ID NDK_YEAST Reviewed; 153 AA. AC P36010; D6VXM0; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 02-SEP-2026, entry version 200. DE RecName: Full=Nucleoside diphosphate kinase {ECO:0000303|PubMed:5793714}; DE Short=NDK; DE Short=NDP kinase; DE EC=2.7.4.6 {ECO:0000269|PubMed:1659321, ECO:0000269|PubMed:16957983, ECO:0000269|PubMed:5793714}; GN Name=YNK1; Synonyms=NDK1, YNK; OrderedLocusNames=YKL067W; GN ORFNames=YKL333; 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=SP1; RX PubMed=8392963; DOI=10.1016/0378-1119(93)90710-k; RA Fukuchi T., Nikawa J., Kimura N., Watanabe K.; RT "Isolation, overexpression and disruption of a Saccharomyces cerevisiae YNK RT gene encoding nucleoside diphosphate kinase."; RL Gene 129:141-146(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8091863; DOI=10.1002/yea.320100009; RA Rasmussen S.W.; RT "Sequence of a 20.7 kb region of yeast chromosome XI includes the NUP100 RT gene, an open reading frame (ORF) possibly representing a nucleoside RT diphosphate kinase gene, tRNAs for His, Val and Trp in addition to seven RT ORFs with weak or no significant similarity to known proteins."; RL Yeast 10:S69-S74(1994). RN [3] 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 [4] 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 [5] 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 [6] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND RP REACTION MECHANISM. RX PubMed=5793714; DOI=10.1021/bi00830a026; RA Garces E., Cleland W.W.; RT "Kinetic studies of yeast nucleoside diphosphate kinase."; RL Biochemistry 8:633-640(1969). RN [7] RP SUBUNIT. RX PubMed=4576138; DOI=10.1016/s0021-9258(19)43793-9; RA Palmieri R., Yue R.H., Jacobs H.K., Maland L., Wu L., Kuby S.A.; RT "Nucleoside triphosphate-nucleoside diphosphate transphosphorylase RT (nucleoside diphosphokinase). 3. Subunit structure of the crystalline RT enzyme from brewers' yeast."; RL J. Biol. Chem. 248:4486-4499(1973). RN [8] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=1659321; DOI=10.1016/0003-9861(91)90129-7; RA Jong A.Y., Ma J.J.; RT "Saccharomyces cerevisiae nucleoside-diphosphate kinase: purification, RT characterization, and substrate specificity."; RL Arch. Biochem. Biophys. 291:241-246(1991). RN [9] RP SUBCELLULAR LOCATION, AND INTERACTION WITH TOM40. RX PubMed=12472466; DOI=10.1042/bj20021415; RA Amutha B., Pain D.; RT "Nucleoside diphosphate kinase of Saccharomyces cerevisiae, Ynk1p: RT localization to the mitochondrial intermembrane space."; RL Biochem. J. 370:805-815(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 CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16957983; DOI=10.1007/s10863-006-9045-y; RA Jeudy S., Claverie J.-M., Abergel C.; RT "The nucleoside diphosphate kinase from mimivirus: a peculiar affinity for RT deoxypyrimidine nucleotides."; RL J. Bioenerg. Biomembr. 38:247-254(2006). RN [12] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=16823961; DOI=10.1021/pr050477f; RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.; RT "Toward the complete yeast mitochondrial proteome: multidimensional RT separation techniques for mitochondrial proteomics."; RL J. Proteome Res. 5:1543-1554(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95, 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 [14] RP FUNCTION. RX PubMed=18983998; DOI=10.1016/j.mrfmmm.2008.09.015; RA Yang M., Jarrett S.G., Craven R., Kaetzel D.M.; RT "YNK1, the yeast homolog of human metastasis suppressor NM23, is required RT for repair of UV radiation- and etoposide-induced DNA damage."; RL Mutat. Res. 660:74-78(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RX PubMed=22984289; DOI=10.1074/mcp.m112.021105; RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.; RT "Intermembrane space proteome of yeast mitochondria."; RL Mol. Cell. Proteomics 11:1840-1852(2012). RN [16] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). RX PubMed=18607079; DOI=10.1107/s1744309108015212; RA Wang H., Bao R., Jiang C., Yang Z., Zhou C.Z., Chen Y.; RT "Structure of Ynk1 from the yeast Saccharomyces cerevisiae."; RL Acta Crystallogr. F 64:572-576(2008). CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates other CC than ATP. The ATP gamma phosphate is transferred to the NDP beta CC