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P03303

- POLG_HRV14

UniProt

P03303 - POLG_HRV14

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Protein

Genome polyprotein

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

Functioni

Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host ICAM1 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks By similarity.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
Sitei69 – 702Cleavage; by autolysis Reviewed prediction
Sitei331 – 3322Cleavage; by Protease 3C Reviewed prediction
Sitei856 – 8572Cleavage; by Protease 2A Reviewed prediction
Active sitei876 – 8761For Protease 2A activity By similarity
Active sitei894 – 8941For Protease 2A activity By similarity
Active sitei965 – 9651For Protease 2A activity By similarity
Sitei1002 – 10032Cleavage; by Protease 3C Reviewed prediction
Sitei1429 – 14302Cleavage; by Protease 3C Reviewed prediction
Sitei1514 – 15152Cleavage; by Protease 3C Reviewed prediction
Sitei1537 – 15382Cleavage; by Protease 3C Reviewed prediction
Active sitei1577 – 15771For Protease 3C activity Reviewed prediction
Active sitei1608 – 16081For Protease 3C activity Reviewed prediction
Active sitei1683 – 16831For Protease 3C activity By similarity
Sitei1719 – 17202Cleavage; by Protease 3C Reviewed prediction
Active sitei2046 – 20461For RdRp activity By similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

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

Keywords - Biological processi

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

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.013.

Names & Taxonomyi

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

Subcellular locationi

Chain Capsid protein VP0 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP2 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP3 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP1 : Virion By similarity. Host cytoplasm By similarity
Chain Protein 2B : Host cytoplasmic vesicle membrane; 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 – 14911490Cytoplasmic Reviewed predictionAdd
BLAST
Intramembranei1492 – 150716 Reviewed predictionAdd
BLAST
Topological domaini1508 – 2179672Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. integral to membrane of host cell Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW
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 – 21792178Genome polyprotein By similarityPRO_0000426536Add
BLAST
Chaini2 – 856855P1 By similarityPRO_0000426537Add
BLAST
Chaini2 – 331330Capsid protein VP0 Reviewed predictionPRO_0000426538Add
BLAST
Chaini2 – 6968Capsid protein VP4 Reviewed predictionPRO_0000426539Add
BLAST
Chaini70 – 331262Capsid protein VP2 Reviewed predictionPRO_0000426540Add
BLAST
Chaini332 – 563232Capsid protein VP3 Reviewed predictionPRO_0000426541Add
BLAST
Chaini564 – 856293Capsid protein VP1 Reviewed predictionPRO_0000426542Add
BLAST
Chaini857 – 1429573P2 By similarityPRO_0000426543Add
BLAST
Chaini857 – 1002146Protease 2A Reviewed predictionPRO_0000040029Add
BLAST
Chaini1003 – 109997Protein 2B Reviewed predictionPRO_0000040030Add
BLAST
Chaini1101 – 1429329Protein 2C Reviewed predictionPRO_0000426544Add
BLAST
Chaini1430 – 2179750P3 By similarityPRO_0000426545Add
BLAST
Chaini1430 – 1537108Protein 3AB Reviewed predictionPRO_0000426546Add
BLAST
Chaini1430 – 151485Protein 3A Reviewed predictionPRO_0000040032Add
BLAST
Chaini1515 – 153723Viral protein genome-linked Reviewed predictionPRO_0000426547Add
BLAST
Chaini1538 – 2179642Protein 3CD Reviewed predictionPRO_0000426548Add
BLAST
Chaini1538 – 1718181Protease 3C Reviewed predictionPRO_0000426549Add
BLAST
Chaini1719 – 2179461RNA-directed RNA polymerase By similarityPRO_0000426550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By similarity
Modified residuei1517 – 15171O-(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 ICAM1. Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid By similarity. Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid By similarity. Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 By similarity. Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis By similarity. Protein 3AB: interacts with protein 3CD By similarity. Viral protein genome-linked: interacts with RNA-directed RNA polymerase By similarity. Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD By similarity.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP03303.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1205 – 1361157SF3 helicaseAdd
BLAST
Domaini1538 – 1702165Peptidase C3Add
BLAST
Domaini1946 – 2060115RdRp catalyticAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni564 – 58421Amphipatic alpha-helix Reviewed predictionAdd
BLAST
Regioni1430 – 145122Disordered By similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

