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 03-AUG-2022, entry version 77.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 REGION 794..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 BINDING 26
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between trimeric 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:0007829|PDB:3IDE"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 32..44
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 93..107
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3IDE"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 236..248
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 254..263
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 271..280
FT /evidence="ECO:0007829|PDB:3IDE"
FT TURN 282..286
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:3IDE"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:3IDE"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 363..376
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 395..404
FT /evidence="ECO:0007829|PDB:3IDE"
FT TURN 405..410
FT /evidence="ECO:0007829|PDB:3IDE"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:3IDE"
FT HELIX 425..427
FT /evidence="ECO:0007829|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
