ID TRXR_PLAF7 Reviewed; 617 AA. AC P61076; A0A143ZVU1; Q71G50; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JAN-2010, sequence version 2. DT 02-SEP-2026, entry version 153. DE RecName: Full=Thioredoxin reductase {ECO:0000303|PubMed:9368022}; DE Short=PfTrxR {ECO:0000303|PubMed:9368022}; DE EC=1.8.1.9 {ECO:0000269|PubMed:11013257, ECO:0000269|PubMed:16910770, ECO:0000269|PubMed:22889878, ECO:0000269|PubMed:23845423, ECO:0000269|PubMed:9368022}; DE Flags: Precursor; GN Name=TRXR {ECO:0000303|PubMed:9368022}; GN ORFNames=PF3D7_0923800, PFI1170c; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Laverania. OX NCBI_TaxID=36329; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16910770; DOI=10.1089/ars.2006.8.1227; RA Nickel C., Rahlfs S., Deponte M., Koncarevic S., Becker K.; RT "Thioredoxin networks in the malarial parasite Plasmodium falciparum."; RL Antioxid. Redox Signal. 8:1227-1239(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3D7; RX PubMed=12368864; DOI=10.1038/nature01097; RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D., RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S., RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M., RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A., RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I., RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J., RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.; RT "Genome sequence of the human malaria parasite Plasmodium falciparum."; RL Nature 419:498-511(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3D7; RX PubMed=12368867; DOI=10.1038/nature01095; RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D., RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K., RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T., RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M., RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A., RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H., RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D., RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N., RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P., RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A., RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M., RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S., RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R., RA Sulston J.E., Craig A., Newbold C., Barrell B.G.; RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13."; RL Nature 419:527-531(2002). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, RP MUTAGENESIS OF CYS-164; CYS-169 AND HIS-585, AND ACTIVE SITE. RX PubMed=9368022; DOI=10.1074/jbc.272.47.29584; RA Gilberger T.W., Walter R.D., Mueller S.; RT "Identification and characterization of the functional amino acids at the RT active site of the large thioredoxin reductase from Plasmodium RT falciparum."; RL J. Biol. Chem. 272:29584-29589(1997). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=11013257; DOI=10.1074/jbc.m007633200; RA Kanzok S.M., Schirmer R.H., Turbachova I., Iozef R., Becker K.; RT "The thioredoxin system of the malaria parasite Plasmodium falciparum. RT Glutathione reduction revisited."; RL J. Biol. Chem. 275:40180-40186(2000). RN [6] RP SUBCELLULAR LOCATION, AND ALTERNATIVE INITIATION. RX PubMed=21203490; DOI=10.1371/journal.ppat.1001242; RA Kehr S., Sturm N., Rahlfs S., Przyborski J.M., Becker K.; RT "Compartmentation of redox metabolism in malaria parasites."; RL PLoS Pathog. 6:e1001242-e1001242(2010). RN [7] {ECO:0007744|PDB:4B1B} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 77-617 IN COMPLEX WITH FAD, RP CATALYTIC ACTIVITY, COFACTOR, AND DISULFIDE BOND. RX PubMed=22889878; DOI=10.1016/j.bbrc.2012.07.156; RA Boumis G., Giardina G., Angelucci F., Bellelli A., Brunori M., RA Dimastrogiovanni D., Saccoccia F., Miele A.E.; RT "Crystal structure of Plasmodium falciparum thioredoxin reductase, a RT validated drug target."; RL Biochem. Biophys. Res. Commun. 