P03303-1 [UniParc]FASTAAdd to Basket

« Hide

MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASTS SAGQSLSMDP     50
SKFTEPVKDL MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA 100
VVCYAEWPEY LPDVDASDVN KTSKPDTSVC RFYTLDSKTW TTGSKGWCWK 150
LPDALKDMGV FGQNMFFHSL GRSGYTVHVQ CNATKFHSGC LLVVVIPEHQ 200
LASHEGGNVS VKYTFTHPGE RGIDLSSANE VGGPVKDVIY NMNGTLLGNL 250
LIFPHQFINL RTNNTATIVI PYINSVPIDS MTRHNNVSLM VIPIAPLTVP 300
TGATPSLPIT VTIAPMCTEF SGIRSKSIVP QGLPTTTLPG SGQFLTTDDR 350
QSPSALPNYE PTPRIHIPGK VHNLLEIIQV DTLIPMNNTH TKDEVNSYLI 400
PLNANRQNEQ VFGTNLFIGD GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG 450
PALSSAKLIL AYTPPGARGP QDRREAMLGT HVVWDIGLQS TIVMTIPWTS 500
GVQFRYTDPD TYTSAGFLSC WYQTSLILPP ETTGQVYLLS FISACPDFKL 550
RLMKDTQTIS QTVALTEGLG DELEEVIVEK TKQTVASISS GPKHTQKVPI 600
LTANETGATM PVLPSDSIET RTTYMHFNGS ETDVECFLGR AACVHVTEIQ 650
NKDATGIDNH REAKLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT 700
ASQPDSANYS SNLVVQAMYV PPGAPNPKEW DDYTWQSASN PSVFFKVGDT 750
SRFSVPYVGL ASAYNCFYDG YSHDDAETQY GITVLNHMGS MAFRIVNEHD 800
EHKTLVKIRV YHRAKHVEAW IPRAPRALPY TSIGRTNYPK NTEPVIKKRK 850
GDIKSYGLGP RYGGIYTSNV KIMNYHLMTP EDHHNLIAPY PNRDLAIVST 900
GGHGAETIPH CNCTSGVYYS TYYRKYYPII CEKPTNIWIE GNPYYPSRFQ 950
AGVMKGVGPA EPGDCGGILR CIHGPIGLLT AGGSGYVCFA DIRQLECIAE 1000
EQGLSDYITG LGRAFGVGFT DQISTKVTEL QEVAKDFLTT KVLSKVVKMV 1050
SALVIICRNH DDLVTVTATL ALLGCDGSPW RFLKMYISKH FQVPYIERQA 1100
NDGWFRKFND ACNAAKGLEW IANKISKLIE WIKNKVLPQA KEKLEFCSKL 1150
KQLDILERQI TTMHISNPTQ EKREQLFNNV LWLEQMSQKF APLYAVESKR 1200
IRELKNKMVN YMQFKSKQRI EPVCVLIHGT PGSGKSLTTS IVGRAIAEHF 1250
NSAVYSLPPD PKHFDGYQQQ EVVIMDDLNQ NPDGQDISMF CQMVSSVDFL 1300
PPMASLDNKG MLFTSNFVLA STNSNTLSPP TILNPEALVR RFGFDLDICL 1350
HTTYTKNGKL NAGMSTKTCK DCHQPSNFKK CCPLVCGKAI SLVDRTTNIR 1400
YSVDQLVTAI ISDFKSKMQI TDSLETLFQG PVYKDLEIDV CNTPPPECIN 1450
DLLKSVDSEE IREYCKKKKW IIPEIPTNIE RAMNQASMII NTILMFVSTL 1500
GIVYVIYKLF AQTQGPYSGN PPHNKLKAPT LRPVVVQGPN TEFALSLLRK 1550
NIMTITTSKG EFTGLGIHDR VCVIPTHAQP GDDVLVNGQK IRVKDKYKLV 1600
DPENINLELT VLTLDRNEKF RDIRGFISED LEGVDATLVV HSNNFTNTIL 1650
EVGPVTMAGL INLSSTPTNR MIRYDYATKT GQCGGVLCAT GKIFGIHVGG 1700
NGRQGFSAQL KKQYFVEKQG QVIARHKVRE FNINPVNTPT KSKLHPSVFY 1750
DVFPGDKEPA VLSDNDPRLE VKLTESLFSK YKGNVNTEPT ENMLVAVDHY 1800
AGQLLSLDIP TSELTLKEAL YGVDGLEPID ITTSAGFPYV SLGIKKRDIL 1850
NKETQDTEKM KFYLDKYGID LPLVTYIKDE LRSVDKVRLG KSRLIEASSL 1900
NDSVNMRMKL GNLYKAFHQN PGVLTGSAVG CDPDVFWSVI PCLMDGHLMA 1950
FDYSNFDASL SPVWFVCLEK VLTKLGFAGS SLIQSICNTH HIFRDEIYVV 2000
EGGMPSGCSG TSIFNSMINN IIIRTLILDA YKGIDLDKLK ILAYGDDLIV 2050
SYPYELDPQV LATLGKNYGL TITPPDKSET FTKMTWENLT FLKRYFKPDQ 2100
QFPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCMLAW HSGEKEYNEF 2150
IQKIRTTDIG KCLILPEYSV LRRRWLDLF 2179
Length:2,179
Mass (Da):242,991
Last modified:January 23, 2007 - v3
Checksum:i827201A3032F0285
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 3681P → L in AAA45756. 1 Publication
Sequence conflicti459 – 4591I → T in AAA45756. 1 Publication
Sequence conflicti722 – 7221P → H in AAA45756. 1 Publication
Sequence conflicti726 – 7272NP → KS1 Publication
Sequence conflicti729 – 7313EWD → RVG1 Publication
Sequence conflicti913 – 9131C → R in AAA45756. 1 Publication
Sequence conflicti942 – 9421N → S in AAA45756. 1 Publication
Sequence conflicti962 – 9621P → L in AAA45756. 1 Publication
Sequence conflicti982 – 9821G → E in AAA45756. 1 Publication
Sequence conflicti1193 – 11931L → F in AAA45756. 1 Publication
Sequence conflicti1193 – 11931L → H in AAA45758. 1 Publication
Sequence conflicti1220 – 12201I → T1 Publication
Sequence conflicti1220 – 12201I → T1 Publication
Sequence conflicti1399 – 13991I → V1 Publication
Sequence conflicti1399 – 13991I → V1 Publication
Sequence conflicti1446 – 14461P → S in AAA45756. 1 Publication
Sequence conflicti1739 – 17391P → A in AAA45756. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01087 Genomic RNA. Translation: CAA25565.1.
L05355 Genomic RNA. Translation: AAA45758.1.
K02121 Genomic RNA. Translation: AAA45756.1.
PIRiA03901. GNNYH4.
RefSeqiNP_041009.1. NC_001490.1.

Genome annotation databases

GeneIDi1461213.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with antiviral compound SCH 38057

Virus Particle ExploreR db

Icosahedral capsid structure complexed with antiviral compound SDZ 35-682

Sequence databases

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

3D structure databases

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

Protein family/group databases

MEROPSi C03.013.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1461213.

Miscellaneous databases

EvolutionaryTracei P03303.

Family and domain databases

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

Publicationsi

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

Entry informationi

Entry nameiPOLG_HRV14
AccessioniPrimary (citable) accession number: P03303
Secondary accession number(s): Q82083
, Q82123, Q84736, Q84737, Q84738, Q84739, Q84740, Q84741, Q84774, Q84775, Q84776, Q84777, Q84778, Q84779, Q89441, Q89649, Q89763, Q89883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Caution

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

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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