UniProtKB - Q8AZM0 (POLS_BSNV)
Protein
Structural polyprotein
Gene
N/A
Organism
Blotched snakehead virus (BSNV) (Channa lucius virus)
Status
Functioni
Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell (By similarity).By similarity
The precursor of VP2 plays an important role in capsid assembly. First, pre-VP2 and VP2 oligomers assemble to form a procapsid. Then, the pre-VP2 intermediates may be processed into VP2 proteins by proteolytic cleavage mediated by VP4 to obtain the mature virion. The final capsid is composed of pentamers and hexamers but VP2 has a natural tendency to assemble into all-pentameric structures. Therefore pre-VP2 may be required to allow formation of the hexameric structures (By similarity).By similarity
Protease VP4 is a serine protease that cleaves the polyprotein into its final products. Pre-VP2 is first partially cleaved, and may be completely processed by VP4 upon capsid maturation.PROSITE-ProRule annotation
Capsid protein VP3 plays a key role in virion assembly by providing a scaffold for the capsid made of VP2. May self-assemble to form a T=4-like icosahedral inner-capsid composed of at least 180 trimers. Plays a role in genomic RNA packaging by recruiting VP1 into the capsid and interacting with the dsRNA genome segments to form a ribonucleoprotein complex. Additionally, the interaction of the VP3 C-terminal tail with VP1 removes the inherent structural blockade of the polymerase active site. Thus, VP3 can also function as a transcriptional activator (By similarity).By similarity
Structural peptide 1 is a small peptide derived from pre-VP2 C-terminus. It destabilizes and perforates cell membranes, suggesting a role during entry (By similarity).By similarity
Structural peptide 2 is a small peptide derived from pre-VP2 C-terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity).By similarity
Structural peptide 3 is a small peptide derived from pre-VP2 C-terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity).By similarity
Structural peptide 4 is a small peptide derived from pre-VP2 C-terminus. It is essential for the virus viability (By similarity).By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 28 | Divalent metal cation; shared with trimeric partnersBy similarity | 1 | |
Active sitei | 692 | NucleophilePROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 729 | PROSITE-ProRule annotation1 Publication | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- serine-type peptidase activity Source: UniProtKB-KW
- structural molecule activity Source: InterPro
Keywordsi
Molecular function | Hydrolase, Protease, Serine protease |
Ligand | Metal-binding |
Enzyme and pathway databases
BRENDAi | 3.4.21.115, 8705 |
Protein family/group databases
MEROPSi | S50.004 |
Names & Taxonomyi
Protein namesi | Recommended name: Structural polyproteinShort name: PP Cleaved into the following 9 chains: Protease VP4 (EC:3.4.21.-) Alternative name(s): Non-structural protein VP4 Short name: NS |
Organismi | Blotched snakehead virus (BSNV) (Channa lucius virus) |
Taxonomic identifieri | 311176 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Birnaviridae › Blosnavirus |
Virus hosti | Channa lucius (Forest snakehead) (Ophicephalus lucius) [TaxID: 64146] |
Proteomesi |
|
Subcellular locationi
- Virion Curated
- Host cytoplasm Curated
