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Non-structural polyprotein (Polyprotein nsP1234) (P1234) [Cleaved into: P123; P123'; mRNA-capping enzyme nsP1 (EC 2.1.1.-) (EC 2.7.7.-) (Non-structural protein 1); Protease nsP2 (EC 3.1.3.33) (EC 3.4.22.-) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 2) (nsP2); Non-structural protein 3 (nsP3); Non-structural protein 3' (nsP3'); RNA-directed RNA polymerase nsP4 (EC 2.7.7.48) (Non-structural protein 4) (nsP4)]

 POLN_EEVVT              Reviewed;        2492 AA.
P27282; O90163; Q5XQC5; Q66592; Q66594;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 2.
23-MAY-2018, entry version 140.
RecName: Full=Non-structural polyprotein;
AltName: Full=Polyprotein nsP1234;
Short=P1234;
Contains:
RecName: Full=P123;
Contains:
RecName: Full=P123';
Contains:
RecName: Full=mRNA-capping enzyme nsP1;
EC=2.1.1.-;
EC=2.7.7.-;
AltName: Full=Non-structural protein 1;
Contains:
RecName: Full=Protease nsP2;
EC=3.1.3.33;
EC=3.4.22.-;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Non-structural protein 2;
Short=nsP2;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsP3;
Contains:
RecName: Full=Non-structural protein 3';
Short=nsP3';
Contains:
RecName: Full=RNA-directed RNA polymerase nsP4;
EC=2.7.7.48;
AltName: Full=Non-structural protein 4;
Short=nsP4;
Venezuelan equine encephalitis virus (strain Trinidad donkey) (VEEV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Alphavirus.
NCBI_TaxID=11038;
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=9268; Didelphis marsupialis (Southern opossum).
NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
NCBI_TaxID=9796; Equus caballus (Horse).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=53535; Melanoconion.
NCBI_TaxID=9272; Philander opossum (Gray four-eyed opossum).
NCBI_TaxID=10162; Proechimys.
NCBI_TaxID=42415; Sigmodon hispidus (Hispid cotton rat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate trinidad donkey, and TC-83;
PubMed=2524126; DOI=10.1016/0042-6822(89)90347-4;
Kinney R.M., Johnson B.J.B., Welch J.B., Tsuchiya K.R., Trent D.W.;
"The full-length nucleotide sequences of the virulent Trinidad donkey
strain of Venezuelan equine encephalitis virus and its attenuated
vaccine derivative, strain TC-83.";
Virology 170:19-30(1989).
[2]
SEQUENCE REVISION.
Kinney R.;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=71-180;
PubMed=1469368; DOI=10.1099/0022-1317-73-12-3301;
Kinney R.M., Tsuchiya K.R., Sneider J.M., Trent D.W.;
"Molecular evidence for the origin of the widespread Venezuelan equine
encephalitis epizootic of 1969 to 1972.";
J. Gen. Virol. 73:3301-3305(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=V3526;
Davis N., Johnston R.E., Smith J.F., Crise B., Parker M.D.;
"Venezuelan equine encephalitis virus strain V3526.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: P123 and P123' are short-lived polyproteins,
accumulating during early stage of infection. P123 is directly
translated from the genome, whereas P123' is a product of the
cleavage of P1234. They localize the viral replication complex to
the cytoplasmic surface of modified endosomes and lysosomes. By
interacting with nsP4, they start viral genome replication into
antigenome. After these early events, P123 and P123' are cleaved
sequentially into nsP1, nsP2 and nsP3/nsP3'. This sequence of
delayed processing would allow correct assembly and membrane
association of the RNA polymerase complex (By similarity).
{ECO:0000250}.
