POLG_BVDVC
ID POLG_BVDVC Reviewed; 3907 AA.
AC Q96662;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=N-terminal protease;
DE Short=N-pro;
DE EC=3.4.22.-;
DE AltName: Full=Autoprotease p20;
DE Contains:
DE RecName: Full=Capsid protein C;
DE Contains:
DE RecName: Full=E(rns) glycoprotein;
DE AltName: Full=gp44/48;
DE Contains:
DE RecName: Full=Envelope glycoprotein E1;
DE AltName: Full=gp33;
DE Contains:
DE RecName: Full=Envelope glycoprotein E2;
DE AltName: Full=gp55;
DE Contains:
DE RecName: Full=Viroporin p7 {ECO:0000250|UniProtKB:P19712};
DE Contains:
DE RecName: Full=Non-structural protein 2-3;
DE Contains:
DE RecName: Full=Cysteine protease NS2;
DE EC=3.4.22.-;
DE AltName: Full=Non-structural protein 2;
DE Contains:
DE RecName: Full=Serine protease NS3;
DE EC=3.4.21.113;
DE EC=3.6.1.15;
DE EC=3.6.4.13;
DE AltName: Full=Non-structural protein 3;
DE Contains:
DE RecName: Full=Non-structural protein 4A;
DE Short=NS4A;
DE Contains:
DE RecName: Full=Non-structural protein 4B;
DE Short=NS4B;
DE Contains:
DE RecName: Full=Non-structural protein 5A;
DE Short=NS5A;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=NS5B;
OS Bovine viral diarrhea virus (strain CP7) (BVDV) (Mucosal disease virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Pestivirus.
OX NCBI_TaxID=268305;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8970985; DOI=10.1128/jvi.70.12.8606-8613.1996;
RA Meyers G., Tautz N., Becher P., Thiel H., Kuemmerer B.M.;
RT "Recovery of cytopathogenic and noncytopathogenic bovine viral diarrhea
RT viruses from cDNA constructs.";
RL J. Virol. 70:8606-8613(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate CP7-5A;
RX PubMed=10933696; DOI=10.1128/jvi.74.17.7884-7894.2000;
RA Becher P., Orlich M., Thiel H.-J.;
RT "Mutations in the 5' nontranslated region of bovine viral diarrhea virus
RT result in altered growth characteristics.";
RL J. Virol. 74:7884-7894(2000).
RN [3]
RP PROTEIN SEQUENCE OF 1067-1083, AND PROTEOLYTIC PROCESSING (GENOME
RP POLYPROTEIN).
RX PubMed=8648755; DOI=10.1128/jvi.70.6.4131-4135.1996;
RA Elbers K., Tautz N., Becher P., Stoll D., Ruemenapf T., Thiel H.-J.;
RT "Processing in the pestivirus E2-NS2 region: identification of proteins p7
RT and E2p7.";
RL J. Virol. 70:4131-4135(1996).
RN [4]
RP PROTEIN SEQUENCE OF 2282-2289; 2693-2705 AND 3189-3202, AND PROTEOLYTIC
RP PROCESSING OF POLYPROTEIN.
RX PubMed=9188613; DOI=10.1128/jvi.71.7.5415-5422.1997;
RA Tautz N., Elbers K., Stoll D., Meyers G., Thiel H.-J.;
RT "Serine protease of pestiviruses: determination of cleavage sites.";
RL J. Virol. 71:5415-5422(1997).
RN [5]
RP PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN).
RX PubMed=11000219; DOI=10.1128/jvi.74.20.9498-9506.2000;
RA Harada T., Tautz N., Thiel H.-J.;
RT "E2-p7 region of the bovine viral diarrhea virus polyprotein: processing
RT and functional studies.";
RL J. Virol. 74:9498-9506(2000).
RN [6]
RP CLEAVAGE BETWEEN NS2 AND NS3, AND ACTIVE SITES (CYSTEINE PROTEASE NS2).
RC STRAIN=CP7, and NCP7;
RX PubMed=15367643; DOI=10.1128/jvi.78.19.10765-10775.2004;
RA Lackner T., Mueller A., Pankraz A., Becher P., Thiel H.-J.,
RA Gorbalenya A.E., Tautz N.;
RT "Temporal modulation of an autoprotease is crucial for replication and
RT pathogenicity of an RNA virus.";
RL J. Virol. 78:10765-10775(2004).
