POLG_TUMVQ
ID POLG_TUMVQ Reviewed; 3163 AA.
AC Q02597;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1 proteinase;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P04517};
DE AltName: Full=N-terminal protein;
DE Contains:
DE RecName: Full=Helper component proteinase;
DE Short=HC-pro;
DE EC=3.4.22.45 {ECO:0000250|UniProtKB:P04517};
DE Contains:
DE RecName: Full=Protein P3;
DE Contains:
DE RecName: Full=6 kDa protein 1;
DE Short=6K1;
DE Contains:
DE RecName: Full=Cytoplasmic inclusion protein;
DE Short=CI;
DE EC=3.6.4.-;
DE Contains:
DE RecName: Full=6 kDa protein 2;
DE Short=6K2;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE Contains:
DE RecName: Full=Nuclear inclusion protein A;
DE Short=NI-a;
DE Short=NIa;
DE EC=3.4.22.44;
DE AltName: Full=49 kDa proteinase;
DE Short=49 kDa-Pro;
DE AltName: Full=NIa-pro;
DE Contains:
DE RecName: Full=Nuclear inclusion protein B;
DE Short=NI-b;
DE Short=NIb;
DE EC=2.7.7.48;
DE AltName: Full=RNA-directed RNA polymerase;
DE Contains:
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
OS Turnip mosaic virus (strain Quebec) (TuMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=36396;
OH NCBI_TaxID=3705; Brassica.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1431807; DOI=10.1099/0022-1317-73-11-2785;
RA Nicolas O., Laliberte J.F.;
RT "The complete nucleotide sequence of turnip mosaic potyvirus RNA.";
RL J. Gen. Virol. 73:2785-2793(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1534-3163, AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=2254757; DOI=10.1099/0022-1317-71-11-2769;
RA Tremblay M.F., Nicolas O., Sinha R., Lazure C., Laliberte J.F.;
RT "Sequence of the 3'-terminal region of turnip mosaic virus RNA and the
RT capsid protein gene.";
RL J. Gen. Virol. 71:2769-2772(1990).
RN [3]
RP INTERACTION WITH HOST EIF(ISO)4E (VIRAL GENOME-LINKED PROTEIN), AND
RP INTERACTION WITH HOST EIF4E (VIRAL GENOME-LINKED PROTEIN).
RX PubMed=10933678; DOI=10.1128/jvi.74.17.7730-7737.2000;
RA Leonard S., Plante D., Wittmann S., Daigneault N., Fortin M.G.,
RA Laliberte J.F.;
RT "Complex formation between potyvirus VPg and translation eukaryotic
RT initiation factor 4E correlates with virus infectivity.";
RL J. Virol. 74:7730-7737(2000).
RN [4]
RP REVIEW.
RX PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT "Potyvirus proteins: a wealth of functions.";
RL Virus Res. 74:157-175(2001).
RN [5]
RP INTERACTION WITH HOST EIF(ISO)4E (VIRAL GENOME-LINKED PROTEIN), AND
RP FUNCTION (VIRAL GENOME-LINKED PROTEIN).
RX PubMed=18582528; DOI=10.1016/j.biochi.2008.03.013;
RA Miyoshi H., Okade H., Muto S., Suehiro N., Nakashima H., Tomoo K.,
RA Natsuaki T.;
RT "Turnip mosaic virus VPg interacts with Arabidopsis thaliana eIF(iso)4E and
RT inhibits in vitro translation.";
RL Biochimie 90:1427-1434(2008).
RN [6]
RP REVIEW.
RX PubMed=28199446; DOI=10.1590/1678-4685-gmb-2016-0092;
RA Machado J.P.B., Calil I.P., Santos A.A., Fontes E.P.B.;
RT "Translational control in plant antiviral immunity.";
RL Genet. Mol. Biol. 40:292-304(2017).
RN [7]
RP MUTAGENESIS OF GLU-2039 AND ASN-2086.
RX PubMed=29504210; DOI=10.1111/pbi.12896;
RA Bastet A., Lederer B., Giovinazzo N., Arnoux X., German-Retana S.,
RA Reinbold C., Brault V., Garcia D., Djennane S., Gersch S., Lemaire O.,
RA Robaglia C., Gallois J.-L.;
RT "Trans-species synthetic gene design allows resistance pyramiding and
RT broad-spectrum engineering of virus resistance in plants.";
RL Plant Biotechnol. J. 16:1569-1581(2018).
