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Database: UniProt
Entry: A0A1B2FQQ0_IBDV
LinkDB: A0A1B2FQQ0_IBDV
Original site: A0A1B2FQQ0_IBDV 
ID   A0A1B2FQQ0_IBDV         Unreviewed;      1012 AA.
AC   A0A1B2FQQ0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   07-OCT-2020, entry version 20.
DE   RecName: Full=Structural polyprotein {ECO:0000256|RuleBase:RU363030};
DE            Short=PP {ECO:0000256|RuleBase:RU363030};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU363030};
OS   Avian infectious bursal disease virus (IBDV) (Gumboro disease virus).
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus.
OX   NCBI_TaxID=10995 {ECO:0000313|EMBL:ANY95155.1, ECO:0000313|Proteomes:UP000099980};
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
OH   NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN   [1] {ECO:0000313|EMBL:ANY95155.1, ECO:0000313|Proteomes:UP000099980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NKL14/ABT/MVC/India {ECO:0000313|EMBL:ANY95155.1};
RA   Senthilkumar T.M.A., Raja P., Kumanan K., Thangavelu A., Palanisammi A.;
RT   "Complete genome sequence of Infectious Bursal Disease virus segment A
RT   NKL14/ABT/MVC/India.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000099980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Senthilkumar T.M.A., Raja P., Kumanan K., Thangavelu A., Palanisammi A.;
RT   "Complete genome sequence of Infectious Bursal Disease virus segment B
RT   NKL14/ABT/MVC/India.";
RL   Submitted (JAN-2016) 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.
CC       {ECO:0000256|RuleBase:RU363030}.
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:ARBA00002880,
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|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:ARBA00002547,
CC       ECO:0000256|RuleBase:RU363030}.
CC   -!- SUBUNIT: Capsid protein VP2 is a homotrimer. A central divalent metal
CC       stabilizes the VP2 trimer. {ECO:0000256|RuleBase:RU363030}.
CC   -!- SUBUNIT: Capsid protein VP3 is a homodimer.
CC       {ECO:0000256|RuleBase:RU363030}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC       cytoplasm {ECO:0000256|ARBA:ARBA00004192,
CC       ECO:0000256|RuleBase:RU363030}. Virion {ECO:0000256|ARBA:ARBA00004328,
CC       ECO:0000256|RuleBase:RU363030}.
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DR   EMBL; KU578098; ANY95155.1; -; Genomic_RNA.
DR   Proteomes; UP000099980; 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   Gene3D; 1.10.150.620; -; 1.
DR   Gene3D; 1.10.8.880; -; 1.
DR   Gene3D; 2.60.120.20; -; 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   PROSITE; PS51548; BIRNAVIRUS_VP4_PRO; 1.
PE   4: Predicted;
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, ECO:0000256|RuleBase:RU363030};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU363030};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00881, ECO:0000256|RuleBase:RU363030};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU00881, ECO:0000256|RuleBase:RU363030};
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|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        692
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00881"
SQ   SEQUENCE   1012 AA;  109465 MW;  04D8CBE79D6EC786 CRC64;
     MTNLQDQTQQ IVPFIRSLLM PTTGPASIPD DTLEKHTLRS ETSTYNLTVG DTGSGLIVFF
     PGFPGSIVGA HYTLQSNGNY KFDQMLLTAQ NLPASYNYCR LVSRSLTVRS STLPGGVYAL
     NGTINAVTFQ GSLSELTDVS YNGLMSATAN INDKIGNVLV GEGVTVLSLP TSYDLGYVRL
     GDPIPAIGLD PKMVATCDSS DRPRVYTITA ANDYQFSSQY QAGGVTITLF SANIDAITSL
     SIGGELVFQT SVQGLILGAT IYLIGFDGTA VITRAVAADN GLTAGTDNLM PFNVVIPTSA
     ITQPITSIKL EIVTSKSGGQ AGDQMSWSAS 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 LRLAGPGAFD VNTGPNWATF
     IKRFPHNPRD WDRLPYLNLP YLPPNAGRQY HLAMAASEFK 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
//
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