RN [7]
RP SUBCELLULAR LOCATION (E(RNS) GLYCOPROTEIN), AND MUTAGENESIS OF GLU-438;
RP GLN-446; GLY-455; LEU-460; GLU-461; SER-462; GLN-465; LYS-469; THR-471;
RP TRP-473; ARG-476; LEU-478; LEU-481; GLU-486; ASN-487; SER-489 AND TRP-492.
RX PubMed=17848558; DOI=10.1074/jbc.m706803200;
RA Tews B.A., Meyers G.;
RT "The pestivirus glycoprotein Erns is anchored in plane in the membrane via
RT an amphipathic helix.";
RL J. Biol. Chem. 282:32730-32741(2007).
CC -!- FUNCTION: [N-terminal protease]: Leader cysteine autoprotease that
CC cleaves itself from the nascent polyprotein during translation of the
CC viral mRNA. Once released, plays a role in the inhibition of host
CC innate immune response by interacting with host IRF3 and inducing its
CC proteasomal degradation. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Capsid protein C]: Packages viral RNA to form a viral
CC nucleocapsid and thereby protects viral RNA. Also plays a role in
CC transcription regulation. Protects the incoming virus against IFN-
CC induced effectors. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [E(rns) glycoprotein]: Initial binding to target cell
CC probably involves interaction of E(rns) with glycosaminoglycans.
CC {ECO:0000250|UniProtKB:P19711}.
CC -!- FUNCTION: [Envelope glycoprotein E1]: E1 and/or E2 are probably
CC responsible of cell attachment with CD46 and subsequent fusion after
CC internalization of the virion by endocytosis.
CC {ECO:0000250|UniProtKB:P19711}.
CC -!- FUNCTION: [Envelope glycoprotein E2]: E1 and/or E2 are probably
CC responsible of cell attachment with CD46 and subsequent fusion after
CC internalization of the virion by endocytosis.
CC {ECO:0000250|UniProtKB:P19711}.
CC -!- FUNCTION: [Viroporin p7]: Plays an essential role in the virus
CC replication cycle by acting as a viroporin (By similarity). Forms ion
CC conductive pores, which alters the cell permeability allowing the
CC transport of ions and other small molecules (By similarity). Forms a
CC leader sequence to properly orient NS2 in the membrane.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 2-3]: Uncleaved NS2-3 is required for
CC production of infectious virus.
CC -!- FUNCTION: [Cysteine protease NS2]: Plays a role in the regulation of
CC viral RNA replication. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Serine protease NS3]: Multifunctional protein that contains
CC an N-terminal protease and a C-terminal helicase, playing essential
CC roles in viral polyprotein processing and viral genome replication. The
CC chymotrypsin-like serine protease activity utilizes NS4A as an
CC essential cofactor and catalyzes the cleavage of the polyprotein
CC leading to the release of NS4A, NS4B, NS5A, and NS5B. Interacts with
CC NS5B to enhance RNA-dependent RNA polymerase activity.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 4A]: Acts as a cofactor for the NS3
CC protease activity. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 4B]: Induces a specific membrane
CC alteration that serves as a scaffold for the virus replication complex.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral (+) and
CC (-) genome.
CC -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC Reaction=Leu is conserved at position P1 for all four cleavage sites.
CC Alanine is found at position P1' of the NS4A-NS4B cleavage site,
CC whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A
CC and NS5A-NS5B cleavage sites.; EC=3.4.21.113;
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
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: [Serine protease NS3]:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: [E(rns) glycoprotein]: Homodimer; disulfide-linked.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [Envelope glycoprotein E1]: Homodimer; disulfide-linked (By
CC similarity). Heterodimer with E1; disulfide-linked (By similarity).
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [Envelope glycoprotein E2]: Homodimer; disulfide-linked (By
CC similarity). Heterodimer with E1; disulfide-linked (By similarity).
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- INTERACTION:
CC PRO_0000038022; P68103: EEF1A1; Xeno; NbExp=2; IntAct=EBI-9350684, EBI-352178;
CC -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [E(rns) glycoprotein]: Host membrane; Peripheral
CC membrane protein. Virion membrane; Peripheral membrane protein
CC {ECO:0000305}. Note=The C-terminus membrane anchor of Erns represents
CC an amphipathic helix embedded in plane into the membrane.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Host cell surface
CC {ECO:0000250|UniProtKB:P19711}. Virion membrane
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [Cysteine protease NS2]: Host membrane
CC {ECO:0000255|PROSITE-ProRule:PRU01029}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU01029}.