- Virion Curated
- Host cytoplasm Curated
- Virion Curated
- Host cytoplasm Curated
- Virion Curated
- Host cytoplasm Curated
- Virion Curated
- Host cytoplasm Curated
- Virion Curated
- Host cytoplasm Curated
GO - Cellular componenti
- host cell cytoplasm Source: UniProtKB-SubCell
- T=13 icosahedral viral capsid Source: UniProtKB-KW
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, T=13 icosahedral capsid protein, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 692 | S → A: Complete loss of polyprotein processing. 1 Publication | 1 | |
Mutagenesisi | 729 | K → A: Complete loss of polyprotein processing. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000392582 | 1 – 1069 | Structural polyproteinAdd BLAST | 1069 | |
ChainiPRO_0000392583 | 1 – 486 | Precursor of VP2Add BLAST | 486 | |
ChainiPRO_0000227865 | 1 – 417 | Capsid protein VP2Add BLAST | 417 | |
PeptideiPRO_0000227866 | 418 – 460 | Structural peptide 1By similarityAdd BLAST | 43 | |
PeptideiPRO_0000227867 | 461 – 467 | Structural peptide 2By similarity | 7 | |
PeptideiPRO_0000227868 | 468 – 474 | Structural peptide 3By similarity | 7 | |
PeptideiPRO_0000227869 | 475 – 486 | Structural peptide 4By similarityAdd BLAST | 12 | |
ChainiPRO_0000227870 | 487 – 557 | Protein XAdd BLAST | 71 | |
ChainiPRO_0000227871 | 558 – 791 | Protease VP4Add BLAST | 234 | |
ChainiPRO_0000227872 | 792 – 1069 | Capsid protein VP3Add BLAST | 278 |
Post-translational modificationi
Specific enzymatic cleavages yield mature proteins. The capsid assembly seems to be regulated by polyprotein processing. The protease VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3 within the infected cell. During capsid assembly, the C-terminus of pre-VP2 is further processed by VP4, giving rise to VP2, the external capsid protein and three small peptides that all stay closely associated with the capsid (By similarity).By similarity
The N-termini of VP2 and VP3 are blocked.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 417 – 418 | Cleavage; by protease VP4 | 2 | |
Sitei | 460 – 461 | Cleavage; by protease VP4By similarity | 2 | |
Sitei | 467 – 468 | Cleavage; by protease VP4By similarity | 2 | |
Sitei | 474 – 475 | Cleavage; by protease VP4By similarity | 2 | |
Sitei | 486 – 487 | Cleavage; by protease VP4 | 2 | |
Sitei | 557 – 558 | Cleavage; by protease VP4 | 2 | |
Sitei | 791 – 792 | Cleavage; by protease VP4 | 2 |
Interactioni
Subunit structurei
Capsid protein VP2 is a homotrimer. A central divalent metal stabilizes the VP2 trimer (By similarity). Capsid protein VP3 is a homodimer. Capsid protein VP3 interacts (via C-terminus) with VP1 in the cytoplasm. Capsid VP3 interacts with VP2 (By similarity).
By similarityStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q8AZM0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q8AZM0 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 558 – 791 | Peptidase S50PROSITE-ProRule annotationAdd BLAST | 234 |
Family and domain databases
Gene3Di | 1.10.150.620, 1 hit 1.10.8.880, 1 hit 2.60.120.20, 1 hit |
InterProi | View protein in InterPro IPR002662, Birna_VP2 IPR002663, Birna_VP3 IPR043048, Birna_VP3_dom1 IPR043049, Birna_VP3_dom2 IPR025775, Birna_VP4_Prtase_dom IPR029053, Viral_coat |
Pfami | View protein in Pfam PF01766, Birna_VP2, 1 hit PF01767, Birna_VP3, 1 hit PF01768, Birna_VP4, 1 hit |
