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Database: UniProt
Entry: POLS_IPNVS
LinkDB: POLS_IPNVS
Original site: POLS_IPNVS 
ID   POLS_IPNVS              Reviewed;         972 AA.
AC   Q703G9; P90205; Q4KTX8; Q69CH7; Q69CI0; Q69CI3; Q6U2N3; Q6U2N5; Q6U2N8;
AC   Q6U2P1; Q6U2P5; Q6U2P7; Q6UAY7; Q82733; Q990Q0; Q9YJV0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   07-OCT-2020, entry version 74.
DE   RecName: Full=Structural polyprotein;
DE            Short=PP;
DE   Contains:
DE     RecName: Full=Precursor of VP2;
DE              Short=Pre-VP2;
DE   Contains:
DE     RecName: Full=Capsid protein VP2;
DE   Contains:
DE     RecName: Full=Structural peptide 1;
DE              Short=p1;
DE   Contains:
DE     RecName: Full=Structural peptide 2;
DE              Short=p2;
DE   Contains:
DE     RecName: Full=Structural peptide 3;
DE              Short=p3;
DE   Contains:
DE     RecName: Full=Protease VP4;
DE              EC=3.4.21.-;
DE     AltName: Full=Non-structural protein VP4;
DE              Short=NS;
DE   Contains:
DE     RecName: Full=Capsid protein VP3;
OS   Infectious pancreatic necrosis virus (strain Sp) (IPNV).
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Aquabirnavirus.
OX   NCBI_TaxID=11005;
OH   NCBI_TaxID=8022; Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OH   NCBI_TaxID=8028; Salmo.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 443-457; 487-495 AND
RP   496-508, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RC   STRAIN=31-75;
RX   PubMed=15269363; DOI=10.1099/vir.0.80012-0;
RA   Galloux M., Chevalier C., Henry C., Huet J.-C., Da Costa B., Delmas B.;
RT   "Peptides resulting from the pVP2 C-terminal processing are present in
RT   infectious pancreatic necrosis virus particles.";
RL   J. Gen. Virol. 85:2231-2236(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Mason;
RA   Mason C.L., Leong J.C.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Tseng;
RA   Tseng C.-C., Lo C.-F., Kou G.-H.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate NVI-001, Isolate NVI-010, Isolate NVI-011, Isolate NVI-013,
RC   Isolate NVI-015, Isolate NVI-016, Isolate NVI-020, and Isolate NVI-023;
RX   PubMed=15063114; DOI=10.1016/j.virol.2003.12.016;
RA   Santi N., Vakharia V.N., Evensen O.;
RT   "Identification of putative motifs involved in the virulence of infectious
RT   pancreatic necrosis virus.";
RL   Virology 322:31-40(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Sp103, Isolate Sp116, and Isolate Sp122;
RX   PubMed=15584407; DOI=10.3354/dao061023;
RA   Shivappa R.B., Song H., Yao K., Aas-Eng A., Evensen O., Vakharia V.N.;
RT   "Molecular characterization of Sp serotype strains of infectious pancreatic
RT   necrosis virus exhibiting differences in virulence.";
RL   Dis. Aquat. Organ. 61:23-32(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Sp103;
RX   PubMed=15994815; DOI=10.1128/jvi.79.14.9206-9216.2005;
RA   Santi N., Song H., Vakharia V.N., Evensen O.;
RT   "Infectious pancreatic necrosis virus VP5 is dispensable for virulence and
RT   persistence.";
RL   J. Virol. 79:9206-9216(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-968.
RC   STRAIN=Isolate Blake;
RX   PubMed=11463106; DOI=10.3354/dao045089;
RA   Blake S., Ma J.Y., Caporale D.A., Jairath S., Nicholson B.L.;
RT   "Phylogenetic relationships of aquatic birnaviruses based on deduced amino
RT   acid sequences of genome segment A cDNA.";
RL   Dis. Aquat. Organ. 45:89-102(2001).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 437-539.
RC   STRAIN=Isolate Heppell;
RX   PubMed=8337850; DOI=10.1006/viro.1993.1441;
RA   Heppell J., Berthiaume L., Corbin F., Tarrab E., Lecomte J., Arella M.;
RT   "Comparison of amino acid sequences deduced from a cDNA fragment obtained
RT   from infectious pancreatic necrosis virus (IPNV) strains of different
RT   serotypes.";
RL   Virology 195:840-844(1993).