CC -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 5A]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- PTM: [E(rns) glycoprotein]: Heavily glycosylated.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- PTM: The viral RNA of pestiviruses is expressed as a single polyprotein
CC which undergoes post-translational proteolytic processing resulting in
CC the production of at least eleven individual proteins. The N-terminal
CC protease cleaves itself from the nascent polyprotein autocatalytically
CC and thereby generates the N-terminus of the adjacent viral capsid
CC protein C. {ECO:0000250|UniProtKB:P19712}.
CC -!- PTM: [Genome polyprotein]: Cleavage between E2 and p7 is partial.
CC -!- MISCELLANEOUS: BVDV is divided in two types: cytopathic and non-
CC cytopathic. Both types of viruses can be found in animals suffering
CC from mucosal disease, as a cytopathic BVDV can develop from a non-
CC cytopathic virus within the infected animal by deletions, mutations or
CC insertions. Both types express uncleaved NS2-3, but cytopathic strains
CC also express NS3.
CC -!- SIMILARITY: Belongs to the pestivirus polyprotein family.
CC {ECO:0000305}.
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DR EMBL; U63479; AAC55984.1; -; Genomic_RNA.
DR EMBL; AF220247; AAG00378.1; -; Genomic_RNA.
DR PDB; 2AJJ; NMR; -; A=2693-2720.
DR PDB; 2AJM; NMR; -; A=2693-2720.
DR PDB; 2AJN; NMR; -; A=2693-2720.
DR PDB; 2AJO; NMR; -; A=2693-2720.
DR PDB; 2CJQ; X-ray; 2.60 A; A=3189-3907.
DR PDB; 4DVK; X-ray; 2.21 A; A/B=271-435.
DR PDB; 4DVL; X-ray; 2.75 A; A/B=271-435.
DR PDB; 4DVN; X-ray; 2.38 A; A/B=271-435.
DR PDB; 4DW3; X-ray; 2.35 A; A/B=271-435.
DR PDB; 4DW4; X-ray; 2.23 A; A/B=271-435.
DR PDB; 4DW5; X-ray; 2.21 A; A/B=271-435.
DR PDB; 4DW7; X-ray; 3.08 A; A/B=271-435.
DR PDB; 4DWA; X-ray; 3.01 A; A/B=271-435.
DR PDB; 4DWC; X-ray; 2.89 A; A/B=271-435.
DR PDBsum; 2AJJ; -.
DR PDBsum; 2AJM; -.
DR PDBsum; 2AJN; -.
DR PDBsum; 2AJO; -.
DR PDBsum; 2CJQ; -.
DR PDBsum; 4DVK; -.
DR PDBsum; 4DVL; -.
DR PDBsum; 4DVN; -.
DR PDBsum; 4DW3; -.
DR PDBsum; 4DW4; -.
DR PDBsum; 4DW5; -.
DR PDBsum; 4DW7; -.
DR PDBsum; 4DWA; -.
DR PDBsum; 4DWC; -.
DR BMRB; Q96662; -.
DR SMR; Q96662; -.
DR IntAct; Q96662; 1.
DR BindingDB; Q96662; -.
DR ChEMBL; CHEMBL3937; -.
DR MEROPS; S31.001; -.
DR TCDB; 1.A.53.1.5; the hepatitis c virus p7 viroporin cation-selective channel (hcv-p7) family.
DR PRIDE; Q96662; -.
DR EvolutionaryTrace; Q96662; -.
DR Proteomes; UP000007618; Genome.
DR Proteomes; UP000173611; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.30.140.40; -; 1.
DR Gene3D; 2.60.320.20; -; 1.
DR Gene3D; 2.60.40.3000; -; 1.
DR Gene3D; 2.60.40.4200; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.730.10; -; 1.
DR InterPro; IPR021824; Capsid-C_pestivirus.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR022120; NS2.
DR InterPro; IPR030399; NS2_C74.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008751; Peptidase_C53.
DR InterPro; IPR042542; Peptidase_C53_interaction.
DR InterPro; IPR032521; Pestivirus_E2.
DR InterPro; IPR042309; Pestivirus_E2_A.