425:806-811(2012). RN [8] {ECO:0007744|PDB:4J56, ECO:0007744|PDB:4J57} RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 77-617 OF MUTANT SER-611 AND RP MUTANT SER-616 IN COMPLEX WITH FAD AND TRX1, FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS, AND RP MUTAGENESIS OF PHE-219; GLU-450; 514-HIS--LEU-528; HIS-514 AND ASP-529. RX PubMed=23845423; DOI=10.1016/j.jmb.2013.06.037; RA Fritz-Wolf K., Jortzik E., Stumpf M., Preuss J., Iozef R., Rahlfs S., RA Becker K.; RT "Crystal structure of the Plasmodium falciparum thioredoxin reductase- RT thioredoxin complex."; RL J. Mol. Biol. 425:3446-3460(2013). CC -!- FUNCTION: Catalyzes the transfer of electrons from NADPH to CC thioredoxins TRX1, TRX2 and TRX3, which in turn act as reductants of CC disulfide containing proteins (PubMed:11013257, PubMed:16910770, CC PubMed:23845423, PubMed:9368022). Able to reduce nitroglutathione CC (GSNO), a compound involved in the transport of nitric oxide (NO); CC however, TRX1 is more efficient in reducing GSNO (PubMed:11013257). Has CC no catalytic activity towards oxidized glutathione (GSSG) CC (PubMed:11013257). {ECO:0000269|PubMed:11013257, CC ECO:0000269|PubMed:16910770, ECO:0000269|PubMed:23845423, CC ECO:0000269|PubMed:9368022}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + CC NADPH + H(+); Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA- CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9; CC Evidence={ECO:0000269|PubMed:11013257, ECO:0000269|PubMed:16910770, CC ECO:0000269|PubMed:22889878, ECO:0000269|PubMed:23845423, CC ECO:0000269|PubMed:9368022}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347; CC Evidence={ECO:0000269|PubMed:11013257, ECO:0000269|PubMed:23845423, CC ECO:0000269|PubMed:9368022}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:23845423, ECO:0000269|PubMed:9368022}; CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:22889878, CC ECO:0000269|PubMed:23845423}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=8.94 uM for TRX1 (at pH 7.4) {ECO:0000269|PubMed:23845423}; CC KM=10.4 uM for TRX1 (at 25 degrees Celsius and pH 7.4) CC {ECO:0000269|PubMed:11013257}; CC KM=35 uM for nitrosoglutathione (GSNO) (at 25 degrees Celsius and pH CC 7.4) {ECO:0000269|PubMed:11013257}; CC KM=9 uM for NADPH (at 20 degrees Celsius, pH 7.4 and the model CC substrate 5,5'-dithiobis (2-nitrobenzoate) (DTNB) as cosubstrate) CC {ECO:0000269|PubMed:9368022}; CC KM=2.8 uM for NADPH (at 25 degrees Celsius, pH 7.4 and TRX1 as CC cosubstrate) {ECO:0000269|PubMed:11013257}; CC Vmax=50.8 umol/min/mg enzyme toward TRX1 (at 25 degrees Celsius and CC pH 7.4) {ECO:0000269|PubMed:11013257}; CC Vmax=29.8 umol/min/mg enzyme (at pH 7.4) CC {ECO:0000269|PubMed:23845423}; CC Note=kcat is 1725 min(-1) with TRX1 as substrate (at pH 7.4) CC (PubMed:23845423). kcat is 51.7 sec(-1) with TRX1 as substrate (at 25 CC degrees Celsius and at pH 7.4) (PubMed:23845423). kcat is 275.2 CC min(-1) with NADPH and DTNB as substrates (at pH 7.4) CC (PubMed:9368022). kcat is 48.3 sec(-1) with NADPH and TRX1 as CC substrates (at 25 degrees Celsius and at pH 7.4) (PubMed:11013257). CC kcat is 9.4 min(-1) with nitrosoglutathione (GSNO) as substrates (at CC 25 degrees Celsius and at pH 7.4) (PubMed:11013257). CC {ECO:0000269|PubMed:11013257, ECO:0000269|PubMed:23845423, CC ECO:0000269|PubMed:9368022}; CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:23845423}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion CC {ECO:0000269|PubMed:21203490}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm CC {ECO:0000269|PubMed:21203490}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; CC IsoId=P61076-1; Sequence=Displayed; CC Name=2; Synonyms=TrxR2 {ECO:0000303|PubMed:16910770}; CC IsoId=P61076-2; Sequence=VSP_061463; CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met- CC 77 of isoform 1. {ECO:0000269|PubMed:21203490}. CC -!- MISCELLANEOUS: In Plasmodium, the C-terminal redox center, which acts CC as the active site, is formed by two cysteines while in mammalian TRXR CC this redox center is composed of a cysteine-selenocysteine active site. CC {ECO:0000305|PubMed:22889878}. