DYP_AURAJ
ID DYP_AURAJ Reviewed; 509 AA.
AC I2DBY1;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Dye-decolorizing peroxidase AauDyP1 {ECO:0000303|PubMed:23111597};
DE EC=1.11.1.19 {ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532};
DE EC=1.11.1.7 {ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606};
DE AltName: Full=AjP I {ECO:0000303|PubMed:19756587};
DE AltName: Full=Manganese-independent peroxidase I {ECO:0000303|PubMed:19756587};
DE Contains:
DE RecName: Full=Dye-decolorizing peroxidase AauDyP2 {ECO:0000303|PubMed:23111597};
DE EC=1.11.1.19 {ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597};
DE EC=1.11.1.7 {ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597};
DE AltName: Full=AjP II {ECO:0000303|PubMed:19756587};
DE AltName: Full=Manganese-independent peroxidase II {ECO:0000303|PubMed:19756587};
DE Flags: Precursor;
GN Name=dyp1 {ECO:0000312|EMBL:AFJ79723.1};
OS Auricularia auricula-judae (Judas ear fungus) (Tremella auricula-judae).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Auriculariaceae; Auricularia.
OX NCBI_TaxID=29892 {ECO:0000312|EMBL:AFJ79723.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 62-75; 171-185 AND 449-467,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSMZ 11326 {ECO:0000303|PubMed:23111597};
RX PubMed=23111597; DOI=10.1007/s00253-012-4521-2;
RA Liers C., Pecyna M.J., Kellner H., Worrich A., Zorn H., Steffen K.T.,
RA Hofrichter M., Ullrich R.;
RT "Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and
RT litter-degrading agaricomycetes compared to other fungal and plant heme-
RT peroxidases.";
RL Appl. Microbiol. Biotechnol. 97:5839-5849(2013).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19756587; DOI=10.1007/s00253-009-2173-7;
RA Liers C., Bobeth C., Pecyna M., Ullrich R., Hofrichter M.;
RT "DyP-like peroxidases of the jelly fungus Auricularia auricula-judae
RT oxidize nonphenolic lignin model compounds and high-redox potential dyes.";
RL Appl. Microbiol. Biotechnol. 85:1869-1879(2010).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25153532; DOI=10.1016/j.pep.2014.08.007;
RA Linde D., Coscolin C., Liers C., Hofrichter M., Martinez A.T.,
RA Ruiz-Duenas F.J.;
RT "Heterologous expression and physicochemical characterization of a fungal
RT dye-decolorizing peroxidase from Auricularia auricula-judae.";
RL Protein Expr. Purif. 103:28-37(2014).
RN [4] {ECO:0007744|PDB:4AU9}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 62-509 IN COMPLEX WITH HEME,
RP COFACTOR, ACTIVE SITE, AND GLYCOSYLATION AT ASN-343; ASN-410 AND ASN-476.
RX PubMed=23235158; DOI=10.1074/jbc.m112.400176;
RA Strittmatter E., Liers C., Ullrich R., Wachter S., Hofrichter M.,
RA Plattner D.A., Piontek K.;
RT "First crystal structure of a fungal high-redox potential dye-decolorizing
RT peroxidase: substrate interaction sites and long-range electron transfer.";
RL J. Biol. Chem. 288:4095-4102(2013).
RN [5] {ECO:0007744|PDB:4UZI}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 64-509 IN COMPLEX WITH HEME,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND GLYCOSYLATION AT ASN-343; ASN-410 AND ASN-476.
RX PubMed=25542606; DOI=10.1016/j.abb.2014.12.016;
RA Strittmatter E., Serrer K., Liers C., Ullrich R., Hofrichter M.,
RA Piontek K., Schleicher E., Plattner D.A.;
RT "The toolbox of Auricularia auricula-judae dye-decolorizing peroxidase
RT - Identification of three new potential substrate-interaction sites.";
RL Arch. Biochem. Biophys. 574:75-85(2015).
RN [6] {ECO:0007744|PDB:4W7M, ECO:0007744|PDB:4W7N, ECO:0007744|PDB:4W7O}
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 62-509 IN COMPLEX WITH HEME,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-208; GLY-230; TYR-398 AND TRP-438.
RX PubMed=25495127; DOI=10.1042/bj20141211;
RA Linde D., Pogni R., Canellas M., Lucas F., Guallar V., Baratto M.C.,
RA Sinicropi A., Saez-Jimenez V., Coscolin C., Romero A., Medrano F.J.,
RA Ruiz-Duenas F.J., Martinez A.T.;
RT "Catalytic surface radical in dye-decolorizing peroxidase: a computational,
RT spectroscopic and site-directed mutagenesis study.";
RL Biochem. J. 466:253-262(2015).
