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P03303

- POLG_HRV14

UniProt

P03303 - POLG_HRV14

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Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 14 (HRV-14)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host ICAM1 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).By similarity
Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).By similarity
Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).By similarity
Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 (By similarity).By similarity
Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity (By similarity).By similarity
Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).By similarity
Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).By similarity
Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).By similarity
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).By similarity
RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated (By similarity).PROSITE-ProRule annotation

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
NTP + H2O = NDP + phosphate.

Enzyme regulationi

RNA-directed RNA polymerase: replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei69 – 702Cleavage; by autolysisSequence Analysis
Sitei331 – 3322Cleavage; by Protease 3CSequence Analysis
Sitei856 – 8572Cleavage; by Protease 2ASequence Analysis
Active sitei876 – 8761For Protease 2A activityBy similarity
Active sitei894 – 8941For Protease 2A activityBy similarity
Active sitei965 – 9651For Protease 2A activityBy similarity
Sitei1002 – 10032Cleavage; by Protease 3CSequence Analysis
Sitei1429 – 14302Cleavage; by Protease 3CSequence Analysis
Sitei1514 – 15152Cleavage; by Protease 3CSequence Analysis
Sitei1537 – 15382Cleavage; by Protease 3CSequence Analysis
Active sitei1577 – 15771For Protease 3C activitySequence Analysis
Active sitei1608 – 16081For Protease 3C activitySequence Analysis
Active sitei1683 – 16831For Protease 3C activityBy similarity
Sitei1719 – 17202Cleavage; by Protease 3CSequence Analysis
Active sitei2046 – 20461For RdRp activityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. ion channel activity Source: UniProtKB-KW
  4. RNA binding Source: UniProtKB-KW
  5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  6. RNA helicase activity Source: InterPro
  7. structural molecule activity Source: InterPro

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
  2. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
  3. induction by virus of host autophagy Source: UniProtKB
  4. lysis of host organelle involved in viral entry into host cell Source: UniProtKB-KW
  5. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  6. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
  7. protein oligomerization Source: UniProtKB-KW
  8. RNA-protein covalent cross-linking Source: UniProtKB-KW
  9. suppression by virus of host gene expression Source: UniProtKB-KW
  10. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
  11. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  12. suppression by virus of host translation initiation factor activity Source: UniProtKB
  13. transcription, DNA-templated Source: InterPro
  14. viral RNA genome replication Source: InterPro
  15. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation of host autophagy by virus, DNA replication, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral penetration via lysis of host organellar membrane, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.020.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 17 chains:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
Protease 2A (EC:3.4.22.29)
Short name:
P2A
Alternative name(s):
Picornain 2A
Protein 2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Alternative name(s):
Protein 3B
Short name:
P3B
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
OrganismiHuman rhinovirus 14 (HRV-14)
Taxonomic identifieri12131 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007679: Genome

Subcellular locationi

Chain Capsid protein VP0 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP2 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP3 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP1 : Virion By similarity. Host cytoplasm By similarity
Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 3AB : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 3CD : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain RNA-directed RNA polymerase : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 14911490CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei1492 – 150716Sequence AnalysisAdd
BLAST
Topological domaini1508 – 2179672CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle Source: UniProtKB-KW
  2. integral to membrane of host cell Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 21792178Genome polyproteinBy similarityPRO_0000426536Add
BLAST
Chaini2 – 856855P1By similarityPRO_0000426537Add
BLAST
Chaini2 – 331330Capsid protein VP0Sequence AnalysisPRO_0000426538Add
BLAST
Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426539Add
BLAST
Chaini70 – 331262Capsid protein VP2Sequence AnalysisPRO_0000426540Add
BLAST
Chaini332 – 563232Capsid protein VP3Sequence AnalysisPRO_0000426541Add
BLAST
Chaini564 – 856293Capsid protein VP1Sequence AnalysisPRO_0000426542Add
BLAST
Chaini857 – 1429573P2By similarityPRO_0000426543Add
BLAST
Chaini857 – 1002146Protease 2ASequence AnalysisPRO_0000040029Add
BLAST
Chaini1003 – 109997Protein 2BSequence AnalysisPRO_0000040030Add
BLAST
Chaini1101 – 1429329Protein 2CSequence AnalysisPRO_0000426544Add
BLAST
Chaini1430 – 2179750P3By similarityPRO_0000426545Add
BLAST
Chaini1430 – 1537108Protein 3ABSequence AnalysisPRO_0000426546Add
BLAST
Chaini1430 – 151485Protein 3ASequence AnalysisPRO_0000040032Add
BLAST
Chaini1515 – 153723Viral protein genome-linkedSequence AnalysisPRO_0000426547Add
BLAST
Chaini1538 – 2179642Protein 3CDSequence AnalysisPRO_0000426548Add
BLAST
Chaini1538 – 1718181Protease 3CSequence AnalysisPRO_0000426549Add
BLAST
Chaini1719 – 2179461RNA-directed RNA polymeraseBy similarityPRO_0000426550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Modified residuei1517 – 15171O-(5'-phospho-RNA)-tyrosineBy similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity).By similarity
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion (By similarity).By similarity
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.By similarity
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion (By similarity).By similarity
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication (By similarity).By similarity

