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P03302

- POLG_POL3L

UniProt

P03302 - POLG_POL3L

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Protein

Genome polyprotein

Gene
N/A
Organism
Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B)
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 through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells. 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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 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.

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
Sitei340 – 3412Cleavage; by Protease 3C Reviewed prediction
Sitei878 – 8792Cleavage; by Protease 2A Reviewed prediction
Active sitei898 – 8981For Protease 2A activity By similarity
Active sitei916 – 9161For Protease 2A activity By similarity
Active sitei987 – 9871For Protease 2A activity By similarity
Sitei1027 – 10282Cleavage; by Protease 3C Reviewed prediction
Sitei1124 – 11252Cleavage; by Protease 3C Reviewed prediction
Sitei1453 – 14542Cleavage; by Protease 3C Reviewed prediction
Sitei1540 – 15412Cleavage; by Protease 3C Reviewed prediction
Sitei1562 – 15632Cleavage; by Protease 3C Reviewed prediction
Active sitei1602 – 16021For Protease 3C activity Reviewed prediction
Active sitei1633 – 16331For Protease 3C activity Reviewed prediction
Active sitei1709 – 17091For Protease 3C activity Reviewed prediction
Sitei1745 – 17462Cleavage; by Protease 3C Reviewed prediction
Active sitei2073 – 20731For RdRp activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1253 – 12608ATP Reviewed prediction

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. caveolin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. DNA replication 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 mRNA export from nucleus Source: UniProtKB-KW
  9. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  10. suppression by virus of host transcription initiation from RNA polymerase II promoter Source: UniProtKB-KW
  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, Caveolin-mediated endocytosis of virus by host, Clathrin- and caveolin-independent endocytosis of virus by host, DNA replication, Eukaryotic host gene expression shutoff by virus, Eukaryotic host transcription 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 eukaryotic host transcription initiation by virus, 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

MEROPSiC03.020.

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
OrganismiPoliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B)
Taxonomic identifieri12088 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000008147: Genome, UP000008995: 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 – 15171516Cytoplasmic Reviewed predictionAdd
BLAST
Intramembranei1518 – 153316 Reviewed predictionAdd
BLAST
Topological domaini1534 – 2206673Cytoplasmic 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 – 22062205Genome polyprotein By similarityPRO_0000426656Add
BLAST
Chaini2 – 878877P1 By similarityPRO_0000426657Add
BLAST
Chaini2 – 340339Capsid protein VP0 Reviewed predictionPRO_0000426658Add
BLAST
Chaini2 – 6968Capsid protein VP4 Reviewed predictionPRO_0000426659Add
BLAST
Chaini70 – 340271Capsid protein VP2 Reviewed predictionPRO_0000426660Add
BLAST
Chaini341 – 578238Capsid protein VP3 Reviewed predictionPRO_0000426661Add
BLAST
Chaini579 – 878300Capsid protein VP1 Reviewed predictionPRO_0000426662Add
BLAST
Chaini879 – 1453575P2 By similarityPRO_0000426663Add
BLAST
Chaini879 – 1027149Protease 2A Reviewed predictionPRO_0000426664Add
BLAST
Chaini1028 – 112497Protein 2B Reviewed predictionPRO_0000040140Add
BLAST
Chaini1125 – 1453329Protein 2C Reviewed predictionPRO_0000040141Add
BLAST
Chaini1454 – 2206753P3 By similarityPRO_0000426665Add
BLAST
Chaini1454 – 1562109Protein 3AB Reviewed predictionPRO_0000426666Add
BLAST
Chaini1454 – 154087Protein 3A Reviewed predictionPRO_0000040142Add
BLAST
Chaini1541 – 156222Viral protein genome-linked Reviewed predictionPRO_0000426667Add
BLAST
Chaini1563 – 2206644Protein 3CD Reviewed predictionPRO_0000426668Add
BLAST
Chaini1563 – 1744182Protease 3C Reviewed predictionPRO_0000426669Add
BLAST
Chaini1745 – 2206462RNA-directed RNA polymerase By similarityPRO_0000426670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By similarity
Modified residuei1543 – 15431O-(5'-phospho-RNA)-tyrosine By similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity.
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.
Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion By similarity.
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins By similarity.
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion By similarity.
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication By similarity.

