Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q82122

- POLG_HRV16

UniProt

Q82122 - POLG_HRV16

Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 16 (HRV-16)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 cell receptor 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
    Sitei330 – 3312Cleavage; by Protease 3CSequence Analysis
    Active sitei871 – 8711For Protease 2A activityBy similarity
    Active sitei888 – 8881For Protease 2A activityBy similarity
    Active sitei959 – 9591For Protease 2A activityBy similarity
    Sitei995 – 9962Cleavage; by Protease 3CSequence Analysis
    Sitei1412 – 14132Cleavage; by Protease 3CSequence Analysis
    Sitei1489 – 14902Cleavage; by Protease 3CSequence Analysis
    Sitei1510 – 15112Cleavage; by Protease 3CSequence Analysis
    Active sitei1550 – 15501For Protease 3C activitySequence Analysis
    Active sitei1581 – 15811For Protease 3C activitySequence Analysis
    Active sitei1657 – 16571For Protease 3C activityBy similarity
    Sitei1693 – 16942Cleavage; by Protease 3CSequence Analysis
    Active sitei2020 – 20201For 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. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    5. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
    6. protein oligomerization Source: UniProtKB-KW
    7. RNA-protein covalent cross-linking Source: UniProtKB-KW
    8. suppression by virus of host gene expression Source: UniProtKB-KW
    9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
    10. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    11. suppression by virus of host translation initiation factor activity Source: UniProtKB
    12. transcription, DNA-templated Source: InterPro
    13. viral RNA genome replication Source: InterPro
    14. virion attachment to host cell Source: UniProtKB-KW

    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 RNA replication, Virus endocytosis by host, Virus entry into host cell

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Protein family/group databases

    MEROPSiC03.007.

    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 16 (HRV-16)
    Taxonomic identifieri31708 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusRhinovirus A
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007680: 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.