RN [7] {ECO:0007744|PDB:5IKD, ECO:0007744|PDB:5IKG}
RP X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 64-509 IN COMPLEX WITH HEME, AND
RP MUTAGENESIS OF ASP-229; ARG-393; LEU-418 AND PHE-420.
RX DOI=10.1039/c6cy00539j;
RA Linde D., Canellas M., Davo-Siguero I., Romero A., Lucas F.,
RA Ruiz-Duenas F.J., Guallar V., Martinez A.T.;
RT "Asymmetric sulfoxidation by engineering the heme pocket of a dye-
RT decolorizing peroxidase.";
RL Catal. Sci. Technol. 6:6277-6285(2016).
RN [8] {ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 64-509 IN COMPLEX WITH HEME, AND
RP GLYCOSYLATION AT ASN-343; ASN-410 AND ASN-476.
RA Strittmatter E., Piontek K., Plattner D.A.;
RT "Crystallographic Trapping of a Covalently Modified Heme in a Dye-
RT Decolorizing Peroxidase.";
RL Submitted (JAN-2015) to the PDB data bank.
CC -!- FUNCTION: Manganese-independent peroxidase that is able to convert a
CC large number of compounds, but its physiological substrate is not
CC known. In addition to classic peroxidase substrates (e.g. 2,6-
CC dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 and Reactive
CC Black 5. {ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597,
CC ECO:0000269|PubMed:25153532, ECO:0000269|PubMed:25495127,
CC ECO:0000269|PubMed:25542606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-
CC amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2
CC H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563,
CC ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:CHEBI:64278;
CC EC=1.11.1.19; Evidence={ECO:0000269|PubMed:19756587,
CC ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532,
CC ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC Evidence={ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597,
CC ECO:0000269|PubMed:25153532, ECO:0000269|PubMed:25495127,
CC ECO:0000269|PubMed:25542606};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25495127,
CC ECO:0000269|PubMed:25542606, ECO:0000269|Ref.7};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.
CC {ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25495127,
CC ECO:0000269|PubMed:25542606, ECO:0000269|Ref.7};
CC -!- ACTIVITY REGULATION: Inhibited by imidazole.
CC {ECO:0000269|PubMed:25542606}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=405 nm;
CC Note=Dye-decolorizing peroxidase AauDyP1. The value for Dye-
CC decolorizing peroxidase AauDyP2 is 406 nm.;
CC Kinetic parameters:
CC KM=20 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid)
CC (ABTS) (Dye-decolorizing peroxidase AauDyP1, at pH 4.5)
CC {ECO:0000269|PubMed:19756587};
CC KM=283 uM for ABTS (Dye-decolorizing peroxidase AauDyP1, at pH 3)
CC {ECO:0000269|PubMed:25153532};
CC KM=20 uM for ABTS (Dye-decolorizing peroxidase AauDyP2, at pH 4.5)
CC {ECO:0000269|PubMed:19756587};
CC KM=10 uM for H(2)O(2) (Dye-decolorizing peroxidase AauDyP1)
CC {ECO:0000269|PubMed:19756587};
CC KM=5 uM for H(2)O(2) (Dye-decolorizing peroxidase AauDyP2)
CC {ECO:0000269|PubMed:19756587};
CC KM=23 uM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1, at
CC pH 3) {ECO:0000269|PubMed:19756587};
CC KM=3.1 uM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1,
CC at pH 3) {ECO:0000269|PubMed:25495127};
CC KM=15 uM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP2, at
CC pH 3) {ECO:0000269|PubMed:19756587};
CC KM=27 uM for 2,6-Dimethoxyphenol (DMP)(Dye-decolorizing peroxidase
CC AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587};
CC KM=27 uM for DMP (Dye-decolorizing peroxidase AauDyP1, at pH 5)
CC {ECO:0000269|PubMed:25542606};
CC KM=23 uM for DMP (Dye-decolorizing peroxidase AauDyP2, at pH 4.5)
CC {ECO:0000269|PubMed:19756587};
CC Vmax=134 umol/min/mg enzyme toward Reactive Blue 5 (Dye-decolorizing
CC peroxidase AauDyP1, at pH 3) {ECO:0000269|PubMed:19756587};
CC Vmax=375 umol/min/mg enzyme toward Reactive Blue 5 (Dye-decolorizing
CC peroxidase AauDyP2, at pH 3) {ECO:0000269|PubMed:19756587};
CC Vmax=331 umol/min/mg enzyme toward ABTS (Dye-decolorizing peroxidase
CC AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587};
CC Vmax=471 umol/min/mg enzyme toward ABTS (Dye-decolorizing peroxidase
CC AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587};
CC Vmax=105 umol/min/mg enzyme toward DMP (Dye-decolorizing peroxidase
CC AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587};
CC Vmax=130 umol/min/mg enzyme toward DMP (Dye-decolorizing peroxidase
CC AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587};
CC Vmax=315 umol/min/mg enzyme toward H(2)O(2) (Dye-decolorizing
CC peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587};
CC Vmax=348 umol/min/mg enzyme toward H(2)O(2) (Dye-decolorizing
CC peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587};
CC pH dependence:
CC Optimum pH is 4.5 for oxidation of 2,6-dimethoxyphenol
CC (PubMed:23111597). Retains 100% activity after incubation at pH 2.5
CC for 4 hours (PubMed:23111597, PubMed:19756587, PubMed:25153532).
