TRI_THEAC
ID TRI_THEAC Reviewed; 1071 AA.
AC P96086;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Tricorn protease;
DE EC=3.4.21.- {ECO:0000269|PubMed:12470958};
GN Name=tri; OrderedLocusNames=Ta1490;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 120-126;
RP 290-304; 376-392; 490-506; 554-560; 634-638; 676-684; 696-708; 709-716 AND
RP 932-946.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=8910281; DOI=10.1126/science.274.5291.1385;
RA Tamura T., Tamura N., Cejka Z., Hegerl R., Lottspeich F., Baumeister W.;
RT "Tricorn protease -- the core of a modular proteolytic system.";
RL Science 274:1385-1389(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [3]
RP CHARACTERIZATION OF PROTEIN INTERACTION.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=9845366; DOI=10.1016/s0092-8674(00)81634-7;
RA Tamura N., Lottspeich F., Baumeister W., Tamura T.;
RT "The role of tricorn protease and its aminopeptidase-interacting factors in
RT cellular protein degradation.";
RL Cell 95:637-648(1998).
RN [4]
RP THREE-DIMENSIONAL RECONSTRUCTION FROM ELECTRON MICROGRAPHS.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=9659903; DOI=10.1016/s1097-2765(00)80007-6;
RA Walz J., Tamura T., Tamura N., Grimm R., Baumeister W., Koster A.J.;
RT "Tricorn protease exists as an icosahedral supermolecule in vivo.";
RL Mol. Cell 1:59-65(1997).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY.
RX PubMed=10600560; DOI=10.1006/jsbi.1999.4169;
RA Walz J., Koster A.J., Tamura T., Baumeister W.;
RT "Capsids of Tricorn protease studied by electron cryomicroscopy.";
RL J. Struct. Biol. 128:65-68(1999).
RN [6]
RP DOMAINS.
RX PubMed=10518749; DOI=10.1111/j.1574-6968.1999.tb08761.x;
RA Ponting C.P., Pallen M.J.;
RT "Beta-propeller repeats and a PDZ domain in the Tricorn protease: predicted
RT self-compartmentalisation and C-terminal polypeptide-binding strategies of
RT substrate selection.";
RL FEMS Microbiol. Lett. 179:447-451(1999).
RN [7]
RP CRYSTALLIZATION.
RX PubMed=11469880; DOI=10.1006/jsbi.2001.4360;
RA Bosch J., Tamura T., Bourenkov G., Baumeister W., Essen L.-O.;
RT "Purification, crystallization, and preliminary X-ray diffraction analysis
RT of the Tricorn protease hexamer from Thermoplasma acidophilum.";
RL J. Struct. Biol. 134:83-87(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 27-1071, SUBUNIT, DOMAIN, REGIONS,
RP ACTIVE SITES, SITES, AND MUTAGENESIS OF 131-ARG-ARG-132; LEU-184; ARG-414;
RP HIS-746 AND SER-965.
RX PubMed=11719810; DOI=10.1038/35106609;
RA Brandstetter H., Kim J.-S., Groll M., Huber R.;
RT "Crystal structure of the tricorn protease reveals a protein disassembly
RT line.";
RL Nature 414:466-470(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEXES WITH INHIBITORS,
RP CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, REGIONS, ACTIVE SITES, SITES, AND
RP MUTAGENESIS OF 131-ARG-ARG-132; LEU-184; ARG-414 AND ALA-643.
RX PubMed=12470958; DOI=10.1016/s0022-2836(02)01153-1;
RA Kim J.-S., Groll M., Musiol H.-J., Behrendt R., Kaiser M., Moroder L.,
RA Huber R., Brandstetter H.;
RT "Navigation inside a protease: substrate selection and product exit in the
RT tricorn protease from Thermoplasma acidophilum.";
RL J. Mol. Biol. 324:1041-1050(2002).
CC -!- FUNCTION: Tricorn degrades oligopeptides (probably derived from the
CC proteasome) and channels the products to F1, F2 and F3 proteases, which
CC then catalyze the terminal degradation step, yielding free amino acids.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-8.8.;
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.;
CC -!- SUBUNIT: Part of the Tricorn proteolytic complex. Assembles to form a
CC hexameric toroid, 20 copies of which may then assemble to form an
CC icosahedral supermolecule of 14.6 MDa. {ECO:0000269|PubMed:10600560,
CC ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958,
CC ECO:0000269|PubMed:9659903}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: It is thought that substrate reaches the active site through
CC the seven-bladed beta propeller channel, while products exit via the
CC six-bladed beta propeller channel. {ECO:0000269|PubMed:10518749,
CC ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958}.
CC -!- SIMILARITY: Belongs to the peptidase S41B family. {ECO:0000305}.
