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Genome polyprotein [Cleaved into: N-terminal protease (N-pro) (EC 3.4.22.-) (Autoprotease p20); Capsid protein C; E(rns) glycoprotein (gp44/48); Envelope glycoprotein E1 (gp33); Envelope glycoprotein E2 (gp55); p7; Non-structural protein 2-3; Cysteine protease NS2 (EC 3.4.22.-) (Non-structural protein 2); Serine protease NS3 (EC 3.4.21.113) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); Non-structural protein 5A (NS5A); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B)]

 POLG_BVDVS              Reviewed;        3898 AA.
Q01499;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
23-MAY-2018, entry version 140.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=N-terminal protease;
Short=N-pro;
EC=3.4.22.-;
AltName: Full=Autoprotease p20;
Contains:
RecName: Full=Capsid protein C;
Contains:
RecName: Full=E(rns) glycoprotein;
AltName: Full=gp44/48;
Contains:
RecName: Full=Envelope glycoprotein E1;
AltName: Full=gp33;
Contains:
RecName: Full=Envelope glycoprotein E2;
AltName: Full=gp55;
Contains:
RecName: Full=p7;
Contains:
RecName: Full=Non-structural protein 2-3;
Contains:
RecName: Full=Cysteine protease NS2;
EC=3.4.22.-;
AltName: Full=Non-structural protein 2;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.113;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=Non-structural protein 5A;
Short=NS5A;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48;
AltName: Full=NS5B;
Bovine viral diarrhea virus (strain SD-1) (BVDV) (Mucosal disease
virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Pestivirus.
NCBI_TaxID=31656;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1333126; DOI=10.1016/0042-6822(92)90262-N;
Deng R., Brock K.V.;
"Molecular cloning and nucleotide sequence of a pestivirus genome,
noncytopathic bovine viral diarrhea virus strain SD-1.";
Virology 191:867-869(1992).
-!- FUNCTION: Initial binding to target cell probably involves
interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are
responsible of cell attachment with CD46 and subsequent fusion
after internalization of the virion by endocytosis (By
similarity). {ECO:0000250}.
-!- FUNCTION: P7 forms a leader sequence to properly orient NS2 in the
membrane. {ECO:0000250}.
-!- FUNCTION: Uncleaved NS2-3 is required for production of infectious
virus. {ECO:0000250}.
-!- FUNCTION: NS2 protease seems to play a vital role in viral RNA
replication control and in the pathogenicity of the virus.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
-!- FUNCTION: NS3 displays three enzymatic activities: serine
protease, NTPase and RNA helicase. {ECO:0000250}.
-!- FUNCTION: NS4A is a cofactor for the NS3 protease activity.
{ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase NS5 replicates the viral (+)
and (-) genome. {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Leu is conserved at position P1 for all four
cleavage sites. Alanine is found at position P1' of the NS4A-NS4B
cleavage site, whereas serine is found at position P1' of the NS3-
NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: The E(rns) glycoprotein is found as a homodimer;
disulfide-linked. The E1 and E2 envelope glycoproteins form
disulfide-linked homodimers as well as heterodimers.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: E(rns) glycoprotein: Host membrane;
Peripheral membrane protein. Virion membrane; Peripheral membrane
protein {ECO:0000305}. Note=The C-terminus membrane anchor of Erns
represents an amphipathic helix embedded in plane into the
membrane. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E2: Host cell surface
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cysteine protease NS2: Host membrane
{ECO:0000255|PROSITE-ProRule:PRU01029}; Multi-pass membrane
protein {ECO:0000255|PROSITE-ProRule:PRU01029}.
-!- PTM: The E(rns) glycoprotein is heavily glycosylated.
{ECO:0000250}.
-!- PTM: The viral RNA of pestiviruses is expressed as a single
polyprotein which undergoes post-translational proteolytic
processing resulting in the production of at least eleven
individual proteins. The N-terminal protease cleaves itself from
the nascent polyprotein autocatalytically and thereby generates
the N-terminus of the adjacent viral capsid protein C (By
similarity). {ECO:0000250}.
-!- PTM: Cleavage between E2 and p7 is partial. {ECO:0000250}.
-!- MISCELLANEOUS: BVDV is divided in two types: cytopathic and non-
cytopathic. Both types of viruses can be found in animals
suffering from mucosal disease, as a cytopathic BVDV can develop
from a non-cytopathic virus within the infected animal by
deletions, mutations or insertions. Both types express uncleaved
NS2-3, but cytopathic strains also express NS3.
