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 03-AUG-2022, entry version 79.
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.
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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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 REGION 504..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 BINDING 28
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 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:0007829|PDB:2GEF"
FT STRAND 576..585
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 587..594
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 599..609
FT /evidence="ECO:0007829|PDB:2GEF"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:2GEF"
FT HELIX 617..620
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 660..670
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 676..682
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:2GEF"
FT HELIX 694..702
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 708..712
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:2GEF"
FT HELIX 726..734
FT /evidence="ECO:0007829|PDB:2GEF"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:2GEF"
FT STRAND 749..752
FT /evidence="ECO:0007829|PDB:2GEF"
FT HELIX 756..765
FT /evidence="ECO:0007829|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
