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 27-MAR-2024, entry version 227. 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; GN 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}. 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; 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; 427. DR DIP; DIP-5753N; -. DR IntAct; P00817; 49. DR MINT; P00817; -. DR STRING; 4932.YBR011C; -. DR BindingDB; P00817; -. DR iPTMnet; P00817; -. DR MaxQB; P00817; -. DR PaxDb; 4932-YBR011C; -. DR PeptideAtlas; P00817; -. DR TopDownProteomics; P00817; -. DR EnsemblFungi; YBR011C_mRNA; YBR011C; YBR011C. DR GeneID; 852296; -. DR KEGG; sce:YBR011C; -. DR AGR; SGD:S000000215; -. 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; LYANEQK; -. DR OrthoDB; 156at2759; -. DR BioCyc; YEAST:YBR011C-MONOMER; -. 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 BioGRID-ORCS; 852296; 6 hits in 10 CRISPR screens. 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:0005634; C:nucleus; HDA:SGD. DR GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IDA:SGD. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central. DR CDD; cd00412; pyrophosphatase; 1. DR Gene3D; 3.90.80.10; Inorganic pyrophosphatase; 1. DR InterPro; IPR008162; Pyrophosphatase. DR InterPro; IPR036649; Pyrophosphatase_sf. DR PANTHER; PTHR10286; INORGANIC PYROPHOSPHATASE; 1. DR PANTHER; PTHR10286:SF3; INORGANIC PYROPHOSPHATASE; 1. DR Pfam; PF00719; Pyrophosphatase; 1. DR SUPFAM; SSF50324; Inorganic pyrophosphatase; 1. DR PROSITE; PS00387; PPASE; 1. DR COMPLUYEAST-2DPAGE; P00817; -. DR SWISS-2DPAGE; P00817; -. 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 //