CC Retains >60% activity after incubation at pH 2-11 at 4 degrees
CC Celsius (PubMed:25153532). Retains >60% activity after incubation at
CC pH 3-9 at room temperature (PubMed:25153532).
CC {ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597,
CC ECO:0000269|PubMed:25153532};
CC Temperature dependence:
CC Retains >80% activity after incubation at temperatures up to 60
CC degrees Celsius for 10 minutes. Retains 50% activity after incubation
CC at 65.5 degrees Celsius for 10 minutes. Activity is lost after
CC incubation at 70 degrees Celsius for 10 minutes.
CC {ECO:0000269|PubMed:25153532};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23111597}.
CC -!- SIMILARITY: Belongs to the DyP-type peroxidase family. {ECO:0000305}.
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DR EMBL; JQ650250; AFJ79723.1; -; mRNA.
DR PDB; 4AU9; X-ray; 2.10 A; A/B=62-509.
DR PDB; 4UZI; X-ray; 2.10 A; A/B=64-509.
DR PDB; 4W7J; X-ray; 1.79 A; A/B/C/D=62-509.
DR PDB; 4W7K; X-ray; 1.05 A; A/B=62-509.
DR PDB; 4W7L; X-ray; 1.05 A; A/B=62-509.
DR PDB; 4W7M; X-ray; 1.15 A; A/B=62-509.
DR PDB; 4W7N; X-ray; 1.40 A; A/B=62-509.
DR PDB; 4W7O; X-ray; 1.20 A; A=62-509.
DR PDB; 5AG0; X-ray; 1.75 A; A/B=64-509.
DR PDB; 5AG1; X-ray; 1.85 A; A/B=64-509.
DR PDB; 5IKD; X-ray; 1.11 A; A=64-509.
DR PDB; 5IKG; X-ray; 1.95 A; A=65-509.
DR PDBsum; 4AU9; -.
DR PDBsum; 4UZI; -.
DR PDBsum; 4W7J; -.
DR PDBsum; 4W7K; -.
DR PDBsum; 4W7L; -.
DR PDBsum; 4W7M; -.
DR PDBsum; 4W7N; -.
DR PDBsum; 4W7O; -.
DR PDBsum; 5AG0; -.
DR PDBsum; 5AG1; -.
DR PDBsum; 5IKD; -.
DR PDBsum; 5IKG; -.
DR AlphaFoldDB; I2DBY1; -.
DR SMR; I2DBY1; -.
DR iPTMnet; I2DBY1; -.
DR BRENDA; 1.11.1.19; 12259.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR006314; Dyp_peroxidase.
DR Pfam; PF04261; Dyp_perox; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR TIGRFAMs; TIGR01413; Dyp_perox_fam; 1.
