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P06210

- POLG_POL2L

UniProt

P06210 - POLG_POL2L

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Protein

Genome polyprotein

Gene
N/A
Organism
Poliovirus type 2 (strain Lansing)
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.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
Sitei340 – 3412Cleavage; by Protease 3CSequence Analysis
Sitei879 – 8802Cleavage; by Protease 2ASequence Analysis
Active sitei899 – 8991For Protease 2A activityBy similarity
Active sitei917 – 9171For Protease 2A activityBy similarity
Active sitei988 – 9881For Protease 2A activityBy similarity
Sitei1028 – 10292Cleavage; by Protease 3CSequence Analysis
Sitei1125 – 11262Cleavage; by Protease 3CSequence Analysis
Sitei1454 – 14552Cleavage; by Protease 3CSequence Analysis
Sitei1541 – 15422Cleavage; by Protease 3CSequence Analysis
Sitei1563 – 15642Cleavage; by Protease 3CSequence Analysis
Active sitei1603 – 16031For Protease 3C activitySequence Analysis
Active sitei1634 – 16341For Protease 3C activitySequence Analysis
Active sitei1710 – 17101For Protease 3C activitySequence Analysis
Sitei1746 – 17472Cleavage; by Protease 3CSequence Analysis
Active sitei2074 – 20741For RdRp activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1254 – 12618ATPPROSITE-ProRule annotation

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. induction by virus of host autophagy Source: UniProtKB
  3. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  4. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
  5. protein oligomerization Source: UniProtKB-KW
  6. receptor-mediated endocytosis of virus by host cell 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, 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

MEROPSiC03.001.

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 2 (strain Lansing)
Taxonomic identifieri12084 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007638: 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.

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 – 22072206Genome polyproteinBy similarityPRO_0000426611Add
BLAST
Chaini2 – 879878P1By similarityPRO_0000426612Add
BLAST
Chaini2 – 340339Capsid protein VP0Sequence AnalysisPRO_0000426613Add
BLAST
Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426614Add
BLAST
Chaini70 – 340271Capsid protein VP2Sequence AnalysisPRO_0000426615Add
BLAST
Chaini341 – 578238Capsid protein VP3Sequence AnalysisPRO_0000426616Add
BLAST
Chaini579 – 879301Capsid protein VP1Sequence AnalysisPRO_0000426617Add
BLAST
Chaini880 – 1454575P2By similarityPRO_0000426618Add
BLAST
Chaini880 – 1028149Protease 2ASequence AnalysisPRO_0000426619Add
BLAST
Chaini1029 – 112597Protein 2BSequence AnalysisPRO_0000040107Add
BLAST
Chaini1126 – 1454329Protein 2CSequence AnalysisPRO_0000040108Add
BLAST
Chaini1455 – 2207753P3By similarityPRO_0000426620Add
BLAST
Chaini1455 – 1563109Protein 3ABSequence AnalysisPRO_0000426621Add
BLAST
Chaini1455 – 154187Protein 3ASequence AnalysisPRO_0000040109Add
BLAST
Chaini1542 – 156322Viral protein genome-linkedSequence AnalysisPRO_0000426622Add
BLAST
Chaini1564 – 2207644Protein 3CDSequence AnalysisPRO_0000426623Add
BLAST
Chaini1564 – 1745182Protease 3CSequence AnalysisPRO_0000426624Add
BLAST
Chaini1746 – 2207462RNA-directed RNA polymeraseBy similarityPRO_0000426625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Modified residuei1544 – 15441O-(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
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
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.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
2207
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74
Helixi17 – 193
Helixi23 – 253
Beta strandi26 – 294
Helixi36 – 383
Helixi51 – 544
Beta strandi57 – 593
Beta strandi63 – 653
Beta strandi83 – 875
Beta strandi90 – 967
Helixi103 – 1053
Turni113 – 1153
Helixi126 – 1283
Beta strandi138 – 1403
Beta strandi147 – 1515
Helixi153 – 1553
Helixi159 – 1679
Beta strandi168 – 18013
Beta strandi187 – 19711
Beta strandi203 – 2075
Helixi213 – 2164
Helixi219 – 2213
Beta strandi226 – 2283
Beta strandi235 – 2373
Helixi246 – 2483
Turni249 – 2524
Helixi255 – 2606
Beta strandi261 – 2677
Turni268 – 2703
Beta strandi272 – 2787
Beta strandi282 – 2876
Turni289 – 2913
Beta strandi295 – 30713
Beta strandi315 – 33117
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
Beta strandi529 – 5368
Beta strandi546 – 55611
Beta strandi561 – 5655
Helixi625 – 6273
Helixi635 – 6373
Helixi655 – 6595
Beta strandi663 – 6719
Beta strandi683 – 6875
Helixi695 – 7006
Beta strandi703 – 72523
Beta strandi732 – 7387
Helixi751 – 7544
Beta strandi756 – 7583
Beta strandi760 – 7645
Beta strandi770 – 7745
Beta strandi779 – 7857
Turni800 – 8034
Beta strandi812 – 8154
Beta strandi817 – 8226
Beta strandi831 – 84919
Beta strandi859 – 8624

