ID THIO_ECOLI Reviewed; 109 AA. AC P0AA25; P00274; P76750; Q2M889; Q47674; Q8XAT2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 165. DE RecName: Full=Thioredoxin 1; DE Short=Trx-1; GN Name=trxA; Synonyms=fipA, tsnC; OrderedLocusNames=b3781, JW5856; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6098320; DOI=10.1007/bf01116889; RA Hoeoeg J.-O., von Bahr-Lindstroem H., Josephson S., Wallace B.J., RA Kushner S.R., Joernvall H., Holmgren A.; RT "Nucleotide sequence of the thioredoxin gene from Escherichia coli."; RL Biosci. Rep. 4:917-923(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6099324; DOI=10.1016/0378-1119(84)90015-5; RA Wallace B.J., Kushner S.R.; RT "Genetic and physical analysis of the thioredoxin (trxA) gene of RT Escherichia coli K-12."; RL Gene 32:399-408(1984). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3891733; DOI=10.1128/jb.163.1.311-316.1985; RA Lim C.-J., Geraghty D., Fuchs J.A.; RT "Cloning and nucleotide sequence of the trxA gene of Escherichia coli RT K-12."; RL J. Bacteriol. 163:311-316(1985). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Wallace B.J., Zownir O., Kushner S.R.; RT "Physical analysis of the thioredoxin gene from Escherichia coli K-12."; RL (In) Holmgren A. (eds.); RL Thioredoxin and glutaredoxin systems, structure and function, pp.11-19, RL Raven Press, New York (1986). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=1379743; DOI=10.1126/science.1379743; RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.; RT "Analysis of the Escherichia coli genome: DNA sequence of the region from RT 84.5 to 86.5 minutes."; RL Science 257:771-778(1992). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [8] RP PROTEIN SEQUENCE OF 2-109. RC STRAIN=B; RX PubMed=4883076; DOI=10.1111/j.1432-1033.1968.tb00470.x; RA Holmgren A.; RT "Thioredoxin. 6. The amino acid sequence of the protein from Escherichia RT coli B."; RL Eur. J. Biochem. 6:475-484(1968). RN [9] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=1094461; DOI=10.1073/pnas.72.6.2305; RA Holmgren A., Soederberg B.-O., Eklund H., Braenden C.-I.; RT "Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8-A RT resolution."; RL Proc. Natl. Acad. Sci. U.S.A. 72:2305-2309(1975). RN [12] RP X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS). RX PubMed=4616096; DOI=10.1016/0022-2836(74)90262-9; RA Soederberg B.-O., Holmgren A., Braenden C.-I.; RT "Structure of oxidized thioredoxin to 4 with 5-A resolution."; RL J. Mol. Biol. 90:143-152(1974). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS). RX PubMed=2181145; DOI=10.1016/0022-2836(90)90313-b; RA Katti S.K., le Master D.M., Eklund H.; RT "Crystal structure of thioredoxin from Escherichia coli at 1.68-A RT resolution."; RL J. Mol. Biol. 212:167-184(1990). