GenomeNet

Database: UniProt
Entry: POLS_BSNV
LinkDB: POLS_BSNV
Original site: POLS_BSNV 
ID   POLS_BSNV               Reviewed;        1069 AA.
AC   Q8AZM0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   02-DEC-2020, 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=Structural peptide 4;
DE              Short=p4;
DE   Contains:
DE     RecName: Full=Protein X;
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   Blotched snakehead virus (BSNV) (Channa lucius virus).
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Blosnavirus.
OX   NCBI_TaxID=311176;
OH   NCBI_TaxID=64146; Channa lucius (Forest snakehead) (Ophicephalus lucius).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 418-442; 475-486;
RP   558-564 AND 792-798, ACTIVE SITES, PROTEOLYTIC PROCESSING OF POLYPROTEIN,
RP   AND MUTAGENESIS OF SER-692 AND LYS-729.
RX   PubMed=12477876; DOI=10.1128/jvi.77.1.719-725.2003;
RA   Da Costa B., Soignier S., Chevalier C., Henry C., Thory C., Huet J.-C.,
RA   Delmas B.;
RT   "Blotched snakehead virus is a new aquatic birnavirus that is slightly more
RT   related to avibirnavirus than to aquabirnavirus.";
RL   J. Virol. 77:719-725(2003).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 558-773.
RX   PubMed=16584747; DOI=10.1016/j.jmb.2006.02.045;
RA   Feldman A.R., Lee J., Delmas B., Paetzel M.;
RT   "Crystal structure of a novel viral protease with a serine/lysine catalytic
RT   dyad mechanism.";
RL   J. Mol. Biol. 358:1378-1389(2006).
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   -!- FUNCTION: Structural peptide 4 is a small peptide derived from pre-VP2
CC       C-terminus. It is essential for the virus viability (By similarity).
CC       {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   -!- SUBCELLULAR LOCATION: [Structural peptide 4]: 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}.
CC   -!- PTM: The N-termini of VP2 and VP3 are blocked.
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; AJ459382; CAD30689.1; -; Genomic_RNA.
DR   RefSeq; YP_052862.1; NC_005982.1.
DR   PDB; 2GEF; X-ray; 2.20 A; A/B=558-773.
DR   PDBsum; 2GEF; -.
DR   SMR; Q8AZM0; -.
DR   MEROPS; S50.004; -.
DR   GeneID; 2943237; -.
DR   KEGG; vg:2943237; -.
DR   BRENDA; 3.4.21.115; 8705.
DR   EvolutionaryTrace; Q8AZM0; -.
DR   Proteomes; UP000007250; 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; 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   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Direct protein sequencing; Host cytoplasm;
KW   Hydrolase; Metal-binding; Protease; Reference proteome; Serine protease;
KW   T=13 icosahedral capsid protein; Virion.
FT   CHAIN           1..1069
FT                   /note="Structural polyprotein"
FT                   /id="PRO_0000392582"
FT   CHAIN           1..486
FT                   /note="Precursor of VP2"
FT                   /id="PRO_0000392583"
FT   CHAIN           1..417
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000227865"
FT   PEPTIDE         418..460
FT                   /note="Structural peptide 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000227866"
FT   PEPTIDE         461..467
FT                   /note="Structural peptide 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000227867"
FT   PEPTIDE         468..474
FT                   /note="Structural peptide 3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000227868"
FT   PEPTIDE         475..486
FT                   /note="Structural peptide 4"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000227869"
FT   CHAIN           487..557
FT                   /note="Protein X"
FT                   /id="PRO_0000227870"
FT   CHAIN           558..791
FT                   /note="Protease VP4"
FT                   /id="PRO_0000227871"
FT   CHAIN           792..1069
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000227872"
FT   DOMAIN          558..791
FT                   /note="Peptidase S50"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        692
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881,
FT                   ECO:0000269|PubMed:12477876"
FT   ACT_SITE        729
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881,
FT                   ECO:0000269|PubMed:12477876"
FT   METAL           28
FT                   /note="Divalent metal cation; shared with trimeric
FT                   partners"
FT                   /evidence="ECO:0000250"
FT   SITE            417..418
FT                   /note="Cleavage; by protease VP4"
FT   SITE            460..461
FT                   /note="Cleavage; by protease VP4"
FT                   /evidence="ECO:0000250"
FT   SITE            467..468
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            486..487
FT                   /note="Cleavage; by protease VP4"
FT   SITE            557..558
FT                   /note="Cleavage; by protease VP4"
FT   SITE            791..792
FT                   /note="Cleavage; by protease VP4"
FT   MUTAGEN         692
FT                   /note="S->A: Complete loss of polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:12477876"
FT   MUTAGEN         729
FT                   /note="K->A: Complete loss of polyprotein processing."