RN   [9]
RP   PROTEIN SEQUENCE OF 509-515; 716-723 AND 735-740, ACTIVE SITES OF PROTEASE
RP   VP4, PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF
RP   486-ALA-ALA-487; 495-ALA-ALA-496; 508-ALA-SER-509; HIS-547; ASP-573;
RP   ASP-585; ASP-595; ASP-601; SER-633; ASP-644; 660-ASP-ASP-661; ASP-672;
RP   LYS-674; ALA-675; ILE-676; ALA-677; ALA-678; HIS-679; GLU-680; GLY-682;
RP   LEU-683; PRO-684; LEU-685; ILE-686; GLY-687; GLN-689; ASP-693; HIS-704 AND
RP   734-ALA-SER-735.
RC   STRAIN=31-75;
RX   PubMed=10666235; DOI=10.1128/jvi.74.5.2057-2066.2000;
RA   Petit S., Lejal N., Huet J.-C., Delmas B.;
RT   "Active residues and viral substrate cleavage sites of the protease of the
RT   birnavirus infectious pancreatic necrosis virus.";
RL   J. Virol. 74:2057-2066(2000).
RN   [10]
RP   3D-STRUCTURE MODELING, AND STRUCTURE BY ELECTRON MICROSCOPY (15 ANGSTROMS)
RP   OF VIRAL PARTICLES.
RC   STRAIN=31-75;
RX   PubMed=16033982; DOI=10.1099/vir.0.80942-0;
RA   Pous J., Chevalier C., Ouldali M., Navaza J., Delmas B., Lepault J.;
RT   "Structure of birnavirus-like particles determined by combined electron
RT   cryomicroscopy and X-ray crystallography.";
RL   J. Gen. Virol. 86:2339-2346(2005).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 514-716.
RX   PubMed=17553791; DOI=10.1074/jbc.m701551200;
RA   Lee J., Feldman A.R., Delmas B., Paetzel M.;
RT   "Crystal structure of the VP4 protease from infectious pancreatic necrosis
RT   virus reveals the acyl-enzyme complex for an intermolecular self-cleavage
RT   reaction.";
RL   J. Biol. Chem. 282:24928-24937(2007).
CC   -!- FUNCTION: Capsid protein VP2 self assembles to form an icosahedral
CC       capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of
CC       260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also
CC       involved in attachment and entry into the host cell (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: The precursor of VP2 plays an important role in capsid
CC       assembly. First, pre-VP2 and VP2 oligomers assemble to form a
CC       procapsid. Then, the pre-VP2 intermediates may be processed into VP2
CC       proteins by proteolytic cleavage mediated by VP4 to obtain the mature
CC       virion. The final capsid is composed of pentamers and hexamers but VP2
CC       has a natural tendency to assemble into all-pentameric structures.
CC       Therefore pre-VP2 may be required to allow formation of the hexameric
CC       structures (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Protease VP4 is a serine protease that cleaves the
CC       polyprotein into its final products. Pre-VP2 is first partially
CC       cleaved, and may be completely processed by VP4 upon capsid maturation.
CC       {ECO:0000255|PROSITE-ProRule:PRU00881}.
CC   -!- FUNCTION: Capsid protein VP3 plays a key role in virion assembly by
CC       providing a scaffold for the capsid made of VP2. May self-assemble to
CC       form a T=4-like icosahedral inner-capsid composed of at least 180
CC       trimers. Plays a role in genomic RNA packaging by recruiting VP1 into
CC       the capsid and interacting with the dsRNA genome segments to form a
CC       ribonucleoprotein complex. Additionally, the interaction of the VP3 C-
CC       terminal tail with VP1 removes the inherent structural blockade of the
CC       polymerase active site. Thus, VP3 can also function as a
CC       transcriptional activator (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Structural peptide 1 is a small peptide derived from pre-VP2
CC       C-terminus. It destabilizes and perforates cell membranes, suggesting a
CC       role during entry (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Structural peptide 2 is a small peptide derived from pVP2 C-
CC       terminus. It is not essential for the virus viability, but viral growth
CC       is affected when missing (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Structural peptide 3 is a small peptide derived from pVP2 C-
CC       terminus. It is not essential for the virus viability, but viral growth
CC       is affected when missing (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Capsid protein VP2 is a homotrimer. A central divalent metal
CC       stabilizes the VP2 trimer, possibly cobalt (By similarity). Capsid
CC       protein VP3 is a homodimer. Capsid protein VP3 interacts (via C-
CC       terminus) with VP1 in the cytoplasm Capsid VP3 interacts with VP2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000305}. Host
CC       cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000305}. Host
CC       cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Structural peptide 1]: Virion {ECO:0000305}.