    GO - Cellular componenti

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

    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 – 21532152Genome polyproteinBy similarityPRO_0000426551Add
    BLAST
    Chaini2 – 853852P1By similarityPRO_0000426552Add
    BLAST
    Chaini2 – 330329Capsid protein VP0Sequence AnalysisPRO_0000426553Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426554Add
    BLAST
    Chaini70 – 330261Capsid protein VP2Sequence AnalysisPRO_0000426555Add
    BLAST
    Chaini331 – 565235Capsid protein VP3Sequence AnalysisPRO_0000426556Add
    BLAST
    Chaini565 – 853289Capsid protein VP1Sequence AnalysisPRO_0000426557Add
    BLAST
    Chaini853 – 1412560P2By similarityPRO_0000426558Add
    BLAST
    Chaini853 – 995143Protease 2ASequence AnalysisPRO_0000426559Add
    BLAST
    Chaini996 – 109095Protein 2BSequence AnalysisPRO_0000040041Add
    BLAST
    Chaini1091 – 1412322Protein 2CSequence AnalysisPRO_0000040042Add
    BLAST
    Chaini1413 – 2153741P3By similarityPRO_0000426560Add
    BLAST
    Chaini1413 – 151098Protein 3ABSequence AnalysisPRO_0000426561Add
    BLAST
    Chaini1413 – 148977Protein 3ASequence AnalysisPRO_0000040043Add
    BLAST
    Chaini1490 – 151021Viral protein genome-linkedSequence AnalysisPRO_0000426562Add
    BLAST
    Chaini1511 – 2153643Protein 3CDSequence AnalysisPRO_0000426563Add
    BLAST
    Chaini1511 – 1692182Protease 3CSequence AnalysisPRO_0000426564Add
    BLAST
    Chaini1693 – 2153461RNA-directed RNA polymeraseBy similarityPRO_0000426565Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei1492 – 14921O-(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. 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
    2153
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Beta strandi28 – 303
    Beta strandi33 – 353
    Helixi36 – 383
    Beta strandi83 – 875
    Beta strandi90 – 967
    Helixi103 – 1053
    Turni113 – 1153
    Helixi126 – 1283
    Beta strandi138 – 1403
    Beta strandi147 – 1515
    Helixi153 – 1553
    Helixi159 – 1679
    Beta strandi168 – 18013
    Beta strandi188 – 19710
    Beta strandi204 – 2063
    Helixi213 – 2164
    Helixi219 – 2213
    Turni225 – 2273
    Helixi239 – 2413
    Turni242 – 2454
    Helixi248 – 2536
    Beta strandi254 – 2607
    Turni261 – 2633
    Beta strandi265 – 2717
    Beta strandi276 – 2805
    Turni282 – 2843
    Beta strandi288 – 29912
    Beta strandi307 – 32317
    Turni338 – 3414
    Beta strandi353 – 3553
    Beta strandi369 – 3724
    Helixi374 – 3774
    Turni389 – 3935
    Helixi395 – 3984
    Beta strandi399 – 4024
    Beta strandi406 – 4094
    Beta strandi411 – 4166
    Turni422 – 4265
    Helixi428 – 4336
    Beta strandi436 – 4416
    Beta strandi443 – 4497
    Beta strandi458 – 4647
    Beta strandi466 – 4683
    Helixi474 – 4785
    Beta strandi480 – 4867
    Beta strandi488 – 4903
    Beta strandi492 – 4976
    Beta strandi502 – 5043
    Beta strandi506 – 5094
    Helixi512 – 5143
    Beta strandi518 – 5258
    Beta strandi537 – 5459
    Beta strandi550 – 5545
    Helixi570 – 57910
    Beta strandi582 – 5843
    Helixi605 – 6073
    Helixi615 – 6184
    Helixi631 – 6333
    Helixi635 – 6395
    Beta strandi643 – 6519
    Helixi656 – 6594
    Beta strandi660 – 6656
    Helixi672 – 6787
    Beta strandi681 – 70121
    Beta strandi707 – 7137
    Helixi726 – 7294
    Beta strandi731 – 7399
    Beta strandi746 – 7494
    Beta strandi754 – 7607
    Beta strandi764 – 7696
    Turni776 – 7794
    Beta strandi784 – 7896
    Beta strandi798 – 81619
    Helixi838 – 8403
    Beta strandi847 – 8493
    Beta strandi1695 – 17017
    Helixi1702 – 17054
    Turni1722 – 17265
    Helixi1747 – 17515
    Helixi1752 – 17543
    Helixi1765 – 177915
    Helixi1790 – 17956
    Beta strandi1805 – 18073
    Turni1811 – 18177
    Helixi1820 – 18234
    Turni1826 – 18294
    Helixi1832 – 184110
    Beta strandi1847 – 18515
    Beta strandi1854 – 18563
    Helixi1859 – 18624
    Beta strandi1868 – 18714
    Helixi1874 – 189320
    Turni1897 – 19004
    Helixi1907 – 191711
    Beta strandi1920 – 193011
    Helixi1931 – 19344
    Helixi1937 – 194913
    Helixi1958 – 19614
    Beta strandi1962 – 19676
    Beta strandi1970 – 19778
    Helixi1985 – 200420
    Helixi2010 – 20123
    Beta strandi2014 – 20185
    Beta strandi2021 – 20288
    Helixi2032 – 20376
    Helixi2038 – 20425
    Beta strandi2046 – 20494
    Turni2060 – 20623
    Beta strandi2068 – 20725
    Beta strandi2079 – 20835
    Helixi2086 – 20938
    Beta strandi2095 – 20973
    Helixi2099 – 21013
    Helixi2102 – 211312
    Helixi2114 – 21163
    Helixi2118 – 212811
    Helixi2132 – 21354
    Helixi2142 – 21509

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AYMX-ray2.151569-853[»]
    270-330[»]
    3331-568[»]
    1AYNX-ray2.901569-853[»]
    270-330[»]
    3331-568[»]
    1C8MX-ray2.801569-853[»]
    279-330[»]
    3331-568[»]
    42-78[»]
    1D3Eelectron microscopy28.001570-853[»]
    279-330[»]
    3331-568[»]
    42-69[»]
    1NCRX-ray2.70A569-853[»]
    B70-330[»]
    C331-568[»]
    D2-69[»]
    1ND2X-ray2.50A569-853[»]
    B70-330[»]
    C331-568[»]
    D2-69[»]
    1ND3X-ray2.80A569-853[»]
    B70-330[»]
    C331-568[»]
    D2-69[»]
    1QJUX-ray2.801569-853[»]
    270-330[»]
    3331-568[»]
    42-69[»]
    1QJXX-ray2.801569-853[»]
    270-330[»]
    3331-568[»]
    42-69[»]
    1QJYX-ray2.801569-853[»]
    270-330[»]
    3331-568[»]
    42-69[»]
    1TP7X-ray2.40A/B/C/D1694-2153[»]
    1XR7X-ray2.30A/B1694-2153[»]
    4K50X-ray2.93A/E/I/M1694-2153[»]
    ProteinModelPortaliQ82122.
    SMRiQ82122. Positions 2-69, 79-992, 1511-1690, 1694-2153.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ82122.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 14661465CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1483 – 2153671CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1467 – 148216Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1186 – 1346161SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1511 – 1676166Peptidase C3Add
    BLAST
    Domaini1921 – 2034114RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni565 – 58218Amphipatic alpha-helixSequence AnalysisAdd
    BLAST
    Regioni1413 – 142715DisorderedBy 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.
    3.40.50.300. 1 hit.
    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.