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase 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; AF508128; AAQ07981.1; -; mRNA. DR EMBL; AL844508; CAX64232.1; -; Genomic_DNA. DR EMBL; AL844508; CZT62537.1; -; Genomic_DNA. DR RefSeq; XP_002808951.1; XM_002808905.1. [P61076-1] DR PDB; 4B1B; X-ray; 2.90 A; A/B=78-617. DR PDB; 4J56; X-ray; 2.37 A; A/B/C/D=77-617. DR PDB; 4J57; X-ray; 2.50 A; A/B=77-617. DR AlphaFoldDB; P61076; -. DR SMR; P61076; -. DR FunCoup; P61076; 195. DR STRING; 36329.A0A143ZVU1; -. DR BindingDB; P61076; -. DR ChEMBL; CHEMBL4547; -. DR SwissPalm; P61076; -. DR PaxDb; 36329-A0A143ZVU1; -. DR EnsemblProtists; PF3D7_0923800.1; PF3D7_0923800.1-p1; PF3D7_0923800. DR KEGG; pfa:PF3D7_0923800.1; -. DR VEuPathDB; PlasmoDB:PF3D7_0923800; -. DR HOGENOM; CLU_016755_2_4_1; -. DR InParanoid; P61076; -. DR OMA; NYHKLAD; -. DR OrthoDB; 5956163at2759; -. DR PhylomeDB; P61076; -. DR Reactome; R-PFA-5263617; Metabolism of ingested MeSeO2H into MeSeH. DR EvolutionaryTrace; P61076; -. DR Proteomes; UP000001450; Chromosome 9. DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB. DR GO; GO:0005739; C:mitochondrion; IDA:GeneDB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB. DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADPH) activity; IDA:UniProtKB. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR FunFam; 3.50.50.60:FF:000190; Thioredoxin reductase; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf. DR InterPro; IPR046952; GSHR/TRXR-like. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase. DR NCBIfam; TIGR01438; TGR; 1. DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1. DR PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. DR PDBsum; 4B1B; -. DR PDBsum; 4J56; -. DR PDBsum; 4J57; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Cytoplasm; Disulfide bond; FAD; KW Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Redox-active center; KW Reference proteome; Transit peptide. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000305|PubMed:21203490" FT CHAIN ?..617 FT /note="Thioredoxin reductase" FT /id="PRO_0000067987" FT REGION 514..528 FT /note="Loop important for the interaction with TRX1" FT /evidence="ECO:0000269|PubMed:23845423" FT ACT_SITE 585 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:9368022" FT BINDING 127..128 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:22889878, FT ECO:0000269|PubMed:23845423, ECO:0007744|PDB:4B1B, FT ECO:0007744|PDB:4J56, ECO:0007744|PDB:4J57" FT BINDING 147..150 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:22889878, FT ECO:0000269|PubMed:23845423, ECO:0007744|PDB:4B1B, FT ECO:0007744|PDB:4J56, ECO:0007744|PDB:4J57" FT BINDING 163..164 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:22889878, FT ECO:0000269|PubMed:23845423, ECO:0007744|PDB:4B1B, FT ECO:0007744|PDB:4J56, ECO:0007744|PDB:4J57" FT BINDING 168..172 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:22889878, FT ECO:0000269|PubMed:23845423, ECO:0007744|PDB:4B1B, FT ECO:0007744|PDB:4J56, ECO:0007744|PDB:4J57" FT BINDING 237 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:22889878, FT ECO:0000269|PubMed:23845423, ECO:0007744|PDB:4B1B, FT ECO:0007744|PDB:4J56, ECO:0007744|PDB:4J57" FT BINDING 433 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:22889878, FT ECO:0000269|PubMed:23845423, ECO:0007744|PDB:4B1B, FT ECO:0007744|PDB:4J56, ECO:0007744|PDB:4J57" FT BINDING 440..442 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:22889878, FT ECO:0000269|PubMed:23845423, ECO:0007744|PDB:4B1B, FT ECO:0007744|PDB:4J56, ECO:0007744|PDB:4J57" FT BINDING 585 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000269|PubMed:23845423, FT ECO:0007744|PDB:4J56, ECO:0007744|PDB:4J57" FT DISULFID 164..169 FT /note="Redox-active" FT /evidence="ECO:0000269|PubMed:22889878, FT ECO:0000269|PubMed:23845423, ECO:0000269|PubMed:9368022, FT ECO:0007744|PDB:4B1B, ECO:0007744|PDB:4J56, FT ECO:0007744|PDB:4J57" FT DISULFID 611..616 FT /note="Redox-active" FT /evidence="ECO:0000269|PubMed:23845423, FT ECO:0007744|PDB:4J56, ECO:0007744|PDB:4J57" FT VAR_SEQ 1..76 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_061463" FT MUTAGEN 164 FT /note="C->A,S: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:9368022" FT MUTAGEN 169 FT /note="C->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:9368022" FT MUTAGEN 219 FT /note="F->S: 12-fold reduction in affinity for TRX1 and FT 25-fold decrease in catalytic