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Database: UniProt
Entry: POLS_DXV96
LinkDB: POLS_DXV96
Original site: POLS_DXV96 
ID   POLS_DXV96              Reviewed;        1032 AA.
AC   Q96724;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-DEC-2020, entry version 73.
DE   RecName: Full=Structural polyprotein;
DE            Short=PP;
DE   Contains:
DE     RecName: Full=Precursor of VP2;
DE              Short=pre-VP2;
DE   Contains:
DE     RecName: Full=Capsid protein VP2;
DE   Contains:
DE     RecName: Full=Structural peptide 1;
DE              Short=p1;
DE   Contains:
DE     RecName: Full=Structural peptide 2;
DE              Short=p2;
DE   Contains:
DE     RecName: Full=Structural peptide 3;
DE              Short=p3;
DE   Contains:
DE     RecName: Full=Protease VP4;
DE              EC=3.4.21.-;
DE     AltName: Full=Non-structural protein VP4;
DE              Short=NS;
DE   Contains:
DE     RecName: Full=Capsid protein VP3;
OS   Drosophila x virus (isolate Chung/1996) (DXV).
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Entomobirnavirus.
OX   NCBI_TaxID=654931;
OH   NCBI_TaxID=7227; Drosophila melanogaster (Fruit fly).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8918922; DOI=10.1006/viro.1996.0610;
RA   Chung H.K., Kordyban S., Cameron L., Dobos P.;
RT   "Sequence analysis of the bicistronic Drosophila X virus genome segment A
RT   and its encoded polypeptides.";
RL   Virology 225:359-368(1996).
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 (By similarity).
CC       {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU00881}.
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Capsid protein VP2 is a homotrimer. A central divalent metal
CC       stabilizes the VP2 trimer (By similarity). Capsid protein VP3 is a
CC       homodimer. Capsid protein VP3 interacts (via C-terminus) with VP1 in
CC       the cytoplasm. Capsid VP3 interacts with VP2 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000305}. Host
CC       cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000305}. Host
CC       cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Structural peptide 1]: Virion {ECO:0000305}.
CC       Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Structural peptide 2]: Virion {ECO:0000305}.
CC       Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Structural peptide 3]: Virion {ECO:0000305}.
CC       Host cytoplasm {ECO:0000305}.
CC   -!- PTM: Specific enzymatic cleavages yield mature proteins. The capsid
CC       assembly seems to be regulated by polyprotein processing. The protease
CC       VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3
CC       within the infected cell. During capsid assembly, the C-terminus of
CC       pre-VP2 is further processed by VP4, giving rise to VP2, the external
CC       capsid protein and three small peptides that all stay closely
CC       associated with the capsid (By similarity). {ECO:0000250}.
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DR   EMBL; U60650; AAB16798.1; -; Genomic_RNA.
DR   RefSeq; NP_690836.1; NC_004177.1.
DR   MEROPS; S50.003; -.
DR   PRIDE; Q96724; -.
DR   GeneID; 993338; -.
DR   KEGG; vg:993338; -.
DR   Proteomes; UP000000515; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0039621; C:T=13 icosahedral 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-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR002662; Birna_VP2.
DR   InterPro; IPR002663; Birna_VP3.
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   3: Inferred from homology;
KW   Capsid protein; Host cytoplasm; Hydrolase; Metal-binding; Protease;
KW   Reference proteome; Serine protease; T=13 icosahedral capsid protein;
KW   Virion.
FT   CHAIN           1..1032
FT                   /note="Structural polyprotein"
FT                   /id="PRO_0000378376"
FT   CHAIN           1..500
FT                   /note="Precursor of VP2"
FT                   /id="PRO_0000378377"
FT   CHAIN           1..431
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000378378"
FT   PEPTIDE         431..474
FT                   /note="Structural peptide 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000378379"
FT   PEPTIDE         475..483
FT                   /note="Structural peptide 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000378380"
FT   PEPTIDE         484..500
FT                   /note="Structural peptide 3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000378381"
FT   CHAIN           501..723
FT                   /note="Protease VP4"
FT                   /id="PRO_0000378382"
FT   CHAIN           724..1032
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000378383"
FT   DOMAIN          501..723
FT                   /note="Peptidase S50"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT   REGION          1021..1030
FT                   /note="Interaction with VP1 protein"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        627
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        670
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT   METAL           23
FT                   /note="Divalent metal cation; shared with trimeric
FT                   partners"
FT                   /evidence="ECO:0000250"
FT   SITE            431..432
FT                   /note="Cleavage; by protease VP4"
FT                   /evidence="ECO:0000250"
FT   SITE            474..475
FT                   /note="Cleavage; by protease VP4"
FT                   /evidence="ECO:0000250"
FT   SITE            483..484
FT                   /note="Cleavage; by protease VP4"
FT                   /evidence="ECO:0000250"
FT   SITE            500..501
FT                   /note="Cleavage; by protease VP4"
FT                   /evidence="ECO:0000250"
FT   SITE            723..724
FT                   /note="Cleavage; by protease VP4"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1032 AA;  114028 MW;  44F5CB82FE191CFB CRC64;
     MNTTNEYLKT LLNPAQFISD IPDDIMIRHV NSAQTITYNL KSGASGTGLI VVYPNTPSSI
     SGFHYIWDSA TSNWVFDQYI YTAQELKDSY DYGRLISGSL SIKSSTLPAG VYALNGTFNA
     VWFQGTLSEV SDYSYDRILS ITSNPLDKVG NVLVGDGIEV LSLPQGFNNP YVRLGDKSPS
     TLSSPTHITN TSQNLATGGA YMIPVTTVPG QGFHNKEFSI NVDSVGPVDI LWSGQMTMQD
     EWTVTANYQP LNISGTLIAN SQRTLTWSNT GVSNGSHYMN MNNLNVSLFH ENPPPEPVAA
     IKININYGNN TNGDSSFSVD SSFTINVIGG ATIGVNSPTV GVGYQGVAEG TAITISGINN
     YELVPNPDLQ KNLPMTYGTC DPHDLTYIKY ILSNREQLGL RSVMTLADYN RMKMYMHVLT
     NYHVDEREAS SFDFWQLLKQ IKNVAVPLAA TLAPQFAPII GAADGLANAI LGDSASGRPV
     GNSASGMPIS MSRRLRNAYS ADSPLGEEHW LPNENENFNK FDIIYDVSHS SMALFPVIMM
     EHDKVIPSDP EELYIAVSLT ESLRKQIPNL NDMPYYEMGG HRVYNSVSSN VRSGNFLRSD
     YILLPCYQLL EGRLASSTSP NKVTGTSHQL AIYAADDLLK SGVLGKAPFA AFTGSVVGSS
     VGEVFGINLK LQLTDSLGIP LLGNSPGLVQ VKTLTSLDKK IKDMGDVKRR TPKQTLPHWT
     AGSASMNPFM NTNPFLEELD QPIPSNAAKP ISEETRDLFL SDGQTIPSSQ EKIATIHEYL
     LEHKELEEAM FSLISQGRGR SLINMVVKSA LNIETQSREV TGERRQRLER KLRNLENQGI
     YVDESKIMSR GRISKEDTEL AMRIARKNQK DAKLRRIYSN NASIQESYTV DDFVSYWMEQ
     ESLPTGIQIA MWLKGDDWSQ PIPPRVQRRH YDSYIMMLGP SPTQEQADAV KDLVDDIYDR
     NQGKGPSQEQ ARELSHAVRR LISHSLVNQP ATAPRVPPRR IVSAQTAQTD PPGRRAALDR
     LRRVRGEDND IV
//
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