ID Q9IGX1_IBDV Unreviewed; 1012 AA.
AC Q9IGX1;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 08-NOV-2023, entry version 70.
DE RecName: Full=Structural polyprotein {ECO:0000256|RuleBase:RU363030};
DE Short=PP {ECO:0000256|RuleBase:RU363030};
DE Contains:
DE RecName: Full=Precursor of VP2 {ECO:0000256|RuleBase:RU363030};
DE Short=Pre-VP2 {ECO:0000256|RuleBase:RU363030};
DE Contains:
DE RecName: Full=Capsid protein VP2 {ECO:0000256|RuleBase:RU363030};
DE Contains:
DE RecName: Full=Structural peptide 1 {ECO:0000256|RuleBase:RU363030};
DE Short=p1 {ECO:0000256|RuleBase:RU363030};
DE AltName: Full=pep46 {ECO:0000256|RuleBase:RU363030};
DE Contains:
DE RecName: Full=Structural peptide 2 {ECO:0000256|RuleBase:RU363030};
DE Short=p2 {ECO:0000256|RuleBase:RU363030};
DE AltName: Full=pep7a {ECO:0000256|RuleBase:RU363030};
DE Contains:
DE RecName: Full=Structural peptide 3 {ECO:0000256|RuleBase:RU363030};
DE Short=p3 {ECO:0000256|RuleBase:RU363030};
DE AltName: Full=pep7b {ECO:0000256|RuleBase:RU363030};
DE Contains:
DE RecName: Full=Protease VP4 {ECO:0000256|RuleBase:RU363030};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU363030};
DE AltName: Full=Non-structural protein VP4 {ECO:0000256|RuleBase:RU363030};
DE Short=NS {ECO:0000256|RuleBase:RU363030};
DE Contains:
DE RecName: Full=Capsid protein VP3 {ECO:0000256|RuleBase:RU363030};
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:AAF85953.1};
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1] {ECO:0000313|EMBL:AAF85953.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10888607; DOI=10.1128/JVI.74.15.6701-6711.2000;
RA Boot H.J., ter Huurne A.A., Hoekman A.J., Peeters B.P., Gielkens A.L.;
RT "Rescue of very virulent and mosaic infectious bursal disease virus from
RT cloned cDNA: VP2 is not the sole determinant of the very virulent
RT phenotype.";
RL J. Virol. 74:6701-6711(2000).
RN [2] {ECO:0000313|EMBL:CDP32872.1, ECO:0000313|Proteomes:UP000158809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=89163 {ECO:0000313|EMBL:CDP32872.1};
RA Li K., Courtillon C., Guionie O., Allee C., Amelot M., Qi X., Gao Y.,
RA Wang X., Eterradossi N.;
RT "Genetic, antigenic and pathogenic characterization of four infectious
RT bursal disease virus isolates from China suggests continued evolution of
RT very virulent viruses.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QIR82434.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SD-2013-1 {ECO:0000313|EMBL:QIR82434.1};
RA Xu A., Zhang G.;
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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 interacting with
CC host ITGA4/ITGB1. {ECO:0000256|ARBA:ARBA00024715}.
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. {ECO:0000256|ARBA:ARBA00025351,
CC ECO:0000256|RuleBase:RU363030}.
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, ECO:0000256|RuleBase:RU363030}.
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. {ECO:0000256|ARBA:ARBA00025236,
CC ECO:0000256|RuleBase:RU363030}.
CC -!- FUNCTION: Structural peptide 2 is a small peptide derived from pre-VP2
CC C-terminus. It is not essential for the virus viability, but viral
CC growth is affected when missing. {ECO:0000256|RuleBase:RU363030}.
CC -!- FUNCTION: Structural peptide 3 is a small peptide derived from pre-VP2
CC C-terminus. It is not essential for the virus viability, but viral
CC growth is affected when missing. {ECO:0000256|RuleBase:RU363030}.
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. {ECO:0000256|ARBA:ARBA00024831,
CC ECO:0000256|RuleBase:RU363030}.
CC -!- SUBUNIT: Homotrimer. A central divalent metal stabilizes the VP2 trimer
CC (By similarity). Interacts with host ITGA4/ITGB1.
CC {ECO:0000256|ARBA:ARBA00034509}.
CC -!- SUBUNIT: [Capsid protein VP2]: Homotrimer. A central divalent metal
CC stabilizes the VP2 trimer. {ECO:0000256|RuleBase:RU363030}.