CC       Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Structural peptide 2]: Virion {ECO:0000305}.
CC       Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Structural peptide 3]: Virion {ECO:0000305}.
CC       Host cytoplasm {ECO:0000305}.
CC   -!- PTM: Specific enzymatic cleavages yield mature proteins. The capsid
CC       assembly seems to be regulated by polyprotein processing. The protease
CC       VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3
CC       within the infected cell. During capsid assembly, the C-terminus of
CC       pre-VP2 is further processed by VP4, giving rise to VP2, the external
CC       capsid protein and three small peptides that all stay closely
CC       associated with the capsid (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: The sequence shown is that of strain 31-75. Isolate
CC       Sp103 is VP5-deficient.
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DR   EMBL; AJ622822; CAF22217.1; -; Genomic_RNA.
DR   EMBL; U48225; AAD11535.1; -; Genomic_RNA.
DR   EMBL; U56907; AAB39512.1; -; Genomic_RNA.
DR   EMBL; AY374435; AAQ75364.1; -; Genomic_RNA.
DR   EMBL; AY379735; AAQ75348.1; -; Genomic_RNA.
DR   EMBL; AY379736; AAQ75350.1; -; Genomic_RNA.
DR   EMBL; AY379737; AAQ75352.1; -; Genomic_RNA.
DR   EMBL; AY379738; AAQ75354.1; -; Genomic_RNA.
DR   EMBL; AY379740; AAQ75357.1; -; Genomic_RNA.
DR   EMBL; AY379742; AAQ75360.1; -; Genomic_RNA.
DR   EMBL; AY379744; AAQ75363.1; -; Genomic_RNA.
DR   EMBL; AY354519; AAR10446.1; -; Genomic_RNA.
DR   EMBL; AY354520; AAR10449.1; -; Genomic_RNA.
DR   EMBL; AY354521; AAR10452.1; -; Genomic_RNA.
DR   EMBL; AY823632; AAX24140.1; -; Genomic_RNA.
DR   EMBL; AF342728; AAK32154.1; -; mRNA.
DR   EMBL; L13988; AAB00986.1; -; Genomic_RNA.
DR   PDB; 2PNL; X-ray; 2.21 A; A/B/C/D/E/F/G/H/I/J=514-716.
DR   PDB; 2PNM; X-ray; 2.30 A; A=524-716.
DR   PDB; 3IDE; X-ray; 3.35 A; A/B/C/D/E=1-442.
DR   PDBsum; 2PNL; -.
DR   PDBsum; 2PNM; -.
DR   PDBsum; 3IDE; -.
DR   SMR; Q703G9; -.
DR   MEROPS; S50.001; -.
DR   PRIDE; Q703G9; -.
DR   BRENDA; 3.4.21.115; 6986.
DR   EvolutionaryTrace; Q703G9; -.
DR   Proteomes; UP000007213; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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   Gene3D; 1.10.150.620; -; 1.
DR   Gene3D; 1.10.8.880; -; 1.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR002662; Birna_VP2.
DR   InterPro; IPR002663; Birna_VP3.
DR   InterPro; IPR043048; Birna_VP3_dom1.
DR   InterPro; IPR043049; Birna_VP3_dom2.
DR   InterPro; IPR025775; Birna_VP4_Prtase_dom.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF01766; Birna_VP2; 1.
DR   Pfam; PF01767; Birna_VP3; 1.
DR   Pfam; PF01768; Birna_VP4; 1.
DR   PROSITE; PS51548; BIRNAVIRUS_VP4_PRO; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Direct protein sequencing; Host cytoplasm;
KW   Hydrolase; Metal-binding; Protease; Reference proteome; Serine protease;
KW   Virion.
