Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P23008

- POLG_HRV1A

UniProt

P23008 - POLG_HRV1A

(max 400 entries)x

Your basket is currently empty.

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

Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 1A (HRV-1A)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).By similarity
Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).By similarity
Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).By similarity
Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 (By similarity).By similarity
Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity (By similarity).By similarity
Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).By similarity
Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).By similarity
Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).By similarity
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).By similarity
RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated (By similarity).PROSITE-ProRule annotation

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
NTP + H2O = NDP + phosphate.

Enzyme regulationi

RNA-directed RNA polymerase: replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei332 – 3332Cleavage; by Protease 3CSequence Analysis
Active sitei875 – 8751For Protease 2A activityBy similarity
Active sitei892 – 8921For Protease 2A activityBy similarity
Active sitei963 – 9631For Protease 2A activityBy similarity
Sitei999 – 10002Cleavage; by Protease 3CSequence Analysis
Sitei1416 – 14172Cleavage; by Protease 3CSequence Analysis
Sitei1493 – 14942Cleavage; by Protease 3CSequence Analysis
Sitei1514 – 15152Cleavage; by Protease 3CSequence Analysis
Active sitei1554 – 15541For Protease 3C activitySequence Analysis
Active sitei1585 – 15851For Protease 3C activitySequence Analysis
Active sitei1661 – 16611For Protease 3C activityBy similarity
Sitei1697 – 16982Cleavage; by Protease 3CSequence Analysis
Active sitei2024 – 20241For RdRp activityBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

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

Keywords - Biological processi

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

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 17 chains:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
Protease 2A (EC:3.4.22.29)
Short name:
P2A
Alternative name(s):
Picornain 2A
Protein 2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Alternative name(s):
Protein 3B
Short name:
P3B
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
OrganismiHuman rhinovirus 1A (HRV-1A)
Taxonomic identifieri12134 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusRhinovirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000013736: Genome

Subcellular locationi

Chain Capsid protein VP0 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP2 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP3 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP1 : Virion By similarity. Host cytoplasm By similarity
Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 3AB : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 3CD : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain RNA-directed RNA polymerase : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 14701469CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei1471 – 148616Sequence AnalysisAdd
BLAST
Topological domaini1487 – 2157671CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 21572156Genome polyproteinBy similarityPRO_0000426476Add
BLAST
Chaini2 – 857856P1By similarityPRO_0000426477Add
BLAST
Chaini2 – 332331Capsid protein VP0Sequence AnalysisPRO_0000426478Add
BLAST
Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426479Add
BLAST
Chaini70 – 332263Capsid protein VP2Sequence AnalysisPRO_0000426480Add
BLAST
Chaini333 – 567235Capsid protein VP3Sequence AnalysisPRO_0000426481Add
BLAST
Chaini567 – 857291Capsid protein VP1Sequence AnalysisPRO_0000426482Add
BLAST
Chaini857 – 1416560P2By similarityPRO_0000426483Add
BLAST
Chaini857 – 999143Protease 2ASequence AnalysisPRO_0000426484Add
BLAST
Chaini1000 – 109495Protein 2BSequence AnalysisPRO_5000438367Add
BLAST
Chaini1095 – 1416322Protein 2CSequence AnalysisPRO_5000438368Add
BLAST
Chaini1417 – 2157741P3By similarityPRO_0000426485Add
BLAST
Chaini1417 – 151498Protein 3ABSequence AnalysisPRO_0000426486Add
BLAST
Chaini1417 – 149377Protein 3ASequence AnalysisPRO_5000438369Add
BLAST
Chaini1494 – 151421Viral protein genome-linkedSequence AnalysisPRO_0000426487Add
BLAST
Chaini1515 – 2157643Protein 3CDSequence AnalysisPRO_0000426488Add
BLAST
Chaini1515 – 1696182Protease 3CSequence AnalysisPRO_0000426489Add
BLAST
Chaini1697 – 2157461RNA-directed RNA polymeraseBy similarityPRO_0000426490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Modified residuei1496 – 14961O-(5'-phospho-RNA)-tyrosineBy similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus 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).By similarity
Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion (By similarity).By similarity
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.By similarity
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion (By similarity).By similarity
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication (By similarity).By similarity

