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Q703G9

- POLS_IPNVS

UniProt

Q703G9 - POLS_IPNVS

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Protein

Structural polyprotein

Gene
N/A
Organism
Infectious pancreatic necrosis virus (strain Sp) (IPNV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 pVP2 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 pVP2 C-terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Divalent metal cation; shared with trimeric partnersBy similarity
Sitei442 – 4432Cleavage; by protease VP4
Sitei486 – 4872Cleavage; by protease VP4
Sitei495 – 4962Cleavage; by protease VP4
Sitei508 – 5092Cleavage; by protease VP4
Active sitei633 – 6331Nucleophile1 PublicationPROSITE-ProRule annotation
Active sitei674 – 67411 PublicationPROSITE-ProRule annotation
Sitei715 – 7162Cleavage; by protease VP4; subsidiary
Sitei734 – 7352Cleavage; by protease VP4

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. serine-type peptidase activity Source: UniProtKB-KW
  3. structural molecule activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiS50.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural polyprotein
Short name:
PP
Cleaved into the following 7 chains:
Precursor of VP2
Short name:
Pre-VP2
Structural peptide 1
Short name:
p1
Structural peptide 2
Short name:
p2
Structural peptide 3
Short name:
p3
Alternative name(s):
Non-structural protein VP4
Short name:
NS
OrganismiInfectious pancreatic necrosis virus (strain Sp) (IPNV)
Taxonomic identifieri11005 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesBirnaviridaeAquabirnavirus
Virus hostiOncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) [TaxID: 8022]
Salmo [TaxID: 8028]
ProteomesiUP000007213: Genome

Subcellular locationi

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. virion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi508 – 5092AS → QL: Complete loss of pVP2-VP4 cleavage. 1 Publication
Mutagenesisi547 – 5471H → S: Strongly reduced VP4-VP3 cleavage. No effect on pVP2-VP4 cleavage. 1 Publication
Mutagenesisi573 – 5731D → Q: No effect on polyprotein processing. 1 Publication
Mutagenesisi585 – 5851D → I: No effect on polyprotein processing. 1 Publication
Mutagenesisi595 – 5951D → L: No effect on polyprotein processing. 1 Publication
Mutagenesisi601 – 6011D → S: No effect on polyprotein processing. 1 Publication
Mutagenesisi633 – 6331S → A, Q or T: Complete loss of protease activity. 1 Publication
Mutagenesisi633 – 6331S → C: Partial loss of protease activity. 1 Publication
Mutagenesisi644 – 6441D → I: No effect on polyprotein processing. 1 Publication
Mutagenesisi660 – 6612DD → GS: No effect on polyprotein processing. 1 Publication
Mutagenesisi672 – 6721D → N: No effect on polyprotein processing. 1 Publication
Mutagenesisi674 – 6741K → A, D, H, Q or R: Complete loss of protease activity. 1 Publication
Mutagenesisi675 – 6751A → D: 60% loss of pVP2-VP4 and VP4-VP3 cleavages. 1 Publication
Mutagenesisi676 – 6761I → A: No effect on polyprotein processing. 1 Publication
Mutagenesisi677 – 6771A → D: 60% loss of pVP2-VP4. Complete loss of VP4-VP3 cleavage. 1 Publication
Mutagenesisi678 – 6781A → S: No effect on polyprotein processing. 1 Publication
Mutagenesisi679 – 6791H → L: Strongly reduced VP4-VP3 cleavage. No effect on pVP2-VP4 cleavage. 1 Publication
Mutagenesisi680 – 6801E → M: No effect on polyprotein processing. 1 Publication
Mutagenesisi682 – 6821G → L: No effect on polyprotein processing. 1 Publication
Mutagenesisi683 – 6831L → A: 60% loss of pVP2-VP4 and VP4-VP3 cleavages. 1 Publication
Mutagenesisi684 – 6841P → Q: No effect on polyprotein processing. 1 Publication
Mutagenesisi685 – 6851L → A: 60% loss of pVP2-VP4 and VP4-VP3 cleavages. 1 Publication
Mutagenesisi686 – 6861I → A: 20% loss of pVP2-VP4 and VP4-VP3 cleavages. 1 Publication
Mutagenesisi687 – 6871G → A: 20% loss of pVP2-VP4 and VP4-VP3 cleavages. 1 Publication
Mutagenesisi689 – 6891Q → I: No effect on polyprotein processing. 1 Publication
Mutagenesisi693 – 6931D → L: Strongly reduced VP4-VP3 cleavage. No effect on pVP2-VP4 cleavage. 1 Publication
Mutagenesisi704 – 7041H → S: No effect on polyprotein processing. 1 Publication
Mutagenesisi734 – 7352AS → LE: Complete loss of VP4-VP3 cleavage. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Precursor of VP2PRO_0000392599Add
BLAST
Chaini1 – 442442Capsid protein VP2PRO_0000227873Add
BLAST
Peptidei443 – 48644Structural peptide 11 PublicationPRO_0000227874Add
BLAST
Peptidei487 – 4959Structural peptide 21 PublicationPRO_0000227875
Peptidei496 – 50813Structural peptide 31 PublicationPRO_0000227876Add
BLAST
Chaini509 – 734226Protease VP4PRO_0000227877Add
BLAST
Chaini735 – 972238Capsid protein VP3PRO_0000227878Add
BLAST

