ID POLS_IBDVE Reviewed; 1012 AA. AC P29802; Q9WHR0; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 2. DT 04-NOV-2008, entry version 44. DE RecName: Full=Structural polyprotein; DE Short=PP; DE Contains: DE RecName: Full=Capsid protein VP2; DE Contains: DE RecName: Full=p1; DE Contains: DE RecName: Full=p2; DE Contains: DE RecName: Full=p3; DE Contains: DE RecName: Full=p4; 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 assembly protein VP3; OS Avian infectious bursal disease virus (strain E) (IBDV) (Gumboro OS disease virus). OC Viruses; dsRNA viruses; Birnaviridae; Avibirnavirus. OX NCBI_TaxID=31560; OH NCBI_TaxID=9031; Gallus gallus (Chicken). OH NCBI_TaxID=9103; Meleagris gallopavo (Common turkey). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX MEDLINE=99435247; PubMed=10507413; DOI=10.1016/S0166-0934(99)00083-X; RA Akin A., Wu C.C., Lin T.L.; RT "Amplification and cloning of infectious bursal disease virus genomic RT RNA segments by long and accurate PCR."; RL J. Virol. Methods 82:55-61(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX MEDLINE=91341469; PubMed=1651980; RA Heine H.G., Haritou M., Failla P., Fahey K.J., Azad A.A.; RT "Sequence analysis and expression of the host-protective immunogen VP2 RT of a variant strain of infectious bursal disease virus which can RT circumvent vaccination with standard type I strains."; RL J. Gen. Virol. 72:1835-1843(1991). CC -!- FUNCTION: VP2 trimers form the shell (By similarity). CC -!- FUNCTION: Protease VP4 is a serine protease that cleaves the CC polyprotein to release the mature proteins (By similarity). CC -!- FUNCTION: VP3 binds to viral double-strand RNA (dsRNA), both of CC the A segment and of the B segment. Might therefore be involved in CC genomic RNA packaging. Although it does not follow the icosahedral CC symmetry, VP3 controls the assembly of the T=13 capsid (By CC similarity). CC -!- FUNCTION: p1 is a small peptide derived from pVP2 C-terminus. It CC is essential for the virus viability (By similarity). CC -!- FUNCTION: p2 is a small peptide derived from pVP2 C-terminus. It CC is not essential for the virus viability, but viral growth is CC affected when missing (By similarity). CC -!- FUNCTION: p3 is a small peptide derived from pVP2 C-terminus. It CC is not essential for the virus viability, but viral growth is CC affected when missing (By similarity). CC -!- FUNCTION: p4 is a small peptide derived from pVP2 C-terminus. It CC is essential for the virus viability (By similarity). CC -!- SUBUNIT: VP2 is trimeric. VP3 interacts with VP1 in the cytoplasm CC (By similarity). CC -!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion (Potential). CC -!- PTM: Specific enzymatic cleavages yield mature proteins. The CC capsid assembly seems to be regulated by polyprotein processing. CC The polyprotein is processed by protease VP4 into the major CC structural proteins of the virion, precursor of VP2 (pVP2) and CC VP3. During capsid assembly, the C-terminus of pVP2 is processed CC by VP4, giving rise to VP2, the external capsid protein and four CC small peptides that all stay closely associated with the capsid CC (By similarity). CC -!