ID   A8IG08_IBDV             Unreviewed;       778 AA.
AC   A8IG08;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   SubName: Full=Polyprotein {ECO:0000313|EMBL:ABW04864.1};
DE   Flags: Fragment;
OS   Avian infectious bursal disease virus (IBDV) (Gumboro disease virus).
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus;
OC   Avibirnavirus gumboroense.
OX   NCBI_TaxID=10995 {ECO:0000313|EMBL:ABW04864.1};
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
OH   NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN   [1] {ECO:0000313|EMBL:ABW04864.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=D78 {ECO:0000313|EMBL:ABW04864.1};
RX   PubMed=18502466; DOI=10.1016/j.virol.2008.04.018;
RA   Jackwood D.J., Sreedevi B., Lefever L.J., Sommer-Wagner S.E.;
RT   "Studies on naturally occurring infectious bursal disease viruses suggest
RT   that a single amino acid substitution at position 253 in VP2 increases
RT   pathogenicity.";
RL   Virology 377:110-116(2008).
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:0000256|PROSITE-ProRule:PRU00881}.
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DR   EMBL; EU162087; ABW04864.1; -; Genomic_RNA.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-UniRule.
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; 6.10.250.1030; -; 1.
DR   Gene3D; 2.60.120.660; icosahedral virus; 1.
DR   InterPro; IPR002662; Birna_VP2.
DR   InterPro; IPR025775; Birna_VP4_Prtase_dom.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF01766; Birna_VP2; 1.
DR   Pfam; PF01768; Birna_VP4; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1.
DR   PROSITE; PS51548; BIRNAVIRUS_VP4_PRO; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00881};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00881};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU00881}.
FT   DOMAIN          513..755
FT                   /note="Peptidase S50"
FT                   /evidence="ECO:0000259|PROSITE:PS51548"
FT   ACT_SITE        652
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602662-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        692
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602662-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00881"
FT   NON_TER         778
FT                   /evidence="ECO:0000313|EMBL:ABW04864.1"
SQ   SEQUENCE   778 AA;  83340 MW;  F3984BA64E2F2B6E CRC64;
     MTNLQDQTQQ IVPFIRSLLM PTTGPASIPD DTLEKHTLRS ETSTYNLTVG DTGSGLIVFF
     PGFPGSIVGA HYTLQGNGNY KFDQMLLTAQ NLPASYNYCR LVSRSLTVRS STLPGGVYAL
     NGTINAVTFQ GSLSELTDVS YNGLMSATAN INDKIGNVLV GEGVTVLSLP TSYDLGYVRL
     GDPIPAIGLD PKMVATCDSS DRPRVYTITA ADDYQFSSQY QPGGVTITLF SANIDAITSL
     SVGGELVFQT SVHGLVLGAT IYLIGFDGTT VITRAVAANN GLTTGTDNLM PFNLVIPTNE
     ITQPITSIKL EIVTSKSGGQ AGDQMSWSAR GSLAVTIHGG NYPGALRPVT LVAYERVATG
     SVVTVAGVSN FELIPNPELA KNLVTEYGRF DPGAMNYTKL ILSERDRLGI KTVWPTREYT
     DFREYFMEVA DLNSPLKIAG AFGFKDIIRA IRRIAVPVVS TLFPPAAPLA HAIGEGVDYL
     LGDEAQAASG TARAASGKAR AASGRIRQLT LAADKGYEVV ANLFQVPQNP VVDGILASPG
     VLRGAHNLDC VLREGATLFP VVITTVEDAM TPKALNSKMF AVIEGVREDL QPPSQRGSFI
     RTLSGHRVYG YAPDGVLPLE TGRDYTVVPI DDVWDDSIML SKDPIPPIVG NSGNLAIAYM
     DVFRPKVPIH VAMTGALNAC GEIEKVSFRS TKLATAHRLG LKLAGPGAFD VNTGPNWATF
     IKRFPHNPRD WDRLPYLNLP YLPPNAGRQY HLAMAASEFK ETPELESAVR AMEAAANV
//