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Capsid protein VP1: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Interact with host ICAM1. Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid (By similarity). Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 (By similarity). Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity). Protein 3AB: interacts with protein 3CD (By similarity). Viral protein genome-linked: interacts with RNA-directed RNA polymerase (By similarity). Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD (By similarity).By similarity

Structurei

Secondary structure

1
2179
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 353Combined sources
Helixi36 – 383Combined sources
Helixi51 – 544Combined sources
Beta strandi57 – 593Combined sources
Beta strandi83 – 875Combined sources
Beta strandi90 – 967Combined sources
Helixi103 – 1053Combined sources
Helixi113 – 1153Combined sources
Helixi126 – 1283Combined sources
Beta strandi138 – 1414Combined sources
Beta strandi147 – 1515Combined sources
Helixi153 – 1553Combined sources
Helixi159 – 1679Combined sources
Beta strandi168 – 18013Combined sources
Beta strandi188 – 19710Combined sources
Helixi213 – 2164Combined sources
Helixi219 – 2213Combined sources
Helixi225 – 2273Combined sources
Helixi238 – 2403Combined sources
Turni241 – 2433Combined sources
Helixi247 – 2526Combined sources
Beta strandi253 – 2597Combined sources
Turni260 – 2623Combined sources
Beta strandi264 – 2707Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi281 – 2844Combined sources
Beta strandi287 – 29812Combined sources
Beta strandi305 – 32319Combined sources
Turni339 – 3424Combined sources
Beta strandi354 – 3563Combined sources
Helixi374 – 3774Combined sources
Turni386 – 3894Combined sources
Beta strandi390 – 3923Combined sources
Helixi395 – 3984Combined sources
Beta strandi399 – 4024Combined sources
Beta strandi410 – 4156Combined sources
Helixi421 – 4255Combined sources
Helixi427 – 4326Combined sources
Beta strandi435 – 4406Combined sources
Beta strandi442 – 4487Combined sources
Beta strandi457 – 4637Combined sources
Helixi473 – 4775Combined sources
Beta strandi479 – 4857Combined sources
Beta strandi487 – 4893Combined sources
Beta strandi491 – 4966Combined sources
Beta strandi501 – 5033Combined sources
Beta strandi505 – 5084Combined sources
Beta strandi509 – 5124Combined sources
Beta strandi517 – 5248Combined sources
Beta strandi536 – 5449Combined sources
Beta strandi549 – 5535Combined sources
Helixi580 – 5823Combined sources
Beta strandi585 – 5873Combined sources
Helixi604 – 6063Combined sources
Helixi614 – 6163Combined sources
Helixi630 – 6323Combined sources
Helixi634 – 6374Combined sources
Beta strandi642 – 65110Combined sources
Turni660 – 6645Combined sources
Beta strandi665 – 6706Combined sources
Beta strandi673 – 6764Combined sources
Helixi677 – 6837Combined sources
Beta strandi686 – 70217Combined sources
Beta strandi714 – 7207Combined sources
Beta strandi722 – 7243Combined sources
Beta strandi729 – 7313Combined sources
Helixi733 – 7364Combined sources
Beta strandi738 – 7403Combined sources
Beta strandi742 – 7465Combined sources
Beta strandi749 – 7557Combined sources
Beta strandi760 – 7667Combined sources
Beta strandi772 – 7743Combined sources
Beta strandi776 – 7783Combined sources
Helixi782 – 7843Combined sources
Beta strandi790 – 7956Combined sources
