ID   P89521_9VIRU            Unreviewed;       972 AA.
AC   P89521;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 91.
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   Yellowtail ascites virus - Y-6.
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Aquabirnavirus;
OC   Aquabirnavirus ascitae.
OX   NCBI_TaxID=360000 {ECO:0000313|EMBL:BAA22055.1, ECO:0000313|Proteomes:UP000208107};
RN   [1] {ECO:0000313|EMBL:BAA22055.1, ECO:0000313|Proteomes:UP000208107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y-6 {ECO:0000313|EMBL:BAA22055.1,
RC   ECO:0000313|Proteomes:UP000208107};
RA   Suzuki S., Kimura M., Kusuda R.;
RT   "The complete nucleotide sequence of the polyprotein and VP5 gene of a
RT   marine birnavirus.";
RL   Fish. Sci. 64:428-433(1998).
RN   [2] {ECO:0000313|Proteomes:UP000208107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y-6 {ECO:0000313|Proteomes:UP000208107};
RX   PubMed=12664297; DOI=10.1007/s00705-002-0951-y;
RA   Zhang C.X., Suzuki S.;
RT   "Comparison of the RNA polymerase genes of marine birnavirus strains and
RT   other birnaviruses.";
RL   Arch. Virol. 148:745-758(2003).
RN   [3] {ECO:0007829|PDB:4IZJ, ECO:0007829|PDB:4IZK}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 508-716, AND DISULFIDE BONDS.
RX   PubMed=23511637; DOI=10.1074/jbc.M112.386953;
RA   Chung I.Y., Paetzel M.;
RT   "Crystal structures of yellowtail ascites virus VP4 protease: trapping an
RT   internal cleavage site trans acyl-enzyme complex in a native Ser/Lys dyad
RT   active site.";
RL   J. Biol. Chem. 288:13068-13081(2013).
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|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:ARBA00024831,
CC       ECO:0000256|RuleBase:RU363030}.
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; AB006783; BAA22055.1; -; Genomic_RNA.
DR   RefSeq; NP_690805.1; NC_004168.1.
DR   PDB; 4IZJ; X-ray; 2.50 A; A/B/C/D/E=508-716.
DR   PDB; 4IZK; X-ray; 2.30 A; A/B=508-716.
DR   PDBsum; 4IZJ; -.
DR   PDBsum; 4IZK; -.
DR   SMR; P89521; -.
DR   MEROPS; S50.001; -.
DR   GeneID; 995355; -.
DR   KEGG; vg:995355; -.
DR   Proteomes; UP000208107; 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; 3.30.230.110; -; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4IZJ, ECO:0007829|PDB:4IZK};
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          509..734
FT                   /note="Peptidase S50"
FT                   /evidence="ECO:0000259|PROSITE:PS51548"
FT   REGION          916..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..939
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        633
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602662-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        674
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602662-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00881"
FT   BINDING         602
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:4IZJ"
FT   DISULFID        588..604
FT                   /evidence="ECO:0007829|PDB:4IZJ, ECO:0007829|PDB:4IZK"
SQ   SEQUENCE   972 AA;  106768 MW;  4F9149F65966F226 CRC64;
     MNTTKATATY LRSIMLPENG PASIPDDITE RHILKQETSS YNLEVSDSGS GLLVCFPGAP
     GSRVGAHYKW NQNQTELEFD QWLETSQDLK KAFNYGRLIS RKYDVQSSTL PAGLYALNGT
     LNAATFEGSL SEVESFSYNS LMSLTTNPQD KVNNQLVTKG VTVLNLPTGF DKPYVRLEDE
     TPQGPQSMNG ARMRCTAAIA PRRYEIDLPS ARLPTVPATG TLTTIYEGNA DIVNSTTVTG
     DISFRLEQDP PNDTKYDFQL DFLGLDNNVP VVSITSSTLA TTDNYRGVSV KFTQSIPTET
     ITKPITRVKL SYKINQQTAI GNAATLGPLG PSSVSFSSGN GNVPGVLRPI TLVAYEKMTP
     QSILTVAGVS NYELIPNPEL LKNMVTKYGK YDPEGLNYAK MILSHREELD IRTVWRTEEY
     KERTRAFNEI TDFSSDLPTS KAWGWRDIVR GIRKVAAPVL STLFPMAAPL IGAADQFIGD
     LTKTNAAGGR YLTHAAGGRY TDVMDSWASG TDTGRFSRNL KDRLESNNYE EMELPPPTKG
     VIIPVVHTVE SAPGEAFGSL LVIIPGAYPE LLDPNQQVLS HFKNDTGCVW GIGEDIPFEG
     DDICYTALPL KEIKKNGNIV VEKVFAGPAM GPSCQLGLSL LVNDIDKGVP RMVFTGEIAN
     DEETIVPICG VDIKAIAAHE HGLPLVGCQP GVDEVVANTS LASHLIQSGA LPVQKAQGAS
     RRIKYLGELM RTTASGMDEE LQKLLHATMA RAKEVKDAEV FKLLKLMSWT RKNGLTDHMY
     EWSKEDPEAV KFGKLISTPP KHQEKPKGPD QHTAQEAKAV RISLDAVKAG ADFASPDWIA
     ENGYRGPSPG QFKYYVITGR VPDPRDEYED YVRKPITRPT DMDKIRRLAN SVYGLPHQEP
     APEEFYQAVV EIFAENGGRG PDQDQMQDLR DLARQMKRRP RPAETRRQNR APPRAAPSGS
     SRFTPSGDNG EV
//