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 03-AUG-2022, entry version 76.
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 PDB; 6SHW; X-ray; 2.00 A; A=724-1032.
DR PDB; 6SI6; X-ray; 1.98 A; A/B=725-1032.
DR PDBsum; 6SHW; -.
DR PDBsum; 6SI6; -.
DR SMR; Q96724; -.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host cytoplasm; Hydrolase; Metal-binding;
KW Protease; Reference proteome; Serine protease;
KW T=13 icosahedral capsid protein; 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 986..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 BINDING 23
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between trimeric 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"
FT HELIX 769..782
FT /evidence="ECO:0007829|PDB:6SI6"
FT HELIX 784..795
FT /evidence="ECO:0007829|PDB:6SI6"
FT HELIX 799..812
FT /evidence="ECO:0007829|PDB:6SI6"
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