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

Interactioni

Subunit structurei

Capsid protein VP2 is a homotrimer. A central divalent metal stabilizes the VP2 trimer, possibly cobalt (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 similarity

Structurei

Secondary structure

1
972
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 157Combined sources
Helixi17 – 193Combined sources
Beta strandi32 – 4413Combined sources
Beta strandi51 – 555Combined sources
Beta strandi60 – 7011Combined sources
Beta strandi74 – 8411Combined sources
Helixi89 – 913Combined sources
Beta strandi93 – 10715Combined sources
Beta strandi120 – 1289Combined sources
Helixi130 – 1323Combined sources
Helixi140 – 1434Combined sources
Helixi148 – 1503Combined sources
Beta strandi151 – 1566Combined sources
Turni157 – 1593Combined sources
Beta strandi161 – 1644Combined sources
Beta strandi202 – 2087Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi223 – 23210Combined sources
Beta strandi236 – 24813Combined sources
Beta strandi254 – 26310Combined sources
Beta strandi271 – 28010Combined sources
Turni282 – 2865Combined sources
Beta strandi287 – 2926Combined sources
Helixi298 – 3003Combined sources
Beta strandi305 – 3139Combined sources
Helixi317 – 3193Combined sources
Beta strandi324 – 3263Combined sources
Helixi327 – 3293Combined sources
Beta strandi332 – 3387Combined sources
Turni339 – 3424Combined sources
Turni344 – 3463Combined sources
Beta strandi350 – 3578Combined sources
Beta strandi363 – 37614Combined sources
Helixi378 – 3814Combined sources
Helixi395 – 40410Combined sources
Turni405 – 4106Combined sources
Beta strandi413 – 4164Combined sources
Helixi417 – 4226Combined sources
Helixi425 – 4273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PNLX-ray2.21A/B/C/D/E/F/G/H/I/J514-716[»]
2PNMX-ray2.30A524-716[»]
3IDEX-ray3.35A/B/C/D/E1-442[»]
ProteinModelPortaliQ703G9.
SMRiQ703G9. Positions 514-716.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ703G9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini509 – 734226Peptidase S50PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 peptidase S50 domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.60.120.20. 2 hits.
InterProiIPR002662. Birna_VP2.
IPR002663. Birna_VP3.
IPR025775. Birna_VP4_Prtase_dom.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF01766. Birna_VP2. 1 hit.
PF01767. Birna_VP3. 1 hit.
PF01768. Birna_VP4. 1 hit.
[Graphical view]
PROSITEiPS51548. BIRNAVIRUS_VP4_PRO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q703G9-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MNTNKATATY LKSIMLPETG PASIPDDITE RHILKQETSS YNLEVSESGS
60 70 80 90 100
GVLVCFPGAP GSRIGAHYRW NANQTGLEFD QWLETSQDLK KAFNYGRLIS
110 120 130 140 150
RKYDIQSSTL PAGLYALNGT LNAATFEGSL SEVESLTYNS LMSLTTNPQD
160 170 180 190 200
KVNNQLVTKG VTVLNLPTGF DKPYVRLEDE TPQGLQSMNG AKMRCTAAIA
210 220 230 240 250
PRRYEIDLPS QRLPPVPATG TLTTLYEGNA DIVNSTTVTG DINFSLAEQP
260 270 280 290 300
ADETKFDFQL DFMGLDNDVP VVTVVSSVLA TNDNYRGVSA KMTQSIPTEN
310 320 330 340 350
ITKPITRVKL SYKINQQTAI GNVATLGTMG PASVSFSSGN GNVPGVLRPI
360 370 380 390 400
TLVAYEKMTP LSILTVAGVS NYELIPNPEL LKNMVTRYGK YDPEGLNYAK
410 420 430 440 450
MILSHREELD IRTVWRTEEY KERTRVFNEI TDFSSDLPTS KAWGWRDIVR