    Q82122-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAQVSRQNV GTHSTQNMVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP     50
    SKFTDPVKDV LEKGIPTLQS PSVEACGYSD RIIQITRGDS TITSQDVANA 100
    VVGYGVWPHY LTPQDATAID KPTQPDTSSN RFYTLDSKMW NSTSKGWWWK 150
    LPDALKDMGI FGENMFYHFL GRSGYTVHVQ CNASKFHQGT LLVVMIPEHQ 200
    LATVNKGNVN AGYKYTHPGE AGREVGTQVE NEKQPSDDNW LNFDGTLLGN 250
    LLIFPHQFIN LRSNNSATLI VPYVNAVPMD SMVRHNNWSL VIIPVCQLQS 300
    NNISNIVPIT VSISPMCAEF SGARAKTVVQ GLPVYVTPGS GQFMTTDDMQ 350
    SPCALPWYHP TKEIFIPGEV KNLIEMCQVD TLIPINSTQS NIGNVSMYTV 400
    TLSPQTKLAE EIFAIKVDIA SHPLATTLIG EIASYFTHWT GSLRFSFMFC 450
    GTANTTLKVL LAYTPPGIGK PRSRKEAMLG THVVWDVGLQ STVSLVVPWI 500
    SASQYRFTTP DTYSSAGYIT CWYQTNFVVP PNTPNTAEML CFVSGCKDFC 550
    LRMARDTDLH KQTGPITQNP VERYVDEVLN EVLVVPNINQ SHPTTSNAAP 600
    VLDAAETGHT NKIQPEDTIE TRYVQSSQTL DEMSVESFLG RSGCIHESVL 650
    DIVDNYNDQS FTKWNINLQE MAQIRRKFEM FTYARFDSEI TMVPSVAAKD 700
    GHIGHIVMQY MYVPPGAPIP TTRDDYAWQS GTNASVFWQH GQPFPRFSLP 750
    FLSIASAYYM FYDGYDGDTY KSRYGTVVTN DMGTLCSRIV TSEQLHKVKV 800
    VTRIYHKAKH TKAWCPRPPR AVQYSHTHTT NYKLSSEVHN DVAIRPRTNL 850
    TTVGPSDMYV HVGNLIYRNL HLFNSDIHDS ILVSYSSDLI IYRTSTQGDG 900
    YIPTCNCTEA TYYCKHKNRY YPINVTPHDW YEIQESEYYP KHIQYNLLIG 950
    EGPCEPGDCG GKLLCKHGVI GIITAGGEGH VAFIDLRHFH CAEEQGITDY 1000
    IHMLGEAFGS GFVDSVKDQI NSINPINNIS SKMVKWMLRI ISAMVIIIRN 1050
    SSDPQTIIAT LTLIGCNGSP WRFLKEKFCK WTQLTYIHKE SDSWLKKFTE 1100
    MCNAARGLEW IGNKISKFID WMKSMLPQAQ LKVKYLSELK KLNFLEKQVE 1150
    NLRAADTNTQ EKIKCEIDTL HDLSCKFLPL YASEAKRIKV LYHKCTNIIK 1200
    QKKRSEPVAV MIHGPPGTGK SITTSFLARM ITNESDIYSL PPDPKYFDGY 1250
    DNQSVVIMDD IMQNPGGEDM TLFCQMVSSV TFIPPMADLP DKGKPFDSRF 1300
    VLCSTNHSLL APPTISSLPA MNRRFYLDLD ILVHDNYKDN QGKLDVSRAF 1350
    RLCDVDSKIG NAKCCPFVCG KAVTFKDRNT CRTYSLSQIY NQILEEDKRR 1400
    RQVVDVMSAI FQGPISMDKP PPPAITDLLR SVRTPEVIKY CQDNKWIVPA 1450
    DCQIERDLNI ANSIITIIAN IISIAGIIYI IYKLFCSLQG PYSGEPKPKT 1500
    KVPERRVVAQ GPEEEFGMSI IKNNTCVVTT TNGKFTGLGI YDRILILPTH 1550
    ADPGSEIQVN GIHTKVLDSY DLFNKEGVKL EITVLKLDRN EKFRDIRKYI 1600
    PESEDDYPEC NLALVANQTE PTIIKVGDVV SYGNILLSGT QTARMLKYNY 1650
    PTKSGYCGGV LYKIGQILGI HVGGNGRDGF SSMLLRSYFT EQQGQIQISK 1700
    HVKDVGLPSI HTPTKTKLQP SVFYDIFPGS KEPAVLTEKD PRLKVDFDSA 1750
    LFSKYKGNTE CSLNEHIQVA VAHYSAQLAT LDIDPQPIAM EDSVFGMDGL 1800
    EALDLNTSAG YPYVTLGIKK KDLINNKTKD ISKLKLALDK YDVDLPMITF 1850
    LKDELRKKDK IAAGKTRVIE ASSINDTILF RTVYGNLFSK FHLNPGVVTG 1900
    CAVGCDPETF WSKIPLMLDG DCIMAFDYTN YDGSIHPIWF KALGMVLDNL 1950
    SFNPTLINRL CNSKHIFKST YYEVEGGVPS GCSGTSIFNS MINNIIIRTL 2000
    VLDAYKHIDL DKLKIIAYGD DVIFSYKYKL DMEAIAKEGQ KYGLTITPAD 2050
    KSSEFKELDY GNVTFLKRGF RQDDKYKFLI HPTFPVEEIY ESIRWTKKPS 2100
    QMQEHVLSLC HLMWHNGPEI YKDFETKIRS VSAGRALYIP PYELLRHEWY 2150
    EKF 2153
    Length:2,153
    Mass (Da):242,244
    Last modified:January 23, 2007 - v4
    Checksum:i6B11D0D93DF11C04
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti547 – 5482KD → NH in AAA69862. (PubMed:7732663)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L24917 Genomic RNA. Translation: AAA69862.1.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure at high resolution