-!- FUNCTION: nsP1 is a cytoplasmic capping enzyme. This function is
necessary since all viral RNAs are synthesized in the cytoplasm,
and host capping enzymes are restricted to the nucleus. The
enzymatic reaction involves a covalent link between 7-methyl-GMP
and nsP1, whereas eukaryotic capping enzymes form a covalent
complex only with GMP. nsP1 capping would consist in the following
reactions: GTP is first methylated and then forms the m7GMp-nsP1
complex, from which 7-methyl-GMP complex is transferred to the
mRNA to create the cap structure. Palmitoylated nsP1 is remodeling
host cell cytoskeleton, and induces filopodium-like structure
formation at the surface of the host cell (By similarity).
{ECO:0000250}.
-!- FUNCTION: nsP2 has two separate domain with different biological
activities. The N-terminal section is part of the RNA polymerase
complex and has RNA trisphosphatase and RNA helicase activity. The
C-terminal section harbors a protease that specifically cleaves
and releases the four mature proteins. Also inhibits cellular
transcription by inducing rapid degradation of POLR2A, a catalytic
subunit of the RNAPII complex. The resulting inhibition of
cellular protein synthesis serves to ensure maximal viral gene
expression and to evade host immune response (By similarity).
{ECO:0000250}.
-!- FUNCTION: nsP3 and nsP3' are essential for minus strand and
subgenomic 26S mRNA synthesis. {ECO:0000250}.
-!- FUNCTION: nsP4 is an RNA dependent RNA polymerase. It replicates
genomic and antigenomic RNA by recognizing replications specific
signals. Transcribes also a 26S subgenomic mRNA by initiating RNA
synthesis internally on antigenomic RNA. This 26S mRNA codes for
structural proteins. nsP4 is a short-lived protein regulated by
several ways: the opal codon readthrough and degradation by
ubiquitin pathway (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + GTP = m(7)GTP.
-!- CATALYTIC ACTIVITY: m7GTP + [nsP1 protein] = m7GMP-[nsP1 protein]
+ diphosphate.
-!- CATALYTIC ACTIVITY: m7GMP-[nsP1 protein] + (5')pp-Pur-mRNA =
m(7)G(5')ppp-Pur-mRNA + [nsP1 protein].
-!- CATALYTIC ACTIVITY: (5')ppp-mRNA + H(2)O = (5')pp-mRNA +
phosphate.
-!- CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H(2)O = a
polynucleotide + phosphate.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: P123 interacts with nsP4; nsP1, nsP2, nsP3 and nsP4
interact with each other, and with uncharacterized host factors.
-!- SUBCELLULAR LOCATION: Non-structural polyprotein: Host endosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Note=Located on the cytoplasmic
surface of modified endosomes and lysosomes, also called
cytopathic vacuoles type I (CPVI). These vacuoles contain numerous
small circular invaginations (spherules) which may be the sites of
RNA synthesis.
-!- SUBCELLULAR LOCATION: P123: Host endosome membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Host lysosome membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
-!- SUBCELLULAR LOCATION: P123': Host endosome membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Host lysosome membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
-!- SUBCELLULAR LOCATION: mRNA-capping enzyme nsP1: Host endosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host cell membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Host cell projection, host filopodium
{ECO:0000250}. Note=In the late phase of infection, the
polyprotein is quickly cleaved before localization to cellular
membranes. Then a fraction of nsP1 localizes to the inner surface
of the plasma membrane and its filopodial extensions (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protease nsP2: Host endosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host nucleus {ECO:0000250}.
Note=In the late phase of infection, the polyprotein is quickly
cleaved before localization to cellular membranes. Then
approximately half of nsP2 is found in the nucleus (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host endosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host cytoplasm {ECO:0000250}.
Note=In the late phase of infection, the polyprotein is quickly
cleaved before localization to cellular membranes. Then nsP3 and
nsP3' seems to aggregate in cytoplasm (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3': Host endosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host cytoplasm {ECO:0000250}.
Note=In the late phase of infection, the polyprotein is quickly
cleaved before localization to cellular membranes. Then nsP3 and
nsP3' seems to aggregate in cytoplasm (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase nsP4: Host
endosome membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Host lysosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}.