-!- SIMILARITY: Belongs to the pestivirus polyprotein family.
{ECO:0000305}.
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EMBL; M96751; AAA42860.1; -; Genomic_RNA.
PIR; A44217; A44217.
PDB; 2YQ2; X-ray; 2.58 A; A/B=696-1026.
PDB; 2YQ3; X-ray; 3.29 A; A/B=696-1026.
PDBsum; 2YQ2; -.
PDBsum; 2YQ3; -.
ProteinModelPortal; Q01499; -.
SMR; Q01499; -.
MEROPS; S31.001; -.
PRIDE; Q01499; -.
OrthoDB; VOG090000YQ; -.
BRENDA; 3.4.21.113; 925.
Proteomes; UP000007619; Genome.
GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0039548; P:suppression by virus of host IRF3 activity; IEA:UniProtKB-KW.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00079; HELICc; 1.
Gene3D; 3.90.730.10; -; 1.
InterPro; IPR021824; Capsid-C_pestivirus.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR022120; NS2.
InterPro; IPR030399; NS2_C74.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008751; Peptidase_C53.
InterPro; IPR032521; Pestivirus_E2.
InterPro; IPR000280; Pestivirus_NS3_S31.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002166; RNA_pol_HCV.
InterPro; IPR036430; RNase_T2-like_sf.
InterPro; IPR033130; RNase_T2_His_AS_2.
Pfam; PF11889; DUF3409; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF05550; Peptidase_C53; 1.
Pfam; PF12387; Peptidase_C74; 1.
Pfam; PF05578; Peptidase_S31; 1.
Pfam; PF16329; Pestivirus_E2; 1.
Pfam; PF00998; RdRP_3; 1.
PRINTS; PR00729; CDVENDOPTASE.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55895; SSF55895; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS00531; RNASE_T2_2; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Disulfide bond; Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host membrane; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host IRF3 by virus;
Inhibition of host RLR pathway by virus; Ion channel; Ion transport;
Membrane; Nucleotide-binding; Nucleotidyltransferase; Protease;
RNA-directed RNA polymerase; Serine protease; Thiol protease;
Transferase; Transmembrane; Transmembrane helix; Transport;
Viral attachment to host cell; Viral immunoevasion; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 168 N-terminal protease. {ECO:0000250}.
/FTId=PRO_0000038037.
CHAIN 169 270 Capsid protein C. {ECO:0000250}.
/FTId=PRO_0000038038.
CHAIN 271 497 E(rns) glycoprotein. {ECO:0000250}.
/FTId=PRO_0000038039.
CHAIN 498 659 Envelope glycoprotein E1. {ECO:0000250}.
/FTId=PRO_0000038040.
CHAIN 660 1066 Envelope glycoprotein E2. {ECO:0000250}.
/FTId=PRO_0000038041.
CHAIN 1067 1136 p7. {ECO:0000250}.
/FTId=PRO_0000038042.
CHAIN 1137 2272 Non-structural protein 2-3.
{ECO:0000250}.
/FTId=PRO_0000038043.
CHAIN 1137 1589 Cysteine protease NS2.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
/FTId=PRO_0000038044.
CHAIN 1590 2272 Serine protease NS3. {ECO:0000250}.
/FTId=PRO_0000038045.
CHAIN 2273 2336 Non-structural protein 4A. {ECO:0000250}.
/FTId=PRO_0000038046.
CHAIN 2337 2683 Non-structural protein 4B. {ECO:0000250}.
/FTId=PRO_0000038047.
CHAIN 2684 3179 Non-structural protein 5A. {ECO:0000250}.
/FTId=PRO_0000038048.
CHAIN 3180 3898 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000038049.
TRANSMEM 1144 1164 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1189 1209 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1217 1237 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1247 1267 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1281 1301 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1360 1380 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1568 1588 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
DOMAIN 1 168 Peptidase C53.
DOMAIN 1441 1589 Peptidase C74. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
DOMAIN 1590 1763 Peptidase S31. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
DOMAIN 1802 1960 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1978 2143 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 3518 3641 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
ACT_SITE 22 22 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046}.
ACT_SITE 49 49 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046}.
ACT_SITE 69 69 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046}.
ACT_SITE 1447 1447 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
ACT_SITE 1461 1461 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
ACT_SITE 1512 1512 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
ACT_SITE 1658 1658 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
ACT_SITE 1695 1695 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
ACT_SITE 1752 1752 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
SITE 168 169 Cleavage; by autolysis. {ECO:0000250}.