phosphate via a ping-pong mechanism, using a phosphorylated active-site CC intermediate (PubMed:5793714). Required for repair of UV radiation- and CC etoposide-induced DNA damage (PubMed:18983998). CC {ECO:0000269|PubMed:18983998, ECO:0000269|PubMed:5793714}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983, ECO:0000269|PubMed:5793714}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:1659321, ECO:0000269|PubMed:16957983, CC ECO:0000269|PubMed:5793714}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:5793714}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=25 uM for ADP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=300 uM for CDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=690 uM for UDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=400 uM for dCDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=220 uM for dGDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=370 uM for dTDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=530 uM for dUDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=220 uM for ATP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=100 uM for CTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=150 uM for GTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=140 uM for UTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=170 uM for dCTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=22 uM for dGTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=110 uM for dTTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=130 uM for dUTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC KM=310 uM for ATP (in the presence of 1mM free Mg(2+) at 30 degrees CC Celsius and pH 8.0); CC KM=43 uM for UDP (in the presence of 1mM free Mg(2+) at 30 degrees CC Celsius and pH 8.0); CC KM=50 uM for ADP (in the presence of 1mM free Mg(2+) at 30 degrees CC Celsius and pH 8.0); CC KM=250 uM for UTP (in the presence of 1mM free Mg(2+) at 30 degrees CC Celsius and pH 8.0); CC Vmax=130 umol/min/mg enzyme toward ADP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=220 umol/min/mg enzyme toward CDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=400 umol/min/mg enzyme toward UDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=380 umol/min/mg enzyme toward dCDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=132 umol/min/mg enzyme toward dGDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=330 umol/min/mg enzyme toward dTDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=8.6 nmol/min/mg enzyme toward dUDP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=170 umol/min/mg enzyme toward ATP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=83 umol/min/mg enzyme toward CTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=350 umol/min/mg enzyme toward GTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=75 umol/min/mg enzyme toward UTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=110 umol/min/mg enzyme toward dCTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=38 umol/min/mg enzyme toward dGTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=105 umol/min/mg enzyme toward dTTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=90 umol/min/mg enzyme toward dUTP {ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:16957983}; CC Vmax=5.9 umol/min/ug enzyme with UDP as substrate for the forward CC reaction (in the presence of 1mM free Mg(2+) at 30 degrees Celsius CC and pH 8.0); CC Vmax=5.1 umol/min/ug enzyme with UTP as substrate for the reverse CC reaction (in the presence of 1mM free Mg(2+) at 30 degrees Celsius CC and pH 8.0); CC -!- SUBUNIT: Homohexamer and homotetramer. Interacts with TOM40 CC preferentially in an unfolded, unphosphorylated form. CC {ECO:0000269|PubMed:12472466, ECO:0000269|PubMed:1659321, CC ECO:0000269|PubMed:4576138}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12472466}. CC Mitochondrion intermembrane space {ECO:0000269|PubMed:12472466, CC ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289}. CC Note=Localizes predominantly to the cytoplasm. A small fraction is CC present in the mitochondrial intermembrane space. CC -!- PTM: The N-terminus is blocked. CC -!