CC -!- FUNCTION: [Helper component proteinase]: Required for aphid
CC transmission and also has proteolytic activity. Only cleaves a Gly-Gly
CC dipeptide at its own C-terminus. Interacts with virions and aphid
CC stylets. Acts as a suppressor of RNA-mediated gene silencing, also
CC known as post-transcriptional gene silencing (PTGS), a mechanism of
CC plant viral defense that limits the accumulation of viral RNAs. May
CC have RNA-binding activity. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Cytoplasmic inclusion protein]: Has helicase activity. It
CC may be involved in replication.
CC -!- FUNCTION: [6 kDa protein 1]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P13529}.
CC -!- FUNCTION: [6 kDa protein 2]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P09814}.
CC -!- FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent,
CC EIF4E-dependent translation of viral genomic RNAs (By similarity).
CC Binds to the cap-binding site of host EIF4E and thus interferes with
CC the host EIF4E-dependent mRNA export and translation (By similarity).
CC VPg-RNA directly binds EIF4E and is a template for transcription (By
CC similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are
CC templates for translation (By similarity).
CC {ECO:0000250|UniProtKB:P18247}.
CC -!- FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and
CC proteolytic activities. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA
CC polymerase that plays an essential role in the virus replication.
CC -!- FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to-
CC cell and systemis movement, encapsidation of the viral RNA and in the
CC regulation of viral RNA amplification. {ECO:0000250|UniProtKB:P04517}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC restricted by preferences for the amino acids in P6 - P1' that vary
CC with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC the viral polyprotein, but other proteins and oligopeptides
CC containing the appropriate consensus sequence are also cleaved.;
CC EC=3.4.22.44; Evidence={ECO:0000250|UniProtKB:P04517};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC potyviral polyprotein.; EC=3.4.22.45;
CC Evidence={ECO:0000250|UniProtKB:P04517};
CC -!- SUBUNIT: [Viral genome-linked protein]: Interacts with host eIF4E
CC protein (via cap-binding region); this interaction mediates the
CC translation of the VPg-viral RNA conjugates (Probable). Part of a
CC complex that comprises VPg, RNA, host EIF4E and EIF4G; this interaction
CC mediates the translation of the VPg-viral RNA conjugates (By
CC similarity). {ECO:0000250|UniProtKB:P18247,
CC ECO:0000305|PubMed:18582528}.
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle.
CC Note=Probably colocalizes with 6K2-induced vesicles associated with
CC host chloroplasts. {ECO:0000250|UniProtKB:P13529}.
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate with
CC host chloroplasts. {ECO:0000250|UniProtKB:P09814}.
CC -!- SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host nucleus
CC {ECO:0000250|UniProtKB:P21231}. Note=Binds to host plant eIF4E proteins
CC in the host nucleus. {ECO:0000250|UniProtKB:P21231}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=Q02597-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK12-1; Sequence=External;
CC -!- DOMAIN: [Helper component proteinase]: The N-terminus is involved in
CC interaction with stylets. The central part is involved in interaction
CC with virions and the C-terminus is involved in cell-to cell movement of
CC the virus.
CC -!- PTM: [Viral genome-linked protein]: VPg is uridylylated by the
CC polymerase and is covalently attached to the 5'-end of the genomic RNA.
CC This uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.
CC -!- PTM: [Genome polyprotein]: Potyviral RNA is expressed as two
CC polyproteins which undergo post-translational proteolytic processing.
CC Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases
CC resulting in the production of at least ten individual proteins. P3N-
CC PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in
CC the production of three individual proteins. The P1 proteinase and the
CC HC-pro cleave only their respective C-termini autocatalytically. 6K1 is
CC essential for proper proteolytic separation of P3 from CI (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced by conventional
CC translation.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {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; D10927; BAA01725.1; -; Genomic_RNA.
DR EMBL; D10601; BAA01452.1; -; Genomic_RNA.
DR PIR; JQ1895; JQ1895.
DR MEROPS; C04.001; -.
DR MEROPS; C06.001; -.
DR Proteomes; UP000008263; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0019048; P:modulation by virus of host process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.70.150; -; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001456; HC-pro.
DR InterPro; IPR031159; HC_PRO_CPD_dom.
DR InterPro; IPR042308; HC_PRO_CPD_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002540; Pept_S30_P1_potyvir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR039560; Potyvirid-P3.
DR InterPro; IPR013648; PP_Potyviridae.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00851; Peptidase_C6; 1.
DR Pfam; PF01577; Peptidase_S30; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 1.
