Q703G9P90205Q4KTX8Q69CH7Q69CI0Q69CI3Q6U2N3Q6U2N5Q6U2N8Q6U2P1Q6U2P5Q6U2P7Q6UAY7Q82733Q990Q0Q9YJV0POLS_IPNVSStructural polyproteinPPPrecursor of VP2Pre-VP2Capsid protein VP2Structural peptide 1p1Structural peptide 2p2Structural peptide 3p3Protease VP43.4.21.-Non-structural protein VP4NSCapsid protein VP3Infectious pancreatic necrosis virus (strain Sp)IPNVVirusesRiboviriaOrthornaviraeBirnaviridaeAquabirnavirusAquabirnavirus salmonidaeOncorhynchus mykissRainbow troutSalmo gairdneriSalmoPeptides resulting from the pVP2 C-terminal processing are present in infectious pancreatic necrosis virus particles.NUCLEOTIDE SEQUENCE [GENOMIC RNA]PROTEIN SEQUENCE OF 443-457; 487-495 AND 496-508PROTEOLYTIC PROCESSING OF POLYPROTEINNUCLEOTIDE SEQUENCE [GENOMIC RNA]NUCLEOTIDE SEQUENCE [GENOMIC RNA]Identification of putative motifs involved in the virulence of infectious pancreatic necrosis virus.NUCLEOTIDE SEQUENCE [GENOMIC RNA]Molecular characterization of Sp serotype strains of infectious pancreatic necrosis virus exhibiting differences in virulence.NUCLEOTIDE SEQUENCE [GENOMIC RNA]Infectious pancreatic necrosis virus VP5 is dispensable for virulence and persistence.NUCLEOTIDE SEQUENCE [GENOMIC RNA]Phylogenetic relationships of aquatic birnaviruses based on deduced amino acid sequences of genome segment A cDNA.NUCLEOTIDE SEQUENCE [MRNA] OF 1-968Comparison of amino acid sequences deduced from a cDNA fragment obtained from infectious pancreatic necrosis virus (IPNV) strains of different serotypes.NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 437-539Active residues and viral substrate cleavage sites of the protease of the birnavirus infectious pancreatic necrosis virus.PROTEIN SEQUENCE OF 509-515; 716-723 AND 735-740ACTIVE SITES OF PROTEASE VP4PROTEOLYTIC PROCESSING OF POLYPROTEINMUTAGENESIS OF 486-ALA-ALA-487; 495-ALA-ALA-496; 508-ALA-SER-509; HIS-547; ASP-573; ASP-585; ASP-595; ASP-601; SER-633; ASP-644; 660-ASP-ASP-661; ASP-672; LYS-674; ALA-675; ILE-676; ALA-677; ALA-678; HIS-679; GLU-680; GLY-682; LEU-683; PRO-684; LEU-685; ILE-686; GLY-687; GLN-689; ASP-693; HIS-704 AND 734-ALA-SER-735Structure of birnavirus-like particles determined by combined electron cryomicroscopy and X-ray crystallography.3D-STRUCTURE MODELINGSTRUCTURE BY ELECTRON MICROSCOPY (15 ANGSTROMS) OF VIRAL PARTICLESCrystal structure of the VP4 protease from infectious pancreatic necrosis virus reveals the acyl-enzyme complex for an intermolecular self-cleavage reaction.X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 514-716Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell (By similarity).The precursor of VP2 plays an important role in capsid assembly. First, pre-VP2 and VP2 oligomers assemble to form a procapsid. Then, the pre-VP2 intermediates may be processed into VP2 proteins by proteolytic cleavage mediated by VP4 to obtain the mature virion. The final capsid is composed of pentamers and hexamers but VP2 has a natural tendency to assemble into all-pentameric structures. Therefore pre-VP2 may be required to allow formation of the hexameric structures (By similarity).Protease VP4 is a serine protease that cleaves the polyprotein into its final products. Pre-VP2 is first partially cleaved, and may be completely processed by VP4 upon capsid maturation.Capsid