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Database: UniProt
Entry: Q9WLE3_9VIRU
LinkDB: Q9WLE3_9VIRU
Original site: Q9WLE3_9VIRU 
ID   Q9WLE3_9VIRU            Unreviewed;       972 AA.
AC   Q9WLE3;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   07-OCT-2020, entry version 52.
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   Infectious pancreatic necrosis virus.
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Aquabirnavirus.
OX   NCBI_TaxID=11002 {ECO:0000313|EMBL:AAC71003.1, ECO:0000313|Proteomes:UP000268519};
RN   [1] {ECO:0000313|EMBL:AAC71003.1, ECO:0000313|Proteomes:UP000268519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=West Buxton {ECO:0000313|EMBL:AAC71003.1,
RC   ECO:0000313|Proteomes:UP000268519};
RX   PubMed=9765436;
RA   Yao K., Vakharia V.N.;
RT   "Generation of infectious pancreatic necrosis virus from cloned cDNA.";
RL   J. Virol. 72:8913-8920(1998).
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: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; AF078668; AAC71003.1; -; Genomic_RNA.
DR   Proteomes; UP000268519; 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          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="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        633
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        674
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00881"
SQ   SEQUENCE   972 AA;  106632 MW;  34C38C26DB55A131 CRC64;
     MNTTKATATY LRSIMLPENG PASIPDDITE RHILKQETSS YNLEVSDSGS GLLVCFPGAP
     GSRVGAHYRW NLNQTELEFD QWLETSQDLK KAFNYGRLIS RKYDIQSSTL PAGLYALNGT
     LNAATFEGSL SEVESLTYNS LMSLTTNPQD KVNNQLVTKG ITVLNLPTGF DKPYVRLEDE
     TPQGPQSMNG ARMRCTAAIA PRRYEIDLPS ERLPTVAATG TPTTIYEGNA DIVNSTTVTG
     DVTFQLAAEP VNETRFDFIL QFLGLDNDVP VVSVTSSTLV TADNYRGASA KFTQSIPTEL
     ITKPITRVKL AYQLNQQTAI GNAATLGAKG PPSVSFSSGN GNVPGVLRPI TLVAYEKMTP
     QSILTVAGVS NYELIPNPDL LKNMVTKYGK YDPEGLNYAK MILSHREELD IRTVWRTEEY
     KERTRAFNEI TDFTSDLPTS KAWGWRDLVR GIRKVAAPVL STLFPMAAPL IGAADQFIGD
     LTKTNSAGGR YLSHAAGGRY RDVMDTWASG SETGSYSKHL KTRLESNNYE EVELPKPTKG
     VIFPVVHTVE SAPGEAFGSL VVVIPGAYPE LLDPNQQVLS YFKNDTGCVW GIGEDIPFEG
     DDMCYTALPL KEIKRNGNIV VEKIFAGPAM GPSAQLALSL LVNDIDEGIP RMVFTGEIAD
     DEETVIPICG VDIKAIAAHE HGLPLIGCQP GVDEMVANTS LASHLIQSGA LPVQKAQGAC
     RKIKYLGQLM RTTASGMDEE LQGLLQATMA RAKEVKDAEV FKLLKLMSWT RKNDLTDHMY
     EWSKEDPDAI KFGRLISTPP KHQEKPKGPD QHTAQEAKAT RISLDAVKAG ADFASPEWIA
     ENNYRGPAPG QFKYYMITGR VPNPGVEYED YVRKPITRPT DMDKIRRLAN SVYGLPHQEP
     APDDFYQAVV EVFAENGGRG PDQDQMQDLR DLARQMKRRP RPADARRQTR TPPRAATSGG
     SRFTPSGDDG EV
//
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