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P04936

- POLG_HRV2

UniProt

P04936 - POLG_HRV2

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Protein
Genome polyprotein
Gene
N/A
Organism
Human rhinovirus 2 (HRV-2)
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 VLDLR 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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 By similarity.3 Publications
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.3 Publications

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 sitei868 – 8681For Protease 2A activity
Active sitei885 – 8851For Protease 2A activity
Active sitei956 – 9561For Protease 2A activity
Sitei992 – 9932Cleavage; by Protease 3C Reviewed prediction
Sitei1409 – 14102Cleavage; by Protease 3C Reviewed prediction
Sitei1486 – 14872Cleavage; by Protease 3C Reviewed prediction
Sitei1507 – 15082Cleavage; by Protease 3C Reviewed prediction
Active sitei1547 – 15471For Protease 3C activity Reviewed prediction
Active sitei1578 – 15781For Protease 3C activity Reviewed prediction
Active sitei1654 – 16541For Protease 3C activity Inferred
Sitei1690 – 16912Cleavage; by Protease 3C Reviewed prediction
Active sitei2017 – 20171For 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
Complete GO annotation...

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

Enzyme and pathway databases

SABIO-RKP04936.

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 2 (HRV-2)
Taxonomic identifieri12130 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusRhinovirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007682: 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 – 14631462Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1464 – 147916 Reviewed prediction
Add
BLAST
Topological domaini1480 – 2150671Cytoplasmic 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 – 21502149Genome polyprotein By similarity
PRO_0000426506Add
BLAST
Chaini2 – 844843P1 By similarity
PRO_0000426507Add
BLAST
Chaini2 – 330329Capsid protein VP0 Reviewed prediction
PRO_0000426508Add
BLAST
Chaini2 – 6968Capsid protein VP4 Reviewed prediction
PRO_0000426509Add
BLAST
Chaini70 – 330261Capsid protein VP2 Reviewed prediction
PRO_0000426510Add
BLAST
Chaini331 – 565235Capsid protein VP3 Reviewed prediction
PRO_0000426511Add
BLAST
Chaini565 – 844280Capsid protein VP1 Reviewed prediction
PRO_0000426512Add
BLAST
Chaini845 – 1409565P2 By similarity
PRO_0000426513Add
BLAST
Chaini845 – 992148Protease 2A Reviewed prediction
PRO_0000426514Add
BLAST
Chaini993 – 108795Protein 2B Reviewed prediction
PRO_0000040015Add
BLAST
Chaini1088 – 1409322Protein 2C Reviewed prediction
PRO_0000040016Add
BLAST
Chaini1410 – 2150741P3 By similarity
PRO_0000426515Add
BLAST
Chaini1410 – 150798Protein 3AB Reviewed prediction
PRO_0000426516Add
BLAST
Chaini1410 – 148677Protein 3A Reviewed prediction
PRO_0000040017Add
BLAST
Chaini1487 – 150721Viral protein genome-linked Reviewed prediction
PRO_0000426517Add
BLAST
Chaini1508 – 2150643Protein 3CD Reviewed prediction
PRO_0000426518Add
BLAST
Chaini1508 – 1689182Protease 3C Reviewed prediction
PRO_0000426519Add
BLAST
Chaini1690 – 2150461RNA-directed RNA polymerase By similarity
PRO_0000426520Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By similarity
Modified residuei1489 – 14891O-(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. Interact with host VLDLR. 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 strandi33 – 353
Helixi36 – 383
Turni52 – 543
Beta strandi83 – 864
Beta strandi91 – 966
Helixi103 – 1053
Turni113 – 1153
Beta strandi117 – 1193
Helixi126 – 1283
Beta strandi138 – 1403
Beta strandi147 – 1515
Helixi153 – 1553
Helixi159 – 1679
Beta strandi168 – 18013
Beta strandi187 – 19711
Beta strandi203 – 2086
Helixi213 – 2164
Helixi219 – 2213
Helixi233 – 2353
Helixi241 – 2433
Turni244 – 2474
Helixi253 – 2553
Beta strandi256 – 2627
Turni263 – 2653
Beta strandi267 – 2737
Beta strandi278 – 2825
Turni284 – 2863
Beta strandi290 – 30516
Beta strandi309 – 32517
Turni338 – 3414
Beta strandi353 – 3553
Beta strandi367 – 3726
Helixi374 – 3774
Turni389 – 3935
Helixi395 – 3984
Beta strandi399 – 4035
Beta strandi411 – 4166
Beta strandi418 – 4214
Helixi424 – 4263
Helixi428 – 4336
Beta strandi436 – 4416
Beta strandi443 – 4497
Beta strandi456 – 4649
Beta strandi466 – 4683
Helixi474 – 4785
Beta strandi480 – 48910
Beta strandi492 – 4976
Beta strandi502 – 5043
Beta strandi506 – 5094
Beta strandi517 – 5248
Beta strandi530 – 5323
Beta strandi534 – 54411
Beta strandi549 – 5535
Turni572 – 5798
Beta strandi581 – 5833
Beta strandi599 – 6024
Helixi604 – 6063
Helixi614 – 6174
Helixi630 – 6323
Helixi634 – 6385
Beta strandi642 – 6509
Turni654 – 6585
Beta strandi661 – 6655
Helixi672 – 6787
Beta strandi681 – 69818
Beta strandi707 – 7137
Helixi726 – 7294
Beta strandi731 – 7333
Beta strandi735 – 7395
Beta strandi746 – 7494
Beta strandi754 – 7607
Turni774 – 7774
Beta strandi782 – 7876
Beta strandi796 – 81419
Beta strandi855 – 86612
Helixi867 – 8693
Helixi874 – 8763
Beta strandi878 – 8814
Helixi882 – 8843
Beta strandi886 – 89611
Beta strandi906 – 9116
Turni912 – 9154
Beta strandi916 – 9216
Beta strandi923 – 9308
Beta strandi938 – 94811
Beta strandi959 – 9624
Beta strandi965 – 9739
Beta strandi975 – 9828
Helixi983 – 9864
Helixi1509 – 152113
Beta strandi1522 – 15276
Beta strandi1530 – 153910
Beta strandi1541 – 15455
Helixi1546 – 15483
Beta strandi1552 – 15565
Beta strandi1559 – 157012
Beta strandi1576 – 15849
Helixi1593 – 15964
Beta strandi1604 – 16118
Beta strandi1615 – 16173
Beta strandi1619 – 162810
Beta strandi1632 – 16343
Beta strandi1637 – 16393
Beta strandi1641 – 16455
Helixi1651 – 16533
Beta strandi1657 – 16604
Beta strandi1663 – 16719
Beta strandi1676 – 16805
Helixi1683 – 16853