efficiency." FT /evidence="ECO:0000269|PubMed:23845423" FT MUTAGEN 450 FT /note="E->S: No effect on catalytic activity." FT /evidence="ECO:0000269|PubMed:23845423" FT MUTAGEN 514..528 FT /note="Missing: 7-fold reduction in affinity for TRX1 and FT 16-fold decrease in catalytic efficiency." FT /evidence="ECO:0000269|PubMed:23845423" FT MUTAGEN 514 FT /note="H->A: No effect on affinity for TRX1 and 2-fold FT decrease in catalytic efficiency." FT /evidence="ECO:0000269|PubMed:23845423" FT MUTAGEN 529 FT /note="D->A: No effect on catalytic activity." FT /evidence="ECO:0000269|PubMed:23845423" FT MUTAGEN 585 FT /note="H->Q,A: Severe loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:9368022" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 127..137 FT /evidence="ECO:0007829|PDB:4J56" FT TURN 138..140 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 162..167 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 169..183 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 184..188 FT /evidence="ECO:0007829|PDB:4J56" FT TURN 189..193 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 194..201 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 203..227 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 244..249 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 257..266 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 276..279 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 281..284 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 288..291 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 300..304 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 308..320 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 324..330 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:4B1B" FT HELIX 338..349 FT /evidence="ECO:0007829|PDB:4J56" FT TURN 350..352 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 354..357 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 361..367 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 369..375 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 380..388 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 392..395 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 397..399 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 401..404 FT /evidence="ECO:0007829|PDB:4J56" FT TURN 410..413 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 428..430 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 442..457 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 475..483 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 486..493 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 495..497 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 498..505 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 508..511 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 519..521 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 530..532 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 534..541 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 542..544 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 547..555 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 558..570 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 575..580 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 582..584 FT /evidence="ECO:0007829|PDB:4J56" FT HELIX 589..594 FT /evidence="ECO:0007829|PDB:4J56" FT TURN 599..601 FT /evidence="ECO:0007829|PDB:4J56" FT STRAND 609..611 FT /evidence="ECO:0007829|PDB:4J56" SQ SEQUENCE 617 AA; 68698 MW; 50E1692E12D73C1D CRC64; MNNVISFIGN SSNKYFQINQ LHFIRIINKN IHSKNNLINS NSSYNVFYNK YFIKNTFQNK NKLSSIYSKL NFSIKNMCKD KNEKKNYEHV NANEKNGYLA SEKNELTKNK VEEHTYDYDY VVIGGGPGGM ASAKEAAAHG ARVLLFDYVK PSSQGTKWGI GGTCVNVGCV PKKLMHYAGH MGSIFKLDSK AYGWKFDNLK HDWKKLVTTV QSHIRSLNFS YMTGLRSSKV KYINGLAKLK DKNTVSYYLK GDLSKEETVT GKYILIATGC RPHIPDDVEG AKELSITSDD IFSLKKDPGK TLVVGASYVA LECSGFLNSL GYDVTVAVRS IVLRGFDQQC AVKVKLYMEE QGVMFKNGIL PKKLTKMDDK ILVEFSDKTS ELYDTVLYAI GRKGDIDGLN LESLNMNVNK SNNKIIADHL SCTNIPSIFA VGDVAENVPE LAPVAIKAGE ILARRLFKDS DEIMDYSYIP TSIYTPIEYG ACGYSEEKAY ELYGKSNVEV FLQEFNNLEI SAVHRQKHIR AQKDEYDLDV SSTCLAKLVC LKNEDNRVIG FHYVGPNAGE VTQGMALALR LKVKKKDFDN CIGIHPTDAE SFMNLFVTIS SGLSYAAKGG CGGGKCG //