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-37. RX PubMed=8098620; DOI=10.1021/bi00070a017; RA Nikkola M., Gleason F.K., Fuchs J.A., Eklund H.; RT "Crystal structure analysis of a mutant Escherichia coli thioredoxin in RT which lysine 36 is replaced by glutamic acid."; RL Biochemistry 32:5093-5098(1993). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DISULFIDE BOND. RX PubMed=10489448; DOI=10.1107/s0907444999008756; RA Schultz L.W., Chivers P.T., Raines R.T.; RT "The CXXC motif: crystal structure of an active-site variant of Escherichia RT coli thioredoxin."; RL Acta Crystallogr. D 55:1533-1538(1999). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXB. RX PubMed=10947986; DOI=10.1126/science.289.5482.1190; RA Lennon B.W., Williams C.H. Jr., Ludwig M.L.; RT "Twists in catalysis: alternating conformations of Escherichia coli RT thioredoxin reductase."; RL Science 289:1190-1194(2000). RN [17] RP STRUCTURE BY NMR. RX PubMed=2193685; DOI=10.1021/bi00469a016; RA Dyson H.J., Gippert G.P., Case D.A., Holmgren A., Wright P.E.; RT "Three-dimensional solution structure of the reduced form of Escherichia RT coli thioredoxin determined by nuclear magnetic resonance spectroscopy."; RL Biochemistry 29:4129-4136(1990). RN [18] RP STRUCTURE BY NMR. RX PubMed=7812718; DOI=10.1016/s0969-2126(94)00086-7; RA Jeng M.F., Campbell A.P., Begley T., Holmgren A., Case D.A., Wright P.E., RA Dyson H.J.; RT "High-resolution solution structures of oxidized and reduced Escherichia RT coli thioredoxin."; RL Structure 2:853-868(1994). CC -!- FUNCTION: Participates in various redox reactions through the CC reversible oxidation of its active center dithiol to a disulfide and CC catalyzes dithiol-disulfide exchange reactions. CC -!- SUBUNIT: Monomer. Interacts with bacteriophage T3 DNA polymerase. CC {ECO:0000269|PubMed:10947986}. CC -!- INTERACTION: CC P0AA25; P0A9P4: trxB; NbExp=2; IntAct=EBI-368542, EBI-1029826; CC P0AA25; P00581: 5; Xeno; NbExp=2; IntAct=EBI-368542, EBI-8664634; CC P0AA25; O22160: At2g44920; Xeno; NbExp=2; IntAct=EBI-368542, EBI-2895776; CC P0AA25; Q9SCY2: FKBP13; Xeno; NbExp=2; IntAct=EBI-368542, EBI-2895757; CC P0AA25; Q9LXX5: PPD6; Xeno; NbExp=2; IntAct=EBI-368542, EBI-2895738; CC P0AA25; Q9LU86: PRXQ; Xeno; NbExp=2; IntAct=EBI-368542, EBI-540311; CC P0AA25; P23321: PSBO1; Xeno; NbExp=2; IntAct=EBI-368542, EBI-449414; CC P0AA25; Q9S841: PSBO2; Xeno; NbExp=2; IntAct=EBI-368542, EBI-449424; CC P0AA25; P81760: TL17; Xeno; NbExp=2; IntAct=EBI-368542, EBI-449573; CC P0AA25; P82281: TL29; Xeno; NbExp=2; IntAct=EBI-368542, EBI-2895799; CC P0AA25; Q39249: VDE1; Xeno; NbExp=2; IntAct=EBI-368542, EBI-2895666; CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA24534.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAA67582.