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Q82081

- POLG_HRV3

UniProt

Q82081 - POLG_HRV3

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Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 3 (HRV-3)
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
Sitei69 – 702Cleavage; by autolysisSequence Analysis
Sitei331 – 3322Cleavage; by Protease 3CSequence Analysis
Sitei855 – 8562Cleavage; by Protease 2ASequence Analysis
Active sitei875 – 8751For Protease 2A activityBy similarity
Active sitei893 – 8931For Protease 2A activityBy similarity
Active sitei964 – 9641For Protease 2A activityBy similarity
Sitei1001 – 10022Cleavage; by Protease 3CSequence Analysis
Sitei1428 – 14292Cleavage; by Protease 3CSequence Analysis
Sitei1513 – 15142Cleavage; by Protease 3CSequence Analysis
Sitei1536 – 15372Cleavage; by Protease 3CSequence Analysis
Active sitei1576 – 15761For Protease 3C activitySequence Analysis
Active sitei1607 – 16071For Protease 3C activitySequence Analysis
Active sitei1682 – 16821For Protease 3C activityBy similarity
Sitei1718 – 17192Cleavage; by Protease 3CSequence Analysis
Active sitei2045 – 20451For RdRp activityBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

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

Keywords - Biological processi

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

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.013.

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 3 (HRV-3)
Taxonomic identifieri44130 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000013737: 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 – 14901489CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei1491 – 150616Sequence AnalysisAdd
BLAST
Topological domaini1507 – 2178672CytoplasmicSequence 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 – 21782177Genome polyproteinBy similarityPRO_0000426521Add
BLAST
Chaini2 – 855854P1By similarityPRO_0000426522Add
BLAST
Chaini2 – 331330Capsid protein VP0Sequence AnalysisPRO_0000426523Add
BLAST
Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426524Add
BLAST
Chaini70 – 331262Capsid protein VP2Sequence AnalysisPRO_0000426525Add
BLAST
Chaini332 – 563232Capsid protein VP3Sequence AnalysisPRO_0000426526Add
BLAST
Chaini564 – 855292Capsid protein VP1Sequence AnalysisPRO_0000426527Add
BLAST
Chaini856 – 1428573P2By similarityPRO_0000426528Add
BLAST
Chaini856 – 1001146Protease 2ASequence AnalysisPRO_0000423099Add
BLAST
Chaini1002 – 109897Protein 2BSequence AnalysisPRO_0000423100Add
BLAST
Chaini1100 – 1428329Protein 2CSequence AnalysisPRO_0000426529Add
BLAST
Chaini1429 – 2178750P3By similarityPRO_0000426530Add
BLAST
Chaini1429 – 1536108Protein 3ABSequence AnalysisPRO_0000426531Add
BLAST
Chaini1429 – 151385Protein 3ASequence AnalysisPRO_0000423102Add
BLAST
Chaini1514 – 153623Viral protein genome-linkedSequence AnalysisPRO_0000426532Add
BLAST
Chaini1537 – 2178642Protein 3CDSequence AnalysisPRO_0000426533Add
BLAST
Chaini1537 – 1717181Protease 3CSequence AnalysisPRO_0000426534Add
BLAST
Chaini1718 – 2178461RNA-directed RNA polymeraseBy similarityPRO_0000426535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Modified residuei1516 – 15161O-(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
2178
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 353Combined sources
Helixi36 – 383Combined sources
Helixi51 – 544Combined sources
Beta strandi57 – 593Combined sources
Beta strandi83 – 875Combined sources
Beta strandi90 – 967Combined sources
Helixi103 – 1053Combined sources
Turni113 – 1153Combined sources
Helixi126 – 1283Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi147 – 1515Combined sources
Helixi153 – 1553Combined sources
Helixi159 – 1657Combined sources
Beta strandi168 – 18013Combined sources
Beta strandi188 – 19710Combined sources
Beta strandi203 – 2053Combined sources
Helixi213 – 2164Combined sources
Helixi219 – 2213Combined sources
Turni238 – 2447Combined sources
Helixi247 – 2526Combined sources
Beta strandi253 – 2597Combined sources
Turni260 – 2623Combined sources
Beta strandi264 – 2707Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi281 – 2844Combined sources
Beta strandi286 – 29813Combined sources
Beta strandi307 – 32317Combined sources
Turni339 – 3424Combined sources
Beta strandi354 – 3563Combined sources
Turni374 – 3796Combined sources
Beta strandi390 – 3923Combined sources
Helixi395 – 3984Combined sources
Beta strandi399 – 4024Combined sources
Beta strandi410 – 4156Combined sources
Helixi421 – 4233Combined sources
Helixi427 – 4326Combined sources
Beta strandi435 – 4406Combined sources
Beta strandi442 – 4487Combined sources
Beta strandi457 – 4637Combined sources
Helixi473 – 4764Combined sources
Beta strandi479 – 4857Combined sources
Beta strandi487 – 4893Combined sources
Beta strandi491 – 4966Combined sources
Beta strandi501 – 5033Combined sources
Beta strandi505 – 5084Combined sources
Helixi511 – 5133Combined sources
Beta strandi517 – 5248Combined sources
Beta strandi536 – 5449Combined sources
Beta strandi549 – 5535Combined sources
Beta strandi585 – 5873Combined sources
Helixi604 – 6063Combined sources
Helixi614 – 6163Combined sources
Helixi630 – 6323Combined sources
Helixi634 – 6374Combined sources
Beta strandi642 – 65110Combined sources
Helixi660 – 6634Combined sources
Beta strandi665 – 6695Combined sources
Beta strandi673 – 6764Combined sources
Helixi677 – 6837Combined sources
Beta strandi686 – 70217Combined sources
Beta strandi714 – 7207Combined sources
Helixi733 – 7364Combined sources
Beta strandi738 – 7403Combined sources
Beta strandi742 – 7465Combined sources
Beta strandi749 – 7557Combined sources
Beta strandi760 – 7667Combined sources
Beta strandi770 – 7745Combined sources
Beta strandi776 – 7783Combined sources
Helixi784 – 7863Combined sources
Beta strandi790 – 7956Combined sources
Beta strandi804 – 82219Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RHIX-ray3.001568-855[»]
270-331[»]
3332-567[»]
42-69[»]
ProteinModelPortaliQ82081.
SMRiQ82081. Positions 2-69, 77-567, 583-855, 1428-1485, 1537-2178.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ82081.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1204 – 1360157SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1537 – 1701165Peptidase C3Add
BLAST
Domaini1946 – 2059114RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni564 – 58421Amphipatic alpha-helixSequence AnalysisAdd
BLAST
Regioni1429 – 145022DisorderedBy 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. 2 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.