DR InterPro; IPR042310; Pestivirus_E2_B.
DR InterPro; IPR042311; Pestivirus_E2_D.
DR InterPro; IPR000280; Pestivirus_NS3_S31.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002166; RNA_pol_HCV.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR033130; RNase_T2_His_AS_2.
DR Pfam; PF11889; DUF3409; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF05550; Peptidase_C53; 1.
DR Pfam; PF12387; Peptidase_C74; 1.
DR Pfam; PF05578; Peptidase_S31; 1.
DR Pfam; PF16329; Pestivirus_E2; 1.
DR Pfam; PF00998; RdRP_3; 1.
DR PRINTS; PR00729; CDVENDOPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
DR PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
DR PROSITE; PS51876; PV_NPRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Clathrin-mediated endocytosis of virus by host; Direct protein sequencing;
KW Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW Host cytoplasm; Host membrane; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW Ion channel; Ion transport; Membrane; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; RNA-directed RNA polymerase;
KW Serine protease; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Transport; Viral attachment to host cell;
KW Viral immunoevasion; Viral ion channel;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1..3907
FT /note="Genome polyprotein"
FT /id="PRO_0000450890"
FT CHAIN 1..168
FT /note="N-terminal protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038011"
FT CHAIN 169..270
FT /note="Capsid protein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038012"
FT CHAIN 271..497
FT /note="E(rns) glycoprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038013"
FT CHAIN 498..659
FT /note="Envelope glycoprotein E1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038014"
FT CHAIN 660..1066
FT /note="Envelope glycoprotein E2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038015"
FT CHAIN 1067..1136
FT /note="Viroporin p7"
FT /id="PRO_0000038016"
FT CHAIN 1137..2281
FT /note="Non-structural protein 2-3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038017"
FT CHAIN 1137..1598
FT /note="Cysteine protease NS2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT /id="PRO_0000038018"
FT CHAIN 1599..2281
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038019"
FT CHAIN 2282..2345
FT /note="Non-structural protein 4A"
FT /id="PRO_0000038020"
FT CHAIN 2346..2692
FT /note="Non-structural protein 4B"
FT /id="PRO_0000038021"
FT CHAIN 2693..3188
FT /note="Non-structural protein 5A"
FT /id="PRO_0000038022"
FT CHAIN 3189..3907
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000038023"
FT TRANSMEM 1144..1164
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1189..1209
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1217..1237
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1247..1267
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1281..1301
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1369..1389
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1577..1597
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT DOMAIN 1..168
FT /note="Peptidase C53"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT DOMAIN 1450..1598
FT /note="Peptidase C74"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT DOMAIN 1599..1772
FT /note="Peptidase S31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT DOMAIN 1811..1969
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1987..2152
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 3527..3650
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 45..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 49
FT /note="For N-terminal protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT ACT_SITE 69
FT /note="For N-terminal protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT ACT_SITE 1456
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029,
FT ECO:0000269|PubMed:15367643"
FT ACT_SITE 1470
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029,
FT ECO:0000269|PubMed:15367643"
FT ACT_SITE 1521
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029,
FT ECO:0000269|PubMed:15367643"
FT ACT_SITE 1667
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1704
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1761
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT SITE 168..169
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT SITE 270..271
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 497..498
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 659..660
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 1066..1067
FT /note="Cleavage; by host signal peptidase; partial"
FT SITE 1136..1137
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 1598..1599
FT /note="Cleavage; by NS2; in cytopathic strains"
FT /evidence="ECO:0000250"
FT SITE 2281..2282
FT /note="Cleavage; by serine protease NS3"
FT SITE 2345..2346
FT /note="Cleavage; by serine protease NS3"
FT SITE 2692..2693
FT /note="Cleavage; by serine protease NS3"
FT SITE 3188..3189
FT /note="Cleavage; by serine protease NS3"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 922
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 990
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1366
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1428
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1460
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1722
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2143
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2226
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2503
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2691
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2900
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3697
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3802
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT MUTAGEN 438
FT /note="E->A: Almost no effect on membrane association of
FT E(rns) glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 446
FT /note="Q->A: Almost no effect on membrane association of
FT E(rns) glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 455
FT /note="G->A: Almost no effect on membrane association of
FT E(rns) glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 460
FT /note="L->A: Reduced membrane association of E(rns)
FT glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 461
FT /note="E->A: Greatly reduced membrane association of E(rns)
FT glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 462
FT /note="S->A: Almost no effect on membrane association of
FT E(rns) glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 465
FT /note="Q->A: Almost no effect on membrane association of
FT E(rns) glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 469
FT /note="K->A: Almost no effect on membrane association of
FT E(rns) glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 471
FT /note="T->A: Almost no effect on membrane association of
FT E(rns) glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 473
FT /note="W->A: Reduced membrane association of E(rns)
FT glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 476
FT /note="R->A: Almost no effect on membrane association of
FT E(rns) glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 478
FT /note="L->A: Reduced membrane association of E(rns)
FT glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 481
FT /note="L->A: Reduced membrane association of E(rns)
FT glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 486
FT /note="E->A: Greatly reduced membrane association of E(rns)
FT glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 487
FT /note="N->A: Almost no effect on membrane association of
FT E(rns) glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 489
FT /note="S->A: Almost no effect on membrane association of
FT E(rns) glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT MUTAGEN 492
FT /note="W->A: Reduced membrane association of E(rns)
FT glycoprotein."