Beta strandi804 – 82219Combined sources
Beta strandi832 – 8343Combined sources
Helixi1539 – 155113Combined sources
Beta strandi1552 – 15576Combined sources
Beta strandi1560 – 156910Combined sources
Beta strandi1571 – 15766Combined sources
Beta strandi1582 – 15865Combined sources
Beta strandi1589 – 15924Combined sources
Beta strandi1594 – 16018Combined sources
Turni1602 – 16043Combined sources
Beta strandi1605 – 16139Combined sources
Helixi1623 – 16253Combined sources
Beta strandi1634 – 164411Combined sources
Beta strandi1646 – 166318Combined sources
Beta strandi1666 – 167611Combined sources
Beta strandi1686 – 16894Combined sources
Beta strandi1692 – 170110Combined sources
Beta strandi1704 – 17096Combined sources
Helixi1712 – 17165Combined sources
Beta strandi1721 – 17266Combined sources
Helixi1728 – 17314Combined sources
Helixi1748 – 17503Combined sources
Helixi1773 – 17786Combined sources
Helixi1791 – 180515Combined sources
Helixi1816 – 18216Combined sources
Beta strandi1824 – 18263Combined sources
Helixi1839 – 18424Combined sources
Helixi1846 – 18494Combined sources
Turni1852 – 18554Combined sources
Helixi1858 – 186710Combined sources
Beta strandi1873 – 18775Combined sources
Helixi1884 – 18885Combined sources
Beta strandi1894 – 18974Combined sources
Helixi1900 – 19067Combined sources
Turni1907 – 19093Combined sources
Helixi1911 – 19199Combined sources
Turni1923 – 19264Combined sources
Helixi1933 – 19364Combined sources
Helixi1937 – 19393Combined sources
Helixi1940 – 19434Combined sources
Beta strandi1949 – 19557Combined sources
Helixi1957 – 19593Combined sources
Helixi1962 – 197514Combined sources
Turni1978 – 19814Combined sources
Helixi1982 – 19876Combined sources
Beta strandi1988 – 19925Combined sources
Beta strandi1994 – 20029Combined sources
Beta strandi2008 – 20103Combined sources
Helixi2011 – 203020Combined sources
Helixi2036 – 20383Combined sources
Beta strandi2040 – 20445Combined sources
Beta strandi2047 – 20515Combined sources
Helixi2058 – 20658Combined sources
Turni2066 – 20694Combined sources
Turni2086 – 20883Combined sources
Beta strandi2094 – 20985Combined sources
Beta strandi2100 – 21023Combined sources
Beta strandi2105 – 21095Combined sources
Helixi2112 – 21198Combined sources
Beta strandi2121 – 21244Combined sources
Turni2125 – 21273Combined sources
Helixi2128 – 213912Combined sources
Helixi2140 – 21423Combined sources
Helixi2144 – 215411Combined sources
Helixi2158 – 21625Combined sources
Helixi2168 – 217710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3Ielectron microscopy26.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1HRIX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1HRVX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1K5MX-ray2.70A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1NA1X-ray3.30A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1NCQX-ray2.50A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1R08X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1R09X-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RMUX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUCX-ray3.101568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUDX-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUEX-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUFX-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUGX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUHX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUIX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUJX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RVFX-ray4.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1VRHX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1XR5X-ray2.80A1720-2179[»]