SITE 270 271 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 497 498 Cleavage. {ECO:0000250}.
SITE 659 660 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1066 1067 Cleavage; by host signal peptidase;
partial. {ECO:0000250}.
SITE 1136 1137 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1589 1590 Cleavage; partial; cysteine protease NS2.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
SITE 2272 2273 Cleavage; by serine protease NS3.
{ECO:0000250}.
SITE 2336 2337 Cleavage; by serine protease NS3.
{ECO:0000250}.
SITE 2683 2684 Cleavage; by serine protease NS3.
{ECO:0000250}.
SITE 3179 3180 Cleavage; by serine protease NS3.
{ECO:0000250}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 487 487 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 597 597 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 809 809 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 878 878 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 922 922 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 990 990 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1357 1357 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1419 1419 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1451 1451 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1713 1713 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2134 2134 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2217 2217 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2494 2494 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2682 2682 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2751 2751 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2891 2891 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2988 2988 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3688 3688 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3777 3777 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3793 3793 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
STRAND 700 706 {ECO:0000244|PDB:2YQ2}.
STRAND 714 716 {ECO:0000244|PDB:2YQ2}.
STRAND 718 720 {ECO:0000244|PDB:2YQ2}.
STRAND 730 732 {ECO:0000244|PDB:2YQ2}.
STRAND 734 750 {ECO:0000244|PDB:2YQ2}.
STRAND 756 765 {ECO:0000244|PDB:2YQ2}.
HELIX 767 769 {ECO:0000244|PDB:2YQ2}.
STRAND 771 776 {ECO:0000244|PDB:2YQ2}.
STRAND 783 786 {ECO:0000244|PDB:2YQ2}.
STRAND 793 795 {ECO:0000244|PDB:2YQ2}.
HELIX 797 799 {ECO:0000244|PDB:2YQ2}.
STRAND 801 808 {ECO:0000244|PDB:2YQ2}.
STRAND 811 814 {ECO:0000244|PDB:2YQ2}.
STRAND 817 820 {ECO:0000244|PDB:2YQ2}.
STRAND 828 835 {ECO:0000244|PDB:2YQ2}.
TURN 837 839 {ECO:0000244|PDB:2YQ2}.
STRAND 842 852 {ECO:0000244|PDB:2YQ2}.
STRAND 863 866 {ECO:0000244|PDB:2YQ2}.
STRAND 869 875 {ECO:0000244|PDB:2YQ2}.
HELIX 878 880 {ECO:0000244|PDB:2YQ2}.
STRAND 882 886 {ECO:0000244|PDB:2YQ2}.
STRAND 894 899 {ECO:0000244|PDB:2YQ2}.
STRAND 902 906 {ECO:0000244|PDB:2YQ2}.
STRAND 910 914 {ECO:0000244|PDB:2YQ2}.
STRAND 916 920 {ECO:0000244|PDB:2YQ2}.
STRAND 924 928 {ECO:0000244|PDB:2YQ2}.
STRAND 934 936 {ECO:0000244|PDB:2YQ2}.
STRAND 939 941 {ECO:0000244|PDB:2YQ2}.
STRAND 946 951 {ECO:0000244|PDB:2YQ2}.
STRAND 954 961 {ECO:0000244|PDB:2YQ2}.
STRAND 964 967 {ECO:0000244|PDB:2YQ2}.
STRAND 969 973 {ECO:0000244|PDB:2YQ2}.
STRAND 976 982 {ECO:0000244|PDB:2YQ2}.
STRAND 985 993 {ECO:0000244|PDB:2YQ2}.
TURN 1005 1007 {ECO:0000244|PDB:2YQ2}.
STRAND 1011 1013 {ECO:0000244|PDB:2YQ2}.
STRAND 1016 1024 {ECO:0000244|PDB:2YQ2}.