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
2206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85
Beta strandi25 – 295
Helixi36 – 383
Helixi51 – 544
Beta strandi57 – 593
Beta strandi83 – 875
Beta strandi90 – 967
Helixi103 – 1053
Turni113 – 1153
Helixi126 – 1283
Beta strandi138 – 1414
Beta strandi147 – 1515
Helixi153 – 1553
Helixi159 – 1679
Beta strandi168 – 18013
Beta strandi187 – 19711
Beta strandi203 – 2075
Helixi213 – 2164
Helixi219 – 2213
Beta strandi226 – 2283
Helixi246 – 2483
Turni249 – 2524
Helixi255 – 2606
Beta strandi261 – 2677
Turni268 – 2703
Beta strandi272 – 2787
Beta strandi282 – 2876
Turni289 – 2913
Beta strandi295 – 30713
Beta strandi314 – 33118
Turni348 – 3514
Beta strandi363 – 3653
Beta strandi379 – 3824
Helixi384 – 3874
Turni399 – 4035
Helixi405 – 4084
Beta strandi410 – 4134
Beta strandi422 – 4276
Turni429 – 4313
Turni433 – 4375
Helixi439 – 4446
Beta strandi447 – 4526
Beta strandi454 – 4607
Beta strandi469 – 4757
Beta strandi477 – 4793
Helixi485 – 4884
Beta strandi491 – 4977
Beta strandi499 – 5013
Beta strandi503 – 5086
Beta strandi513 – 5208
Helixi523 – 5253
Beta strandi529 – 5368
Beta strandi546 – 55611
Beta strandi561 – 5655
Helixi623 – 6253
Helixi633 – 6353
Helixi649 – 6513
Helixi653 – 6575
Beta strandi661 – 67111
Beta strandi675 – 6773
Beta strandi680 – 6856
Beta strandi690 – 6923
Helixi693 – 6986
Beta strandi701 – 71818
Beta strandi730 – 7367
Helixi749 – 7524
Beta strandi754 – 7563
Beta strandi758 – 7625
Beta strandi768 – 7725
Beta strandi777 – 7837
Turni799 – 8024
Beta strandi810 – 8123
Beta strandi816 – 8216
Beta strandi830 – 84819
Beta strandi858 – 8614

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PIVX-ray2.901578-878[»]
270-340[»]
3341-578[»]
42-69[»]
1PVCX-ray2.401578-878[»]
270-340[»]
3341-578[»]
42-69[»]
1VBAX-ray2.901579-878[»]
270-340[»]
3341-575[»]
42-69[»]
1VBBX-ray2.801579-878[»]
270-340[»]
3341-575[»]
42-69[»]
1VBCX-ray2.801579-878[»]
270-340[»]
3341-575[»]
42-69[»]
1VBEX-ray2.801579-878[»]
270-340[»]
3341-575[»]
42-69[»]
3EPDelectron microscopy-1600-878[»]
275-340[»]
3341-575[»]
42-69[»]
3IYBelectron microscopy-283-96[»]
3IYCelectron microscopy-283-96[»]
ProteinModelPortaliP03302.
SMRiP03302. Positions 2-575, 600-1027, 1454-1512, 1563-2206.

Miscellaneous databases

EvolutionaryTraceiP03302.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1229 – 1385157SF3 helicaseAdd
BLAST
Domaini1563 – 1728166Peptidase C3Add
BLAST
Domaini1972 – 2087116RdRp catalyticAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni579 – 60325Amphipatic alpha-helix Reviewed predictionAdd
BLAST
Regioni1454 – 147623Disordered 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.