PROSITEi | View protein in PROSITE PS51548, BIRNAVIRUS_VP4_PRO, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q8AZM0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDFSKENTQI RYLNSLLVPE TGSTSIPDDT LDRHCLKTET TTENLVAALG
60 70 80 90 100
GSGLIVLFPN SPSGLLGAHY TKTPQGSLIF DKAITTSQDL KKAYNYARLV
110 120 130 140 150
SRIVQVRSST LPAGVYALNG TFNGVTYIGS LSEIKDLDYN SLLSATANIN
160 170 180 190 200
DKVGNVLVGD GVAVLSLPAG SDLPYVRLGD EVPSSAGVAR CSPSDRPRHY
210 220 230 240 250
NANNKQVQVG TTDTKTNGFN IDATTPTEVT VDMQIAQIAA GKTLTVTVKL
260 270 280 290 300
MGLTGAKVAS RSETVSGNGG TFHFSTTAVF GETEITQPVV GVQVLAKTNG
310 320 330 340 350
DPIVVDSYVG VTVHGGNMPG TLRPVTIIAY ESVATGSVLT LSGISNYELI
360 370 380 390 400
PNPELAKNIQ TSYGKLNPAE MTYTKVVLSH RDELGLRSIW SIPQYRDMMS
410 420 430 440 450
YFREVSDRSS PLKIAGAFGW GDLLSGIRKW VFPVVDTLLP AARPLTDLAS
460 470 480 490 500
GWIKNKYPEA ASGRPLAASG RPMAASGTFS KRIPLASSDE IDYQSVLALT
510 520 530 540 550
IPGTHPKLVP PTEREPNSTP DGHKITGAKT KDNTGGDVTV VKPLDWLFKL
560 570 580 590 600
PCLRPQAADL PISLLQTLAY KQPLGRNSRI VHFTDGALFP VVAFGDNHST
610 620 630 640 650
SELYIAVRGD HRDLMSPDVR DSYALTGDDH KVWGATHHTY YVEGAPKKPL
660 670 680 690 700
KFNVKTRTDL TILPVADVFW RADGSADVDV VWNDMPAVAG QSSSIALALA
710 720 730 740 750
SSLPFVPKAA YTGCLSGTNV QPVQFGNLKA RAAHKIGLPL VGMTQDGGED
760 770 780 790 800
TRICTLDDAA DHAFDSMEST VTRPESVGHQ AAFQGWFYCG AADEETIEEL
810 820 830 840 850
EDFLDSIELH SKPTVEQPQT EEAMELLMEL ARKDPQMSKI LVILGWVEGA
860 870 880 890 900
GLIDALYNWA QLDDGGVRMR NMLRNLPHEG SKSQRRKHGP APESRESTRM
910 920 930 940 950
EVLRREAAAK RKKAQRISED AMDNGFEFAT IDWVLENGSR GPNPAQAKYY
960 970 980 990 1000
KATGLDPEPG LTEFLPEPTH APENKAAKLA ATIYGSPNQA PAPPEFVEEV
1010 1020 1030 1040 1050
AAVLMENNGR GPNQAQMREL RLKALTMKSG SGAAATFKPR NRRPAQEYQP
1060
RPPITSRAGR FLNISTTLS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ459382 Genomic RNA Translation: CAD30689.1 |
RefSeqi | YP_052862.1, NC_005982.1 |
Genome annotation databases
GeneIDi | 2943237 |
KEGGi | vg:2943237 |
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ459382 Genomic RNA Translation: CAD30689.1 |
RefSeqi | YP_052862.1, NC_005982.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2GEF | X-ray | 2.20 | A/B | 558-773 | [»] | |
SMRi | Q8AZM0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
MEROPSi | S50.004 |
Genome annotation databases
GeneIDi | 2943237 |
KEGGi | vg:2943237 |
Enzyme and pathway databases
BRENDAi | 3.4.21.115, 8705 |
Miscellaneous databases
EvolutionaryTracei | Q8AZM0 |
Family and domain databases
Gene3Di | 1.10.150.620, 1 hit 1.10.8.880, 1 hit 2.60.120.20, 1 hit |
InterProi | View protein in InterPro IPR002662, Birna_VP2 IPR002663, Birna_VP3 IPR043048, Birna_VP3_dom1 IPR043049, Birna_VP3_dom2 IPR025775, Birna_VP4_Prtase_dom IPR029053, Viral_coat |
Pfami | View protein in Pfam PF01766, Birna_VP2, 1 hit PF01767, Birna_VP3, 1 hit PF01768, Birna_VP4, 1 hit |
PROSITEi | View protein in PROSITE PS51548, BIRNAVIRUS_VP4_PRO, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | POLS_BSNV | |
Accessioni | Q8AZM0Primary (citable) accession number: Q8AZM0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 21, 2006 |
Last sequence update: | March 1, 2003 | |
Last modified: | December 2, 2020 | |
This is version 76 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references