FT /evidence="ECO:0000269|PubMed:17848558"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:4DVK"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:4DVK"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:4DVK"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:4DVK"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:4DVK"
FT HELIX 340..349
FT /evidence="ECO:0007829|PDB:4DVK"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:4DVK"
FT HELIX 357..373
FT /evidence="ECO:0007829|PDB:4DVK"
FT STRAND 377..387
FT /evidence="ECO:0007829|PDB:4DVK"
FT TURN 388..391
FT /evidence="ECO:0007829|PDB:4DVK"
FT STRAND 392..401
FT /evidence="ECO:0007829|PDB:4DVK"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:4DVK"
FT STRAND 419..426
FT /evidence="ECO:0007829|PDB:4DVK"
FT HELIX 2697..2718
FT /evidence="ECO:0007829|PDB:2AJJ"
FT HELIX 3283..3291
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3301..3308
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3325..3334
FT /evidence="ECO:0007829|PDB:2CJQ"
FT TURN 3338..3340
FT /evidence="ECO:0007829|PDB:2CJQ"
FT TURN 3350..3352
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3353..3360
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3372..3380
FT /evidence="ECO:0007829|PDB:2CJQ"
FT TURN 3381..3383
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3386..3388
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3397..3401
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3418..3424
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3426..3438
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3446..3450
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3474..3478
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3480..3494
FT /evidence="ECO:0007829|PDB:2CJQ"
FT TURN 3510..3512
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3513..3521
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3524..3532
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3534..3536
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3537..3540
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3543..3556
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3559..3561
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3562..3572
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3574..3579
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3582..3589
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3598..3618
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3627..3634
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3637..3643
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3644..3661
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3669..3671
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3675..3678
