OXLA_BOTAT
ID OXLA_BOTAT Reviewed; 506 AA.
AC P0CC17; A0A0S1LJ33; A0A1L8D690;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:18804547};
DE Short=BatroxLAAO {ECO:0000303|PubMed:18804547, ECO:0000303|PubMed:21300133, ECO:0000303|PubMed:28137621};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:18804547};
DE Flags: Precursor;
OS Bothrops atrox (Barba amarilla) (Fer-de-lance).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8725;
RN [1] {ECO:0000312|EMBL:JAV01887.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Amazonas D.R., Nishiyama M.Y. Jr., Gibbs H.L., Rokyta D.R.,
RA Junqueira-de-Azevedo I.L., Moura-da-Silva A.M.;
RT "Transcriptomic analysis of venom glands from five Bothrops atrox snakes.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:ALL27300.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-506.
RA Vivas D.E., Lazo F.E., Sandoval G.A., Rodriguez E.F., Yarleque A.,
RA Sanchez E.F.;
RT "Molecular and biological study of the L-amino acid oxidase from the
RT Peruvian Bothrops atrox venom.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 19-27; 121-143; 147-182; 241-249; 320-329; 352-363 AND
RP 470-489, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, CATALYTIC ACTIVITY,
RP AND SUBSTRATE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=18804547; DOI=10.1016/j.cbpa.2008.07.007;
RA Alves R.M., Antonucci G.A., Paiva H.H., Cintra A.C., Franco J.J.,
RA Mendonca-Franqueiro E.P., Dorta D.J., Giglio J.R., Rosa J.C., Fuly A.L.,
RA Dias-Baruffi M., Soares A.M., Sampaio S.V.;
RT "Evidence of caspase-mediated apoptosis induced by l-amino acid oxidase
RT isolated from Bothrops atrox snake venom.";
RL Comp. Biochem. Physiol. 151:542-550(2008).
RN [4]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=21300133; DOI=10.1016/j.biochi.2011.01.009;
RA de Melo Alves Paiva R., de Freitas Figueiredo R., Antonucci G.A.,
RA Paiva H.H., de Lourdes Pires Bianchi M., Rodrigues K.C., Lucarini R.,
RA Caetano R.C., Linhari Rodrigues Pietro R.C., Gomes Martins C.H.,
RA de Albuquerque S., Sampaio S.V.;
RT "Cell cycle arrest evidence, parasiticidal and bactericidal properties
RT induced by L-amino acid oxidase from Bothrops atrox snake venom.";
RL Biochimie 93:941-947(2011).
RN [5]
RP CRYSTALLIZATION.
RC TISSUE=Venom;
RX PubMed=21505245; DOI=10.1107/s1744309111003770;
RA Alves R.M., Feliciano P.R., Sampaio S.V., Nonato M.C.;
RT "A rational protocol for the successful crystallization of L-amino-acid
RT oxidase from Bothrops atrox.";
RL Acta Crystallogr. F 67:475-478(2011).
RN [6] {ECO:0007744|PDB:5TS5}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 12-495 IN COMPLEX WITH FAD AND
RP ZINC IONS, GLYCOSYLATION AT ASN-190, DISULFIDE BONDS, AND COFACTOR.
RX PubMed=28137621; DOI=10.1016/j.toxicon.2017.01.017;
RA Feliciano P.R., Rustiguel J.K., Soares R.O., Sampaio S.V.,
RA Cristina Nonato M.;
RT "Crystal structure and molecular dynamics studies of L-amino acid oxidase
RT from Bothrops atrox.";
RL Toxicon 128:50-59(2017).
CC -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC hydrophobic and aromatic L-amino acids, thus producing hydrogen
CC peroxide that may contribute to the diverse toxic effects of this
CC enzyme (PubMed:18804547). Shows high catalytic activity against L-Met,
CC L-Leu, L-Phe, L-Trp, L-Tyr, L-Ile (PubMed:18804547). Shows no or weak
CC activity on L-Cys, L-Val, L-Gln, L-Thr, L-Ser, L-Lys, L-Arg, L-Asn, L-
CC Glu, L-Gly, L-Pro, L-Asp and L-His (PubMed:18804547). Induces platelet
CC aggregation in platelet-rich plasma, probably due to hydrogen peroxide
CC production, since catalase inhibits aggregation effect
CC (PubMed:18804547). Induces moderate mouse paw edema (PubMed:18804547).