-!- INDUCTION: Viral replication produces dsRNA in the late phase of
infection, resulting in a strong activation of host EIF2AK2/PKR,
leading to almost complete phosphorylation of EIF2A. This
inactivates completely cellular translation initiation, resulting
in a dramatic shutoff of proteins synthesis. Translation of viral
non-structural polyprotein and all cellular proteins are stopped
in infected cell between 2 and 4 hours post infection. Only the
26S mRNA is still translated into viral structural proteins,
presumably through a unique mechanism of enhancer element which
counteract the translation inhibition mediated by EIF2A. By doing
this, the virus uses the cellular defense for its own advantage:
shutoff of cellular translation allows to produce big amounts of
structural proteins needed for the virus to bud out of the doomed
cell.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
The polyprotein is synthesized as P123, or P1234 by stop codon
readthrough. These polyproteins are processed differently
depending on the stage of infection. In early stages, P1234 is
first cleaved in trans, through its nsP2 protease activity,
releasing P123' and nsP4. P123/P123' and nsP4 start to replicate
the viral genome into its antigenome. After these early events,
nsP1 is cleaved in cis by nsP2 protease, releasing the P23/P23'
polyprotein. Cleavage of nsP1 exposes an 'activator' at the N-
terminus of P23/P23' which induces its cleavage into nsP2 and nsP3
by the viral protease. This sequence of delayed processing would
allow correct assembly and membrane association of the RNA-
polymerase complex. In the late stage of infection, the presence
of free nsP2 in the cytoplasm cleaves P1234 quickly into P12 and
P34, then into the four nsP (By similarity). {ECO:0000250}.
-!- PTM: nsP1 is palmitoylated by host. {ECO:0000250}.
-!- PTM: nsP4 is ubiquitinated; targets the protein for rapid
degradation via the ubiquitin system. {ECO:0000250}.
-!- MISCELLANEOUS: The genome codes for P123, but readthrough of a
terminator codon UGA occurs between the codons for Gln-1879 and
Arg-1880. This readthrough produces P1234, cleaved quickly by nsP2
into P123' and nsP4. Further processing of p123' gives nsP1, nsP2
and nsP3' which is 7 amino acids longer than nsP3 since the
cleavage site is after the readthrough. This unusual molecular
mechanism ensures that few nsP4 are produced compared to other
non-structural proteins. Mutant viruses with no alternative
termination site grow significantly slower than wild-type virus
(By similarity). {ECO:0000250}.
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EMBL; J04332; AAB02518.1; -; Genomic_RNA.
EMBL; L01442; AAC19321.2; -; Genomic_RNA.
EMBL; L01443; AAB02516.1; -; Genomic_RNA.
EMBL; AF069903; AAC24033.1; -; Genomic_RNA.
EMBL; AY741139; AAU89533.1; -; Genomic_RNA.
PIR; A31467; MNWVTD.
PDB; 2HWK; X-ray; 2.45 A; A=1003-1322.
PDB; 5EZQ; X-ray; 1.66 A; A=992-1327.
PDB; 5EZS; X-ray; 2.16 A; A=992-1327.
PDBsum; 2HWK; -.
PDBsum; 5EZQ; -.
PDBsum; 5EZS; -.
ProteinModelPortal; P27282; -.
SMR; P27282; -.
MEROPS; C09.002; -.
PRIDE; P27282; -.
OrthoDB; VOG09000007; -.
EvolutionaryTrace; P27282; -.
Proteomes; UP000008659; Genome.
Proteomes; UP000100999; Genome.
Proteomes; UP000127220; Genome.
Proteomes; UP000146452; Genome.
Proteomes; UP000158519; Genome.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0044176; C:host cell filopodium; IEA:UniProtKB-SubCell.
GO; GO:0044188; C:host cell lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
GO; GO:0039523; P:suppression by virus of host RNA polymerase II activity; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR002588; Alphavirus-like_MT_dom.
InterPro; IPR002620; Alphavirus_nsp2pro.
InterPro; IPR002589; Macro_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
Pfam; PF01661; Macro; 1.