460 470 480 490 500
GIRKVAAPVL STLFPMAAPL IGMADQFIGD LTKTNAAGGR YHSMAAGGRY
510 520 530 540 550
KDVLESWASG GPDGKFSRAL KNRLESANYE EVELPPPSKG VIVPVVHTVK
560 570 580 590 600
SAPGEAFGSL AIIIPGEYPE LLDANQQVLS HFANDTGSVW GIGEDIPFEG
610 620 630 640 650
DNMCYTALPL KEIKRNGNIV VEKIFAGPIM GPSAQLGLSL LVNDIEDGVP
660 670 680 690 700
RMVFTGEIAD DEETIIPICG VDIKAIAAHE QGLPLIGNQP GVDEEVRNTS
710 720 730 740 750
LAAHLIQTGT LPVQRAKGSN KRIKYLGELM ASNASGMDEE LQRLLNATMA
760 770 780 790 800
RAKEVQDAEI YKLLKLMAWT RKNDLTDHMY EWSKEDPDAL KFGKLISTPP
810 820 830 840 850
KHPEKPKGPD QHHAQEARAT RISLDAVRAG ADFATPEWVA LNNYRGPSPG
860 870 880 890 900
QFKYYLITGR EPEPGDEYED YIKQPIVKPT DMNKIRRLAN SVYGLPHQEP
910 920 930 940 950
APEEFYDAVA AVFAQNGGRG PDQDQMQDLR ELARQMKRRP RNADAPRRTR
960 970
APAEPAPPGR SRFTPSGDNA EV
Length:972
Mass (Da):106,646
Last modified:July 5, 2004 - v1
Checksum:i7B1448E99800E3C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti883 – 8831N → Y in AAR10446. (PubMed:15584407)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361Q → P in strain: Isolate Mason.
Natural varianti46 – 461S → P in strain: Isolate Mason.
Natural varianti52 – 521V → I in strain: Isolate Mason, Isolate Tseng, Isolate Blake, Isolate Sp103, Isolate Sp116, Isolate Sp122, Isolate NVI-001, Isolate NVI-011, Isolate NVI-013, Isolate NVI-015, Isolate NVI-016, Isolate NVI-020 and NVI-023.
Natural varianti54 – 541V → I in strain: Isolate NVI-010.
Natural varianti82 – 854WLET → CWRA in strain: Isolate Mason.
Natural varianti152 – 1521V → A in strain: Isolate Mason, Isolate Blake and Isolate Tseng.
Natural varianti192 – 1921K → R in strain: Isolate Mason, Isolate Blake and Isolate Tseng.
Natural varianti199 – 1991I → T in strain: Isolate Sp103 and Isolate Sp122.
Natural varianti212 – 2121R → S in strain: Isolate Mason, Isolate Blake and Isolate Tseng.
Natural varianti217 – 2171P → T in strain: Isolate Sp122, Isolate NVI-001, Isolate NVI-011, Isolate NVI-013, Isolate NVI-015, Isolate NVI-020 and Isolate NVI-023.
Natural varianti219 – 2191T → I in strain: Isolate NVI-010.
Natural varianti221 – 2211T → A in strain: Isolate NVI-001, Isolate NVI-013, Isolate NVI-015, Isolate Sp116 and Isolate NVI-023.
Natural varianti222 – 2221L → P in strain: Isolate NVI-011.
Natural varianti234 – 2341N → S in strain: Isolate Tseng.
Natural varianti247 – 2471A → T in strain: Isolate Sp122, Isolate NVI-001, Isolate NVI-013, Isolate NVI-015 and Isolate NVI-023.
Natural varianti249 – 2491Q → R in strain: Isolate Tseng.
Natural varianti252 – 2521D → N in strain: Isolate Mason, Isolate Tseng, Isolate Blake, Isolate Sp103, Isolate NVI-010 and Isolate NVI-016.
Natural varianti252 – 2521D → V in strain: Isolate NVI-001, Isolate NVI-011, Isolate NVI-013, Isolate NVI-015, Isolate NVI-020, Isolate NVI-023, Isolate Sp116 and Isolate Sp122.
Natural varianti255 – 2551K → R in strain: Isolate Mason, Isolate Blake and Isolate Tseng.
Natural varianti262 – 2621F → L in strain: Isolate Mason.
Natural varianti288 – 2881V → A in strain: Isolate Sp116.
Natural varianti319 – 3191A → E in strain: Isolate NVI-016.
Natural varianti323 – 3231V → A in strain: Isolate NVI-020.
Natural varianti323 – 3231V → F in strain: Isolate NVI-016.