FT                   /evidence="ECO:0000269|PubMed:12477876"
FT   STRAND          562..571
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          576..585
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          587..594
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          599..609
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   HELIX           612..614
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   HELIX           617..620
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          623..625
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          631..633
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          660..670
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          676..682
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          688..691
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   HELIX           694..702
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          708..712
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          714..716
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          719..721
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   HELIX           726..734
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   TURN            735..737
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          740..742
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   STRAND          749..752
FT                   /evidence="ECO:0000244|PDB:2GEF"
FT   HELIX           756..765
FT                   /evidence="ECO:0000244|PDB:2GEF"
SQ   SEQUENCE   1069 AA;  115494 MW;  93F308D387DCB091 CRC64;
     MDFSKENTQI RYLNSLLVPE TGSTSIPDDT LDRHCLKTET TTENLVAALG GSGLIVLFPN
     SPSGLLGAHY TKTPQGSLIF DKAITTSQDL KKAYNYARLV SRIVQVRSST LPAGVYALNG
     TFNGVTYIGS LSEIKDLDYN SLLSATANIN DKVGNVLVGD GVAVLSLPAG SDLPYVRLGD
     EVPSSAGVAR CSPSDRPRHY NANNKQVQVG TTDTKTNGFN IDATTPTEVT VDMQIAQIAA
     GKTLTVTVKL MGLTGAKVAS RSETVSGNGG TFHFSTTAVF GETEITQPVV GVQVLAKTNG
     DPIVVDSYVG VTVHGGNMPG TLRPVTIIAY ESVATGSVLT LSGISNYELI PNPELAKNIQ
     TSYGKLNPAE MTYTKVVLSH RDELGLRSIW SIPQYRDMMS YFREVSDRSS PLKIAGAFGW
     GDLLSGIRKW VFPVVDTLLP AARPLTDLAS GWIKNKYPEA ASGRPLAASG RPMAASGTFS
     KRIPLASSDE IDYQSVLALT IPGTHPKLVP PTEREPNSTP DGHKITGAKT KDNTGGDVTV
     VKPLDWLFKL PCLRPQAADL PISLLQTLAY KQPLGRNSRI VHFTDGALFP VVAFGDNHST
     SELYIAVRGD HRDLMSPDVR DSYALTGDDH KVWGATHHTY YVEGAPKKPL KFNVKTRTDL
     TILPVADVFW RADGSADVDV VWNDMPAVAG QSSSIALALA SSLPFVPKAA YTGCLSGTNV
     QPVQFGNLKA RAAHKIGLPL VGMTQDGGED TRICTLDDAA DHAFDSMEST VTRPESVGHQ
     AAFQGWFYCG AADEETIEEL EDFLDSIELH SKPTVEQPQT EEAMELLMEL ARKDPQMSKI
     LVILGWVEGA GLIDALYNWA QLDDGGVRMR NMLRNLPHEG SKSQRRKHGP APESRESTRM
     EVLRREAAAK RKKAQRISED AMDNGFEFAT IDWVLENGSR GPNPAQAKYY KATGLDPEPG
     LTEFLPEPTH APENKAAKLA ATIYGSPNQA PAPPEFVEEV AAVLMENNGR GPNQAQMREL
     RLKALTMKSG SGAAATFKPR NRRPAQEYQP RPPITSRAGR FLNISTTLS
//
DBGET integrated database retrieval system