Pfam; PF01707; Peptidase_C9; 1.
Pfam; PF00978; RdRP_2; 1.
Pfam; PF01443; Viral_helicase1; 1.
Pfam; PF01660; Vmethyltransf; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51743; ALPHAVIRUS_MT; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51520; NSP2PRO; 1.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host transcription shutoff by virus; GTP-binding; Helicase;
Host cell membrane; Host cell projection; Host cytoplasm;
Host endosome; Host gene expression shutoff by virus; Host lysosome;
Host membrane; Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host RNA polymerase II by virus; Lipoprotein; Membrane;
Methyltransferase; mRNA capping; mRNA processing;
Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
Palmitate; Phosphoprotein; Protease; RNA suppression of termination;
RNA-binding; RNA-directed RNA polymerase; S-adenosyl-L-methionine;
Thiol protease; Transferase; Ubl conjugation; Viral RNA replication.
CHAIN 1 2492 Non-structural polyprotein.
/FTId=PRO_0000308391.
CHAIN 1 1885 P123'.
/FTId=PRO_0000228770.
CHAIN 1 1879 P123.
/FTId=PRO_0000228771.
CHAIN 1 535 mRNA-capping enzyme nsP1.
/FTId=PRO_0000041208.
CHAIN 536 1329 Protease nsP2.
/FTId=PRO_0000041209.
CHAIN 1330 1885 Non-structural protein 3'.
/FTId=PRO_0000228772.
CHAIN 1330 1879 Non-structural protein 3.
/FTId=PRO_0000041210.
CHAIN 1886 2492 RNA-directed RNA polymerase nsP4.
/FTId=PRO_0000041211.
DOMAIN 28 259 Alphavirus-like MT. {ECO:0000255|PROSITE-
ProRule:PRU01079}.
DOMAIN 690 841 (+)RNA virus helicase ATP-binding.
DOMAIN 842 990 (+)RNA virus helicase C-terminal.
DOMAIN 1003 1322 Peptidase C9. {ECO:0000255|PROSITE-
ProRule:PRU00853}.
DOMAIN 1330 1489 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 2249 2364 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 721 728 ATP. {ECO:0000255}.
REGION 244 263 nsP1 membrane-binding. {ECO:0000250}.
REGION 1004 1023 Nucleolus localization signal.
{ECO:0000250}.
MOTIF 1179 1183 Nuclear localization signal.
{ECO:0000250}.
ACT_SITE 1012 1012 For cysteine protease nsP2 activity.
{ECO:0000255|PROSITE-ProRule:PRU00853}.
ACT_SITE 1081 1081 For cysteine protease nsP2 activity.
{ECO:0000255|PROSITE-ProRule:PRU00853}.
SITE 535 536 Cleavage; by nsP2. {ECO:0000250}.
SITE 1329 1330 Cleavage; by nsP2. {ECO:0000250}.
SITE 1885 1886 Cleavage; by nsP2. {ECO:0000250}.
LIPID 419 419 S-palmitoyl cysteine; by host.
{ECO:0000250}.
VARIANT 222 222 R -> C (in strain: 71-180).
VARIANT 551 551 A -> D (in strain: TC-83).
CONFLICT 21 21 S -> T (in Ref. 1; AAB02518).
{ECO:0000305}.
CONFLICT 497 497 A -> R (in Ref. 1; AAB02518).
{ECO:0000305}.
CONFLICT 1589 1589 T -> S (in Ref. 1; AAB02518).
{ECO:0000305}.
CONFLICT 1880 1880 R -> RR (in Ref. 1; AAC19321/AAB02516 and
2; AAC24033). {ECO:0000305}.
TURN 1004 1007 {ECO:0000244|PDB:5EZS}.
HELIX 1012 1022 {ECO:0000244|PDB:5EZS}.
TURN 1023 1025 {ECO:0000244|PDB:5EZS}.
HELIX 1030 1033 {ECO:0000244|PDB:5EZS}.