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Capsid protein VP1: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid (By similarity). Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 (By similarity). Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity). Protein 3AB: interacts with protein 3CD (By similarity). Viral protein genome-linked: interacts with RNA-directed RNA polymerase (By similarity). Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD (By similarity).By similarity

Structurei

Secondary structure

1
2157
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi27 – 304Combined sources
Beta strandi33 – 353Combined sources
Helixi36 – 383Combined sources
Beta strandi83 – 864Combined sources
Beta strandi91 – 966Combined sources
Helixi103 – 1053Combined sources
Turni113 – 1153Combined sources
Beta strandi127 – 1315Combined sources
Beta strandi146 – 1505Combined sources
Helixi151 – 1544Combined sources
Beta strandi156 – 1583Combined sources
Helixi161 – 1644Combined sources
Beta strandi167 – 18014Combined sources
Beta strandi190 – 1989Combined sources
Beta strandi203 – 2086Combined sources
Turni214 – 2163Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi231 – 2333Combined sources
Turni240 – 2467Combined sources
Helixi252 – 2543Combined sources
Beta strandi255 – 2617Combined sources
Turni262 – 2643Combined sources
Beta strandi266 – 2727Combined sources
Beta strandi276 – 2827Combined sources
Turni283 – 2853Combined sources
Beta strandi289 – 2979Combined sources
Beta strandi310 – 32516Combined sources
Turni340 – 3434Combined sources
Beta strandi355 – 3573Combined sources
Helixi375 – 3795Combined sources
Helixi391 – 3933Combined sources
Helixi398 – 4003Combined sources
Beta strandi401 – 4044Combined sources
Beta strandi408 – 4114Combined sources
Beta strandi413 – 4186Combined sources
Beta strandi421 – 4233Combined sources
Helixi432 – 4354Combined sources
Beta strandi438 – 4436Combined sources
Beta strandi445 – 4517Combined sources
Beta strandi458 – 4669Combined sources
Helixi476 – 4805Combined sources
Beta strandi482 – 4887Combined sources
Beta strandi490 – 4923Combined sources
Beta strandi494 – 4996Combined sources
Beta strandi504 – 5118Combined sources
Beta strandi520 – 53011Combined sources
Beta strandi533 – 5353Combined sources
Beta strandi539 – 5479Combined sources
Beta strandi552 – 5565Combined sources
Helixi576 – 5805Combined sources
Beta strandi584 – 5863Combined sources
Helixi607 – 6093Combined sources
Helixi617 – 6204Combined sources
Beta strandi633 – 6364Combined sources
Helixi637 – 6415Combined sources
Beta strandi645 – 6539Combined sources
Beta strandi656 – 6605Combined sources
Beta strandi667 – 6704Combined sources
Helixi679 – 6835Combined sources
Beta strandi686 – 70318Combined sources
Beta strandi713 – 7186Combined sources
Beta strandi720 – 7223Combined sources
Beta strandi726 – 7294Combined sources
Helixi732 – 7343Combined sources
Beta strandi738 – 7436Combined sources
Beta strandi751 – 7544Combined sources
Beta strandi759 – 7657Combined sources
Beta strandi789 – 7935Combined sources
Beta strandi803 – 82119Combined sources
Beta strandi831 – 8344Combined sources
Beta strandi840 – 8423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYMX-ray2.1542-69[»]
1AYNX-ray2.9042-69[»]
1R1AX-ray3.201571-857[»]
270-332[»]
3333-570[»]
42-45[»]
2HWDX-ray3.801571-857[»]
270-332[»]
3333-570[»]
42-45[»]
2HWEX-ray3.801571-857[»]
270-332[»]
3333-570[»]
42-45[»]
2HWFX-ray3.801571-857[»]
270-332[»]
3333-570[»]
42-45[»]
ProteinModelPortaliP23008.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23008.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1188 – 1350163SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1515 – 1680166Peptidase C3Add
BLAST