P03302-1 [UniParc]FASTAAdd to Basket

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MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYKDSASNA ASKQDYSQDP     50
SKFTEPLKDV LIKTAPALNS PNVEACGYSD RVLQLTLGNS TITTQEAANS 100
VVAYGRWPEF IRDDEANPVD QPTEPDVATC RFYTLDTVMW GKESKGWWWK 150
LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAIPEYC 200
LAGDSDKQRY TSYANANPGE RGGKFYSQFN KDNAVTSPKR EFCPVDYLLG 250
CGVLLGNAFV YPHQIINLRT NNSATIVLPY VNALAIDSMV KHNNWGIAIL 300
PLSPLDFAQD SSVEIPITVT IAPMCSEFNG LRNVTAPKFQ GLPVLNTPGS 350
NQYLTSDNHQ SPCAIPEFDV TPPIDIPGEV KNMMELAEID TMIPLNLEST 400
KRNTMDMYRV TLSDSADLSQ PILCLSLSPA SDPRLSHTML GEVLNYYTHW 450
AGSLKFTFLF CGSMMATGKI LVAYAPPGAQ PPTSRKEAML GTHVIWDLGL 500
QSSCTMVVPW ISNVTYRQTT QDSFTEGGYI SMFYQTRIVV PLSTPKSMSM 550
LGFVSACNDF SVRLLRDTTH ISQSALPQGI EDLISEVAQG ALTLSLPKQQ 600
DSLPDTKASG PAHSKEVPAL TAVETGATNP LAPSDTVQTR HVVQRRSRSE 650
STIESFFARG ACVAIIEVDN EQPTTRAQKL FAMWRITYKD TVQLRRKLEF 700
FTYSRFDMEF TFVVTANFTN ANNGHALNQV YQIMYIPPGA PTPKSWDDYT 750
WQTSSNPSIF YTYGAAPARI SVPYVGLANA YSHFYDGFAK VPLKTDANDQ 800
IGDSLYSAMT VDDFGVLAVR VVNDHNPTKV TSKVRIYMKP KHVRVWCPRP 850
PRAVPYYGPG VDYKNNLDPL SEKGLTTYGF GHQNKAVYTA GYKICNYHLA 900
TKEDLQNTVS IMWNRDLLVV ESKAQGTDSI ARCNCNAGVY YCESRRKYYP 950
VSFVGPTFQY MEANDYYPAR YQSHMLIGHG FASPGDCGGI LRCQHGVIGI 1000
VTAGGEGLVA FSDIRDLYAY EEEAMEQGIS NYIESLGAAF GSGFTQQIGD 1050
KISELTSMVT STITEKLLKN LIKIISSLVI ITRNYEDTTT VLATLALLGC 1100
DVSPWQWLKK KACDTLEIPY VIRQGDSWLK KFTEACNAAK GLEWVSNKIS 1150
KFIDWLRERI IPQARDKLEF VTKLKQLEML ENQISTIHQS CPSQEHQEIL 1200
FNNVRWLSIQ SKRFAPLYAL EAKRIQKLEH TINNYIQFKS KHRIEPVCLL 1250
VHGSPGTGKS VATNLIARAI AEKENTSTYS LPPDPSHFDG YKQQGVVIMD 1300
DLNQNPDGAD MKLFCQMVST VEFIPPMASL EEKGILFTSN YVLASTNSSR 1350
ITPPTVAHSD ALARRFAFDM DIQVMGEYSR DGKLNMAMAT ETCKDCHQPA 1400
NFKRCCPLVC GKAIQLMDKS SRVRYSVDQI TTMIINERNR RSNIGNCMEA 1450
LFQGPLQYKD LKIDIKTRPP PECINDLLQA VDSQEVRDYC EKKGWIVNIT 1500
SQVQTERNIN RAMTILQAVT TFAAVAGVVY VMYKLFAGHQ GAYTGLPNKR 1550
PNVPTIRAAK VQGPGFDYAV AMAKRNIVTA TTSKGEFTML GVHDNVAILP 1600
THASPGESIV IDGKEVEILD AKALEDQAGT NLEITIITLK RNEKFRDIRQ 1650
HIPTQITETN DGVLIVNTSK YPNMYVPVGA VTEQGYLNLG GRQTARILMY 1700
NFPTRAGQCG GVITCTGKVI GMHVGGNGSH GFAAALKRSY FTQSQGEIQW 1750
MRPSKEAGYP IINAPTKTKL EPSAFHYVFE GVKEPAVLTK NDPRLKTDFE 1800
EAIFSKYVGN KITEVDEYMK EAVDHYAGQL MSLDISTEQM CLEDAMYGTD 1850
GLEALDLSTS AGYPYVAMGK KKRDILNKQT RDTKEMQRLL DAYGINLPLV 1900
TYVKDELRSK TKVEQGKSRL IEASSLNDSV AMRMAFGNLY AAFHRNPGVV 1950
TGSAVGCDPD LFWSKIPVLM EEKLFAFDYT GYDASLSPAW FEALKMVLEK 2000
IGFGDRVDYI DYLNHSHHLY KNKIYCVKGG MPSGCSGTSI FNSMINNLII 2050
RTLLLKTYKG IDLDHLKMIA YGDDVIASYP HEVDASLLAQ SGKDYGLTMT 2100
PADKSATFET VTWENVTFLK RFFRADEKYP FLIHPVMPMK EIHESIRWTK 2150
DPRNTQDHVR SLCLLAWHNG EEEYNKFLAK IRSVPIGRAL LLPEYSTLYR 2200
RWLDSF 2206
Length:2,206
Mass (Da):246,165
Last modified:January 23, 2007 - v3
Checksum:i4766B15C861F66D3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti431 – 4311S → F in strain: P3/Leon 12a[1]b.
Natural varianti864 – 8641K → R in strain: P3/Leon 12a[1]b.
Natural varianti908 – 9081T → A in strain: P3/Leon 12a[1]b.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K01392 Genomic RNA. Translation: AAA46914.1.
X00925 Genomic RNA. Translation: CAA25444.1.
PIRiA93987. GNNY4P.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound R78206