HELIX 1037 1040 {ECO:0000244|PDB:5EZS}.
HELIX 1047 1059 {ECO:0000244|PDB:5EZS}.
HELIX 1063 1065 {ECO:0000244|PDB:5EZS}.
STRAND 1076 1078 {ECO:0000244|PDB:5EZS}.
STRAND 1081 1083 {ECO:0000244|PDB:5EZS}.
STRAND 1090 1092 {ECO:0000244|PDB:5EZS}.
HELIX 1095 1102 {ECO:0000244|PDB:5EZS}.
HELIX 1108 1114 {ECO:0000244|PDB:5EZS}.
TURN 1120 1122 {ECO:0000244|PDB:5EZS}.
HELIX 1158 1162 {ECO:0000244|PDB:5EZS}.
STRAND 1167 1174 {ECO:0000244|PDB:5EZS}.
STRAND 1181 1189 {ECO:0000244|PDB:5EZS}.
STRAND 1193 1195 {ECO:0000244|PDB:5EZS}.
HELIX 1198 1200 {ECO:0000244|PDB:5EZS}.
STRAND 1209 1215 {ECO:0000244|PDB:5EZS}.
HELIX 1224 1237 {ECO:0000244|PDB:5EZS}.
TURN 1238 1240 {ECO:0000244|PDB:5EZS}.
HELIX 1241 1245 {ECO:0000244|PDB:5EZS}.
STRAND 1246 1256 {ECO:0000244|PDB:5EZS}.
HELIX 1262 1272 {ECO:0000244|PDB:5EZS}.
STRAND 1275 1281 {ECO:0000244|PDB:5EZS}.
STRAND 1292 1299 {ECO:0000244|PDB:5EZS}.
HELIX 1309 1320 {ECO:0000244|PDB:5EZS}.
SEQUENCE 2492 AA; 277776 MW; A3154E15BF45DD08 CRC64;
MEKVHVDIEE DSPFLRALQR SFPQFEVEAK QVTDNDHANA RAFSHLASKL IETEVDPSDT
ILDIGSAPAR RMYSKHKYHC ICPMRCAEDP DRLYKYATKL KKNCKEITDK ELDKKMKELA
AVMSDPDLET ETMCLHDDES CRYEGQVAVY QDVYAVDGPT SLYHQANKGV RVAYWIGFDT
TPFMFKNLAG AYPSYSTNWA DETVLTARNI GLCSSDVMER SRRGMSILRK KYLKPSNNVL
FSVGSTIYHE KRDLLRSWHL PSVFHLRGKQ NYTCRCETIV SCDGYVVKRI AISPGLYGKP
SGYAATMHRE GFLCCKVTDT LNGERVSFPV CTYVPATLCD QMTGILATDV SADDAQKLLV
GLNQRIVVNG RTQRNTNTMK NYLLPVVAQA FARWAKEYKE DQEDERPLGL RDRQLVMGCC
WAFRRHKITS IYKRPDTQTI IKVNSDFHSF VLPRIGSNTL EIGLRTRIRK MLEEHKEPSP
LITAEDVQEA KCAADEAKEV REAEELRAAL PPLAADVEEP TLEADVDLML QEAGAGSVET
PRGLIKVTSY AGEDKIGSYA VLSPQAVLKS EKLSCIHPLA EQVIVITHSG RKGRYAVEPY
HGKVVVPEGH AIPVQDFQAL SESATIVYNE REFVNRYLHH IATHGGALNT DEEYYKTVKP
SEHDGEYLYD IDRKQCVKKE LVTGLGLTGE LVDPPFHEFA YESLRTRPAA PYQVPTIGVY
GVPGSGKSGI IKSAVTKKDL VVSAKKENCA EIIRDVKKMK GLDVNARTVD SVLLNGCKHP
VETLYIDEAF ACHAGTLRAL IAIIRPKKAV LCGDPKQCGF FNMMCLKVHF NHEICTQVFH