Natural varianti432 – 4343DFS → EKT in strain: Isolate Mason.
Natural varianti455 – 4551V → I in strain: Isolate Mason.
Natural varianti473 – 4731M → T in strain: Isolate Mason, Isolate Heppel and Isolate Blake.
Natural varianti500 – 5001Y → H in strain: Isolate Heppel, Isolate NVI-010, Isolate NVI-011, Isolate NVI-020, Isolate Sp103 and Isolate Sp116.
Natural varianti565 – 5651P → R in strain: Isolate Mason.
Natural varianti570 – 5712EL → SF in strain: Isolate Mason.
Natural varianti672 – 6721D → A in strain: Isolate NVI-016.
Natural varianti717 – 7171K → Q in strain: Isolate NVI-016.
Natural varianti788 – 7881D → G in strain: Isolate NVI-011.
Natural varianti788 – 7881D → Y in strain: Isolate NVI-001.
Natural varianti802 – 8021H → R in strain: Isolate NVI-015 and Isolate NVI-016.
Natural varianti841 – 8411L → M in strain: Isolate NVI-016.
Natural varianti867 – 8671E → Q in strain: Isolate Mason and Isolate Blake.
Natural varianti875 – 8751P → S in strain: Isolate NVI-016.
Natural varianti882 – 8821M → T in strain: Isolate Tseng.
Natural varianti953 – 9542AE → GK in strain: Isolate Mason.
Natural varianti959 – 9602GR → DV in strain: Isolate Mason.
Natural varianti968 – 9681D → N in strain: Isolate Sp116.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ622822 Genomic RNA. Translation: CAF22217.1.
U48225 Genomic RNA. Translation: AAD11535.1.
U56907 Genomic RNA. Translation: AAB39512.1.
AY374435 Genomic RNA. Translation: AAQ75364.1.
AY379735 Genomic RNA. Translation: AAQ75348.1.
AY379736 Genomic RNA. Translation: AAQ75350.1.
AY379737 Genomic RNA. Translation: AAQ75352.1.
AY379738 Genomic RNA. Translation: AAQ75354.1.
AY379740 Genomic RNA. Translation: AAQ75357.1.
AY379742 Genomic RNA. Translation: AAQ75360.1.
AY379744 Genomic RNA. Translation: AAQ75363.1.
AY354519 Genomic RNA. Translation: AAR10446.1.
AY354520 Genomic RNA. Translation: AAR10449.1.
AY354521 Genomic RNA. Translation: AAR10452.1.
AY823632 Genomic RNA. Translation: AAX24140.1.
AF342728 mRNA. Translation: AAK32154.1.
L13988 Genomic RNA. Translation: AAB00986.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ622822 Genomic RNA. Translation: CAF22217.1 .
U48225 Genomic RNA. Translation: AAD11535.1 .
U56907 Genomic RNA. Translation: AAB39512.1 .
AY374435 Genomic RNA. Translation: AAQ75364.1 .
AY379735 Genomic RNA. Translation: AAQ75348.1 .
AY379736 Genomic RNA. Translation: AAQ75350.1 .
AY379737 Genomic RNA. Translation: AAQ75352.1 .
AY379738 Genomic RNA. Translation: AAQ75354.1 .
AY379740 Genomic RNA. Translation: AAQ75357.1 .
AY379742 Genomic RNA. Translation: AAQ75360.1 .
AY379744 Genomic RNA. Translation: AAQ75363.1 .
AY354519 Genomic RNA. Translation: AAR10446.1 .
AY354520 Genomic RNA. Translation: AAR10449.1 .
AY354521 Genomic RNA. Translation: AAR10452.1 .
AY823632 Genomic RNA. Translation: AAX24140.1 .
AF342728 mRNA. Translation: AAK32154.1 .
L13988 Genomic RNA. Translation: AAB00986.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2PNL X-ray 2.21 A/B/C/D/E/F/G/H/I/J 514-716 [» ]
2PNM X-ray 2.30 A 524-716 [» ]
3IDE X-ray 3.35 A/B/C/D/E 1-442 [» ]
ProteinModelPortali Q703G9.
SMRi Q703G9. Positions 514-716.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S50.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q703G9.