FT   CHAIN           1..508
FT                   /note="Precursor of VP2"
FT                   /id="PRO_0000392599"
FT   CHAIN           1..442
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000227873"
FT   PEPTIDE         443..486
FT                   /note="Structural peptide 1"
FT                   /evidence="ECO:0000269|PubMed:15269363"
FT                   /id="PRO_0000227874"
FT   PEPTIDE         487..495
FT                   /note="Structural peptide 2"
FT                   /evidence="ECO:0000269|PubMed:15269363"
FT                   /id="PRO_0000227875"
FT   PEPTIDE         496..508
FT                   /note="Structural peptide 3"
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT                   /id="PRO_0000227876"
FT   CHAIN           509..734
FT                   /note="Protease VP4"
FT                   /id="PRO_0000227877"
FT   CHAIN           735..972
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000227878"
FT   DOMAIN          509..734
FT                   /note="Peptidase S50"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        633
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881,
FT                   ECO:0000269|PubMed:10666235"
FT   ACT_SITE        674
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881,
FT                   ECO:0000269|PubMed:10666235"
FT   METAL           26
FT                   /note="Divalent metal cation; shared with trimeric
FT                   partners"
FT                   /evidence="ECO:0000250"
FT   SITE            442..443
FT                   /note="Cleavage; by protease VP4"
FT   SITE            486..487
FT                   /note="Cleavage; by protease VP4"
FT   SITE            495..496
FT                   /note="Cleavage; by protease VP4"
FT   SITE            508..509
FT                   /note="Cleavage; by protease VP4"
FT   SITE            715..716
FT                   /note="Cleavage; by protease VP4; subsidiary"
FT   SITE            734..735
FT                   /note="Cleavage; by protease VP4"
FT   VARIANT         36
FT                   /note="Q -> P (in strain: Isolate Mason)"
FT   VARIANT         46
FT                   /note="S -> P (in strain: Isolate Mason)"
FT   VARIANT         52
FT                   /note="V -> I (in strain: Isolate Mason, Isolate Tseng,
FT                   Isolate Blake, Isolate Sp103, Isolate Sp116, Isolate Sp122,
FT                   Isolate NVI-001, Isolate NVI-011, Isolate NVI-013, Isolate
FT                   NVI-015, Isolate NVI-016, Isolate NVI-020 and NVI-023)"
FT   VARIANT         54
FT                   /note="V -> I (in strain: Isolate NVI-010)"
FT   VARIANT         82..85
FT                   /note="WLET -> CWRA (in strain: Isolate Mason)"
FT   VARIANT         152
FT                   /note="V -> A (in strain: Isolate Mason, Isolate Blake and
FT                   Isolate Tseng)"
FT   VARIANT         192
FT                   /note="K -> R (in strain: Isolate Mason, Isolate Blake and
FT                   Isolate Tseng)"
FT   VARIANT         199
FT                   /note="I -> T (in strain: Isolate Sp103 and Isolate Sp122)"
FT   VARIANT         212
FT                   /note="R -> S (in strain: Isolate Mason, Isolate Blake and
FT                   Isolate Tseng)"
FT   VARIANT         217
FT                   /note="P -> T (in strain: Isolate Sp122, Isolate NVI-001,
FT                   Isolate NVI-011, Isolate NVI-013, Isolate NVI-015, Isolate
FT                   NVI-020 and Isolate NVI-023)"
FT   VARIANT         219
FT                   /note="T -> I (in strain: Isolate NVI-010)"
FT   VARIANT         221
FT                   /note="T -> A (in strain: Isolate NVI-001, Isolate NVI-013,
FT                   Isolate NVI-015, Isolate Sp116 and Isolate NVI-023)"
FT   VARIANT         222
FT                   /note="L -> P (in strain: Isolate NVI-011)"
FT   VARIANT         234
FT                   /note="N -> S (in strain: Isolate Tseng)"
FT   VARIANT         247
FT                   /note="A -> T (in strain: Isolate Sp122, Isolate NVI-001,
FT                   Isolate NVI-013, Isolate NVI-015 and Isolate NVI-023)"
FT   VARIANT         249
FT                   /note="Q -> R (in strain: Isolate Tseng)"
FT   VARIANT         252
FT                   /note="D -> N (in strain: Isolate Mason, Isolate Tseng,
FT                   Isolate Blake, Isolate Sp103, Isolate NVI-010 and Isolate
FT                   NVI-016)"
FT   VARIANT         252
FT                   /note="D -> V (in strain: Isolate NVI-001, Isolate NVI-011,
FT                   Isolate NVI-013, Isolate NVI-015, Isolate NVI-020, Isolate
FT                   NVI-023, Isolate Sp116 and Isolate Sp122)"
FT   VARIANT         255
FT                   /note="K -> R (in strain: Isolate Mason, Isolate Blake and
FT                   Isolate Tseng)"
FT   VARIANT         262
FT                   /note="F -> L (in strain: Isolate Mason)"
FT   VARIANT         288
FT                   /note="V -> A (in strain: Isolate Sp116)"
FT   VARIANT         319
FT                   /note="A -> E (in strain: Isolate NVI-016)"
FT   VARIANT         323
FT                   /note="V -> A (in strain: Isolate NVI-020)"
FT   VARIANT         323
FT                   /note="V -> F (in strain: Isolate NVI-016)"
FT   VARIANT         432..434