2B0FNMR-A1538-1719[»]
2HWBX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2HWCX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2IN2NMR-A1538-1719[»]
2R04X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2R06X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2R07X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RM2X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RMUX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RR1X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RS1X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RS3X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RS5X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
4PDWX-ray3.00A568-856[»]
B70-331[»]
C332-567[»]
4RHVX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
ProteinModelPortaliP03303.
SMRiP03303. Positions 2-69, 77-567, 574-856, 1429-1486, 1538-2179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03303.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1205 – 1361157SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1538 – 1702165Peptidase C3Add
BLAST
Domaini1946 – 2060115RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni564 – 58421Amphipatic alpha-helixSequence AnalysisAdd
BLAST
Regioni1430 – 145122DisorderedBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 1 peptidase C3 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
ProDomiPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P03303-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASTS SAGQSLSMDP
60 70 80 90 100
SKFTEPVKDL MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA
110 120 130 140 150
VVCYAEWPEY LPDVDASDVN KTSKPDTSVC RFYTLDSKTW TTGSKGWCWK
160 170 180 190 200
LPDALKDMGV FGQNMFFHSL GRSGYTVHVQ CNATKFHSGC LLVVVIPEHQ
210 220 230 240 250
LASHEGGNVS VKYTFTHPGE RGIDLSSANE VGGPVKDVIY NMNGTLLGNL
260 270 280 290 300
LIFPHQFINL RTNNTATIVI PYINSVPIDS MTRHNNVSLM VIPIAPLTVP
310 320 330 340 350
TGATPSLPIT VTIAPMCTEF SGIRSKSIVP QGLPTTTLPG SGQFLTTDDR
360 370 380 390 400
QSPSALPNYE PTPRIHIPGK VHNLLEIIQV DTLIPMNNTH TKDEVNSYLI
410 420 430 440 450
PLNANRQNEQ VFGTNLFIGD GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG
460 470 480 490 500
PALSSAKLIL AYTPPGARGP QDRREAMLGT HVVWDIGLQS TIVMTIPWTS
510 520 530 540 550
GVQFRYTDPD TYTSAGFLSC WYQTSLILPP ETTGQVYLLS FISACPDFKL
560 570 580 590 600
RLMKDTQTIS QTVALTEGLG DELEEVIVEK TKQTVASISS GPKHTQKVPI
610 620 630 640 650
LTANETGATM PVLPSDSIET RTTYMHFNGS ETDVECFLGR AACVHVTEIQ
660 670 680 690 700
NKDATGIDNH REAKLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT
710 720 730 740 750
ASQPDSANYS SNLVVQAMYV PPGAPNPKEW DDYTWQSASN PSVFFKVGDT
760 770 780 790 800
SRFSVPYVGL ASAYNCFYDG YSHDDAETQY GITVLNHMGS MAFRIVNEHD
810 820 830 840 850
EHKTLVKIRV YHRAKHVEAW IPRAPRALPY TSIGRTNYPK NTEPVIKKRK
860 870 880 890 900
GDIKSYGLGP RYGGIYTSNV KIMNYHLMTP EDHHNLIAPY PNRDLAIVST
910 920 930 940 950
GGHGAETIPH CNCTSGVYYS TYYRKYYPII CEKPTNIWIE GNPYYPSRFQ
960 970 980 990 1000
AGVMKGVGPA EPGDCGGILR CIHGPIGLLT AGGSGYVCFA DIRQLECIAE
1010 1020 1030 1040 1050