Family and domain databases

Gene3Di 2.60.120.20. 2 hits.
InterProi IPR002662. Birna_VP2.
IPR002663. Birna_VP3.
IPR025775. Birna_VP4_Prtase_dom.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF01766. Birna_VP2. 1 hit.
PF01767. Birna_VP3. 1 hit.
PF01768. Birna_VP4. 1 hit.
[Graphical view ]
PROSITEi PS51548. BIRNAVIRUS_VP4_PRO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Peptides resulting from the pVP2 C-terminal processing are present in infectious pancreatic necrosis virus particles."
    Galloux M., Chevalier C., Henry C., Huet J.-C., Da Costa B., Delmas B.
    J. Gen. Virol. 85:2231-2236(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 443-457; 487-495 AND 496-508, PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    Strain: 31-75.
  2. Mason C.L., Leong J.C.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate Mason.
  3. Tseng C.-C., Lo C.-F., Kou G.-H.
    Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate Tseng.
  4. "Identification of putative motifs involved in the virulence of infectious pancreatic necrosis virus."
    Santi N., Vakharia V.N., Evensen O.
    Virology 322:31-40(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate NVI-001, Isolate NVI-010, Isolate NVI-011, Isolate NVI-013, Isolate NVI-015, Isolate NVI-016, Isolate NVI-020 and Isolate NVI-023.
  5. "Molecular characterization of Sp serotype strains of infectious pancreatic necrosis virus exhibiting differences in virulence."
    Shivappa R.B., Song H., Yao K., Aas-Eng A., Evensen O., Vakharia V.N.
    Dis. Aquat. Organ. 61:23-32(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate Sp103, Isolate Sp116 and Isolate Sp122.
  6. "Infectious pancreatic necrosis virus VP5 is dispensable for virulence and persistence."
    Santi N., Song H., Vakharia V.N., Evensen O.
    J. Virol. 79:9206-9216(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate Sp103.
  7. "Phylogenetic relationships of aquatic birnaviruses based on deduced amino acid sequences of genome segment A cDNA."
    Blake S., Ma J.Y., Caporale D.A., Jairath S., Nicholson B.L.
    Dis. Aquat. Organ. 45:89-102(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-968.
    Strain: Isolate Blake.
  8. "Comparison of amino acid sequences deduced from a cDNA fragment obtained from infectious pancreatic necrosis virus (IPNV) strains of different serotypes."
    Heppell J., Berthiaume L., Corbin F., Tarrab E., Lecomte J., Arella M.
    Virology 195:840-844(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 437-539.
    Strain: Isolate Heppell.
  9. "Active residues and viral substrate cleavage sites of the protease of the birnavirus infectious pancreatic necrosis virus."
    Petit S., Lejal N., Huet J.-C., Delmas B.
    J. Virol. 74:2057-2066(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 509-515; 716-723 AND 735-740, ACTIVE SITES OF PROTEASE VP4, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF 486-ALA-ALA-487; 495-ALA-ALA-496; 508-ALA-SER-509; HIS-547; ASP-573; ASP-585; ASP-595; ASP-601; SER-633; ASP-644; 660-ASP-ASP-661; ASP-672; LYS-674; ALA-675; ILE-676; ALA-677; ALA-678; HIS-679; GLU-680; GLY-682; LEU-683; PRO-684; LEU-685; ILE-686; GLY-687; GLN-689; ASP-693; HIS-704 AND 734-ALA-SER-735.
    Strain: 31-75.
  10. "Structure of birnavirus-like particles determined by combined electron cryomicroscopy and X-ray crystallography."
    Pous J., Chevalier C., Ouldali M., Navaza J., Delmas B., Lepault J.
    J. Gen. Virol. 86:2339-2346(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY (15 ANGSTROMS) OF VIRAL PARTICLES.
    Strain: 31-75.
  11. "Crystal structure of the VP4 protease from infectious pancreatic necrosis virus reveals the acyl-enzyme complex for an intermolecular self-cleavage reaction."
    Lee J., Feldman A.R., Delmas B., Paetzel M.
    J. Biol. Chem. 282:24928-24937(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 514-716.

Entry informationi

Entry nameiPOLS_IPNVS
AccessioniPrimary (citable) accession number: Q703G9
Secondary accession number(s): P90205
, Q4KTX8, Q69CH7, Q69CI0, Q69CI3, Q6U2N3, Q6U2N5, Q6U2N8, Q6U2P1, Q6U2P5, Q6U2P7, Q6UAY7, Q82733, Q990Q0, Q9YJV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence shown is that of strain 31-75. Isolate Sp103 is VP5-deficient.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3