson R.L.;
RT "Covalent structural analysis of yeast inorganic pyrophosphatase.";
RL J. Biol. Chem. 253:889-897(1978).
RN [6]
RP PROTEIN SEQUENCE OF 26-36 AND 240-252.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [7]
RP PROTEIN SEQUENCE OF 240-250.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA Norbeck J., Blomberg A.;
RT "Protein expression during exponential growth in 0.7 M NaCl medium of
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 137:1-8(1996).
RN [8]
RP ACTIVE SITE TYR-90.
RX PubMed=1322842; DOI=10.1016/0014-5793(92)81051-m;
RA Raznikov A.V., Sklyankina V.A., Avaeva S.M.;
RT "Tyrosine-89 is important for enzymatic activity of S. cerevisiae inorganic
RT pyrophosphatase.";
RL FEBS Lett. 308:62-64(1992).
RN [9]
RP ACTIVE SITE.
RX PubMed=6101539; DOI=10.1021/bi00542a015;
RA Bond M.W., Chiu N.Y., Cooperman B.S.;
RT "Identification of an arginine important for enzymatic activity within the
RT covalent structure of yeast inorganic pyrophosphatase.";
RL Biochemistry 19:94-102(1980).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251 AND SER-286, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65 AND SER-266, AND
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, 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 [15]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RA Arutiunian E.G., Terzian S.S., Voronova A.A., Kuranova I.P., Smirnova E.A.,
RA Vainstein B.K., Hohne W.E., Hansen G.;
RT "X-ray diffraction study of inorganic pyrophosphatase from baker's yeast at
RT the 3-A resolution.";
RL Dokl. Akad. Nauk SSSR 258:1481-1492(1981).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=8994974; DOI=10.1016/s0969-2126(96)00155-4;
RA Heikinheimo P., Lehtonen J., Baykov A., Lahti R., Cooperman B.S.,
RA Goldman A.;
RT "The structural basis for pyrophosphatase catalysis.";
RL Structure 4:1491-1508(1996).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RA Swaminathan K., Cooperman B.S., Lahti R., Voet D.;
RL Submitted (DEC-1997) to the PDB data bank.
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF MUTANTS LYS-79 AND LYS-118.
RX PubMed=9878371; DOI=10.1006/jmbi.1998.2266;
RA Tuominen V., Heikinheimo P., Kajander T., Torkkel T., Hyytia T., Kapyla J.,
RA Lahti R., Cooperman B.S., Goldman A.;
RT "The R78K and D117E active-site variants of Saccharomyces cerevisiae
RT soluble inorganic pyrophosphatase: structural studies and mechanistic
RT implications.";
RL J. Mol. Biol. 284:1565-1580(1998).
RN [20]
RP SIMILARITY TO E.COLI AND K.LACTIS PPASES.
RX PubMed=2160278; DOI=10.1016/0167-4838(90)90246-c;
RA Lahti R., Kolakowski L.F. Jr., Heinonen J., Vihinen M., Pohjanoksa K.,
RA Cooperman B.S.;
RT "Conservation of functional residues between yeast and E. coli inorganic
RT pyrophosphatases.";
RL Biochim. Biophys. Acta 1038:338-345(1990).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P00817; P39940: RSP5; NbExp=2; IntAct=EBI-9338, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 68400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR EMBL; X13253; CAA31629.1; -; Genomic_DNA.
DR EMBL; Z35880; CAA84949.1; -; Genomic_DNA.
DR EMBL; AY692953; AAT92972.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07132.1; -; Genomic_DNA.
DR PIR; S45864; PWBY.
DR RefSeq; NP_009565.1; NM_001178359.1.
DR PDB; 117E; X-ray; 2.15 A; A/B=2-287.
DR PDB; 1E6A; X-ray; 1.90 A; A/B=2-287.
DR PDB; 1E9G; X-ray; 1.15 A; A/B=2-287.
DR PDB; 1HUJ; X-ray; 2.10 A; A/B=2-282.
DR PDB; 1HUK; X-ray; 2.20 A; A/B=2-282.
DR PDB; 1M38; X-ray; 1.80 A; A/B=1-287.
DR PDB; 1PYP; X-ray; 3.00 A; A/B=2-287.
DR PDB; 1WGI; X-ray; 2.20 A; A/B=2-287.
DR PDB; 1WGJ; X-ray; 2.00 A; A/B=2-287.
DR PDB; 1YPP; X-ray; 2.40 A; A/B=2-287.
DR PDB; 2IHP; X-ray; 1.50 A; A/B=2-287.
DR PDB; 2IK0; X-ray; 1.70 A; A/B=2-287.
DR PDB; 2IK1; X-ray; 1.70 A; A/B=2-287.