DR Pfam; PF13608; Potyvirid-P3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR PRINTS; PR00966; NIAPOTYPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51744; HC_PRO_CPD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR PROSITE; PS51871; PV_P1_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW Direct protein sequencing; Helical capsid protein; Helicase;
KW Host cytoplasmic vesicle; Host nucleus; Host-virus interaction; Hydrolase;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
KW Suppressor of RNA silencing; Thiol protease; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..3163
FT /note="Genome polyprotein"
FT /id="PRO_0000420030"
FT CHAIN 1..362
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040473"
FT CHAIN 363..820
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040474"
FT CHAIN 821..1175
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040475"
FT CHAIN 1176..1227
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040476"
FT CHAIN 1228..1870
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040477"
FT CHAIN 1871..1923
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040478"
FT CHAIN 1924..2115
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040479"
FT CHAIN 2116..2358
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040480"
FT CHAIN 2359..2875
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040481"
FT CHAIN 2876..3163
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040482"
FT DOMAIN 219..362
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 698..820
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1300..1452
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1471..1630
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2116..2334
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2600..2724
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1983..2017
FT /note="Binding to host eIF(iso)4E"
FT /evidence="ECO:0000269|PubMed:10933678"
FT REGION 2883..2934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 414..417
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 672..674
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1402..1405
FT /note="DECH box"
FT MOTIF 1964..1971
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2883..2930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 270
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 279
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 313
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 706
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 779
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2161
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2196
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2266
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1313..1320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 362..363
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 820..821
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1175..1176
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1227..1228
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1870..1871
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2115..2116
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2358..2359
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2875..2876
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1986
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
FT MUTAGEN 2039
FT /note="E->Q: Replicates in eIF(iso)4G1-knockout host."
FT /evidence="ECO:0000269|PubMed:29504210"
FT MUTAGEN 2086
FT /note="N->Y: Replicates in eIF(iso)4G1-knockout host."
FT /evidence="ECO:0000269|PubMed:29504210"
FT CONFLICT 2862