Domaini1925 – 2038114RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni567 – 58418Amphipatic alpha-helixSequence AnalysisAdd
BLAST
Regioni1417 – 143115DisorderedBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 1 peptidase C3 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
4.10.80.10. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
ProDomiPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P23008-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP
60 70 80 90 100
SKFTDPVKDV LEKGIPTLQS PSVEACGYSD RIMQITRGDS TITSQDVANA
110 120 130 140 150
VVGYGVWPHY LTPQDATAID KPTQPDTSSN RFYTLESKHW NGSSKGWWWK
160 170 180 190 200
LPDALKDMGI FGENMYYHFL GRSGYTVHVQ CNASKFHQGT LLVAMIPEHQ
210 220 230 240 250
LASAKHGSVT AGYKLTHPGE AGRDVSQERD ASLRQPSDDS WLNFDGTLLG
260 270 280 290 300
NLLIFPHQFI NLRSNNSATL IVPYVNAVPM DSMLRHNNWS LVIIPISPLR
310 320 330 340 350
SETTSSNIVP ITVSISPMCA EFSGARAKNI KQGLPVYITP GSGQFMTTDD
360 370 380 390 400
MQSPCALPWY HPTKEISIPG EVKNLIEMCQ VDTLIPVNNV GNNVGNVSMY
410 420 430 440 450
TVQLGNQTGM AQKVFSIKVD ITSQPLATTL IGEIASYYTH WTGSLRFSFM
460 470 480 490 500
FCGTANTTLK LLLAYTPPGI DEPTTRKDAM LGTHVVWDVG LQSTISLVVP
510 520 530 540 550
WVSASHFRLT ADNKYSMAGY ITCWYQTNLV VPPSTPQTAD MLCFVSACKD
560 570 580 590 600
FCLRMARDTD LHIQSGPIEQ NPVENYIDEV LNEVLVVPNI KESHHTTSNS
610 620 630 640 650
APLLDAAETG HTSNVQPEDA IETRYVITSQ TRDEMSIESF LGRSGCVHIS
660 670 680 690 700
RIKVDYTDYN GQDINFTKWK ITLQEMAQIR RKFELFTYVR FDSEITLVPC
710 720 730 740 750
IAGRGDDIGH IVMQYMYVPP GAPIPSKRND FSWQSGTNMS IFWQHGQPFP
760 770 780 790 800
RFSLPFLSIA SAYYMFYDGY DGDNTSSKYG SVVTNDMGTI CSRIVTEKQK
810 820 830 840 850
HSVVITTHIY HKAKHTKAWC PRPPRAVPYT HSHVTNYMPE TGDVTTAIVR
860 870 880 890 900
RNTITTAGPS DLYVHVGNLI YRNLHLFNSE MHDSILISYS SDLIIYRTNT
910 920 930 940 950
IGDDYIPNCN CTEATYYCRH KNRYYPIKVT PHDWYEIQES EYYPKHIQYN
960 970 980 990 1000
LLIGEGPCEP GDCGGKLLCR HGVIGIITAG GEGHVAFIDL RQFHCAEEQG
1010 1020 1030 1040 1050
ITDYIHMLGE AFGNGFVDSV KEQINAINPI NNISKKVIKW LLRIISAMVI
1060 1070 1080 1090 1100
IIRNSSDPQT IIATLTLIGC NGSPWRFLKE KFCKWTQLTY IHKESDSWLK
1110 1120 1130 1140 1150
KFTEMCNAAR GLEWIGNKIS KFIDWMKSML PQAQLKVKYL NEIKKLSLLE
1160 1170 1180 1190 1200
KQIENLRAAD SATQEKIKCE IDTLHDLSCK FLPLYAHEAK RIKVLYNKCS
1210 1220 1230 1240 1250
NIIKQRKRSE PVAVMIHGPP GTGKSITTNF LARMITNESD VYSLPPDPKY
1260 1270 1280 1290 1300
FDGYDNQSVV IMDDIMQNPD GEDMTLFCQM VSSVTFIPPM ADLPDKGKPF
1310 1320 1330 1340 1350
DSRFILCSTN HSLLAPPTIS SLPAMNRRFF FDLDIVVHDN YKDTQGKLDV
1360 1370 1380 1390 1400
SKAFRPCNVN TKIGNAKCCP FVCGKAVXFK DRSTCSTYTL AQVYNHILEE
1410 1420 1430 1440 1450
DKRRRQVVDV MSAIFQGPIS LDXPPPPAIX DLLQSVRTPE VIKYCQDNKW
1460 1470 1480 1490 1500
VIPAECQVER DLNIANSIIA IIANIISIAG IIFVIYKLFC SLQGPYSGEP
1510 1520 1530 1540 1550
KPKTKVPERR VVAQGPEEEF GRSILKNNTC VITTGNGKFT GLGIHDRILI
1560 1570 1580 1590 1600
IPTHADPGRE VQVNGVHTKV LDSYDLYNRD GVKLEITVIQ LDRNEKFRDI
1610 1620 1630 1640 1650
RKYIPETEDD YPECNLALSA NQDEPTIIKV GDVVSYGNIL LSGNQTARML
1660 1670 1680 1690 1700
KYNYPTKSGY CGGVLYKIGQ ILGIHVGGNG RDGFSAMLLR SYFTDTQGQI
1710 1720 1730 1740 1750
KVNKHATECG LPTIHTPSKT KLQPSVFYDV FPGSKEPAVL TDNDPRLEVN
1760 1770 1780 1790 1800
FKEALFSKYK GNVECNLNEH MEIAIAHYSA QLMTLDIDSR PIALEDSVFG
1810 1820 1830 1840 1850
IEGLEALDLN TSAGFPYVTM GIKKRDLINN KTKDISRLKE ALDKYGVDLP
1860 1870 1880 1890 1900
MITFLKDELR KKEKISTGKT RVIEASSIND TILFRTTFGN LFSKFHLNPG
1910 1920 1930 1940 1950
VVTGSAVGCD PETFWSKIPV MLDGDCIMAF DYTNYDGSIH PVWFQALKKV
1960 1970 1980 1990 2000
LENLSFQSNL IDRLCYSKHL FKSTYYEVAG GVPSGCSGTS IFNTMINNII
2010 2020 2030 2040 2050
IRTLVLDAYK NIDLDKLKII AYGDDVIFSY KYTLDMEAIA NEGKKYGLTI
2060 2070 2080 2090 2100
TPADKSNEFK KLDYSNVTFL KRGFKQDERH TFLIHPTFPV EEIHESIRWT
2110 2120 2130 2140 2150
KKPSQMQEHV LSLCHLMWHN GRKVYEDFSS KIRSVSAGRA LYIPPYDLLK