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; M26133; AAA24693.1; -; Genomic_DNA. DR EMBL; K02845; AAA24534.1; ALT_INIT; Genomic_DNA. DR EMBL; M10424; AAA24533.1; -; Genomic_DNA. DR EMBL; M54881; AAA24696.1; -; Genomic_DNA. DR EMBL; M12779; AAA24694.1; -; Genomic_DNA. DR EMBL; M87049; AAA67582.1; ALT_INIT; Genomic_DNA. DR EMBL; U00096; AAC76786.2; -; Genomic_DNA. DR EMBL; AP009048; BAE77517.1; -; Genomic_DNA. DR PIR; A91519; TXEC. DR RefSeq; NP_418228.2; NC_000913.3. DR RefSeq; WP_001280776.1; NZ_STEB01000021.1. DR PDB; 1F6M; X-ray; 2.95 A; C/D/G/H=2-109. DR PDB; 1KEB; X-ray; 1.80 A; A/B=2-109. DR PDB; 1M7T; NMR; -; A=32-108. DR PDB; 1OAZ; X-ray; 2.78 A; A/B=2-109. DR PDB; 1SKR; X-ray; 2.40 A; B=2-109. DR PDB; 1SKS; X-ray; 2.30 A; B=2-109. DR PDB; 1SKW; X-ray; 2.30 A; B=2-109. DR PDB; 1SL0; X-ray; 3.20 A; B/D=2-109. DR PDB; 1SL1; X-ray; 2.20 A; B=2-109. DR PDB; 1SL2; X-ray; 2.30 A; B=2-109. DR PDB; 1SRX; X-ray; 2.80 A; A=2-109. DR PDB; 1T7P; X-ray; 2.20 A; B=2-109. DR PDB; 1T8E; X-ray; 2.54 A; B=2-109. DR PDB; 1THO; X-ray; 2.30 A; A=2-109. DR PDB; 1TK0; X-ray; 2.30 A; B=2-109. DR PDB; 1TK5; X-ray; 2.20 A; B=2-109. DR PDB; 1TK8; X-ray; 2.50 A; B=2-109. DR PDB; 1TKD; X-ray; 2.49 A; B=2-109. DR PDB; 1TXX; X-ray; 2.20 A; A=2-109. DR PDB; 1X9M; X-ray; 2.10 A; B=2-109. DR PDB; 1X9S; X-ray; 2.70 A; B=2-109. DR PDB; 1X9W; X-ray; 2.30 A; B=2-109. DR PDB; 1XOA; NMR; -; A=2-109. DR PDB; 1XOB; NMR; -; A=2-109. DR PDB; 1ZCP; X-ray; 2.30 A; A/B/C/D=2-109. DR PDB; 1ZYQ; X-ray; 2.70 A; B=2-109. DR PDB; 1ZZY; X-ray; 2.50 A; A/B=2-109. DR PDB; 2AJQ; X-ray; 2.60 A; B/I=2-109. DR PDB; 2BTO; X-ray; 2.50 A; T=2-109. DR PDB; 2EIO; X-ray; 2.60 A; A/B/C/D=2-109. DR PDB; 2EIQ; X-ray; 1.90 A; A/B=2-109. DR PDB; 2EIR; X-ray; 2.50 A; A/B/C/D=2-109. DR PDB; 2FCH; X-ray; 2.60 A; A/B/C/D/E/F/G=2-109. DR PDB; 2FD3; X-ray; 2.45 A; A/B=2-109. DR PDB; 2H6X; X-ray; 2.60 A; A/B=2-109. DR PDB; 2H6Y; X-ray; 2.40 A; A/B=2-109. DR PDB; 2H6Z; X-ray; 2.25 A; A/B=2-109. DR PDB; 2H70; X-ray; 2.70 A; A/B=2-109. DR PDB; 2H71; X-ray; 2.20 A; A/B=2-109. DR PDB; 2H72; X-ray; 2.25 A; A/B=2-109. DR PDB; 2H73; X-ray; 2.45 A; A/B=2-109. DR PDB; 2H74; X-ray; 2.40 A; A/B=4-109. DR PDB; 2H75; X-ray; 2.20 A; A/B=2-109. DR PDB; 2H76; X-ray; 2.25 A; A/B=2-109. DR PDB; 2O8V; X-ray; 3.00 A; B=2-109. DR PDB; 2TIR; X-ray; 2.00 A; A=2-109. DR PDB; 2TRX; X-ray; 1.68 A; A/B=2-109. DR PDB; 3DYR; X-ray; 2.00 A; A/B=2-109. DR PDB; 4HU7; X-ray; 1.40 A; A/B=2-109. DR PDB; 4HU9; X-ray; 1.55 A; A=2-109. DR PDB; 4HUA; X-ray; 1.10 A; A=2-109. DR PDB; 4X43; X-ray; 1.65 A; A/B/C=2-109. DR PDB; 5HR0; X-ray; 1.31 A; A/B=1-109. DR PDB; 5HR1; X-ray; 2.14 A; A/B/C/D/E/F/G=1-107. DR PDB; 5HR2; X-ray; 1.20 A; A=1-109. DR PDB; 5HR3; X-ray; 1.10 A; A/B=1-109. DR PDB; 