TRXR_PLAF7
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 03-AUG-2022, entry version 137.
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}; ORFNames=PF3D7_0923800, PFI1170c;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; 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:9368022, PubMed:11013257,
CC PubMed:16910770, PubMed:23845423). 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 H(+) + NADPH; 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 min(-
CC 1) with NADPH and DTNB as substrates (at pH 7.4) (PubMed:9368022).
CC kcat is 48.3 sec(-1) with NADPH and TRX1 as substrates (at 25 degrees
CC Celsius and at pH 7.4) (PubMed:11013257). kcat is 9.4 min(-1) with
CC nitrosoglutathione (GSNO) as substrates (at 25 degrees Celsius and at
CC pH 7.4) (PubMed:11013257). {ECO:0000269|PubMed:11013257,
CC ECO:0000269|PubMed:23845423, 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}.
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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.
DR PDB; 4B1B; X-ray; 2.90 A; A/B=77-617.
DR PDB; 4J56; X-ray; 2.37 A; A/B/C/D=77-617.
DR PDB; 4J57; X-ray; 2.50 A; A/B=77-615.
DR PDBsum; 4B1B; -.
DR PDBsum; 4J56; -.
DR PDBsum; 4J57; -.
DR AlphaFoldDB; P61076; -.
DR SMR; P61076; -.
DR STRING; 5833.PFI1170c; -.
DR BindingDB; P61076; -.
DR ChEMBL; CHEMBL4547; -.
DR SwissPalm; P61076; -.
DR PRIDE; P61076; -.
DR EnsemblProtists; CAX64232; CAX64232; PF3D7_0923800.1. [P61076-1]
DR EnsemblProtists; CZT62537; CZT62537; PF3D7_0923800.2. [P61076-2]
DR GeneID; 813514; -.
DR KEGG; pfa:PF3D7_0923800.1; -.
DR VEuPathDB; PlasmoDB:PF3D7_0923800; -.
DR HOGENOM; CLU_016755_2_4_1; -.
DR InParanoid; P61076; -.
DR OMA; CFDYVKP; -.
DR OrthoDB; 581771at2759; -.
DR PhylomeDB; P61076; -.
DR Reactome; R-PFA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-PFA-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-PFA-5263617; Metabolism of ingested MeSeO2H into MeSeH.
DR Reactome; R-PFA-5628897; TP53 Regulates Metabolic Genes.
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 activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01438; TGR; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
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 25-
FT 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 162..167
FT /evidence="ECO:0007829|PDB:4J56"
FT HELIX 169..187
FT /evidence="ECO:0007829|PDB:4J56"
FT TURN 188..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 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 370..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 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 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