KSISRRCTKS VTSVVSTLFY DKKMRTTNPK ETKIVIDTTG STKPKQDDLI LTCFRGWVKQ
LQIDYKGNEI MTAAASQGLT RKGVYAVRYK VNENPLYAPT SEHVNVLLTR TEDRIVWKTL
AGDPWIKTLT AKYPGNFTAT IEEWQAEHDA IMRHILERPD PTDVFQNKAN VCWAKALVPV
LKTAGIDMTT EQWNTVDYFE TDKAHSAEIV LNQLCVRFFG LDLDSGLFSA PTVPLSIRNN
HWDNSPSPNM YGLNKEVVRQ LSRRYPQLPR AVATGRVYDM NTGTLRNYDP RINLVPVNRR
LPHALVLHHN EHPQSDFSSF VSKLKGRTVL VVGEKLSVPG KMVDWLSDRP EATFRARLDL
GIPGDVPKYD IIFVNVRTPY KYHHYQQCED HAIKLSMLTK KACLHLNPGG TCVSIGYGYA
DRASESIIGA IARQFKFSRV CKPKSSLEET EVLFVFIGYD RKARTHNPYK LSSTLTNIYT
GSRLHEAGCA PSYHVVRGDI ATATEGVIIN AANSKGQPGG GVCGALYKKF PESFDLQPIE
VGKARLVKGA AKHIIHAVGP NFNKVSEVEG DKQLAEAYES IAKIVNDNNY KSVAIPLLST
GIFSGNKDRL TQSLNHLLTA LDTTDADVAI YCRDKKWEMT LKEAVARREA VEEICISDDS
SVTEPDAELV RVHPKSSLAG RKGYSTSDGK TFSYLEGTKF HQAAKDIAEI NAMWPVATEA
NEQVCMYILG ESMSSIRSKC PVEESEASTP PSTLPCLCIH AMTPERVQRL KASRPEQITV
CSSFPLPKYR ITGVQKIQCS QPILFSPKVP AYIHPRKYLV ETPPVDETPE PSAENQSTEG
TPEQPPLITE DETRTRTPEP IIIEEEEEDS ISLLSDGPTH QVLQVEADIH GPPSVSSSSW
SIPHASDFDV DSLSILDTLE GASVTSGATS AETNSYFAKS MEFLARPVPA PRTVFRNPPH
PAPRTRTPSL APSRACSRTS LVSTPPGVNR VITREELEAL TPSRTPSRSV SRTSLVSNPP
GVNRVITREE FEAFVAQQQR FDAGAYIFSS DTGQGHLQQK SVRQTVLSEV VLERTELEIS
YAPRLDQEKE ELLRKKLQLN PTPANRSRYQ SRKVENMKAI TARRILQGLG HYLKAEGKVE
CYRTLHPVPL YSSSVNRAFS SPKVAVEACN AMLKENFPTV ASYCIIPEYD AYLDMVDGAS
CCLDTASFCP AKLRSFPKKH SYLEPTIRSA VPSAIQNTLQ NVLAAATKRN CNVTQMRELP
VLDSAAFNVE CFKKYACNNE YWETFKENPI RLTEENVVNY ITKLKGPKAA ALFAKTHNLN
MLQDIPMDRF VMDLKRDVKV TPGTKHTEER PKVQVIQAAD PLATAYLCGI HRELVRRLNA
VLLPNIHTLF DMSAEDFDAI IAEHFQPGDC VLETDIASFD KSEDDAMALT ALMILEDLGV
DAELLTLIEA AFGEISSIHL PTKTKFKFGA MMKSGMFLTL FVNTVINIVI ASRVLRERLT
GSPCAAFIGD DNIVKGVKSD KLMADRCATW LNMEVKIIDA VVGEKAPYFC GGFILCDSVT
GTACRVADPL KRLFKLGKPL AADDEHDDDR RRALHEESTR WNRVGILSEL CKAVESRYET
VGTSIIVMAM TTLASSVKSF SYLRGAPITL YG


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