5XOC; X-ray; 2.40 A; B=2-109. DR PDB; 6GD1; X-ray; 2.01 A; A/B=1-109. DR PDB; 6GDG; EM; 4.11 A; A=2-109. DR PDB; 6H7J; X-ray; 2.80 A; E/F=2-109. DR PDB; 6H7L; X-ray; 2.70 A; E/F=2-109. DR PDB; 6H7M; X-ray; 2.76 A; E/F=2-109. DR PDB; 6H7N; X-ray; 2.50 A; E/F=2-109. DR PDB; 6H7O; X-ray; 2.80 A; E/F=2-109. DR PDB; 6IBL; X-ray; 2.70 A; A/B=2-109. DR PDB; 6LUR; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-109. DR PDB; 6N7W; EM; 4.50 A; I=1-109. DR PDB; 6P7E; X-ray; 3.00 A; E/F/G/H=1-109. DR PDB; 6Y4Y; X-ray; 1.75 A; A/B/C/D=1-109. DR PDB; 6Y4Z; X-ray; 1.90 A; A/B/C/D=1-109. DR PDB; 6YEV; X-ray; 2.94 A; E/F/G=1-109. DR PDB; 7SCD; X-ray; 2.90 A; A=1-108. DR PDB; 7SCE; X-ray; 2.75 A; A=1-108. DR PDB; 8KGZ; X-ray; 2.21 A; A/B=1-109. DR PDBsum; 1F6M; -. DR PDBsum; 1KEB; -. DR PDBsum; 1M7T; -. DR PDBsum; 1OAZ; -. DR PDBsum; 1SKR; -. DR PDBsum; 1SKS; -. DR PDBsum; 1SKW; -. DR PDBsum; 1SL0; -. DR PDBsum; 1SL1; -. DR PDBsum; 1SL2; -. DR PDBsum; 1SRX; -. DR PDBsum; 1T7P; -. DR PDBsum; 1T8E; -. DR PDBsum; 1THO; -. DR PDBsum; 1TK0; -. DR PDBsum; 1TK5; -. DR PDBsum; 1TK8; -. DR PDBsum; 1TKD; -. DR PDBsum; 1TXX; -. DR PDBsum; 1X9M; -. DR PDBsum; 1X9S; -. DR PDBsum; 1X9W; -. DR PDBsum; 1XOA; -. DR PDBsum; 1XOB; -. DR PDBsum; 1ZCP; -. DR PDBsum; 1ZYQ; -. DR PDBsum; 1ZZY; -. DR PDBsum; 2AJQ; -. DR PDBsum; 2BTO; -. DR PDBsum; 2EIO; -. DR PDBsum; 2EIQ; -. DR PDBsum; 2EIR; -. DR PDBsum; 2FCH; -. DR PDBsum; 2FD3; -. DR PDBsum; 2H6X; -. DR PDBsum; 2H6Y; -. DR PDBsum; 2H6Z; -. DR PDBsum; 2H70; -. DR PDBsum; 2H71; -. DR PDBsum; 2H72; -. DR PDBsum; 2H73; -. DR PDBsum; 2H74; -. DR PDBsum; 2H75; -. DR PDBsum; 2H76; -. DR PDBsum; 2O8V; -. DR PDBsum; 2TIR; -. DR PDBsum; 2TRX; -. DR PDBsum; 3DYR; -. DR PDBsum; 4HU7; -. DR PDBsum; 4HU9; -. DR PDBsum; 4HUA; -. DR PDBsum; 4X43; -. DR PDBsum; 5HR0; -. DR PDBsum; 5HR1; -. DR PDBsum; 5HR2; -. DR PDBsum; 5HR3; -. DR PDBsum; 5XOC; -. DR PDBsum; 6GD1; -. DR PDBsum; 6GDG; -. DR PDBsum; 6H7J; -. DR PDBsum; 6H7L; -. DR PDBsum; 6H7M; -. DR PDBsum; 6H7N; -. DR PDBsum; 6H7O; -. DR PDBsum; 6IBL; -. DR PDBsum; 6LUR; -. DR PDBsum; 6N7W; -. DR PDBsum; 6P7E; -. DR PDBsum; 6Y4Y; -. DR PDBsum; 6Y4Z; -. DR PDBsum; 6YEV; -. DR PDBsum; 7SCD; -. DR PDBsum; 7SCE; -. DR PDBsum; 8KGZ; -. DR AlphaFoldDB; P0AA25; -. DR BMRB; P0AA25; -. DR SASBDB; P0AA25; -. DR SMR; P0AA25; -. DR BioGRID; 4263316; 300. DR BioGRID; 852588; 8. DR DIP; DIP-31856N; -. DR IntAct; P0AA25; 99. DR MINT; P0AA25; -. DR STRING; 511145.b3781; -. DR CarbonylDB; P0AA25; -. DR iPTMnet; P0AA25; -. DR jPOST; P0AA25; -. DR PaxDb; 511145-b3781; -. DR EnsemblBacteria; AAC76786; AAC76786; b3781. DR GeneID; 83648940; -. DR GeneID; 948289; -. DR KEGG; ecj:JW5856; -. DR KEGG; eco:b3781; -. DR PATRIC; fig|511145.12.peg.3896; -. DR EchoBASE; EB1024; -. DR