- MISCELLANEOUS: Present with 7130 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the NDK 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; D13562; BAA02758.1; -; Genomic_DNA. DR EMBL; X75780; CAA53407.1; -; Genomic_DNA. DR EMBL; Z28067; CAA81904.1; -; Genomic_DNA. DR EMBL; AY558263; AAS56589.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09090.1; -; Genomic_DNA. DR PIR; S37889; S37889. DR RefSeq; NP_012856.1; NM_001179633.1. DR PDB; 3B54; X-ray; 3.10 A; A/B=1-153. DR AlphaFoldDB; P36010; -. DR SMR; P36010; -. DR BioGRID; 34067; 145. DR DIP; DIP-1969N; -. DR FunCoup; P36010; 1129. DR IntAct; P36010; 47. DR MINT; P36010; -. DR STRING; 4932.YKL067W; -. DR iPTMnet; P36010; -. DR PaxDb; 4932-YKL067W; -. DR PeptideAtlas; P36010; -. DR EnsemblFungi; YKL067W_mRNA; YKL067W; YKL067W. DR GeneID; 853798; -. DR KEGG; sce:YKL067W; -. DR AGR; SGD:S000001550; -. DR SGD; S000001550; YNK1. DR VEuPathDB; FungiDB:YKL067W; -. DR eggNOG; KOG0888; Eukaryota. DR HOGENOM; CLU_060216_6_3_1; -. DR InParanoid; P36010; -. DR OMA; QHYGEHK; -. DR OrthoDB; 2162449at2759; -. DR BioCyc; MetaCyc:YKL067W-MONOMER; -. DR BioCyc; YEAST:YKL067W-MONOMER; -. DR Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR Reactome; R-SCE-9748787; Azathioprine ADME. DR Reactome; R-SCE-9755088; Ribavirin ADME. DR SABIO-RK; P36010; -. DR BioGRID-ORCS; 853798; 2 hits in 10 CRISPR screens. DR CD-CODE; E03F929F; Stress granule. DR EvolutionaryTrace; P36010; -. DR PRO; PR:P36010; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P36010; protein. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB. DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro. DR GO; GO:0006974; P:DNA damage response; IMP:SGD. DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IDA:UniProtKB. DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro. DR CDD; cd04413; NDPk_I; 1. DR FunFam; 3.30.70.141:FF:000002; Nucleoside diphosphate kinase; 1. DR Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 1. DR HAMAP; MF_00451; NDP_kinase; 1. DR InterPro; IPR034907; NDK-like_dom. DR InterPro; IPR036850; NDK-like_dom_sf. DR InterPro; IPR001564; Nucleoside_diP_kinase. DR InterPro; IPR023005; Nucleoside_diP_kinase_AS. DR NCBIfam; NF001908; PRK00668.1; 1. DR PANTHER; PTHR11349; NUCLEOSIDE DIPHOSPHATE KINASE; 1. DR Pfam; PF00334; NDK; 1. DR PRINTS; PR01243; NUCDPKINASE. DR SMART; SM00562; NDK; 1. DR SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1. DR PROSITE; PS00469; NDPK; 1. DR PROSITE; PS51374; NDPK_LIKE; 1. DR PDBsum; 3B54; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA repair; Kinase; KW Magnesium; Metal-binding; Mitochondrion; Nucleotide metabolism; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1..153 FT /note="Nucleoside diphosphate kinase" FT /id="PRO_0000137153" FT ACT_SITE 119 FT /note="Pros-phosphohistidine intermediate" FT /evidence="ECO:0000250|UniProtKB:P22392" FT BINDING 13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P22392" FT BINDING 61 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P22392" FT BINDING 89 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P22392" FT BINDING 95 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P22392" FT BINDING 106 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P22392" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P22392" FT MOD_RES 95 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18407956" FT STRAND 7..12 FT /evidence="ECO:0007829|PDB:3B54" FT HELIX 14..19 FT /evidence="ECO:0007829|PDB:3B54" FT HELIX 22..32 FT /evidence="ECO:0007829|PDB:3B54" FT STRAND 35..42 FT /evidence="ECO:0007829|PDB:3B54" FT HELIX 43..45 FT /evidence="ECO:0007829|PDB:3B54" FT HELIX 46..52 FT /evidence="ECO:0007829|PDB:3B54" FT HELIX 63..70 FT /evidence="ECO:0007829|PDB:3B54" FT STRAND 74..81 FT /evidence="ECO:0007829|PDB:3B54" FT HELIX 84..92 FT /evidence="ECO:0007829|PDB:3B54" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:3B54" FT HELIX 105..109 FT /evidence="ECO:0007829|PDB:3B54" FT STRAND 117..120 FT /evidence="ECO:0007829|PDB:3B54" FT HELIX 124..134 FT /evidence="ECO:0007829|PDB:3B54" FT HELIX 148..151 FT /evidence="ECO:0007829|PDB:3B54" SQ SEQUENCE 153 AA; 17167 MW; BE37ACED90A44D00 CRC64; MSSQTERTFI AVKPDGVQRG LVSQILSRFE KKGYKLVAIK LVKADDKLLE QHYAEHVGKP FFPKMVSFMK SGPILATVWE GKDVVRQGRT ILGATNPLGS APGTIRGDFG IDLGRNVCHG SDSVDSAERE INLWFKKEEL VDWESNQAKW IYE //