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3RX-ray2.10P225-239[»]
1CQQX-ray1.85A1508-1687[»]
1FPNX-ray2.601568-856[»]
270-330[»]
3331-567[»]
42-69[»]
1V9UX-ray3.601568-856[»]
270-330[»]
3331-567[»]
42-69[»]
2HRVX-ray1.95A/B851-992[»]
2XYAX-ray2.40A1508-1687[»]
3DPRX-ray3.50A568-856[»]
B70-330[»]
C331-567[»]
D2-69[»]
3TN9X-ray3.001568-856[»]
270-330[»]
3331-567[»]
3VDDX-ray3.20A568-850[»]
B70-330[»]
C331-567[»]
D1-69[»]
4L3BX-ray6.50A568-856[»]
B70-330[»]
C331-567[»]
ProteinModelPortaliP04936.
SMRiP04936. Positions 2-68, 81-567, 582-989, 1508-1687, 1691-2150.

Miscellaneous databases

EvolutionaryTraceiP04936.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1181 – 1343163SF3 helicase
Add
BLAST
Domaini1508 – 1673166Peptidase C3
Add
BLAST
Domaini1918 – 2031114RdRp catalytic
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni565 – 58117Amphipatic alpha-helix Reviewed prediction
Add
BLAST
Regioni1410 – 142415Disordered 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.