CC -!- SUBUNIT: [Capsid protein VP3]: Homodimer. Interacts (via C-terminus)
CC with VP1 in the cytoplasm. Interacts with VP2.
CC {ECO:0000256|RuleBase:RU363030}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
CC -!- SUBCELLULAR LOCATION: [Structural peptide 2]: Virion
CC {ECO:0000256|RuleBase:RU363030}. Host cytoplasm
CC {ECO:0000256|RuleBase:RU363030}.
CC -!- SUBCELLULAR LOCATION: [Structural peptide 3]: Virion
CC {ECO:0000256|RuleBase:RU363030}. Host cytoplasm
CC {ECO:0000256|RuleBase:RU363030}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000256|RuleBase:RU363030}. Host cytoplasm
CC {ECO:0000256|RuleBase:RU363030}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC {ECO:0000256|RuleBase:RU363030}. Host cytoplasm
CC {ECO:0000256|RuleBase:RU363030}.
CC -!- SUBCELLULAR LOCATION: [Structural peptide 1]: Virion
CC {ECO:0000256|RuleBase:RU363030}. Host cytoplasm
CC {ECO:0000256|RuleBase:RU363030}.
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DR EMBL; AF240686; AAF85953.1; -; mRNA.
DR EMBL; HG974563; CDP32872.1; -; Genomic_RNA.
DR EMBL; MN485880; QIR82434.1; -; Genomic_RNA.
DR PIR; JC1327; JC1327.
DR PIR; JQ2198; JQ2198.
DR MEROPS; S50.002; -.
DR Proteomes; UP000158809; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-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; 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 2: Evidence at transcript level;
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561,
KW ECO:0000256|RuleBase:RU363030};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200,
KW ECO:0000256|RuleBase:RU363030};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00881};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363030};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00881};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU00881};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU363030}.
FT DOMAIN 513..755
FT /note="Peptidase S50"
FT /evidence="ECO:0000259|PROSITE:PS51548"
FT REGION 968..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 1012 AA; 109538 MW; D75FA8DA0EF5E147 CRC64;
MTNLQDQTQQ IVPFIRSLLM PTTGPASIPD DTLEKHTLRS ETSTYNLTVG DTGSGLIVFF
PGFPGSIVGA HYTLQSNGNY KFDQMLLTAQ NLPASYNYCR LVSRSLTVRS STLPGGVYAL
NGTINAVTFQ GSLSELTDVS YNGLMSATAN INDKIGNVLV GEGVTVLSLP TSYDLGYVRL
GDPIPAIGLD PKMVATCDSS DRPRVYTITA ADDYQFSSQY QAGGVTITLF SANIDAITSL
SIGGELVFQT SVQGLILGAT IYLIGFDGTA VITRAVAADN GLTAGTDNLM PFNIVIPTSE
ITQPITSIKL EIVTSKSGGQ AGDQMSWSAS GSLAVTIHGG NYPGALRPVT LVAYERVATG
SVVTVAGVSN FELIPNPELA KNLVTEYGRF DPGAMNYTKL ILSERDRLGI KTVWPTREYT
DFREYFMEVA DLNSPLKIAG AFGFKDIIRA LRRIAVPVVS TLFPPAAPLA HAIGEGVDYL
LGDEAQAASG TARAASGKAR AASGRIRQLT LAADKGYEVV ANLFQVPQNP VVDGILASPG
ILRGAHNLDC VLREGATLFP VVITTVEDAM TPKALNSKMF AVIEGVREDL QPPSQRGSFI
RTLSGHRVYG YAPDGVLPLE TGRDYTVVPI DDVWDDSIML SKDPIPPIVG NSGNLAIAYM
DVFRPKVPIH VAMTGALNAY GEIENVSFRS TKLATAHRLG LKLAGPGAFD VNTGSNWATF
IKRFPHNPRD WDRLPYLNLP YLPPNAGRQY DLAMAASEFK ETPELESAVR AMEAAANVDP
LFQSALSVFM WLEENGIVTD MANFALSDPN AHRMRNFLAN APQAGSKSQR AKYGTAGYGV
EARGPTPEEA QREKDTRISK KMETMGIYFA TPEWVALNGH RGPSPGQLKY WQNTREIPDP
NEDYLDYVHA EKSRLASEEQ ILRAATSIYG APGQAEPPQA FIDEVAKVYE INHGRGPNQE
QMKDLLLTAM EMKHRNPRRA PPKPKPKPNA PTQRPPGRLG RWIRAVSDED LE
//