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DR EMBL; U72850; AAC44621.1; -; Genomic_DNA.
DR EMBL; AL445067; CAC12608.1; -; Genomic_DNA.
DR PIR; T43255; T43255.
DR RefSeq; WP_010901890.1; NC_002578.1.
DR PDB; 1K32; X-ray; 2.00 A; A/B/C/D/E/F=27-1071.
DR PDB; 1N6D; X-ray; 2.80 A; A/B/C/D/E/F=1-1071.
DR PDB; 1N6E; X-ray; 2.60 A; A/C/E/G/I/K=1-1071.
DR PDB; 1N6F; X-ray; 2.70 A; A/B/C/D/E/F=1-1071.
DR PDBsum; 1K32; -.
DR PDBsum; 1N6D; -.
DR PDBsum; 1N6E; -.
DR PDBsum; 1N6F; -.
DR AlphaFoldDB; P96086; -.
DR SASBDB; P96086; -.
DR SMR; P96086; -.
DR STRING; 273075.Ta1490; -.
DR MEROPS; S41.005; -.
DR EnsemblBacteria; CAC12608; CAC12608; CAC12608.
DR GeneID; 1456939; -.
DR KEGG; tac:Ta1490; -.
DR eggNOG; arCOG03384; Archaea.
DR HOGENOM; CLU_005503_1_0_2; -.
DR OMA; YLHVPDM; -.
DR OrthoDB; 456at2157; -.
DR BRENDA; 3.4.21.B34; 6324.
DR EvolutionaryTrace; P96086; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR028204; Tricorn_C1.
DR InterPro; IPR029414; Tricorn_PDZ.
DR InterPro; IPR012393; Tricorn_protease.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43253; PTHR43253; 1.
DR Pfam; PF07676; PD40; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR Pfam; PF14685; Tricorn_PDZ; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Protease;
KW Reference proteome; Serine protease.
FT CHAIN 1..1071
FT /note="Tricorn protease"
FT /id="PRO_0000207197"
FT REGION 39..310
FT /note="Six-bladed beta propeller"
FT /evidence="ECO:0000269|PubMed:12470958"
FT REGION 131..132
FT /note="Binds the substrate's C-terminus"
FT /evidence="ECO:0000269|PubMed:11719810,
FT ECO:0000269|PubMed:12470958"
FT REGION 326..675
FT /note="Seven-bladed beta propeller"
FT /evidence="ECO:0000269|PubMed:12470958"
FT REGION 679..745
FT /note="C-1; helical bundle"
FT /evidence="ECO:0000269|PubMed:12470958"
FT REGION 761..855
FT /note="PDZ-like"
FT /evidence="ECO:0000269|PubMed:12470958"
FT REGION 856..1061
FT /note="C-2; alpha-beta sandwich"
FT /evidence="ECO:0000269|PubMed:12470958"
FT ACT_SITE 746
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:11719810,
FT ECO:0000269|PubMed:12470958"
FT ACT_SITE 965
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:11719810,
FT ECO:0000269|PubMed:12470958"
FT ACT_SITE 1023
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:11719810"
FT BINDING 916..918
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11719810,
FT ECO:0000269|PubMed:12470958"
FT BINDING 993..995
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12470958"
FT SITE 936
FT /note="Substrate specificity switch"
FT /evidence="ECO:0000269|PubMed:11719810"
FT SITE 966
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000269|PubMed:11719810,
FT ECO:0000269|PubMed:12470958"
FT MUTAGEN 131..132
FT /note="RR->EE: Decreased catalytic activity towards protein
FT substrates. Retains 10% of wild-type activity towards
FT casein and about 30% towards oxidized insulin beta chain.
FT However, there is no change in the activity for a
FT tripeptide substrate."
FT /evidence="ECO:0000269|PubMed:11719810,
FT ECO:0000269|PubMed:12470958"
FT MUTAGEN 184
FT /note="L->C: Both peptidolytic and proteolytic activities
FT doubled, probably due to the increase of the diameter of
FT the channel for product exit. Retains less than 50% of
FT wild-type activity after modification of the thiol group by
FT maleimide, which decreases the diameter of the exit channel
FT and impairs product exit from the catalytic chamber."
FT /evidence="ECO:0000269|PubMed:11719810,
FT ECO:0000269|PubMed:12470958"
FT MUTAGEN 414
FT /note="R->C: Retains 50% of wild-type activity after
FT modification of the thiol group by maleimide, which
FT decreases the diameter of the access channel and impairs
FT substrate access to the active site. Decreased catalytic
FT activity towards fluorogenic substrate and insulin beta
FT chain prior to any modification or oxidation, probably due
FT to the decrease of the diameter of the substrate access
FT channel. Further decreased catalytic activity towards these
FT substrates after modification with fluorescein-5-maleimide
FT or oxidation by oxidized glutathione; when associated with
FT C-643."
