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 27-MAR-2024, entry version 83. 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; OC Aquabirnavirus salmonidae. 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 RC NVI-013, Isolate NVI-015, Isolate NVI-016, Isolate NVI-020, and RC 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]: Homotrimer. A central divalent metal CC (possibly cobalt) stabilizes the VP2 trimer. {ECO:0000305}. CC -!- SUBUNIT: [Capsid protein VP3]: Homodimer. interacts (via C-terminus) CC with VP1 in the cytoplasm. Interacts with VP2 (By similarity). CC {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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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; 2.60.120.20; -; 1. DR Gene3D; 3.30.230.110; -; 1. DR Gene3D; 6.10.250.1030; -; 1. DR Gene3D; 1.10.8.880; Birnavirus VP3 protein, domain 2; 1. DR Gene3D; 1.10.150.620; Capsid protein VP3, domain 1; 1. DR Gene3D; 2.60.120.660; icosahedral virus; 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 SUPFAM; SSF88633; Positive stranded ssRNA viruses; 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; Serine protease; 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 FT NVI-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 //