P04936-1 [UniParc]FASTAAdd to Basket

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MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASNG ASKLEFTQDP     50
SKFTDPVKDV LEKGIPTLQS PTVEACGYSD RIIQITRGDS TITSQDVANA 100
IVAYGVWPHY LSSKDASAID KPSQPDTSSN RFYTLRSVTW SSSSKGWWWK 150
LPDALKDMGI FGENMFYHYL GRSGYTIHVQ CNASKFHQGT LIVALIPEHQ 200
IASALHGNVN VGYNYTHPGE TGREVKAETR LNPDLQPTEE YWLNFDGTLL 250
GNITIFPHQF INLRSNNSAT IIAPYVNAVP MDSMRSHNNW SLVIIPICPL 300
ETSSAINTIP ITISISPMCA EFSGARAKRQ GLPVFITPGS GQFLTTDDFQ 350
SPCALPWYHP TKEISIPGEV KNLVEICQVD SLVPINNTDT YINSENMYSV 400
VLQSSINAPD KIFSIRTDVA SQPLATTLIG EISSYFTHWT GSLRFSFMFC 450
GTANTTVKLL LAYTPPGIAE PTTRKDAMLG THVIWDVGLQ STISMVVPWI 500
SASHYRNTSP GRSTSGYITC WYQTRLVIPP QTPPTARLLC FVSGCKDFCL 550
RMARDTNLHL QSGAIAQNPV ENYIDEVLNE VLVVPNINSS NPTTSNSAPA 600
LDAAETGHTS SVQPEDVIET RYVQTSQTRD EMSLESFLGR SGCIHESKLE 650
VTLANYNKEN FTVWAINLQE MAQIRRKFEL FTYTRFDSEI TLVPCISALS 700
QDIGHITMQY MYVPPGAPVP NSRDDYAWQS GTNASVFWQH GQAYPRFSLP 750
FLSVASAYYM FYDGYDEQDQ NYGTANTNNM GSLCSRIVTE KHIHKVHIMT 800
RIYHKAKHVK AWCPRPPRAL EYTRAHRTNF KIEDRSIQTA IVTRPIITTA 850
GPSDMYVHVG NLIYRNLHLF NSEMHESILV SYSSDLIIYR TNTVGDDYIP 900
SCDCTQATYY CKHKNRYFPI TVTSHDWYEI QESEYYPKHI QYNLLIGEGP 950
CEPGDCGGKL LCKHGVIGIV TAGGDNHVAF IDLRHFHCAE EQGVTDYIHM 1000
LGEAFGNGFV DSVKEHIHAI NPVGNISKKI IKWMLRIISA MVIIIRNSSD 1050
PQTILATLTL IGCSGSPWRF LKEKFCKWTQ LNYIHKESDS WLKKFTEACN 1100
AARGLEWIGN KISKFIEWMK SMLPQAQLKV KYLNELKKLN LYEKQVESLR 1150
VADMKTQEKI KMEIDTLHDL SRKFLPLYAS EAKRIKTLYI KCDNIIKQKK 1200
RCEPVAIVIH GPPGAGKSIT TNFLAKMITN DSDIYSLPPD PKYFDGYDQQ 1250
SVVIMDDIMQ NPAGDDMTLF CQMVSSVTFI PPMADLPDKG KAFDSRFVLC 1300
STNHSLLTPP TITSLPAMNR RFFLDLDIIV HDNFKDPQGK LNVAAAFRPC 1350
DVDNRIGNAR CCPFVCGKAV SFKDRNSCNK YSLAQVYNIM IEEDRRRRQV 1400
VDVMTAIFQG PIDMKNPPPP AITDLLQSVR TPEVIKYCEG NRWIIPAECK 1450
IEKELNLANT IITIIANVIG MARIIYVIYK LFCTLQGPYS GEPKPKTKIP 1500
ERRVVTQGPE EEFGMSLIKH NSCVITTENG KFTGLGVYDR FVVVPTHADP 1550
GKEIQVDGIT TKVIDSYDLY NKNGIKLEIT VLKLDRNEKF RDIRRYIPNN 1600
EDDYPNCNLA LLANQPEPTI INVGDVVSYG NILLSGNQTA RMLKYSYPTK 1650
SGYCGGVLYK IGQVLGIHVG GNGRDGFSAM LLRSYFTDVQ GQITLSKKTS 1700
ECNLPSIHTP CKTKLQPSVF YDVFPGSKEP AVLSEKDARL QVDFNEALFS 1750
KYKGNTDCSI NDHIRIASSH YAAQLITLDI DPKPITLEDS VFGTDGLEAL 1800
DLNTSAGFPY IAMGVKKRDL INNKTKDISK LKEAIDKYGV DLPMVTFLKD 1850
ELRKHEKVIK GKTRVIEASS VNDTLLFRTT FGNLFSKFHL NPGIVTGSAV 1900
GCDPEVFWSK IPAMLDDKCI MAFDYTNYDG SIHPIWFEAL KQVLVDLSFN 1950
PTLIDRLCKS KHIFKNTYYE VEGGVPSGCS GTSIFNTMIN NIIIRTLVLD 2000
AYKNIDLDKL KIIAYGDDVI FSYIHELDME AIAIEGVKYG LTITPADKSN 2050
TFVKLDYSNV TFLKRGFKQD EKYNFLIHPT FPEDEIFESI RWTKKPSQMH 2100
EHVLSLCHLM WHNGRDAYKK FVEKIRSVSA GRALYIPPYD LLLHEWYEKF 2150
Length:2,150
Mass (Da):241,978
Last modified:January 23, 2007 - v3
Checksum:i6E0DF9F4945D9D0C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02316 Genomic RNA. Translation: CAA26181.1.
PIRiA03902. GNNYH2.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure complexed with cellular receptor fragment