DR PDB; 2IK2; X-ray; 1.80 A; A/B=2-287.
DR PDB; 2IK4; X-ray; 1.80 A; A/B=2-287.
DR PDB; 2IK6; X-ray; 1.80 A; A/B=2-287.
DR PDB; 2IK7; X-ray; 1.90 A; A/B=2-287.
DR PDB; 2IK9; X-ray; 1.50 A; A/B=2-287.
DR PDB; 8PRK; X-ray; 1.85 A; A/B=1-287.
DR PDBsum; 117E; -.
DR PDBsum; 1E6A; -.
DR PDBsum; 1E9G; -.
DR PDBsum; 1HUJ; -.
DR PDBsum; 1HUK; -.
DR PDBsum; 1M38; -.
DR PDBsum; 1PYP; -.
DR PDBsum; 1WGI; -.
DR PDBsum; 1WGJ; -.
DR PDBsum; 1YPP; -.
DR PDBsum; 2IHP; -.
DR PDBsum; 2IK0; -.
DR PDBsum; 2IK1; -.
DR PDBsum; 2IK2; -.
DR PDBsum; 2IK4; -.
DR PDBsum; 2IK6; -.
DR PDBsum; 2IK7; -.
DR PDBsum; 2IK9; -.
DR PDBsum; 8PRK; -.
DR AlphaFoldDB; P00817; -.
DR SMR; P00817; -.
DR BioGRID; 32712; 416.
DR DIP; DIP-5753N; -.
DR IntAct; P00817; 49.
DR MINT; P00817; -.
DR STRING; 4932.YBR011C; -.
DR BindingDB; P00817; -.
DR iPTMnet; P00817; -.
DR COMPLUYEAST-2DPAGE; P00817; -.
DR SWISS-2DPAGE; P00817; -.
DR MaxQB; P00817; -.
DR PaxDb; P00817; -.
DR PRIDE; P00817; -.
DR TopDownProteomics; P00817; -.
DR EnsemblFungi; YBR011C_mRNA; YBR011C; YBR011C.
DR GeneID; 852296; -.
DR KEGG; sce:YBR011C; -.
DR SGD; S000000215; IPP1.
DR VEuPathDB; FungiDB:YBR011C; -.
DR eggNOG; KOG1626; Eukaryota.
DR GeneTree; ENSGT00390000017004; -.
DR HOGENOM; CLU_040684_0_2_1; -.
DR InParanoid; P00817; -.
DR OMA; TLEHRIF; -.
DR BioCyc; YEAST:YBR011C-MON; -.
DR BRENDA; 3.6.1.1; 984.
DR Reactome; R-SCE-379716; Cytosolic tRNA aminoacylation.
DR Reactome; R-SCE-379726; Mitochondrial tRNA aminoacylation.
DR Reactome; R-SCE-71737; Pyrophosphate hydrolysis.
DR EvolutionaryTrace; P00817; -.
DR PRO; PR:P00817; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P00817; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IDA:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central.
DR CDD; cd00412; pyrophosphatase; 1.
DR Gene3D; 3.90.80.10; -; 1.
DR InterPro; IPR008162; Pyrophosphatase.
DR InterPro; IPR036649; Pyrophosphatase_sf.
DR PANTHER; PTHR10286; PTHR10286; 1.
DR Pfam; PF00719; Pyrophosphatase; 1.
DR SUPFAM; SSF50324; SSF50324; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Isopeptide bond; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:340461"
FT CHAIN 2..287
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137588"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:1322842"
FT BINDING 79
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 41
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="D -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="E -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="Q -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="D -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="P -> L (in Ref. 1; CAA31629)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1YPP"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1E9G"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1E9G"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2IK1"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1PYP"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1E9G"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2IHP"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1M38"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1PYP"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1E9G"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:1E9G"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:1E9G"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1E9G"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1E6A"
FT HELIX 213..231
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1E9G"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1E9G"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1E9G"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:1E9G"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:1E9G"
SQ SEQUENCE 287 AA; 32300 MW; 1DC19A702A389BA9 CRC64;
MTYTTRQIGA KNTLEYKVYI EKDGKPVSAF HDIPLYADKE NNIFNMVVEI PRWTNAKLEI
TKEETLNPII QDTKKGKLRF VRNCFPHHGY IHNYGAFPQT WEDPNVSHPE TKAVGDNDPI
DVLEIGETIA YTGQVKQVKA LGIMALLDEG ETDWKVIAID INDPLAPKLN DIEDVEKYFP
GLLRATNEWF RIYKIPDGKP ENQFAFSGEA KNKKYALDII KETHDSWKQL IAGKSSDSKG
IDLTNVTLPD TPTYSKAASD AIPPASPKAD APIDKSIDKW FFISGSV