eggNOG; COG3118; Bacteria. DR HOGENOM; CLU_090389_10_2_6; -. DR InParanoid; P0AA25; -. DR OMA; QVGVAPK; -. DR OrthoDB; 9790390at2; -. DR PhylomeDB; P0AA25; -. DR BioCyc; EcoCyc:RED-THIOREDOXIN-MONOMER; -. DR BioCyc; MetaCyc:RED-THIOREDOXIN-MONOMER; -. DR EvolutionaryTrace; P0AA25; -. DR PRO; PR:P0AA25; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IDA:FlyBase. DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:EcoCyc. DR GO; GO:0045454; P:cell redox homeostasis; IMP:EcoCyc. DR CDD; cd02947; TRX_family; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR005746; Thioredoxin. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR NCBIfam; TIGR01068; thioredoxin; 1. DR PANTHER; PTHR45663; GEO12009P1; 1. DR PANTHER; PTHR45663:SF11; GEO12009P1; 1. DR Pfam; PF00085; Thioredoxin; 1. DR PIRSF; PIRSF000077; Thioredoxin; 1. DR PRINTS; PR00421; THIOREDOXIN. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. DR SWISS-2DPAGE; P0AA25; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Disulfide bond; KW Electron transport; Host-virus interaction; Redox-active center; KW Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:4883076" FT CHAIN 2..109 FT /note="Thioredoxin 1" FT /id="PRO_0000120096" FT DOMAIN 2..109 FT /note="Thioredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT ACT_SITE 33 FT /note="Nucleophile" FT ACT_SITE 36 FT /note="Nucleophile" FT SITE 27 FT /note="Deprotonates C-terminal active site Cys" FT SITE 34 FT /note="Contributes to redox potential value" FT SITE 35 FT /note="Contributes to redox potential value" FT MOD_RES 70 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT DISULFID 33..36 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691, FT ECO:0000269|PubMed:10489448" FT CONFLICT 72..73 FT /note="GI -> IG (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 88 FT /note="A -> AS (in Ref. 5; AAA24696)" FT /evidence="ECO:0000305" FT STRAND 5..8 FT /evidence="ECO:0007829|PDB:4HUA" FT TURN 10..12 FT /evidence="ECO:0007829|PDB:4HUA" FT HELIX 13..16 FT /evidence="ECO:0007829|PDB:4HUA" FT TURN 17..19 FT /evidence="ECO:0007829|PDB:4HUA" FT STRAND 22..29 FT /evidence="ECO:0007829|PDB:4HUA" FT HELIX 34..49 FT /evidence="ECO:0007829|PDB:4HUA" FT TURN 50..53 FT /evidence="ECO:0007829|PDB:4HUA" FT STRAND 55..60 FT /evidence="ECO:0007829|PDB:4HUA" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:4HUA" FT HELIX 65..70 FT /evidence="ECO:0007829|PDB:4HUA" FT STRAND 75..83 FT /evidence="ECO:0007829|PDB:4HUA" FT STRAND 86..93 FT /evidence="ECO:0007829|PDB:4HUA" FT HELIX 97..105 FT /evidence="ECO:0007829|PDB:4HUA" SQ SEQUENCE 109 AA; 11807 MW; EF5933EA29668EE9 CRC64; MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY QGKLTVAKLN IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL KEFLDANLA //