SEQUENCE 3898 AA; 437808 MW; 31ACEE140D407ED3 CRC64;
MELITNELLY KTYKQKPVGV EEPVYDQAGN PLFGERGAIH PQSTLKLPHK RGERNVPTSL
ASLPKRGDCR SGNSKGPVSG IYLKPGPLFY QDYKGPVYHR APLELFEEGS MCETTKRIGR
VTGSDGKLYH IYICIDGCIT VKSATRSHQR VLRWVHNRLD CPLWVTSCSD TKEEGATKKK
QQKPDRLEKG RMKIVPKESE KDSKTKPPDA TIVVDGVKYQ VKKKGKVKSK NTQDGLYHNK
NKPPESRKKL EKALLAWAIL AVVLIEVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH
GIWPEKICTG VPSHLATDVE LKTIHGMMDA SEKTNYTCCR LQRHEWNKHG WCNWYNIEPW
ILIMNRTQAN LTEGQPPREC AVTCRYDRDS DLNVVTQARD SPTPLTGCKK GKNFSFAGVL
TRGPCNFEIA ASDVLFKEHE CTGVFQDTAH YLVDGVTNSL ESARQGTAKL TTWLGKQLGI
LGKKLENKSK TWFGAYAASP YCDVDRKIGY IWFTKNCTPA CLPKNTKIIG PGKFDTNAED
GKILHEMGGH LSEVLLLSLV VLSDFAPETA SAMYLILHFS IPQSHVDITD CDKTQLNLTI
ELTTADVIPG SVWNLGKYVC IRPDWWPYET AAVLAFEEVG QVVKIVLRAL RDLTRIWNAA
TTTAFLVCLI KMVRGQVVQG ILWLLLITGV QGHLDCKPEY SYAIAKNDRV GPLGAEGLTT
VWKDYSHEMK LEDTMVIAWC KGGKFTYLSR CTRETRYLAI LHSRALPTSV VFKKLFEGQK
QEDTVEMDDD FEFGLCPCDA KPIVRGKFNT TLLNGPAFQM VCPIGWTGTV SCMLANRDTL
DTAVVRTYRR SVPFPYRQGC ITQKTLGEDL YDCALGGNWT CVTGDQSRYT GGLIESCKWC
GYKFQKSEGL PHYPIGKCRL NNETGYRLVD DTSCDREGVA IVPHGLVKCK IGDTTVQVIA
TDTKLGPMPC KPHEIISSEG PIEKTACTFN YTRTLKNKYF EPRDSYFQQY MLKGDYQYWF
DLEVTDHHRD YFAESILVVV VALLGGRYVL WLLVTYMVLS EQKASGAQYG AGEVVMMGNL
LTHDNVEVVT YFFLLYLLLR EESVKKWVLL LYHILVAHPL KSVIVILLMI GDVVKADPGG
QGYLGQIDVC FTMVVIIIIG LIIARRDPTI VPLITIVASL RVTGLTYSPG VDAAMAVITI
TLLMVSYVTD YFRYKRWLQC ILSLVSGVFL IRCLIHLGRI ETPEVTIPNW RPLTLILFYL
ISTTVVTMWK IDLAGLLLQG VPILLLITTL WADFLTLILI LPTYELVKLY YLKTIKTDIE
KSWLGGLDYK RVDSIYDVDE SGEGVYLFPS RQKAQKNFSM LLPLVRATLI SCVSSKWQLI
YMAYLSVDFM YYMHRKVIEE ISGGTNMISR IVAALIELNW SMEEEESKGL KKFYLLSGRL
RNLIIKHKVR NETVAGWYGE EEVYGMPKIM TIIKASTLNK NKHCIICTVC EGRKWKGGTC
PKCGRHGKPI TCGMSLADFE ERHYKRIFIR EGNFEGPFRQ EYNGFIQYTA RGQLFLRNLP
ILATKVKMLM VGNLGEEVGD LEHLGWILRG PAVCKKITEH ERCHINILDK LTAFFGIMPR
GTTPRAPVRF PTSLLKVRRG LETGWAYTHQ GGISSVDHVT AGKDLLVCDS MGRTRVVCQS
NNKLTDETEY GVKTDSGCPD GARCYVLNPE AVNISGSKGA VVHLQKTGGE FTCVTASGTP
AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEESKPTK IMSGIQTVSK NTADLTEMVK
KITSMNRGDF KQITLATGAG KTTELPKAVI EEIGRHKRVL VLIPLRAAAE SVYQYMRLKH
PSISFNLRIG DMKEGDMATG ITYASYGYFC QMPQPKLRAA MVEYSYIFLD EYHCATPEQL