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EAHX-ray2.901579-879[»]
270-340[»]
3341-578[»]
42-69[»]
3EPFelectron microscopy9.001602-879[»]
279-340[»]
3341-575[»]
42-69[»]
ProteinModelPortaliP06210.
SMRiP06210. Positions 2-575, 602-1028, 1455-1513, 1564-2207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06210.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 15181517CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1535 – 2207673CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei1519 – 153416Sequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1230 – 1386157SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1564 – 1729166Peptidase C3Add
BLAST
Domaini1973 – 2088116RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni579 – 59921Amphipatic alpha-helixSequence AnalysisAdd
BLAST
Regioni1455 – 147723DisorderedBy 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.
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.

P06210-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFAQDP
60 70 80 90 100
SKFTEPIKDV LIKTAPTLNS PNIEACGYSD RVMQLTLGNS TITTQEAANS
110 120 130 140 150
VVAYGRWPEY IKDSEANPVD QPTEPDVAAC RFYTLDTVTW RKESRGWWWK
160 170 180 190 200
LPDALKDMGL FGQNMFYHYL GRAGYTVHVQ CNASKFHQGA LGVFAVPEMC
210 220 230 240 250
LAGDSTTHMF TKYENANPGE KGGEFKGSFT LDTNATNPAR NFCPVDYLFG
260 270 280 290 300
SGVLAGNAFV YPHQIINLRT NNCATLVLPY VNSLSIDSMT KHNNWGIAIL
310 320 330 340 350
PLAPLDFATE SSTEIPITLT IAPMCCEFNG LRNITVPRTQ GLPVLNTPGS
360 370 380 390 400
NQYLTADNYQ SPCAIPEFDV TPPIDIPGEV RNMMELAEID TMIPLNLTNQ
410 420 430 440 450
RKNTMDMYRV ELNDAAHSDT PILCLSLSPA SDPRLAHTML GEILNYYTHW
460 470 480 490 500
AGSLKFTFLF CGSMMATGKL LVSYAPPGAE APKSRKEAML GTHVIWDIGL
510 520 530 540 550
QSSCTMVVPW ISNTTYRQTI NDSFTEGGYI SMFYQTRVVV PLSTPRKMDI
560 570 580 590 600
LGFVSACNDF SVRLLRDTTH ISQEAMPQGL GDLIEGVVEG VTRNALTPLT
610 620 630 640 650
PANNLPDTQS SGPAHSKETP ALTAVETGAT NPLVPSDTVQ TRHVIQKRTR
660 670 680 690 700
SESTVESFFA RGACVAIIEV DNDAPTKRAS KLFSVWKITY KDTVQLRRKL
710 720 730 740 750
EFFTYSRFDM EFTFVVTSNY TDANNGHALN QVYQIMYIPP GAPIPGKWND
760 770 780 790 800
YTWQTSSNPS VFYTYGAPPA RISVPYVGIA NAYSHFYDGF AKVPLAGQAS
810 820 830 840 850
TEGDSLYGAA SLNDFGSLAV RVVNDHNPTK LTSKIRVYMK PKHVRVWCPR
860 870 880 890 900
PPRAVPYYGP GVDYKDGLAP LPGKGLTTYG FGHQNKAVYT AGYKICNYHL
910 920 930 940 950
ATQEDLQNAV NIMWIRDLLV VESKAQGIDS IARCNCHTGV YYCESRRKYY
960 970 980 990 1000
PVSFTGPTFQ YMEANEYYPA RYQSHMLIGH GFASPGDCGG ILRCQHGVIG
1010 1020 1030 1040 1050
IITAGGEGLV AFSDIRDLYA YEEEAMEQGV SNYIESLGAA FGSGFTQQIG
1060 1070 1080 1090 1100
NKISELTSMV TSTITEKLLK NLIKIISSLV IITRNYEDTT TVLATLALLG
1110 1120 1130 1140 1150
CDASPWQWLK KKACDILEIP YIMRQGDSWL KKFTEACNAA KGLEWVSNKI
1160 1170 1180 1190 1200
SKFIDWLKEK IIPQARDKLE FVTKLKQLEM LENQIATIHQ SCPSQEHQEI