Q82081-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASSS SAGQSFSMDP
60 70 80 90 100
SKFTEPVKDL MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA
110 120 130 140 150
IVCYAEWPEY LSDNDASDVN KTSKPDISVC RFYTLDSKTW KATSKGWCWK
160 170 180 190 200
LPDALKDMGV FGQNMFYHSL GRTGYTIHVQ CNATKFHSGC LLVVVIPEHQ
210 220 230 240 250
LASHEGGTVS VKYKYTHPGD RGIDLDTVEV AGGPTSDAIY NMDGTLLGNL
260 270 280 290 300
LIFPHQFINL RTNNTATIVV PYINSVPIDS MTRHNNVSLM VVPIAPLNAP
310 320 330 340 350
TGSSPTLPVT VTIAPMCTEF TGIRSRSIVP QGLPTTTLPG SGQFLTTDDR
360 370 380 390 400
QSPSALPSYE PTPRIHIPGK VRNLLEIIQV GTLIPMNNTG TNDNVTNYLI
410 420 430 440 450
PLHADRQNEQ IFGTKLYIGD GVFKTTLLGE IAQYYTHWSG SLRISLMYTG
460 470 480 490 500
PALSSAKIIL AYTPPGTRGP EDRKEAMLGT HVVWDIGLQS TIVMTIPWTS
510 520 530 540 550
GVQFRYTDPD TYTSAGYLSC WYQTSLILPP QTSGQVYLLS FISACPDFKL
560 570 580 590 600
RLMKDTQTIS QTDALTEGLS DELEEVIVEK TKQTLASVSS GPKHTQSVPA
610 620 630 640 650
LTANETGATL PTRPSDNVET RTTYMHFNGS ETDVESFLGR AACVHVTEIK
660 670 680 690 700
NKNAAGLDNH RKEGLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT
710 720 730 740 750
ASQPEASSYS SNLTVQAMYV PPGAPNPKEW DDYTWQSASN PSVFFKVGET
760 770 780 790 800
SRFSVPFVGI ASAYNCFYDG YSHDDPDTPY GITVLNHMGS MAFRVVNEHD
810 820 830 840 850
VHTTIVKIRV YHRAKHVEAW IPRAPRALPY VSIGRTNYPR DSKTIIKKRT
860 870 880 890 900
NIKTYGLGPR FGGVFTSNVK IINYHLMTPD DHLNLVAPYP NRDLAVVATG
910 920 930 940 950
AHGAETIPHC NCTSGVYYSR YYRKFYPIIC ERPTNIWIEG SSYYPSRYQA
960 970 980 990 1000
GVMKGVGPAE PGDCGGILRC IHGPIGLLTA GGGGYVCFAD IRQLDFIADE
1010 1020 1030 1040 1050
QGLGDYITSL GRAFGTGFTD QISAKVCELQ DVAKDFLTTK VLSKVVKMIS
1060 1070 1080 1090 1100
ALVIICRNHD DLVTVTATLA LLGCDGSPWR FLKMYISKHF QVPYIERQAN
1110 1120 1130 1140 1150
DGWFRKFNDA CNAAKGLEWI ANKISKLIEW IKNKVLPQAR EKLEFCSKLK
1160 1170 1180 1190 1200
QLDILERQIA SIHDSNPTQE KREQLFNNVL WLEQMSQKFS PLYASEAKRI
1210 1220 1230 1240 1250
RDLKNKITNY MQFKSKQRTE PVCVLIHGTP GSGKSLTTSI VGRALAEHFN
1260 1270 1280 1290 1300
SSVYSLPPDP KHFDGYQQQE VVIMDDLNQN PDGQDISMFC QMVSSVDFLP
1310 1320 1330 1340 1350
PMASLDNKGM LFTSNFVLAS TNSNTLSPPT ILNPEALIRR FGFDLDICMH
1360 1370 1380 1390 1400
STYTKNGKLN AAMATSLCKD CHQPSNFKKC CPLVCGKAIS LVDRVSNVRF
1410 1420 1430 1440 1450
SIDQLVTAII NDYKNKVKIT DSLEVLFQGP VYKDLEIDIC NTPPPECISD
1460 1470 1480 1490 1500
LLKSVDSEEV REYCKKKKWI IPQISTNIER AVNQASMIIN TILMFVSTLG
1510 1520 1530 1540 1550
IVYVIYKLFA QTQGPYSGNP VHNKLKPPTL KPVVVQGPNT EFALSLLRKN
1560 1570 1580 1590 1600
ILTITTEKGE FTSLGIHDRI CVLPTHAQPG DNVLVNGQKI QIKDKYKLVD
1610 1620 1630 1640 1650
PDNTNLELTI IELDRNEKFR DIRGFISEDL EGLDATLVVH SNGFTNTILD
1660 1670 1680 1690 1700
VGPITMAGLI NLSNTPTTRM IRYDYPTKTG QCGGVLCTTG KIFGIHVGGN
1710 1720 1730 1740 1750
GRRGFSAQLK KQYFVEKQGL IVSKQKVRDI GLNPINTPTK TKLHPSVFYN
1760 1770 1780 1790 1800