FT                   /note="DFS -> EKT (in strain: Isolate Mason)"
FT   VARIANT         455
FT                   /note="V -> I (in strain: Isolate Mason)"
FT   VARIANT         473
FT                   /note="M -> T (in strain: Isolate Mason, Isolate Heppel and
FT                   Isolate Blake)"
FT   VARIANT         500
FT                   /note="Y -> H (in strain: Isolate Heppel, Isolate NVI-010,
FT                   Isolate NVI-011, Isolate NVI-020, Isolate Sp103 and Isolate
FT                   Sp116)"
FT   VARIANT         565
FT                   /note="P -> R (in strain: Isolate Mason)"
FT   VARIANT         570..571
FT                   /note="EL -> SF (in strain: Isolate Mason)"
FT   VARIANT         672
FT                   /note="D -> A (in strain: Isolate NVI-016)"
FT   VARIANT         717
FT                   /note="K -> Q (in strain: Isolate NVI-016)"
FT   VARIANT         788
FT                   /note="D -> G (in strain: Isolate NVI-011)"
FT   VARIANT         788
FT                   /note="D -> Y (in strain: Isolate NVI-001)"
FT   VARIANT         802
FT                   /note="H -> R (in strain: Isolate NVI-015 and Isolate NVI-
FT                   016)"
FT   VARIANT         841
FT                   /note="L -> M (in strain: Isolate NVI-016)"
FT   VARIANT         867
FT                   /note="E -> Q (in strain: Isolate Mason and Isolate Blake)"
FT   VARIANT         875
FT                   /note="P -> S (in strain: Isolate NVI-016)"
FT   VARIANT         882
FT                   /note="M -> T (in strain: Isolate Tseng)"
FT   VARIANT         953..954
FT                   /note="AE -> GK (in strain: Isolate Mason)"
FT   VARIANT         959..960
FT                   /note="GR -> DV (in strain: Isolate Mason)"
FT   VARIANT         968
FT                   /note="D -> N (in strain: Isolate Sp116)"
FT   MUTAGEN         508..509
FT                   /note="AS->QL: Complete loss of pVP2-VP4 cleavage."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         547
FT                   /note="H->S: Strongly reduced VP4-VP3 cleavage. No effect
FT                   on pVP2-VP4 cleavage."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         573
FT                   /note="D->Q: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         585
FT                   /note="D->I: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         595
FT                   /note="D->L: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         601
FT                   /note="D->S: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         633
FT                   /note="S->A,Q,T: Complete loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         633
FT                   /note="S->C: Partial loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         644
FT                   /note="D->I: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         660..661
FT                   /note="DD->GS: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         672
FT                   /note="D->N: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         674
FT                   /note="K->A,D,H,Q,R: Complete loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         675
FT                   /note="A->D: 60% loss of pVP2-VP4 and VP4-VP3 cleavages."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         676
FT                   /note="I->A: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         677
FT                   /note="A->D: 60% loss of pVP2-VP4. Complete loss of VP4-VP3
FT                   cleavage."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         678
FT                   /note="A->S: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         679
FT                   /note="H->L: Strongly reduced VP4-VP3 cleavage. No effect
FT                   on pVP2-VP4 cleavage."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         680
FT                   /note="E->M: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         682
FT                   /note="G->L: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         683
FT                   /note="L->A: 60% loss of pVP2-VP4 and VP4-VP3 cleavages."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         684
FT                   /note="P->Q: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         685
FT                   /note="L->A: 60% loss of pVP2-VP4 and VP4-VP3 cleavages."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         686
FT                   /note="I->A: 20% loss of pVP2-VP4 and VP4-VP3 cleavages."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         687
FT                   /note="G->A: 20% loss of pVP2-VP4 and VP4-VP3 cleavages."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         689
FT                   /note="Q->I: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         693
FT                   /note="D->L: Strongly reduced VP4-VP3 cleavage. No effect
FT                   on pVP2-VP4 cleavage."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         704
FT                   /note="H->S: No effect on polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   MUTAGEN         734..735
FT                   /note="AS->LE: Complete loss of VP4-VP3 cleavage."
