NDK_YEAST
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 03-AUG-2022, entry version 184.
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; 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}.
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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 PDBsum; 3B54; -.
DR AlphaFoldDB; P36010; -.
DR SMR; P36010; -.
DR BioGRID; 34067; 126.
DR DIP; DIP-1969N; -.
DR IntAct; P36010; 37.
DR MINT; P36010; -.
DR STRING; 4932.YKL067W; -.
DR iPTMnet; P36010; -.
DR UCD-2DPAGE; P36010; -.
DR MaxQB; P36010; -.
DR PaxDb; P36010; -.
DR PRIDE; P36010; -.
DR EnsemblFungi; YKL067W_mRNA; YKL067W; YKL067W.
DR GeneID; 853798; -.
DR KEGG; sce:YKL067W; -.
DR SGD; S000001550; YNK1.
DR VEuPathDB; FungiDB:YKL067W; -.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000164818; -.
DR HOGENOM; CLU_060216_6_3_1; -.
DR InParanoid; P36010; -.
DR OMA; ALWFGEQ; -.
DR BioCyc; MetaCyc:YKL067W-MON; -.
DR BioCyc; YEAST:YKL067W-MON; -.
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 SABIO-RK; P36010; -.
DR ChiTaRS; YNK1; yeast.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IDA:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.141; -; 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 Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00562; NDK; 1.
DR SUPFAM; SSF54919; SSF54919; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
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 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