VFPGSKQPAV LNDNDPRLEV KLAESLFSKY KGNVQMEPTE NMLIAVDHYA
1810 1820 1830 1840 1850
GQLMSLDIST KELTLKEALY GVDGLEPIDV TTSAGYPYVS LGIKKRDILN
1860 1870 1880 1890 1900
KETQDVEKMK FYLDKYGIDL PLVTYIKDEL RSVDKVRLGK SRLIEASSLN
1910 1920 1930 1940 1950
DSVNMRMKLG NLYKAFHQNP GIITESAVGC DPDVFWSVIP CLMDGHLMAF
1960 1970 1980 1990 2000
DYSNFDASLS PVWFECLEKV LNKLGFKQPS LIQSICNTHH IFRDEIYRVE
2010 2020 2030 2040 2050
GGMPSGCSGT SIFNSMINNI IIRTLILDAY KGIDLDSLRI LAYGDDLIVS
2060 2070 2080 2090 2100
YPFELDSNIL AAIGKNYGLT ITPPDKSDAF TKITWENITF LKRYFRPDPQ
2110 2120 2130 2140 2150
FPFLIHPVMP MQDIYESIRW TRDPRNTQDH VRSLCMLAWH SGEKDYNDFI
2160 2170
TKIRTTDIGK CLNLPEYSVL RRRWLDLF
Length:2,178
Mass (Da):242,794
Last modified:July 24, 2013 - v4
Checksum:i0DFED5280AF25CCF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti87 – 871L → M.
Natural varianti98 – 981A → R.
Natural varianti260 – 2601L → M.
Natural varianti475 – 4751E → K.
Natural varianti523 – 5231Q → L.
Natural varianti846 – 8461I → V.
Natural varianti1349 – 13491M → L.
Natural varianti1389 – 13891I → V.
Natural varianti1703 – 17031R → Q.
Natural varianti1925 – 19251E → G.
Natural varianti1978 – 19781Q → H.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ473485 Genomic RNA. Translation: ABF51179.1.
EF173422 Genomic RNA. Translation: ABO69378.1.
U60874 Genomic RNA. Translation: AAB05616.1.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ473485 Genomic RNA. Translation: ABF51179.1 .
EF173422 Genomic RNA. Translation: ABO69378.1 .
U60874 Genomic RNA. Translation: AAB05616.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RHI X-ray 3.00 1 568-855 [» ]
2 70-331 [» ]
3 332-567 [» ]
4 2-69 [» ]
ProteinModelPortali Q82081.
SMRi Q82081. Positions 2-69, 77-567, 583-855, 1428-1485, 1537-2178.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.013.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q82081.

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
3.40.50.300. 2 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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "New complete genome sequences of human rhinoviruses shed light on their phylogeny and genomic features."
    Tapparel C., Junier T., Gerlach D., Cordey S., Van Belle S., Perrin L., Zdobnov E.M., Kaiser L.
    BMC Genomics 8:224-224(2007)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-855, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  4. "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_HRV3
AccessioniPrimary (citable) accession number: Q82081
Secondary accession number(s): A5GZD4, A7KC14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 24, 2013
Last modified: November 26, 2014
This is version 104 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3