FT                   /evidence="ECO:0000269|PubMed:10666235"
FT   CONFLICT        883
FT                   /note="N -> Y (in Ref. 5; AAR10446)"
FT                   /evidence="ECO:0000305"
FT   HELIX           9..15
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           17..19
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          32..44
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          51..55
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          60..70
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          74..84
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           89..91
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          93..107
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          120..128
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           130..132
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           140..143
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           148..150
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          151..156
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   TURN            157..159
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          161..164
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          202..208
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          210..212
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          223..232
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          236..248
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          254..263
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          271..280
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   TURN            282..286
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          287..292
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           298..300
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          305..313
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           317..319
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          324..326
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           327..329
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          332..338
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   TURN            339..342
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   TURN            344..346
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          350..357
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          363..376
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           378..381
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           395..404
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   TURN            405..410
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   STRAND          413..416
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           417..422
FT                   /evidence="ECO:0000244|PDB:3IDE"
FT   HELIX           425..427
FT                   /evidence="ECO:0000244|PDB:3IDE"
SQ   SEQUENCE   972 AA;  106646 MW;  7B1448E99800E3C9 CRC64;
     MNTNKATATY LKSIMLPETG PASIPDDITE RHILKQETSS YNLEVSESGS GVLVCFPGAP
     GSRIGAHYRW NANQTGLEFD QWLETSQDLK KAFNYGRLIS RKYDIQSSTL PAGLYALNGT
     LNAATFEGSL SEVESLTYNS LMSLTTNPQD KVNNQLVTKG VTVLNLPTGF DKPYVRLEDE
     TPQGLQSMNG AKMRCTAAIA PRRYEIDLPS QRLPPVPATG TLTTLYEGNA DIVNSTTVTG
     DINFSLAEQP ADETKFDFQL DFMGLDNDVP VVTVVSSVLA TNDNYRGVSA KMTQSIPTEN
     ITKPITRVKL SYKINQQTAI GNVATLGTMG PASVSFSSGN GNVPGVLRPI TLVAYEKMTP
     LSILTVAGVS NYELIPNPEL LKNMVTRYGK YDPEGLNYAK MILSHREELD IRTVWRTEEY
     KERTRVFNEI TDFSSDLPTS KAWGWRDIVR GIRKVAAPVL STLFPMAAPL IGMADQFIGD
     LTKTNAAGGR YHSMAAGGRY KDVLESWASG GPDGKFSRAL KNRLESANYE EVELPPPSKG
     VIVPVVHTVK SAPGEAFGSL AIIIPGEYPE LLDANQQVLS HFANDTGSVW GIGEDIPFEG
     DNMCYTALPL KEIKRNGNIV VEKIFAGPIM GPSAQLGLSL LVNDIEDGVP RMVFTGEIAD
     DEETIIPICG VDIKAIAAHE QGLPLIGNQP GVDEEVRNTS LAAHLIQTGT LPVQRAKGSN
     KRIKYLGELM ASNASGMDEE LQRLLNATMA RAKEVQDAEI YKLLKLMAWT RKNDLTDHMY
     EWSKEDPDAL KFGKLISTPP KHPEKPKGPD QHHAQEARAT RISLDAVRAG ADFATPEWVA
     LNNYRGPSPG QFKYYLITGR EPEPGDEYED YIKQPIVKPT DMNKIRRLAN SVYGLPHQEP
     APEEFYDAVA AVFAQNGGRG PDQDQMQDLR ELARQMKRRP RNADAPRRTR APAEPAPPGR
     SRFTPSGDNA EV
//
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