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3679..3681
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3687..3694
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3699..3704
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3707..3715
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3727..3741
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3745..3754
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3765..3773
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3775..3783
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3787..3789
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3790..3793
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3795..3801
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3803..3807
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3815..3828
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3829..3831
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3834..3837
FT /evidence="ECO:0007829|PDB:2CJQ"
FT HELIX 3839..3845
FT /evidence="ECO:0007829|PDB:2CJQ"
FT STRAND 3854..3858
FT /evidence="ECO:0007829|PDB:2CJQ"
SQ SEQUENCE 3907 AA; 439104 MW; 9E4B019FF8042410 CRC64;
MELITNELLY KTYKQKPAGV EEPVYDQAGN PLFGERGVIH PQSTLKLPHK RGEREVPTNL
ASLPKRGDCR SGNSKGPVSG IYLKPGPLFY QDYKGPVYHR APLEFFEEAS MCETTKRIGR
VTGSDSRLYH IYVCIDGCII VKSATKDRQK VLKWVHNKLN CPLWVSSCSD TKDEGVVRKK
QQKPDRLEKG RMKITPKESE KDSKTKPPDA TIVVDGVKYQ VKKKGKVKSK NTQDGLYHNK
NKPQESRKKL EKALLAWAII ALVFFQVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH
GIWPEKICTG VPSHLATDTE LKAIHGMMDA SEKTNYTCCR LQRHEWNKHG WCNWYNIEPW
ILLMNKTQAN LTEGQPLREC AVTCRYDRDS DLNVVTQARD SPTPLTGCKK GKNFSFAGIL
VQGPCNFEIA VSDVLFKEHD CTSVIQDTAH YLVDGMTNSL ESARQGTAKL TTWLGRQLGI
LGKKLENKSK TWFGAYAASP YCEVERKLGY IWYTKNCTPA CLPRNTKIIG PGRFDTNAED
GKILHEMGGH LSEVLLLSVV VLSDFAPETA SVIYLILHFS IPQGHTDIQD CDKNQLNLTV
ELTTAEVIPG SVWNLGKYVC VRPDWWPYET ATVLVIEEVG QVIKVVLRAL KDLTRIWTAA
TTTAFLVCLV KVVRGQVLQG ILWLMLITGA QGYPDCKPGF SYAIAKNDEI GPLGATGLTT
QWYEYSDGMR LQDSVVEVWC KNGEIKYLIR CGREARYLAV LHTRALPTSV VFEKIFDGKE
QEDIVEMDDN FEFGLCPCDA RPLIRGKFNT TLLNGPAFQM VCPIGWTGTV SCTLANKDTL
ATIVVRTYKR VRPFPYRQDC VTQKTIGEDL YDCALGGNWT CVPGDALRYV AGPVESCEWC
GYKFLKSEGL PHFPIGKCRL KNESGYRQVD ETSCNRNGVA IVPSGTVKCK IGDTVVQVIA
MDDKLGPMPC KPHEIISSEG PVEKTACTFN YTRTLKNKYF EPRDNYFQQY MLKGEYQYWF
DLEITDHHRD YFAESLLVIV VALLGGRYVL WLLVTYMILS EQMASGVQYG AGEIVMMGNL
LTHDSVEVVT YFLLLYLLLR EENTKKWVIL IYHIIVMHPL KSVTVILLMV GGMAKAEPGA
QGYLEQVDLS FTMITIIVIG LVIARRDPTV VPLVTIVAAL KITGLGFGPG VDAAMAVLTL
TLLMTSYVTD YFRYKRWIQC ILSLVAGVFL IRTLKHLGEL KTPELTIPNW RPLTFILLYL
TSATVVTRWK IDIAGIFLQG APILLMIATL WADFLTLVLI LPTYELAKLY YLKNVKTDVE
KSWGVPYPDP QTLGGLDYRT IDSVYDVDES GEGVYLFPSR QKKNKNISIL LPLIRATLIS
CISSKWQMVY MAYLTLDFMY YMHRKVIEEI SGSTNVMSRV IAALIELNWS MEEEESKGLK