- MISCELLANEOUS: Birnavirus particles are about 60 nm in diameter CC and are composed of a single, non-enveloped, T=13 icosahedral CC shell, made of 260 VP2 trimers. The major components of the CC particles are VP2 and VP3. The capsid contains two genome segments CC A and B of double-strand RNA. Minor amounts of VP1, VP4, p1, p2, CC p3, p4 and trace amount of the polyprotein are also incorporated CC in the virion (By similarity). CC -!- MISCELLANEOUS: This protein is encoded by the large RNA segment A CC coding for the structural polyprotein and VP5. CC -!- SIMILARITY: Contains 1 peptidase S50 domain. 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; AF133904; AAD32617.1; -; Genomic_RNA. DR EMBL; D10065; BAA00954.1; -; Genomic_RNA. DR PIR; PQ0283; GNXSIE. DR SMR; P29802; 8-440. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR002662; Birna_VP2. DR InterPro; IPR002663; Birna_VP3. DR InterPro; IPR002664; Peptidase_S50. DR Pfam; PF01766; Birna_VP2; 1. DR Pfam; PF01767; Birna_VP3; 1. DR Pfam; PF01768; Birna_VP4; 1. PE 3: Inferred from homology; KW Capsid protein; Hydrolase; Protease; Serine protease; Virion. FT CHAIN 1 441 Capsid protein VP2. FT /FTId=PRO_0000036768. FT PEPTIDE 442 487 p1 (By similarity). FT /FTId=PRO_0000227835. FT PEPTIDE 488 494 p2 (By similarity). FT /FTId=PRO_0000227836. FT PEPTIDE 495 501 p3 (By similarity). FT /FTId=PRO_0000227837. FT PEPTIDE 502 512 p4 (By similarity). FT /FTId=PRO_0000227838. FT CHAIN 513 755 Protease VP4 (By similarity). FT /FTId=PRO_0000227839. FT CHAIN 756 1012 Capsid assembly protein VP3 (By FT similarity). FT /FTId=PRO_0000227840. FT REGION 1003 1012 Interaction with VP1 protein (By FT similarity). FT ACT_SITE 652 652 Nucleophile (By similarity). FT ACT_SITE 692 692 By similarity. FT SITE 441 442 Cleavage; by protease VP4 (By FT similarity). FT SITE 487 488 Cleavage; by protease VP4 (By FT similarity). FT SITE 494 495 Cleavage; by protease VP4 (By FT similarity). FT SITE 501 502 Cleavage; by protease VP4 (By FT similarity). FT SITE 512 513 Cleavage; by protease VP4 (By FT similarity). FT SITE 755 756 Cleavage; by protease VP4 (By FT similarity). FT CONFLICT 5 5 Q -> S (in Ref. 2; BAA00954). FT CONFLICT 262 262 C -> Y (in Ref. 2; BAA00954). FT CONFLICT 469 469 V -> L (in Ref. 2; BAA00954). FT CONFLICT 481 481 R -> L (in Ref. 2; BAA00954). FT CONFLICT 495 496 AS -> KL (in Ref. 2; BAA00954). SQ SEQUENCE 1012 AA; 110035 MW; 9651DE7FCCAFDE20 CRC64; MTNLQDQTQQ IVPFIRSLLM PTTGPASIPD DTLEKHTLRS ETSTYNLTVG DTGSGLIVFF PGFPGSIVGA HYTLQSNGNY KFDQMLLTAQ NLPASYNYCR LVSRSLTVRS STLPGGVYAL NGTINAVTFQ GSLSELTDVS YNGLMSATAN INDKIGNVLV GEGVTVLSLP TSYDLGYVRL GDPIPAIGLD PKMVATCDSS DRPRVYTITA ADNYQFSSQY QTGGVTITLF SANIDAITSL SVGGELVFKT SVQSLVLGAT ICLIGFDGTA VITRAVAANN GLTAGIDNLM PFNLVIPTNE ITQPITSIKL EIVTSKSDGQ AGEQMSWSAS GSLAVTIHGG NYPGALRPVT LVAYERVATG SVVTVAGVSN FELIPNPELA KNLVTEYGRF DPGAMNYTKL ILSERDRLGI KTVWPTREYT DFREYFMEVA DLNSPLKIAG AFGFKDIIRA IRRIAVPVVS TLFPPAAPVA HAIGEGVDYL RGDEAQAASG TARAASGKAR AASGRIRQLT LAADKGYEVV ANLFQVPQNP VVDGILASPG ILRGAHNLDC VLREGATLFP VVITTVEDAM TPKALNNKMF AVIEGVREDL QPPSQRGSFI RTLSGHRVYG YAPDGVLPLE TGRDYTVVPI DDVWDDSIML SKDPIPPIVG NSGNLAIAYM DVFRPKVPIH VAMTGALNAC GEIEKISFRS TKLATAHRLG LKLAGPGAFD VNTGPNWATF IKRFPHNPRD WDRLPYLNLP YLPPNAGRQY HLAMAASEFK ETPELESAVR AMEAAANVDP LFQSALSVFM WLEENGIVTD MANFALSDPN AHRMRNFLAN ALQAGSKSQR AKYGTAGYGV EARGPTLEGA QREKDTRISK KMETMGIYFA TQEWVAFNRH RRPSPGQLKY WQNTREIPDP NEYYLDYVHA EKSRLASEEQ ILRAATSIYG APVQAEPLQA FIDEVAKVYE INHGRGPNQE QMKDLLLTAM EMKHRNPRRA PPKPKPKPNA PTQRPPGRLG RWIRTVSDED LE //