protein VP3 plays a key role in virion assembly by providing a scaffold for the capsid made of VP2. May self-assemble to form a T=4-like icosahedral inner-capsid composed of at least 180 trimers. Plays a role in genomic RNA packaging by recruiting VP1 into the capsid and interacting with the dsRNA genome segments to form a ribonucleoprotein complex. Additionally, the interaction of the VP3 C-terminal tail with VP1 removes the inherent structural blockade of the polymerase active site. Thus, VP3 can also function as a transcriptional activator (By similarity).Structural peptide 1 is a small peptide derived from pre-VP2 C-terminus. It destabilizes and perforates cell membranes, suggesting a role during entry (By similarity).Structural peptide 2 is a small peptide derived from pVP2 C-terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity).Structural peptide 3 is a small peptide derived from pVP2 C-terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity).Capsid protein VP2Homotrimer. A central divalent metal (possibly cobalt) stabilizes the VP2 trimer.Capsid protein VP3Homodimer. interacts (via C-terminus) with VP1 in the cytoplasm. Interacts with VP2 (By similarity).Capsid protein VP2VirionHost cytoplasmCapsid protein VP3VirionHost cytoplasmStructural peptide 1VirionHost cytoplasmStructural peptide 2VirionHost cytoplasmStructural peptide 3VirionHost cytoplasmSpecific enzymatic cleavages yield mature proteins. The capsid assembly seems to be regulated by polyprotein processing. The protease VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3 within the infected cell. During capsid assembly, the C-terminus of pre-VP2 is further processed by VP4, giving rise to VP2, the external capsid protein and three small peptides that all stay closely associated with the capsid (By similarity).The sequence shown is that of strain 31-75. Isolate Sp103 is VP5-deficient.3D-structureCapsid proteinDirect protein sequencingHost cytoplasmHydrolaseMetal-bindingProteaseReference proteomeSerine proteaseViriona divalent metal cationligand shared between trimeric partnersQPSPVIVIWLETCWRAVAKRITRSPTTITALPNSATQRDNDVKRFLVAAEVAVFDFSEKTVIMTYHPRELSFDAKQDGDYHRLMEQPSMTAEGKGRDVDNASQLHSDQDIDLDSSAQTSCDIDDGSDNKADHQRADIAADASHLEMGLLAPQLAIAGAQIDLHSASLENYMNTNKATATYLKSIMLPETGPASIPDDITERHILKQETSSYNLEVSESGSGVLVCFPGAPGSRIGAHYRWNANQTGLEFDQWLETSQDLKKAFNYGRLISRKYDIQSSTLPAGLYALNGTLNAATFEGSLSEVESLTYNSLMSLTTNPQDKVNNQLVTKGVTVLNLPTGFDKPYVRLEDETPQGLQSMNGAKMRCTAAIAPRRYEIDLPSQRLPPVPATGTLTTLYEGNADIVNSTTVTGDINFSLAEQPADETKFDFQLDFMGLDNDVPVVTVVSSVLATNDNYRGVSAKMTQSIPTENITKPITRVKLSYKINQQTAIGNVATLGTMGPASVSFSSGNGNVPGVLRPITLVAYEKMTPLSILTVAGVSNYELIPNPELLKNMVTRYGKYDPEGLNYAKMILSHREELDIRTVWRTEEYKERTRVFNEITDFSSDLPTSKAWGWRDIVRGIRKVAAPVLSTLFPMAAPLIGMADQFIGDLTKTNAAGGRYHSMAAGGRYKDVLESWASGGPDGKFSRALKNRLESANYEEVELPPPSKGVIVPVVHTVKSAPGEAFGSLAIIIPGEYPELLDANQQVLSHFANDTGSVWGIGEDIPFEGDNMCYTALPLKEIKRNGNIVVEKIFAGPIMGPSAQLGLSLLVNDIEDGVPRMVFTGEIADDEETIIPICGVDIKAIAAHEQGLPLIGNQPGVDEEVRNTSLAAHLIQTGTLPVQRAKGSNKRIKYLGELMASNASGMDEELQRLLNATMARAKEVQDAEIYKLLKLMAWTRKNDLTDHMYEWSKEDPDALKFGKLISTPPKHPEKPKGPDQHHAQEARATRISLDAVRAGADFATPEWVALNNYRGPSPGQFKYYLITGREPEPGDEYEDYIKQPIVKPTDMNKIRRLANSVYGLPHQEPAPEEFYDAVAAVFAQNGGRGPDQDQMQDLRELARQMKRRPRNADAPRRTRAPAEPAPPGRSRFTPSGDNAEV
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