ID A0PBU2_9VIRU Unreviewed; 972 AA.
AC A0PBU2;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 08-NOV-2023, entry version 41.
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};
GN Name=VP2-NS-VP3 {ECO:0000313|EMBL:BAF37013.1};
OS Yellowtail ascites virus.
OC Viruses; Riboviria; Orthornavirae; Birnaviridae; Aquabirnavirus;
OC Aquabirnavirus ascitae.
OX NCBI_TaxID=59816 {ECO:0000313|EMBL:BAF37013.1};
RN [1] {ECO:0000313|EMBL:BAF37013.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YTAV-06 {ECO:0000313|EMBL:BAF37013.1};
RX PubMed=17446679;
RA Hirayama T., Nagano I., Shinmoto H., Yagyu K., Oshima S.;
RT "Isolation and characterization of virulent yellowtail ascites virus.";
RL Microbiol. Immunol. 51:397-406(2007).
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; AB281673; BAF37013.1; -; Genomic_RNA.
DR MEROPS; S50.001; -.
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 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};
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 798..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..814
FT /note="Basic and acidic residues"
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"
SQ SEQUENCE 972 AA; 106776 MW; 2F4C5187579B58B1 CRC64;
MNTTKATATY LRSIMLPENG PASIPDDITE RHILKQETSS YNLEVSDSGS GLLVCFPGAP
GSRVGAHYKW NQNQTELEFD QWLETSQDLK KAFNYGRLIS RKYDVQSSTL PAGLYALNGT
LNAATFEGSL SEVESFSYNS LMSLTTNPQD KVNNQLVTKG VTVLNLPTGF DKPYVRLEDE
TPQGPQSMNG ARMRCTAAIA PRRYEIDLPS ARLPTAPATG TLTTIYEGNA DIVNSTTVTG
DISFRLEQDP PNDTKYDFQL DFLGLDNNVP VVSITSSTLA TTDNYRGVSV KFTQSIPTEA
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 LVNDIDRGVP RMVFTGEIAD
DEETIIPIYG VDIKAIAAHE HGLPLVGCQP GVDEVVANTS LASHLIQSGA LPVQKAQGAS
RRIKYLGELM RTTASGMDEE LQKLLQATMA RAKEVKDAEV FKLLKLMSWT RKNGLTDHMY
EWSKEDPEAV KFGKLISTPP KHQEKPKGPD QHTAQEAKAA RISLDAVKAG ADFASPDWIA
ENGYRGPSPG QFKYYVITGR VPDPRDEYED YVRKPITRPT DMDKIRRLAN SVYGLPHQEP
APEEFYQAVV EIFAENGGRG PDQDQMQDLR DLARQMKRRP RPAETRRQNR APPRAAPSGS
SRFTPSGDNG EV
//