HEWYEKF
Length:2,157
Mass (Da):242,487
Last modified:July 24, 2013 - v3
Checksum:i8B7807D279FC0A84
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41Q → G.
Natural varianti93 – 953TSQ → SSD.
Natural varianti120 – 1201D → N.
Natural varianti290 – 2901S → C.
Natural varianti424 – 4241Q → T.
Natural varianti754 – 7541L → I.
Natural varianti801 – 8011H → L.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ445111 Genomic RNA. Translation: ACK37367.1.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound Win56291

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound Win54954

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound R61837

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ445111 Genomic RNA. Translation: ACK37367.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AYM X-ray 2.15 4 2-69 [» ]
1AYN X-ray 2.90 4 2-69 [» ]
1R1A X-ray 3.20 1 571-857 [» ]
2 70-332 [» ]
3 333-570 [» ]
4 2-45 [» ]
2HWD X-ray 3.80 1 571-857 [» ]
2 70-332 [» ]
3 333-570 [» ]
4 2-45 [» ]
2HWE X-ray 3.80 1 571-857 [» ]
2 70-332 [» ]
3 333-570 [» ]
4 2-45 [» ]
2HWF X-ray 3.80 1 571-857 [» ]
2 70-332 [» ]
3 333-570 [» ]
4 2-45 [» ]
ProteinModelPortali P23008.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.007.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P23008.

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. "Sequencing and analyses of all known human rhinovirus genomes reveal structure and evolution."
    Palmenberg A.C., Spiro D., Kuzmickas R., Wang S., Djikeng A., Rathe J.A., Fraser-Liggett C.M., Liggett S.B.
    Science 324:55-59(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: ATCC VR-1559.
  2. Cited for: NUCLEOTIDE SEQUENCE OF 1-45 AND 70-857, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
  3. "Productive entry pathways of human rhinoviruses."
    Fuchs R., Blaas D.
    Adv. Virol. 2012:826301-826301(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiPOLG_HRV1A
AccessioniPrimary (citable) accession number: P23008
Secondary accession number(s): B9V432
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 24, 2013
Last modified: November 26, 2014
This is version 109 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