KFFILSGRLR NLIIKHKVRN QTVASWYGEE EVYGMPKVVT IIRACTLNKN KHCIICTVCE
ARKWKGGNCP KCGRHGKPII CGMTLADFEE RHYKRIFIRE GNFEGPFRQE YNGFVQYTAR
GQLFLRNLPI LATKVKMIMV GNLGEEIGDL EHLGWILRGP AVCKKITEHE KCHVNILDKL
TAFFGVMPRG TTPRAPVRFP TALLKVRRGL ETGWAYTHQG GISSVDHVTA GKDLLVCDSM
GRTRVVCQSN NKLTDETEYG VKTDSGCPDG ARCYVLNPEA VNISGSKGAV VHLQKTGGEF
TCVTASGTPA FFDLKNLKGW SGLPIFEASS GRVVGRVKVG KNEESKPTKL MSGIQTVSKN
TADLTEMVKK ITSMNRGDFR QITLATGAGK TTELPKAVIE EIGRHKRVLV LIPLRAAAES
VYQYMRLKHP SISFNLRIGD MKEGDMATGI TYASYGYFCQ MPQPKLRAAM IEYSYIFLDE
YHCATPEQLA VIGKIHRFSE SIRVVAMTAT PAGSVTTTGQ KHPIEEFIAP EVMKGEDLGS
QFLDIAGLKI PVEEMKGNML VFVPTRNMAV EVAKKLKAKG YNSGYYYSGE DPANLRVVTS
QSPYVVVATN AIESGVTLPD LDTVVDTGLK CEKRVRVSSK IPFIVTGLKR MAVTVGEQAQ
RRGRVGRVKP GRYYRSQETA TGSKDYHYDL LQAQRYGIED GINVTKSFRE MNYDWSLYEE
DSLLITQLEI LNNLLISEDL PAAVKNIMAR TDHPEPIQLA YNSYEVQVPV LFPKIRNGEV
TDTYENYSFL NARKLGEDVP VYVYATEDED LAVDLLGLDW PDPGNQQVVE TGKALKQVVG
LSSAENALLI ALFGYVGYQA LSKRHVPMIT DIYTIEDQRL EDTTHLQYAP NAIRTEGKET
ELKELAVGDL DKIMGSISDY ASEGLNFVRS QAEKMRSAPA FKENVEAAKG YVQKFIDSLI
ENKETIIRYG LWGTHTALYK SIAARLGHET AFATLVIKWL AFGGESVSDH MRQAAVDLVV
YYVINKPSFP GDSETQQEGR RFVASLFISA LATYTYKTWN YNNLSKVVEP ALAYLPYATN
ALKMFTPTRL ESVVILSTTI YKTYLSIRKG KSDGLLGTGI SAAMEILSQN PVSVGISVML
GVGAIAAHNA IESSEQKRTL LMKVFVKNFL DQAATDELVK ENPEKIIMAL FEAVQTIGNP
LRLIYHLYGV YYKGWEAKEL SERTAGRNLF TLIMFEAFEL LGMDSEGKIR NLSGNYVLDL
IYSLHKQINR GLKKIVLGWA PAPFSCDWTP SDERIRLPTN NYLRVETKCP CGYEMKALRN
VGGSLTKVEE KGPFLCRNRL GRGPVNYRVT KYYDDNLKEI KPVAKLEGFV DHYYKGVTAR
IDYGRGKMLL ATDKWEVEHG VVTRLAKRYT GVGFKGAYLG DEPNHRDLVE RDCATITKNT
VQFLKMKKGC AFTYDLTLSN LTRLIELVHK NNLEEKDIPA ATVTTWLAYT FVNEDIGTIK
PVLGERVVTD PVVDVNLQPE VQVDTSEVGI TLVGRAALMT TGTTPVVEKT EPNADGGPSS
IKIGLDEGRY PGPGLQDRTL TDEIHSRDER PFVLVLGSKN SMSNRAKTAR NINLYKGNNP
REIRDLMAQG RMLVVALKDF NPELSELVDF KGTFLDREAL EALSLGRPKS KQVTTATVRE
LLEQEVQVEI PSWFGAGDPV FLEVTLKGDR YHLVGDVDRV KDQAKELGAT DQTRIVKEVG
ARTYTMKLSS WFLQATNKQM SLTPLFEELL LRCPPKIKSN KGHMASAYQL AQGNWEPLDC
GVHLGTIPAR RVKIHPYEAY LKLKDLLEEE EKKPKCRDTV IREHNKWILK KVRHQGNLNT
KKILNPGKLS EQLDREGHKR NIYNNQIGTI MTEAGSRLEK LPVVRAQTDT KSFHEAIRDK
IDKNENQQSP GLHDKLLEIF HTIAQPSLRH TYSDVTWEQL EAGVNRKGAA GFLEKKNVGE
VLDSEKHLVE QLIRDLKTGR KIRYYETAIP KNEKRDVSDD WQSGDLVDEK KPRVIQYPEA
KTRLAITKVM YNWVKQQPVV IPGYEGKTPL FNIFNKVRKE WDLFNEPVAV SFDTKAWDTQ
VTSRDLRLIG EIQKYYYRKE WHKFIDTITD HMVEVPVITA DGEVYIRNGQ RGSGQPDTSA
GNSMLNVLTM MYAFCESTGV PYKSFNRVAR IHVCGDDGFL ITEKGLGLKF ANNGMQILHE
AGKPQKITEG ERMKVAYRFE DIEFCSHTPV PVRWSDNTSS YMAGRDTAVI LSKMATRLDS
SGERGTIAYE KAVAFSFLLM YSWNPLVRRI CLLVLSQQPE TTPSTQTTYY YKGDPIGAYK
DVIGKNLCEL KRTGFEKLAN LNLSLSTLGI WSKHTSKRII QDCVTIGKEE GNWLVNADRL
ISSKTGHLYI PDKGYTLQGK HYEQLQLQAR TSPVTGVGTE RYKLGPIVNL LLRRLRVLLM
AAVGASS
