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Q82122

- POLG_HRV16

UniProt

Q82122 - POLG_HRV16

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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

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
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 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 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 – 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

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        10         20         30         40         50
MGAQVSRQNV GTHSTQNMVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP
60 70 80 90 100
SKFTDPVKDV LEKGIPTLQS PSVEACGYSD RIIQITRGDS TITSQDVANA
110 120 130 140 150
VVGYGVWPHY LTPQDATAID KPTQPDTSSN RFYTLDSKMW NSTSKGWWWK
160 170 180 190 200
LPDALKDMGI FGENMFYHFL GRSGYTVHVQ CNASKFHQGT LLVVMIPEHQ
210 220 230 240 250
LATVNKGNVN AGYKYTHPGE AGREVGTQVE NEKQPSDDNW LNFDGTLLGN
260 270 280 290 300
LLIFPHQFIN LRSNNSATLI VPYVNAVPMD SMVRHNNWSL VIIPVCQLQS
310 320 330 340 350
NNISNIVPIT VSISPMCAEF SGARAKTVVQ GLPVYVTPGS GQFMTTDDMQ
360 370 380 390 400
SPCALPWYHP TKEIFIPGEV KNLIEMCQVD TLIPINSTQS NIGNVSMYTV
410 420 430 440 450
TLSPQTKLAE EIFAIKVDIA SHPLATTLIG EIASYFTHWT GSLRFSFMFC
460 470 480 490 500
GTANTTLKVL LAYTPPGIGK PRSRKEAMLG THVVWDVGLQ STVSLVVPWI
510 520 530 540 550
SASQYRFTTP DTYSSAGYIT CWYQTNFVVP PNTPNTAEML CFVSGCKDFC
560 570 580 590 600
LRMARDTDLH KQTGPITQNP VERYVDEVLN EVLVVPNINQ SHPTTSNAAP
610 620 630 640 650
VLDAAETGHT NKIQPEDTIE TRYVQSSQTL DEMSVESFLG RSGCIHESVL
660 670 680 690 700
DIVDNYNDQS FTKWNINLQE MAQIRRKFEM FTYARFDSEI TMVPSVAAKD
710 720 730 740 750
GHIGHIVMQY MYVPPGAPIP TTRDDYAWQS GTNASVFWQH GQPFPRFSLP
760 770 780 790 800
FLSIASAYYM FYDGYDGDTY KSRYGTVVTN DMGTLCSRIV TSEQLHKVKV
810 820 830 840 850
VTRIYHKAKH TKAWCPRPPR AVQYSHTHTT NYKLSSEVHN DVAIRPRTNL
860 870 880 890 900
TTVGPSDMYV HVGNLIYRNL HLFNSDIHDS ILVSYSSDLI IYRTSTQGDG
910 920 930 940 950
YIPTCNCTEA TYYCKHKNRY YPINVTPHDW YEIQESEYYP KHIQYNLLIG
960 970 980 990 1000
EGPCEPGDCG GKLLCKHGVI GIITAGGEGH VAFIDLRHFH CAEEQGITDY
1010 1020 1030 1040 1050
IHMLGEAFGS GFVDSVKDQI NSINPINNIS SKMVKWMLRI ISAMVIIIRN
1060 1070 1080 1090 1100
SSDPQTIIAT LTLIGCNGSP WRFLKEKFCK WTQLTYIHKE SDSWLKKFTE
1110 1120 1130 1140 1150
MCNAARGLEW IGNKISKFID WMKSMLPQAQ LKVKYLSELK KLNFLEKQVE
1160 1170 1180 1190 1200
NLRAADTNTQ EKIKCEIDTL HDLSCKFLPL YASEAKRIKV LYHKCTNIIK
1210 1220 1230 1240 1250
QKKRSEPVAV MIHGPPGTGK SITTSFLARM ITNESDIYSL PPDPKYFDGY
1260 1270 1280 1290 1300
DNQSVVIMDD IMQNPGGEDM TLFCQMVSSV TFIPPMADLP DKGKPFDSRF
1310 1320 1330 1340 1350
VLCSTNHSLL APPTISSLPA MNRRFYLDLD ILVHDNYKDN QGKLDVSRAF
1360 1370 1380 1390 1400
RLCDVDSKIG NAKCCPFVCG KAVTFKDRNT CRTYSLSQIY NQILEEDKRR
1410 1420 1430 1440 1450
RQVVDVMSAI FQGPISMDKP PPPAITDLLR SVRTPEVIKY CQDNKWIVPA
1460 1470 1480 1490 1500
DCQIERDLNI ANSIITIIAN IISIAGIIYI IYKLFCSLQG PYSGEPKPKT
1510 1520 1530 1540 1550
KVPERRVVAQ GPEEEFGMSI IKNNTCVVTT TNGKFTGLGI YDRILILPTH
1560 1570 1580 1590 1600
ADPGSEIQVN GIHTKVLDSY DLFNKEGVKL EITVLKLDRN EKFRDIRKYI
1610 1620 1630 1640 1650
PESEDDYPEC NLALVANQTE PTIIKVGDVV SYGNILLSGT QTARMLKYNY
1660 1670 1680 1690 1700
PTKSGYCGGV LYKIGQILGI HVGGNGRDGF SSMLLRSYFT EQQGQIQISK
1710 1720 1730 1740 1750
HVKDVGLPSI HTPTKTKLQP SVFYDIFPGS KEPAVLTEKD PRLKVDFDSA
1760 1770 1780 1790 1800
LFSKYKGNTE CSLNEHIQVA VAHYSAQLAT LDIDPQPIAM EDSVFGMDGL
1810 1820 1830 1840 1850
EALDLNTSAG YPYVTLGIKK KDLINNKTKD ISKLKLALDK YDVDLPMITF
1860 1870 1880 1890 1900
LKDELRKKDK IAAGKTRVIE ASSINDTILF RTVYGNLFSK FHLNPGVVTG
1910 1920 1930 1940 1950
CAVGCDPETF WSKIPLMLDG DCIMAFDYTN YDGSIHPIWF KALGMVLDNL
1960 1970 1980 1990 2000
SFNPTLINRL CNSKHIFKST YYEVEGGVPS GCSGTSIFNS MINNIIIRTL
2010 2020 2030 2040 2050
VLDAYKHIDL DKLKIIAYGD DVIFSYKYKL DMEAIAKEGQ KYGLTITPAD
2060 2070 2080 2090 2100
KSSEFKELDY GNVTFLKRGF RQDDKYKFLI HPTFPVEEIY ESIRWTKKPS
2110 2120 2130 2140 2150
QMQEHVLSLC HLMWHNGPEI YKDFETKIRS VSAGRALYIP PYELLRHEWY

EKF
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 29, 2014
This is version 143 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