EQGLSDYITG LGRAFGVGFT DQISTKVTEL QEVAKDFLTT KVLSKVVKMV
1060 1070 1080 1090 1100
SALVIICRNH DDLVTVTATL ALLGCDGSPW RFLKMYISKH FQVPYIERQA
1110 1120 1130 1140 1150
NDGWFRKFND ACNAAKGLEW IANKISKLIE WIKNKVLPQA KEKLEFCSKL
1160 1170 1180 1190 1200
KQLDILERQI TTMHISNPTQ EKREQLFNNV LWLEQMSQKF APLYAVESKR
1210 1220 1230 1240 1250
IRELKNKMVN YMQFKSKQRI EPVCVLIHGT PGSGKSLTTS IVGRAIAEHF
1260 1270 1280 1290 1300
NSAVYSLPPD PKHFDGYQQQ EVVIMDDLNQ NPDGQDISMF CQMVSSVDFL
1310 1320 1330 1340 1350
PPMASLDNKG MLFTSNFVLA STNSNTLSPP TILNPEALVR RFGFDLDICL
1360 1370 1380 1390 1400
HTTYTKNGKL NAGMSTKTCK DCHQPSNFKK CCPLVCGKAI SLVDRTTNIR
1410 1420 1430 1440 1450
YSVDQLVTAI ISDFKSKMQI TDSLETLFQG PVYKDLEIDV CNTPPPECIN
1460 1470 1480 1490 1500
DLLKSVDSEE IREYCKKKKW IIPEIPTNIE RAMNQASMII NTILMFVSTL
1510 1520 1530 1540 1550
GIVYVIYKLF AQTQGPYSGN PPHNKLKAPT LRPVVVQGPN TEFALSLLRK
1560 1570 1580 1590 1600
NIMTITTSKG EFTGLGIHDR VCVIPTHAQP GDDVLVNGQK IRVKDKYKLV
1610 1620 1630 1640 1650
DPENINLELT VLTLDRNEKF RDIRGFISED LEGVDATLVV HSNNFTNTIL
1660 1670 1680 1690 1700
EVGPVTMAGL INLSSTPTNR MIRYDYATKT GQCGGVLCAT GKIFGIHVGG
1710 1720 1730 1740 1750
NGRQGFSAQL KKQYFVEKQG QVIARHKVRE FNINPVNTPT KSKLHPSVFY
1760 1770 1780 1790 1800
DVFPGDKEPA VLSDNDPRLE VKLTESLFSK YKGNVNTEPT ENMLVAVDHY
1810 1820 1830 1840 1850
AGQLLSLDIP TSELTLKEAL YGVDGLEPID ITTSAGFPYV SLGIKKRDIL
1860 1870 1880 1890 1900
NKETQDTEKM KFYLDKYGID LPLVTYIKDE LRSVDKVRLG KSRLIEASSL
1910 1920 1930 1940 1950
NDSVNMRMKL GNLYKAFHQN PGVLTGSAVG CDPDVFWSVI PCLMDGHLMA
1960 1970 1980 1990 2000
FDYSNFDASL SPVWFVCLEK VLTKLGFAGS SLIQSICNTH HIFRDEIYVV
2010 2020 2030 2040 2050
EGGMPSGCSG TSIFNSMINN IIIRTLILDA YKGIDLDKLK ILAYGDDLIV
2060 2070 2080 2090 2100
SYPYELDPQV LATLGKNYGL TITPPDKSET FTKMTWENLT FLKRYFKPDQ
2110 2120 2130 2140 2150
QFPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCMLAW HSGEKEYNEF
2160 2170
IQKIRTTDIG KCLILPEYSV LRRRWLDLF
Length:2,179
Mass (Da):242,991
Last modified:January 23, 2007 - v3
Checksum:i827201A3032F0285
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 3681P → L in AAA45756. (PubMed:2983312)Curated
Sequence conflicti459 – 4591I → T in AAA45756. (PubMed:2983312)Curated
Sequence conflicti722 – 7221P → H in AAA45756. (PubMed:2983312)Curated
Sequence conflicti726 – 7272NP → KS(PubMed:2983312)Curated
Sequence conflicti729 – 7313EWD → RVG(PubMed:2983312)Curated
Sequence conflicti913 – 9131C → R in AAA45756. (PubMed:2983312)Curated
Sequence conflicti942 – 9421N → S in AAA45756. (PubMed:2983312)Curated
Sequence conflicti962 – 9621P → L in AAA45756. (PubMed:2983312)Curated
Sequence conflicti982 – 9821G → E in AAA45756. (PubMed:2983312)Curated
Sequence conflicti1193 – 11931L → F in AAA45756. (PubMed:2983312)Curated
Sequence conflicti1193 – 11931L → H in AAA45758. (PubMed:8383233)Curated
Sequence conflicti1220 – 12201I → T(PubMed:8383233)Curated
Sequence conflicti1220 – 12201I → T(PubMed:2983312)Curated
Sequence conflicti1399 – 13991I → V(PubMed:8383233)Curated
Sequence conflicti1399 – 13991I → V(PubMed:2983312)Curated
Sequence conflicti1446 – 14461P → S in AAA45756. (PubMed:2983312)Curated
Sequence conflicti1739 – 17391P → A in AAA45756. (PubMed:2983312)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01087 Genomic RNA. Translation: CAA25565.1.
L05355 Genomic RNA. Translation: AAA45758.1.
K02121 Genomic RNA. Translation: AAA45756.1.
PIRiA03901. GNNYH4.
RefSeqiNP_041009.1. NC_001490.1.

