POLS_IBDVP
ID POLS_IBDVP Reviewed; 993 AA.
AC P25220;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Structural polyprotein;
DE Short=PP;
DE Contains:
DE RecName: Full=Precursor of VP2;
DE Short=Pre-VP2;
DE Contains:
DE RecName: Full=Capsid protein VP2;
DE Contains:
DE RecName: Full=Structural peptide 1;
DE Short=p1;
DE AltName: Full=pep46;
DE Contains:
DE RecName: Full=Structural peptide 2;
DE Short=p2;
DE AltName: Full=pep7a;
DE Contains:
DE RecName: Full=Structural peptide 3;
DE Short=p3;
DE AltName: Full=pep7b;
DE Contains:
DE RecName: Full=Structural peptide 4;
DE Short=p4;
DE AltName: Full=pep11;
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 protein VP3;
DE Flags: Fragment;
OS Avian infectious bursal disease virus (strain PBG-98) (IBDV) (Gumboro
OS disease virus).
OC Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus.
OX NCBI_TaxID=11000;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2161902; DOI=10.1099/0022-1317-71-6-1303;
RA Bayliss C.D., Spies U., Shaw K., Peters R.W., Papageorgiou A., Mueller H.,
RA Boursnell M.E.G.;
RT "A comparison of the sequences of segment A of four infectious bursal
RT disease virus strains and identification of a variable region in VP2.";
RL J. Gen. Virol. 71:1303-1312(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 818-956, AND SUBUNIT.
RX PubMed=18184581; DOI=10.1016/j.str.2007.10.023;
RA Casanas A., Navarro A., Ferrer-Orta C., Gonzalez D., Rodriguez J.F.,
RA Verdaguer N.;
RT "Structural insights into the multifunctional protein VP3 of
RT birnaviruses.";
RL Structure 16:29-37(2008).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU00881}.
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Structural peptide 2 is a small peptide derived from pVP2 C-
CC terminus. It is not essential for the virus viability, but viral growth
CC is affected when missing (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Structural peptide 3 is a small peptide derived from pVP2 C-
CC terminus. It is not essential for the virus viability, but viral growth
CC is affected when missing (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Structural peptide 4 is a small peptide derived from pVP2 C-
CC terminus. It is essential for the virus viability (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Capsid protein VP2 is a homotrimer. A central divalent metal
CC stabilizes the VP2 trimer, possibly calcium (By similarity). Capsid
CC protein VP3 is a homodimer. Capsid protein VP2 interacts with host
CC ITGA4/ITGB1. Capsid protein VP3 interacts (via C-terminus) with VP1 in
CC the cytoplasm (By similarity). Capsid VP3 interacts with VP2.
CC {ECO:0000250, ECO:0000269|PubMed:18184581}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000305}. Host
CC cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000305}. Host
CC cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Structural peptide 1]: Virion {ECO:0000305}.
CC Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Structural peptide 2]: Virion {ECO:0000305}.
CC Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Structural peptide 3]: Virion {ECO:0000305}.
CC Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Structural peptide 4]: Virion {ECO:0000305}.
CC Host cytoplasm {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages yield mature proteins. The capsid
CC assembly seems to be regulated by polyprotein processing. The protease
CC VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3
CC within the infected cell. During capsid assembly, the C-terminus of
CC pre-VP2 is further processed by VP4, giving rise to VP2, the external
CC capsid protein and three small peptides that all stay closely
CC associated with the capsid (By similarity). {ECO:0000250}.
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DR EMBL; D00868; BAA00741.1; -; Genomic_RNA.
DR PIR; JQ0944; GNXS98.
DR PDB; 2R18; X-ray; 2.30 A; A=818-956.
DR PDB; 2Z7J; X-ray; 2.40 A; A=831-955.
DR PDBsum; 2R18; -.
DR PDBsum; 2Z7J; -.
DR BMRB; P25220; -.
DR SMR; P25220; -.
DR MEROPS; S50.002; -.
DR EvolutionaryTrace; P25220; -.
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-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host cytoplasm; Hydrolase; Metal-binding;
KW Protease; Serine protease; Virion.
