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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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 By similarity.1 Publication
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.1 Publication

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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 3C Reviewed prediction
Active sitei871 – 8711For Protease 2A activity By similarity
Active sitei888 – 8881For Protease 2A activity By similarity
Active sitei959 – 9591For Protease 2A activity By similarity
Sitei995 – 9962Cleavage; by Protease 3C Reviewed prediction
Sitei1412 – 14132Cleavage; by Protease 3C Reviewed prediction
Sitei1489 – 14902Cleavage; by Protease 3C Reviewed prediction
Sitei1510 – 15112Cleavage; by Protease 3C Reviewed prediction
Active sitei1550 – 15501For Protease 3C activity Reviewed prediction
Active sitei1581 – 15811For Protease 3C activity Reviewed prediction
Active sitei1657 – 16571For Protease 3C activity By similarity
Sitei1693 – 16942Cleavage; by Protease 3C Reviewed prediction
Active sitei2020 – 20201For RdRp activity By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
  2. RNA-protein covalent cross-linking Source: UniProtKB-KW
  3. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
  4. induction by virus of host autophagy Source: UniProtKB
  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. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
  10. suppression by virus of host translation Source: UniProtKB-KW
  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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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 – 14661465Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1467 – 148216 Reviewed prediction
Add
BLAST
Topological domaini1483 – 2153671Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW
  2. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  3. integral to membrane of host cell Source: UniProtKB-KW
  4. membrane 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 host By similarity
Chaini2 – 21532152Genome polyprotein By similarity
PRO_0000426551Add
BLAST
Chaini2 – 853852P1 By similarity
PRO_0000426552Add
BLAST
Chaini2 – 330329Capsid protein VP0 Reviewed prediction
PRO_0000426553Add
BLAST
Chaini2 – 6968Capsid protein VP4 Reviewed prediction
PRO_0000426554Add
BLAST
Chaini70 – 330261Capsid protein VP2 Reviewed prediction
PRO_0000426555Add
BLAST
Chaini331 – 565235Capsid protein VP3 Reviewed prediction
PRO_0000426556Add
BLAST
Chaini565 – 853289Capsid protein VP1 Reviewed prediction
PRO_0000426557Add
BLAST
Chaini853 – 1412560P2 By similarity
PRO_0000426558Add
BLAST
Chaini853 – 995143Protease 2A Reviewed prediction
PRO_0000426559Add
BLAST
Chaini996 – 109095Protein 2B Reviewed prediction
PRO_0000040041Add
BLAST
Chaini1091 – 1412322Protein 2C Reviewed prediction
PRO_0000040042Add
BLAST
Chaini1413 – 2153741P3 By similarity
PRO_0000426560Add
BLAST
Chaini1413 – 151098Protein 3AB Reviewed prediction
PRO_0000426561Add
BLAST
Chaini1413 – 148977Protein 3A Reviewed prediction
PRO_0000040043Add
BLAST
Chaini1490 – 151021Viral protein genome-linked Reviewed prediction
PRO_0000426562Add
BLAST
Chaini1511 – 2153643Protein 3CD Reviewed prediction
PRO_0000426563Add
BLAST
Chaini1511 – 1692182Protease 3C Reviewed prediction
PRO_0000426564Add
BLAST
Chaini1693 – 2153461RNA-directed RNA polymerase By similarity
PRO_0000426565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By similarity
Modified residuei1492 – 14921O-(5'-phospho-RNA)-tyrosine By 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.
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.
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.
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.
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.

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.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ82122.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1186 – 1346161SF3 helicase
Add
BLAST
Domaini1511 – 1676166Peptidase C3
Add
BLAST
Domaini1921 – 2034114RdRp catalytic
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni565 – 58218Amphipatic alpha-helix Reviewed prediction
Add
BLAST
Regioni1413 – 142715Disordered By similarity
Add
BLAST

Sequence similaritiesi

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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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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti547 – 5482KD → NH in AAA69862. 1 Publication

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: July 9, 2014
This is version 141 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

Similar proteinsi