FT /evidence="ECO:0000269|PubMed:11719810,
FT ECO:0000269|PubMed:12470958"
FT MUTAGEN 643
FT /note="A->C: Decreased catalytic activity towards
FT fluorogenic substrate and insulin beta chain prior to any
FT modification or oxidation. Further decreased catalytic
FT activity towards these substrates after modification with
FT fluorescein-5-maleimide or oxidation by oxidized
FT glutathione; when associated with C-414."
FT /evidence="ECO:0000269|PubMed:12470958"
FT MUTAGEN 746
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:11719810"
FT MUTAGEN 965
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:11719810"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 371..381
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 406..412
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 416..423
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 460..467
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 477..484
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 485..488
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 496..505
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 511..517
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 537..545
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 585..590
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 606..611
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 617..623
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 629..641
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:1N6D"
FT STRAND 647..652
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 657..663
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 678..681
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 682..700
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 704..719
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 720..724
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 728..740
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 766..772
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 775..781
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:1N6F"
FT HELIX 794..798
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 806..810
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 816..819
FT /evidence="ECO:0007829|PDB:1N6F"
FT HELIX 821..826
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 827..830
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 831..838
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 840..842
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 844..850
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 856..874
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 875..877
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 878..883
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 889..902
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 905..911
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 921..928
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 934..941
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 944..947
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 953..959
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 966..976
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 979..985
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 992..994
FT /evidence="ECO:0007829|PDB:1N6E"
FT STRAND 1011..1015
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 1016..1018
FT /evidence="ECO:0007829|PDB:1K32"
FT TURN 1020..1025
FT /evidence="ECO:0007829|PDB:1K32"
FT STRAND 1030..1032
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 1037..1041
FT /evidence="ECO:0007829|PDB:1K32"
FT HELIX 1046..1058
FT /evidence="ECO:0007829|PDB:1K32"
SQ SEQUENCE 1071 AA; 121623 MW; D8C5579436870710 CRC64;
MPSLMSFGSC QWIDQGRFSR SLYRNFKTFK LHEMHGLCMP NLLLNPDIHG DRIIFVCCDD
LWEHDLKSGS TRKIVSNLGV INNARFFPDG RKIAIRVMRG SSLNTADLYF YNGENGEIKR
ITYFSGKSTG RRMFTDVAGF DPDGNLIIST DAMQPFSSMT CLYRVENDGI NFVPLNLGPA
THILFADGRR VIGRNTFELP HWKGYRGGTR GKIWIEVNSG AFKKIVDMST HVSSPVIVGH
RIYFITDIDG FGQIYSTDLD GKDLRKHTSF TDYYPRHLNT DGRRILFSKG GSIYIFNPDT
EKIEKIEIGD LESPEDRIIS IPSKFAEDFS PLDGDLIAFV SRGQAFIQDV SGTYVLKVPE
PLRIRYVRRG GDTKVAFIHG TREGDFLGIY DYRTGKAEKF EENLGNVFAM GVDRNGKFAV
VANDRFEIMT VDLETGKPTV IERSREAMIT DFTISDNSRF IAYGFPLKHG ETDGYVMQAI
HVYDMEGRKI FAATTENSHD YAPAFDADSK NLYYLSYRSL DPSPDRVVLN FSFEVVSKPF
VIPLIPGSPN PTKLVPRSMT SEAGEYDLND MYKRSSPINV DPGDYRMIIP LESSILIYSV
PVHGEFAAYY QGAPEKGVLL KYDVKTRKVT EVKNNLTDLR LSADRKTVMV RKDDGKIYTF
PLEKPEDERT VETDKRPLVS SIHEEFLQMY DEAWKLARDN YWNEAVAKEI SERIYEKYRN
LVPLCKTRYD LSNVIVEMQG EYRTSHSYEM GGTFTDKDPF RSGRIACDFK LDGDHYVVAK
AYAGDYSNEG EKSPIFEYGI DPTGYLIEDI DGETVGAGSN IYRVLSEKAG TSARIRLSGK
GGDKRDLMID ILDDDRFIRY RSWVEANRRY VHERSKGTIG YIHIPDMGMM GLNEFYRLFI
NESSYQGLIV DVRFNGGGFV SQLIIEKLMN KRIGYDNPRR GTLSPYPTNS VRGKIIAITN
EYAGSDGDIF SFSFKKLGLG KLIGTRTWGG VVGITPKRRL IDGTVLTQPE FAFWFRDAGF
GVENYGVDPD VEIEYAPHDY LSGKDPQIDY AIDALIEELR NWNEELPQRP S