AIIGKIHRFS ESIRVVAMTA TPAGSVTTTG QKHPIEEFIA PEVMEGEDLG SQFLDIAGLK
IPVDEMKGNM LVFVPTRNMA VEVAKKLKAK GYNSGYYYSG EDPANLRVVT SQSPYVIVAT
NAIESGVTLP DLDTVVDTGL KCEKRVRVSS KIPFIVTGLK RMAVTVGEQA QRRGRVGRVK
PGRYYRSQET ATGSKDYHYD LLQAQRYGIE DGINVTKSFR EMNYDWSLYE EDSLLITQLE
ILNNLLISED LPAAVKNIMA RTDHPEPIQL AYNSYEVQVP VLFPKIRNGE VTDTYENYSF
LNARKLGEDV PVYIYATEDE DLAVDLLGLD WPDPGNQQVV ETGKALKQVA GLSSAENALL
VALFGYVGYQ ALSKRHVPMI TDIYTIEDQR LEDTTHLQYA PNAIKTEGTE TELKELASGD
VEKIMGAISD YAAGGLDFVK SQAEKIKTAP LFKENVEAAR GYVQKLIDSL IEDKDVIIRY
GLWGTHTALY KSIAARLGHE TAFATLVLKW LAFGGETVSD HIRQAAVDLV VYYVMNKPSF
PGDTETQQEG RRFVASLFIS ALATYTYKTW NYNNLSKVVE PALAYLPYAT SALKMFTPTR
LESVVILSTT IYKTYLSIRK GKSDGLLGTG ISAAMEILSQ NPVSVGISVM LGVGAIAAHN
AIESSEQKRT LLMKVFVKNF LDQAATDELV KENPEKIIMA LFEAVQTIGN PLRLIYHLYG
VYYKGWEAKE LSERTAGRNL FTLIMFEAFE LLGMDSEGKI RNLSGNYILD LIHGLHKQIN
RGLKKIVLGW APAPFSCDWT PSDERIRLPT DSYLRVETKC PCGYEMKALK NVSGKLTKVE
ESGPFLCRNR PGRGPVNYRV TKYYDDNLRE IRPVAKLEGQ VEHYYKGVTA RIDYSKGKTL
LATDKWEVEH GTLTRLTKRY TGVGFRGAYL GDEPNHRDLV ERDCATITKN TVQFLKMKKG
CAFTYDLTIS NLTRLIELVH RNNLEEKEIP TATVTTWLAY TFVNEDVGTI KPVLGERVIP
DPVVDINLQP EVQVDTSEVG ITIIGKEAVM TTGVTPVMEK VEPDTDNNQS SVKIGLDEGN
YPGPGVQTHT LVEEIHNKDA RPFIMVLGSK SSMSNRAKTA RNINLYTGND PREIRDLMAE
GRILVVALRD IDPDLSELVD FKGTFLDREA LEALSLGQPK PKQVTKAAIR DLLKEERQVE
IPDWFTSDDP VFLDIAMKKD KYHLIGDVVE VKDQAKALGA TDQTRIVKEV GSRTYTMKLS
SWFLQASSKQ MSLTPLFEEL LLRCPPATKS NKGHMASAYQ LAQGNWEPLG CGVHLGTVPA
RRVKMHPYEA YLKLKDLVEE EEKKPRIRDT VIREHNKWIL KKIKFQGNLN TKKMLNPGKL
SEQLDREGHK RNIYNNQIST VMSSAGIRLE KLPIVRAQTD TKSFHEAIRD KIDKNENRQN
PELHNKLLEI FHTIADPSLK HTYGEVTWEQ LEAGINRKGA AGFLEKKNIG EVLDSEKHLV
EQLVRDLKAG RKIRYYETAI PKNEKRDVSD DWQAGDLVDE KKPRVIQYPE AKTRLAITKV
MYNWVKQQPV VIPGYEGKTP LFNIFNKVRK EWDLFNEPVA VSFDTKAWDT QVTSRDLHLI
GEIQKYYYRK EWHKFIDTIT DHMVEVPVIT ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT
MIYAFCESTG VPYKSFNRVA KIHVCGDDGF LITEKGLGLK FSNKGMQILH EAGKPQKLTE
GEKMKVAYKF EDIEFCSHTP VPVRWSDNTS SYMAGRDTAV ILSKMATRLD SSGERGTTAY
EKAVAFSFLL MYSWNPLVRR ICLLVLSQRP ETAPSTQTTY YYKGDPIGAY KDVIGRNLSE
LKRTGFEKLA NLNLSLSTLG IWTKHTSKRI IQDCVAIGKE EGNWLVNADR LISSKTGHLY
IPDKGFTLQG KHYEQLQLGA ETNPVMGVGT ERYKLGPIVN LLLRRLKVLL MAAVGASS


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