CC Induces apoptosis and shows cytotoxicity against several cancer cell
CC lines, which is inhibited by catalase (PubMed:18804547,
CC PubMed:21300133). Shows hemolytic activity and antibacterial activities
CC against both Gram-positive and Gram-negative bacteria
CC (PubMed:21300133). Has parasiticidal activities against both
CC trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen
CC peroxide production (PubMed:21300133). Unlike other snake venom L-amino
CC acid oxidases, does not induce hemorrhage (with 50 ug of enzyme)
CC (PubMed:18804547). {ECO:0000269|PubMed:18804547,
CC ECO:0000269|PubMed:21300133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59869; EC=1.4.3.2;
CC Evidence={ECO:0000269|PubMed:18804547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:18804547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:18804547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+);
CC Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:18804547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate +
CC H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57844;
CC Evidence={ECO:0000269|PubMed:18804547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2
CC + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146,
CC ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:18804547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:18804547};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:28137621};
CC -!- SUBUNIT: Homodimer; non-covalently linked. Stabilized by a single zinc-
CC binding site located at the dimer interface (Asp-219, His-332 and His-
CC 458). Other zinc-bind sites can be understood as transient and non-
CC specific, and appear due to the high concentration of zinc ions used in
CC the crystallization experiments. {ECO:0000305|PubMed:28137621}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18804547}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18804547}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; GEDR01000075; JAV01887.1; -; mRNA.
DR EMBL; KT150252; ALL27300.1; -; mRNA.
DR PDB; 5TS5; X-ray; 2.30 A; A/B/C/D=19-502.
DR PDBsum; 5TS5; -.
DR AlphaFoldDB; P0CC17; -.
DR SMR; P0CC17; -.
DR iPTMnet; P0CC17; -.
DR BRENDA; 1.4.3.2; 910.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0044478; P:envenomation resulting in positive regulation of platelet aggregation in another organism; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0044532; P:modulation of apoptotic process in another organism; IDA:UniProtKB.
DR GO; GO:0090330; P:regulation of platelet aggregation; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Apoptosis; Cytolysis;
KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW Hemolysis; Hemostasis impairing toxin; Metal-binding; Oxidoreductase;
KW Platelet aggregation activating toxin; Secreted; Signal; Toxin; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:18804547"
FT CHAIN 19..506
FT /note="L-amino-acid oxidase"
FT /evidence="ECO:0000305|PubMed:18804547, ECO:0000305|Ref.1"
FT /id="PRO_0000390927"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28137621,
FT ECO:0007744|PDB:5TS5"
FT BINDING 61..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:5TS5"
FT BINDING 81..82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:5TS5"
FT BINDING 89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:5TS5"
FT BINDING 105..108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:5TS5"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28137621,
FT ECO:0007744|PDB:5TS5"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28137621,
FT ECO:0007744|PDB:5TS5"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:5TS5"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28137621,
FT ECO:0007744|PDB:5TS5"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28137621,
FT ECO:0007744|PDB:5TS5"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:5TS5"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:28137621,
FT ECO:0007744|PDB:5TS5"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28137621"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28137621,
FT ECO:0007744|PDB:5TS5"
FT BINDING 475
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:5TS5"
FT BINDING 482..487
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:5TS5"
FT BINDING 482..483
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28137621,
FT ECO:0007744|PDB:5TS5"
FT DISULFID 28..191
FT /evidence="ECO:0000269|PubMed:28137621,
FT ECO:0007744|PDB:5TS5"
FT DISULFID 349..430
FT /evidence="ECO:0000269|PubMed:28137621,
FT ECO:0007744|PDB:5TS5"
FT CONFLICT 8..13
FT /note="SLLFLA -> FMFSWL (in Ref. 2; ALL27300)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="R -> K (in Ref. 1; JAV01887)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="E -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="S -> SS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="Q -> H (in Ref. 2; ALL27300)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="R -> S (in Ref. 1; JAV01887)"
FT /evidence="ECO:0000305"
FT CONFLICT 503..506
FT /note="Missing (in Ref. 1; JAV01887)"
FT /evidence="ECO:0000305"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5TS5"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 273..284
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 300..310
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 353..357
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:5TS5"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 404..419
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:5TS5"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 455..464
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:5TS5"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:5TS5"
FT HELIX 484..501
FT /evidence="ECO:0007829|PDB:5TS5"
SQ SEQUENCE 506 AA; 57408 MW; 594E1E8B435DFF94 CRC64;
MNVFFTFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI AKNGLSTTSN PKRVVIVGAG
MSGLSAAYVL ANAGHQVTVL EASERAGGRV KTYRNEKEGW YANLGPMRLP EKHRIVREYI
RKFDLQLNEF SQENENAWYF IKNIRKRVGE VNKDPGVLEY PVKPSEVGKS AGQLYEESLQ
KAVEELRRTN CSYMLNKYDT YSTKEYLLKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK
HDDIFAYEKR FDEIVGGMDK LPTSMYQAIQ EKVHLNARVI KIQQDVKEVT VTYQTSEKET
LSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIH
GGKSTTDLPS RFIYYPNHNF PNGVGVIIAY GIGDDANYFQ ALDFEDCGDI VINDLSLIHQ
LPKEEIQAIC RPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPVDRI YFAGEYTAQA
HGWIDSTIKS GLRAARDVNR ASEIKK