Genome annotation databases

GeneIDi1461213.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with antiviral compound SCH 38057

Virus Particle ExploreR db

Icosahedral capsid structure complexed with antiviral compound SDZ 35-682

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01087 Genomic RNA. Translation: CAA25565.1 .
L05355 Genomic RNA. Translation: AAA45758.1 .
K02121 Genomic RNA. Translation: AAA45756.1 .
PIRi A03901. GNNYH4.
RefSeqi NP_041009.1. NC_001490.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D3I electron microscopy 26.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1HRI X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1HRV X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1K5M X-ray 2.70 A 568-856 [» ]
B 70-331 [» ]
C 332-567 [» ]
D 2-69 [» ]
1NA1 X-ray 3.30 A 568-856 [» ]
B 70-331 [» ]
C 332-567 [» ]
D 2-69 [» ]
1NCQ X-ray 2.50 A 568-856 [» ]
B 70-331 [» ]
C 332-567 [» ]
D 2-69 [» ]
1R08 X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1R09 X-ray 2.90 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1RMU X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1RUC X-ray 3.10 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1RUD X-ray 2.90 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1RUE X-ray 2.90 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1RUF X-ray 2.90 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1RUG X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1RUH X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1RUI X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1RUJ X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1RVF X-ray 4.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1VRH X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
1XR5 X-ray 2.80 A 1720-2179 [» ]
2B0F NMR - A 1538-1719 [» ]
2HWB X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
2HWC X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
2IN2 NMR - A 1538-1719 [» ]
2R04 X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
2R06 X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
2R07 X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
2RM2 X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
2RMU X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
2RR1 X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
2RS1 X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
2RS3 X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
2RS5 X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
4PDW X-ray 3.00 A 568-856 [» ]
B 70-331 [» ]
C 332-567 [» ]
4RHV X-ray 3.00 1 568-856 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
ProteinModelPortali P03303.
SMRi P03303. Positions 2-69, 77-567, 574-856, 1429-1486, 1538-2179.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.020.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1461213.

Miscellaneous databases

EvolutionaryTracei P03303.

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view ]
ProDomi PD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The complete nucleotide sequence of a common cold virus: human rhinovirus 14."
    Stanway G., Hughes P.J., Mountford R.C., Minor P.D., Almond J.W.
    Nucleic Acids Res. 12:7859-7875(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Role of maturation cleavage in infectivity of picornaviruses: activation of an infectosome."
    Lee W.M., Monroe S., Rueckert R.R.
    J. Virol. 67:2110-2122(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Molecular cloning and complete sequence determination of RNA genome of human rhinovirus type 14."
    Callahan P.L., Mizutani S., Colonno R.J.
    Proc. Natl. Acad. Sci. U.S.A. 82:732-736(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  4. "Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus."
    Gustin K.E., Sarnow P.
    J. Virol. 76:8787-8796(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF PROTEASE 2A.
  5. Cited for: REVIEW.
  6. "Productive entry pathways of human rhinoviruses."
    Fuchs R., Blaas D.
    Adv. Virol. 2012:826301-826301(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  8. "The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure."
    Arnold E., Rossman M.G.
    Acta Crystallogr. A 44:270-282(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  9. "Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor."
    Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., Rossmann M.G.
    EMBO J. 18:6249-6259(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF 70-856 IN COMPLEX WITH ICAM1.
  10. "Analysis of the structure of a common cold virus, human rhinovirus 14, refined at a resolution of 3.0 A."
    Arnold E., Rossman M.G.
    J. Mol. Biol. 211:763-801(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiPOLG_HRV14
AccessioniPrimary (citable) accession number: P03303
Secondary accession number(s): Q82083
, Q82123, Q84736, Q84737, Q84738, Q84739, Q84740, Q84741, Q84774, Q84775, Q84776, Q84777, Q84778, Q84779, Q89441, Q89649, Q89763, Q89883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 173 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Caution

The PDB data bank contains the 3D-structure coordinates of proteins VP1, VP2, VP3 and VP4.Curated

Keywords - Technical termi

3D-structure, Complete proteome

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