DR PROSITE; PS51404; DYP_PEROXIDASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Heme; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..61
FT /evidence="ECO:0000305|PubMed:23111597"
FT /id="PRO_0000444023"
FT CHAIN 62..509
FT /note="Dye-decolorizing peroxidase AauDyP1"
FT /evidence="ECO:0000269|PubMed:23235158"
FT /id="PRO_5003657170"
FT CHAIN 171..509
FT /note="Dye-decolorizing peroxidase AauDyP2"
FT /evidence="ECO:0000305|PubMed:23111597"
FT /id="PRO_0000444024"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:23235158"
FT BINDING 365
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:23235158,
FT ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9,
FT ECO:0007744|PDB:4UZI, ECO:0007744|PDB:4W7J,
FT ECO:0007744|PDB:4W7K, ECO:0007744|PDB:4W7L,
FT ECO:0007744|PDB:4W7M, ECO:0007744|PDB:4W7N,
FT ECO:0007744|PDB:4W7O, ECO:0007744|PDB:5AG0,
FT ECO:0007744|PDB:5IKD, ECO:0007744|PDB:5IKG"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23235158,
FT ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI,
FT ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23235158,
FT ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI,
FT ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23235158,
FT ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI,
FT ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1"
FT MUTAGEN 208
FT /note="Y->F: No significant effect on enzyme kinetics; when
FT associated with F-398."
FT /evidence="ECO:0000269|PubMed:25495127"
FT MUTAGEN 208
FT /note="Y->S: No significant effect on enzyme kinetics."
FT /evidence="ECO:0000269|PubMed:25495127"
FT MUTAGEN 229
FT /note="D->N: Drastically decreased catalytic efficiency in
FT reducing H(2)O(2)."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 230
FT /note="G->L: Complete loss of activity for ABTS and
FT Reactive Blue 19 but not DMP."
FT /evidence="ECO:0000269|PubMed:25495127"
FT MUTAGEN 393
FT /note="R->L: Drastically decreased catalytic efficiency in
FT reducing H(2)O(2)."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 398
FT /note="Y->F: No significant effect on enzyme kinetics; when
FT associated with F-208."
FT /evidence="ECO:0000269|PubMed:25495127"
FT MUTAGEN 398
FT /note="Y->S: No significant effect on enzyme kinetics."
FT /evidence="ECO:0000269|PubMed:25495127"
FT MUTAGEN 418
FT /note="L->G: Acquires new moderate non-stereoselective
FT sulfoxidase activity (KM=0.6 mM for methyl-phenyl
FT sulfide(MPS)). No activity towards the bigger substrate
FT methyl-p-tolyl sulfide (MTS)."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 420
FT /note="F->G: Acquires new strong stereoselective
FT sulfoxidase activity favoring the S enantiomer (KM=0.37 mM
FT for methyl-phenyl sulfide(MPS), KM=0.13 mM for methyl-p-
FT tolyl sulfide (MTS))."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 420
FT /note="F->H: Does not acquire new sulfoxidase activity."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 420
FT /note="F->W: Does not acquire new sulfoxidase activity."
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 438
FT /note="W->S: Complete loss of activity or at least greatly
FT reduced substrate affinity, enzyme activity and catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:25495127"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5IKD"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4W7K"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:4AU9"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 273..282
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:4W7L"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:4W7K"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:4W7K"
FT TURN 338..342
FT /evidence="ECO:0007829|PDB:4W7K"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 417..425
FT /evidence="ECO:0007829|PDB:4W7K"
FT TURN 427..430
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 431..436
FT /evidence="ECO:0007829|PDB:4W7K"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:4W7O"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:4W7K"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:4W7K"
FT STRAND 486..497
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 500..504
FT /evidence="ECO:0007829|PDB:4W7K"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:4W7K"
SQ SEQUENCE 509 AA; 52992 MW; 5BAE13D122C13C8A CRC64;
MRLSPVFVAL LSGLLAADLG LARSVAPRVA DSPAAVTGTR KTSLLKNVAG LPPVPSAAQV
AATSLNTDDI QGDILVGMHK QKQLFYFFAI NDPATFKTHL ASDIAPVVAS VTQLSNVATQ
PLVALNIAFS NTGLLALGVT DNLGDSLFAN GQAKDATSFK ESTSSWVPQF AGTGIHGVII
LASDTTDLID QQVASIESTF GSSISKLYSL SASIRPGNEA GHEMFGFLDG IAQPAINGFN
TPLPGQNIVD AGVIITGATN DPITRPSWAV GGSFLAFRQL EQLVPEFNKY LLDNAPAGSG
SLQARADLLG ARMVGRWKSG APIDLTPTAD DPALGADAQR NNNFTYSHAG FDLGSDQSHC
PFSAHIRKTR PRADLGGSLT PPNLSAGANS IMRSGIPYGP EVTSAESASN TTTQERGLAF
VAYQAQLSQG FHFLQQTWAD NANFPPGKTP ATVGLDPIIG QNNGQPRVVN GLLPSNSSAS
LSIPQFVVSH GGEYFFSPPI SAIGGRLSA