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02316 Genomic RNA. Translation: CAA26181.1 .
PIRi A03902. GNNYH2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A3R X-ray 2.10 P 225-239 [» ]
1CQQ X-ray 1.85 A 1508-1687 [» ]
1FPN X-ray 2.60 1 568-856 [» ]
2 70-330 [» ]
3 331-567 [» ]
4 2-69 [» ]
1V9U X-ray 3.60 1 568-856 [» ]
2 70-330 [» ]
3 331-567 [» ]
4 2-69 [» ]
2HRV X-ray 1.95 A/B 851-992 [» ]
2XYA X-ray 2.40 A 1508-1687 [» ]
3DPR X-ray 3.50 A 568-856 [» ]
B 70-330 [» ]
C 331-567 [» ]
D 2-69 [» ]
3TN9 X-ray 3.00 1 568-856 [» ]
2 70-330 [» ]
3 331-567 [» ]
3VDD X-ray 3.20 A 568-850 [» ]
B 70-330 [» ]
C 331-567 [» ]
D 1-69 [» ]
4L3B X-ray 6.50 A 568-856 [» ]
B 70-330 [» ]
C 331-567 [» ]
ProteinModelPortali P04936.
SMRi P04936. Positions 2-68, 81-567, 582-989, 1508-1687, 1691-2150.
ModBasei Search...

Protein family/group databases

MEROPSi C03.007.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P04936.

Miscellaneous databases

EvolutionaryTracei P04936.

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. "Human rhinovirus 2: complete nucleotide sequence and proteolytic processing signals in the capsid protein region."
    Skern T., Sommergruber W., Blaas D., Gruendler P., Fraundorfer F., Pieler C., Fogy I., Kuechler E.
    Nucleic Acids Res. 13:2111-2126(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Kuechler E.
    Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro."
    Glaser W., Skern T.
    FEBS Lett. 480:151-155(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE LEADER PROTEASE.
  4. "The concerted conformational changes during human rhinovirus 2 uncoating."
    Hewat E.A., Neumann E., Blaas D.
    Mol. Cell 10:317-326(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF VP1 AND VP4.
  5. "Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease."
    Park N., Skern T., Gustin K.E.
    J. Biol. Chem. 285:28796-28805(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF PROTEASE 2A.
  6. Cited for: REVIEW.
  7. "Productive entry pathways of human rhinoviruses."
    Fuchs R., Blaas D.
    Adv. Virol. 2012:826301-826301(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. "Three-dimensional structure of the Fab fragment of a neutralizing antibody to human rhinovirus serotype 2."
    Tormo J., Stadler E., Skern T., Auer H., Kanzler O., Betzel C., Blaas D., Fita I.
    Protein Sci. 1:1154-1161(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-239.
  9. "The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis."
    Petersen J.F., Cherney M.M., Liebig H.D., Skern T., Kuechler E., James M.N.
    EMBO J. 18:5463-5475(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 851-992.
  10. "Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes."
    Matthews D.A., Dragovich P.S., Webber S.E., Fuhrman S.A., Patick A.K., Zalman L.S., Hendrickson T.F., Love R.A., Prins T.J., Marakovits J.T., Zhou R., Tikhe J., Ford C.E., Meador J.W., Ferre R.A., Brown E.L., Binford S.L., Brothers M.A., DeLisle D.M., Worland S.T.
    Proc. Natl. Acad. Sci. U.S.A. 96:11000-11007(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1508-1687.
  11. "Structure of human rhinovirus serotype 2 (HRV2)."
    Verdaguer N., Blaas D., Fita I.
    J. Mol. Biol. 300:1179-1194(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 71-856.

Entry informationi

Entry nameiPOLG_HRV2
AccessioniPrimary (citable) accession number: P04936
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 157 of the entry and version 3 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

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