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
//