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with antiviral drug VP63843 (pleconaril)

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with a two-domain fragment of its cellular receptor ICAM1

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with antiviral compound pleconaril

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with antiviral compound pleconaril

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with antiviral compound VP61209

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with antiviral compound WIN68934

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with antiviral compound VP65099

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L24917 Genomic RNA. Translation: AAA69862.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AYM X-ray 2.15 1 569-853 [» ]
    2 70-330 [» ]
    3 331-568 [» ]
    1AYN X-ray 2.90 1 569-853 [» ]
    2 70-330 [» ]
    3 331-568 [» ]
    1C8M X-ray 2.80 1 569-853 [» ]
    2 79-330 [» ]
    3 331-568 [» ]
    4 2-78 [» ]
    1D3E electron microscopy 28.00 1 570-853 [» ]
    2 79-330 [» ]
    3 331-568 [» ]
    4 2-69 [» ]
    1NCR X-ray 2.70 A 569-853 [» ]
    B 70-330 [» ]
    C 331-568 [» ]
    D 2-69 [» ]
    1ND2 X-ray 2.50 A 569-853 [» ]
    B 70-330 [» ]
    C 331-568 [» ]
    D 2-69 [» ]
    1ND3 X-ray 2.80 A 569-853 [» ]
    B 70-330 [» ]
    C 331-568 [» ]
    D 2-69 [» ]
    1QJU X-ray 2.80 1 569-853 [» ]
    2 70-330 [» ]
    3 331-568 [» ]
    4 2-69 [» ]
    1QJX X-ray 2.80 1 569-853 [» ]
    2 70-330 [» ]
    3 331-568 [» ]
    4 2-69 [» ]
    1QJY X-ray 2.80 1 569-853 [» ]
    2 70-330 [» ]
    3 331-568 [» ]
    4 2-69 [» ]
    1TP7 X-ray 2.40 A/B/C/D 1694-2153 [» ]
    1XR7 X-ray 2.30 A/B 1694-2153 [» ]
    4K50 X-ray 2.93 A/E/I/M 1694-2153 [» ]
    ProteinModelPortali Q82122.
    SMRi Q82122. Positions 2-69, 79-992, 1511-1690, 1694-2153.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q82122.
    ChEMBLi CHEMBL5296.

    Protein family/group databases

    MEROPSi C03.007.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q82122.

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    3.40.50.300. 1 hit.
    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. "Complete sequence of the RNA genome of human rhinovirus 16, a clinically useful common cold virus belonging to the ICAM-1 receptor group."
      Lee W.M., Wang W., Rueckert R.R.
      Virus Genes 9:177-181(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Rhinovirus 3C protease can localize in the nucleus and alter active and passive nucleocytoplasmic transport."
      Ghildyal R., Jordan B., Li D., Dagher H., Bardin P.G., Gern J.E., Jans D.A.
      J. Virol. 83:7349-7352(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF PROTEASE 3C.
    3. "Productive entry pathways of human rhinoviruses."
      Fuchs R., Blaas D.
      Adv. Virol. 2012:826301-826301(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-853.
    5. "The refined structure of human rhinovirus 16 at 2.15-A resolution: implications for the viral life cycle."
      Hadfield A.T., Lee W.M., Zhao R., Oliveira M.A., Minor I., Rueckert R.R., Rossmann M.G.
      Structure 5:427-441(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-853, SEQUENCE REVISION TO 547-548.

    Entry informationi

    Entry nameiPOLG_HRV16
    AccessioniPrimary (citable) accession number: Q82122
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 142 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    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