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound R80633

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound R77975

Virus Particle ExploreR db

Icosahedral capsid structure of mutant F700L, F710L in complex with antiviral compound R78206

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound WIN51711

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K01392 Genomic RNA. Translation: AAA46914.1 .
X00925 Genomic RNA. Translation: CAA25444.1 .
PIRi A93987. GNNY4P.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PIV X-ray 2.90 1 578-878 [» ]
2 70-340 [» ]
3 341-578 [» ]
4 2-69 [» ]
1PVC X-ray 2.40 1 578-878 [» ]
2 70-340 [» ]
3 341-578 [» ]
4 2-69 [» ]
1VBA X-ray 2.90 1 579-878 [» ]
2 70-340 [» ]
3 341-575 [» ]
4 2-69 [» ]
1VBB X-ray 2.80 1 579-878 [» ]
2 70-340 [» ]
3 341-575 [» ]
4 2-69 [» ]
1VBC X-ray 2.80 1 579-878 [» ]
2 70-340 [» ]
3 341-575 [» ]
4 2-69 [» ]
1VBE X-ray 2.80 1 579-878 [» ]
2 70-340 [» ]
3 341-575 [» ]
4 2-69 [» ]
3EPD electron microscopy - 1 600-878 [» ]
2 75-340 [» ]
3 341-575 [» ]
4 2-69 [» ]
3IYB electron microscopy - 2 83-96 [» ]
3IYC electron microscopy - 2 83-96 [» ]
ProteinModelPortali P03302.
SMRi P03302. Positions 2-575, 600-1027, 1454-1512, 1563-2206.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.020.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03302.

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. "Comparison of the complete nucleotide sequences of the genomes of the neurovirulent poliovirus P3/Leon/37 and its attenuated Sabin vaccine derivative P3/Leon 12a1b."
    Stanway G., Hughes P.J., Mountford R.C., Reeve P., Minor P.D., Schild G.C., Almond J.W.
    Proc. Natl. Acad. Sci. U.S.A. 81:1539-1543(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: P3/Leon/37.
  2. "The nucleotide sequence of poliovirus type 3 Leon 12 a1b: comparison with poliovirus type 1."
    Stanway G., Cann A.J., Hauptmann R., Hughes P.J., Clarke L.D., Mountford R.C., Minor P.D., Schild G.C., Almond J.W.
    Nucleic Acids Res. 11:5629-5643(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: P3/Leon 12A[1]B.
  3. "Structures of poliovirus complexes with anti-viral drugs: implications for viral stability and drug design."
    Grant R.A., Hiremath C.N., Filman D.J., Syed R., Andries K., Hogle J.M.
    Curr. Biol. 4:784-797(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-878.
  4. "Binding of the antiviral drug win51711 to the Sabin strain of type-3 poliovirus -structural comparison with drug-binding in rhinovirus-14."
    Hiremath C.N., Grant R.A., Filman D.J., Hogle J.M.
    Acta Crystallogr. D 51:473-489(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-878.

Entry informationi

Entry nameiPOLG_POL3L
AccessioniPrimary (citable) accession number: P03302
Secondary accession number(s): Q84783
, Q84784, Q84785, Q84786, Q84787, Q84788, Q84789, Q84790, Q98592, Q98593, Q98594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence of strain Sabin vaccine P3/Leon/37 is shown.
The strain Sabin vaccine P3/Leon/37 is the progenitor of the strain Sabin vaccine P3/Leon 12a[1]b.

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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