FT /note="E -> G (in Ref. 2; BAA01452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3163 AA; 357822 MW; 61B0F73B58DF6D59 CRC64;
MAAVTFASAI TNAITNKTTS TGMVQFGSFP PMPLRSTTVT TVATPVGQPK LYTVRFGSLD
PVIVKGGAGS LAKATRQQPS VEIDVSLSEA AALEVAKPKS SAVLRMHEEA NKERALFLDW
EASLKRRSYG IAENEKVVMT TRGVSKIVPR SSRAMKQKRA RERRRAQQPI ILKWEPKLSG
FSIGGGFSAS AIEAEEVRTK WPLHKTPSMK KRMVHKTCKM SDQGVDMLIR SLVKIFKAKS
ANIEYIGKKP IKVDFIRKER TKFARIQVAH LLGKRAQRDL LAGMEENHFI DILSEYSGNG
TTINPGVVCA GWSGIVVRNE TLTQKRSRSP SKAFVIRGEH EDKLYDARIK ITKTMSLKIV
HFSARGANFW KGFDRCFLAY RSDNREHTCY SGLDVTECGE VAALMCLAMF PCGKITCPDC
VIDSELSQGQ ASGPSMKHRL TQLRDVIKSS YPRFKHAVQI LDRYEQSLSS ANENYQDFAE
IQSISDGVEK AAFPHVNKLN AILIKGATAT GEEFSQATKH LLEIARYLKN RTENIEKGSL
KSFRNKVSQK AHINPTLMCD NQLDKNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
RVVPNGSRKL AIGKLIVPTN FEVLREQMRG EPVEPYPVTV ECVSKSQGDF VHACCCVTTE
SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE
SQAKEFTKVV RDKLVSELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV
VDSYGSLSTG YHVLKTNTVE QLIKFTRCNL ESSLKHYRVG GTEWENAHGA DNIDNPQWCI
KRLVKGVYRP KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEHLMNHY ISADSNVAVL
LVVLKSLAKK VSTSQSVLAQ LQIIERSLPE LIEAKANING PDDAATRACN RFMGMLLHMA
EPNYELANGG YTFLRDHSIS ILEKSYLQIL DEAWNELSWS ERCVIRYYPS KQAIFTQKDL
PMQSEADLGG RYSESVISSY EWSKQQAKGV KDSVVNKLRS SMSWTSSKVS NSVCRTINYL
VPDVFKFMNV LVCISLLIKM TAEANHIITT QRRLKLDIEE TERKKIEWEL AFHHNILTHS
ASQHPTLDEF TAYIAEKAPH LSEHIEPEEK EVVHQAKRQS EQELERVIAF VALVLMMFDA
ERSDCVTKIL NKLKGLVATV EPTVYHQTLN EIEDDLNERN LFVDFELSSD SEMLQQLPAE
KTFASWWSHQ LSRGFTIPHY RTEGKFMTFT RATATEVAGK IAHESDKDIL LMGAVGSGKS
TGLPYHLSRK GNVLLLEPTR PLAENVHKQL SQAPFHQNTT LRMRGLTAFG SAPISVMTSG
FALNYFANNR SRIEEFDFVI FDECHVHDAN AMAMRCLIHE CDYSGKIIKV SATPPGREVE
FSTQYPVSIS TEDTLSFQDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD TLSKLLIERD
FKVTKVDGRT MKVGNIEITT SGTPSRKHFI VATNIIENGV TLDIDVVADF GTKVLPYLDT
DNRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTER GLSEVPSCIA TEAALKCFTY
GLPVITNNVS TSILGNVTVK QARTMSVFEI TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD
SEIVLTKLAI PNRGVNAGSQ PVSMHDSVQM LKIGVTLRIP FMCRDIPEKL HLDMWDVVVK
FKGDAGFGRL SSSASKVAYT LQTDVNSIQR TVTIIDTLIA EERRKQEYFK TVTSNCVSSS
NFSLQSITNA IKSRMMKDHP CENISVLEGA KSQLLEFRNL NSDHSFVTKT DGISRSFMRD
YGALEAVNHQ STNEMSKFLQ LKGKWNKTLI TRDVLVICGV LGGGVWMVVQ HFRSKVSEPV
THEAKGKKQR QKLKFRNARD NKMGREVYGD DDTIEHFFGD AYTKKGKSKG RTRGIGHKNR
KFINMYGFDP EDFSAVRFVD PLTGATLDDN PFTDITLVQK HFGDIRMDLL GEDELDSNEI
RMNKTIQAYY MNNKTGKALK VDLTPHIPLK VCDLHATIAG FPERENELRQ TGKAQPINID
EVPRANNELV PVDHESNSMF RGLRDYNPIS NNICHLTNVS DGASNSLYGV GFGPLILTNR
HLFERNNGEL IIKSRHGEFV IKNTTQLHLL PIPDRDLLLI RLPKDVPPFP QKLGFRQPEK
GERICMVGSN FQTKSITSIV SETSTIMPVE NSQFWKHWIS TKDGQCGSPM VSTKDGKILG
LHSLANFQNS INYFAAFPDD FTEKYLHTIE AHEWVKHWKY NTSAISWGSL NIQASQPVSL
FKVSKLISDL DSTAVYAQTQ QNRWMFEQLT GNLKAIAHCP SQLVTKHTVK GKCQMFDLYL
KLHDEAREYF QPMLGQYQKS KLNREAYAKD LLKYATPIEA GNIDCDLFEK TVEIVISDLR
GYGFETCNYV TDENDIFEAL NMKSAVGALY KGKKKDYFAE FTPEVKEEIL KQSCERLFLG
KMGVWNGSLK AELRPLEKVE ANKTRTFTAA PLDTLLGGKV CVDDFNNQFY DHNLRAPWDV
GMTKFYCGWD RLLESLPDGW VYCDADGSQF DSSLSPYLIN AVLNIRLGFM EEWDVGEVML
RNLYTEIVYT PISTPDGTLV KKFKGNNSGQ PSTVVDNTLM VILAVNYSLK KGGIPSELRD
SIIRFFVNGD DLLLSVHPEY EYILDTMADN FRELGLKYTF DSRTREKGDL WFMSHQGHRR
EGIWIPKLEP ERIVSILEWD RSKEPCHRLE AICAAMIESW GYDKLTHEIR KFYAWMIEQA
PFSSLAQEGK APYIAETALR KLYLDKEPAQ EDLTQYLQAI FEDYEDGVEA CVYHQAGETL
DADLTEEQKQ AEKEKKEREK AEKERERQKQ LAFKKGKDVA QEEGKRDKEV NAGTSGTFSV
PRLKSLTSKM RVPRYEKRVA LNLDHLILYT PEQTDLSNTR STRKQFDTWF EGVMADYELT
EDKMQIILNG LRVWCIENGT SPNINGMWVM MDGDDQVEFP IKPLIDHAKP TFRQIMAHFS
DVAEAYIEKR NQDRPYMPRY GLQRNLTDMS LARYAFDFYE MTSRTPIRAR EAHIQMKAAA
LRGANNNLFG LDGNVGTTVE NTERHTTEDV NRNMHNLLGV QGL
