ID D0U495_9VIRU Unreviewed; 979 AA.
AC D0U495;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 08-NOV-2023, entry version 32.
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 Drosophila melanogaster birnavirus SW-2009a.
OC Viruses; Riboviria; Orthornavirae; Birnaviridae.
OX NCBI_TaxID=663281 {ECO:0000313|EMBL:ACU32790.1, ECO:0000313|Proteomes:UP000170672};
RN [1] {ECO:0000313|EMBL:ACU32790.1, ECO:0000313|Proteomes:UP000170672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DBV {ECO:0000313|EMBL:ACU32790.1};
RX PubMed=20080648; DOI=10.1073/pnas.0911353107;
RA Wu Q., Luo Y., Lu R., Lau N., Lai E.C., Li W.X., Ding S.W.;
RT "Virus discovery by deep sequencing and assembly of virus-derived small
RT silencing RNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1606-1611(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GQ342962; ACU32790.1; -; Genomic_RNA.
DR Proteomes; UP000170672; 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000170672};
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 517..721
FT /note="Peptidase S50"
FT /evidence="ECO:0000259|PROSITE:PS51548"
FT REGION 850..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 626
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR602662-1,
FT ECO:0000256|PROSITE-ProRule:PRU00881"
FT ACT_SITE 664
FT /evidence="ECO:0000256|PIRSR:PIRSR602662-1,
FT ECO:0000256|PROSITE-ProRule:PRU00881"
SQ SEQUENCE 979 AA; 106766 MW; 6770D91B25B6D63A CRC64;
MSNEYLRSIL MPERGPSSIP DDNVRRHCVR QETITANIVV GSSGKGAFVL FPNNPSSLIG
AHFKYDDQGK SYKYTQSLVV AQRLNESYNY GRKSAGVIYI RSSTLPSGVY NISGTINAAT
YEGPPSEVGL PEYNKILSIT SNPMDKLGNV GVLEGVAVLT LPASYDIDYT RLADLSPSSA
KNGCVVNDSG QSLIYTQYDE INYTGSQEKQ LLSFNIDSNI LVTTTATLDF YTTASDAQVT
IKIKYLGIDG LVVSENEIIS RIDSLERTVS IDAFYPFPQV IKEGGQEPVA AVELYLTSDK
STSITGTIRS ITTAHSAARP GITSPTTIVA YEGVQSGASI TVAGVSNYEL IPNPELARNM
ETRYARTDPY GMIYTKYVLA NRDRLGIRSV WPTNDYKARF PLFEELGLMQ SDASITEAMA
FGIHDVISWI RGLVPAASDW ANRMLPGSGD VIKGINRTAG HLLYGEAASG RLIAQSASGS
LIGQLGHRDA LACDVDPTLM GHNAAQLICY NTALGVRSTG NRIYMIRLKT PKRNPRVTIF
PALVFNTTPL GPEVSGTQLY AVIEGLYNQV PQSRFKVTGK NGRTIYGIKP GAYIPPGPNC
TVVPISSITQ NEITTTATPP IPRGGSMEAA LALLQYIPPG VTPFAVTGNV IEGKIVPNKW
ADLKREGMKG TGIPLVTDQD YKTIKDLAKA TEMLQRITTA QHPAVIGTIA SAMDYDDFPP
PPPPVTDENI METLEDLLVA AADRDPRMAK LKDVVLWLAK IDNNNPGVLD TLHNFSRQDV
EGEKMNRIVQ NSLTTAVHNR GPTQEVLQHQ KAVRIRENYL NQGVDLSIEW IKNNGFRGPS
ADQMKTIKAG LEPPPDTTTK SPTPHNDTST PALVMKIIKN SLGIHYDNAS PETQKEINER
ITTMVINNGN RGLNQYQAKE IVQDYGKTKK SAQMNLRYVG PRKIGYTPPS ANQVVDVPPP
ENTRDVYRTT YSAGYPPMC
//