FT CHAIN <1..993
FT /note="Structural polyprotein"
FT /id="PRO_0000392594"
FT CHAIN <1..422
FT /note="Capsid protein VP2"
FT /id="PRO_0000036773"
FT CHAIN 1..493
FT /note="Precursor of VP2"
FT /id="PRO_0000392595"
FT PEPTIDE 423..468
FT /note="Structural peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227845"
FT PEPTIDE 469..475
FT /note="Structural peptide 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227846"
FT PEPTIDE 476..482
FT /note="Structural peptide 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227847"
FT PEPTIDE 483..493
FT /note="Structural peptide 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227848"
FT CHAIN 494..736
FT /note="Protease VP4"
FT /id="PRO_0000036774"
FT CHAIN 737..993
FT /note="Capsid protein VP3"
FT /id="PRO_0000036775"
FT DOMAIN 494..736
FT /note="Peptidase S50"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT REGION 950..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..993
FT /note="Interaction with VP1 protein"
FT /evidence="ECO:0000250"
FT ACT_SITE 633
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT ACT_SITE 673
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT BINDING 11
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between trimeric partners"
FT /evidence="ECO:0000250"
FT SITE 422..423
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
FT SITE 468..469
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
FT SITE 475..476
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
FT SITE 482..483
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
FT SITE 493..494
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
FT SITE 736..737
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT HELIX 828..845
FT /evidence="ECO:0007829|PDB:2R18"
FT HELIX 853..858
FT /evidence="ECO:0007829|PDB:2R18"
FT HELIX 866..875
FT /evidence="ECO:0007829|PDB:2R18"
FT TURN 886..889
FT /evidence="ECO:0007829|PDB:2R18"
FT HELIX 899..910
FT /evidence="ECO:0007829|PDB:2R18"
FT HELIX 913..915
FT /evidence="ECO:0007829|PDB:2R18"
FT HELIX 920..932
FT /evidence="ECO:0007829|PDB:2R18"
FT TURN 933..935
FT /evidence="ECO:0007829|PDB:2R18"
FT HELIX 940..954
FT /evidence="ECO:0007829|PDB:2R18"
SQ SEQUENCE 993 AA; 107532 MW; 8CD7E94BB0CB3AF2 CRC64;
MPTTGPASIP DDTLEKHTLR SETSTYNLTV GDTGSGLIVF FPGFPGSIVG AHYTLQSNGN
YKFDQMLLTA QNLPASYNYC RLVSRSLTVR SSTLPGGVYA LNGTINAVTF QGSLSELTDV
SYNGLMSATA NINDKIGNVL VGEGVTVLSL PTSYDLGYVR LGDPIPAIGL DPKMVATCDS
SDRPRVYTIT AADDYQFSSQ YQPGGVTITL FSANIDAITS LSVGGELVFR TSVHGLVLGA
TIYLIGFDGT TVITRAVAAN TGLTTGTDNL MPFNLVIPTN EITQPITSIK LEIVTSKSGG
QAGDQMLWSA RGSLAVTIHG GNYPGALRPV TLVAYERVAT GSVVTVAGVS NFELIPNPEL
AKNLVTEYGR FDPGAMNYTK LILSERDRLG IKTVWPTREY TDFREYFMEV ADLNSPLKIA
GAFGFKDIIR AIRRIAVPVV STLFPPAAPL AHAIGEGVDY LLGDEAQAAS GTARAASGKA
RAASGRIRQL TLAADKGYEV VANLFQVPQN PVVDGILASP GVLRGAHNLD CVLREGATLF
PVVITTVEDA MTPKALNSKM FAVIEGVRED LQPPSQRGSF IRTLSGHRVY GYAPDGVLPL
ETGRDYTVVP IDDVWDDSIM LSKDPIPPIV GNSGNLAIAY MDVFRPKVPI HVAMTGALNA
CGEIEKVSFR STKLATAHRL GLKLAGPGAF DVNTGPNWAT FIKRFPHNPR DWDRLPYLNL
PYLPPNAGRQ YHLAMAASEF KETPELESAV RAMEAAANVD PLFQSALSVF MWLEENGIVT
DMANFALSDP NAHRMRNFLA NAPQAGSKSQ RAKYGTAGYG VEARGPTPEE AQREKDTRIS
KKMETMGIYF ATPEWVALNG HRGPSPGQLK YWQNTREIPD PNEDYLDYVH AEKSRLASEE
QILRAATSIY GAPGQAEPPQ AFIDEVAKVY EINHGRGPNQ EQMKDLLLTA MEMKHRNPRR
ALPKPKPKPN APTQRPPGRL GRWIRTVSDE DLE