1210 1220 1230 1240 1250
LFNNVRWLSI QSKRFAPLYA VEAKRIQKLE HTINNYVQFK SKHRIEPVCL
1260 1270 1280 1290 1300
LVHGSPGTGK SVATNLIARA IAEKENTSTY SLPPDPSHFD GYKQQGVVIM
1310 1320 1330 1340 1350
DDLNQNPDGA DMKLFCQMVS TVEFIPPMAS LEEKGILFTS NYVLASTNSS
1360 1370 1380 1390 1400
RITPPTVAHS DALARRFAFD MDIQIMSEYS RDGKLNMAMA TEMCKNCHHP
1410 1420 1430 1440 1450
ANFKRCCPLV CGKAIQLMDK SSRVRYSIDQ ITTMIINERN RRSSIGNCME
1460 1470 1480 1490 1500
ALFQGPLQYK DLKIDIKTTP PPECINDLLQ AVDSQEVRDY CEKKGWIVDI
1510 1520 1530 1540 1550
TSQVQTERNI NRAMTILQAV TTFAAVAGVV YVMYKLFAGH QGAYTGLPNK
1560 1570 1580 1590 1600
RPNVPTIRTA KVQGPGFDYA VAMAKRNILT ATTIKGEFTM LGVHDNVAIL
1610 1620 1630 1640 1650
PTHASPGETI VIDGKEVEVL DAKALEDQAG TNLEITIVTL KRNEKFRDIR
1660 1670 1680 1690 1700
PHIPTQITET NDGVLIVNTS KYPNMYVPVG AVTEQGYLNL SGRQTARTLM
1710 1720 1730 1740 1750
YNFPTRAGQC GGVITCTGKV IGMHVGGNGS HGFAAALKRS YFTQSQGEIQ
1760 1770 1780 1790 1800
WMRPSKEVGY PVINAPSKTK LEPSAFHYVF EGVKEPAVLT KSDPRLKTDF
1810 1820 1830 1840 1850
EEAIFSKYVG NKITEVDEYM KEAVDHYAGQ LMSLDINTEQ MCLEDAMYGT
1860 1870 1880 1890 1900
DGLEALDLST SAGYPYVAMG KKKRDILNKQ TRDTKEMQRL LDTYGINLPL
1910 1920 1930 1940 1950
VTYVKDELRS KTKVEQGKSR LIEASSLNDS VAMRMAFGNL YAAFHKNPGV
1960 1970 1980 1990 2000
VTGSAVGCDP DLFWSKIPVL MEEKLFAFDY TGYDASLSPA WFEALKMVLE
2010 2020 2030 2040 2050
KIGFGDRVDY IDYLNHSHHL YKNKTYCVKG GMPSGCSGTS IFNSMINNLI
2060 2070 2080 2090 2100
IRTLLLKTYK GIDLDHLKMI AYGDDVIASY PHEVDASLLA QSGKDYGLTM
2110 2120 2130 2140 2150
TPADKSATFE TVTWENVTFL KRFFRADEKY PFLVHPVMPM KEIHESIRWT
2160 2170 2180 2190 2200
KDPRNTQDHV RSLCLLAWHN GEEEYNKFLA KIRSVPIGRA LLLPEYSTLY

RRWLDSF
Length:2,207
Mass (Da):245,831
Last modified:January 23, 2007 - v3
Checksum:i2B1E2070B7D44F99
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12197 Genomic RNA. Translation: AAA46912.1.
PIRiA29507. GNNY5P.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12197 Genomic RNA. Translation: AAA46912.1 .
PIRi A29507. GNNY5P.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EAH X-ray 2.90 1 579-879 [» ]
2 70-340 [» ]
3 341-578 [» ]
4 2-69 [» ]
3EPF electron microscopy 9.00 1 602-879 [» ]
2 79-340 [» ]
3 341-575 [» ]
4 2-69 [» ]
ProteinModelPortali P06210.
SMRi P06210. Positions 2-575, 602-1028, 1455-1513, 1564-2207.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P06210.

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. "Mapping of sequences required for mouse neurovirulence of poliovirus type 2 Lansing."
    la Monica N., Meriam C., Racaniello V.R.
    J. Virol. 57:515-525(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOLG_POL2L
AccessioniPrimary (citable) accession number: P06210
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 151 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