Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P03302 (POLG_POL3L) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 17 chains:

  1. P3
  2. Protein 3AB
  3. P1
  4. Capsid protein VP0
    Alternative name(s):
    VP4-VP2
  5. Capsid protein VP4
    Alternative name(s):
    P1A
    Virion protein 4
  6. Capsid protein VP2
    Alternative name(s):
    P1B
    Virion protein 2
  7. Capsid protein VP3
    Alternative name(s):
    P1C
    Virion protein 3
  8. Capsid protein VP1
    Alternative name(s):
    P1D
    Virion protein 1
  9. P2
  10. Protease 2A
    Short name=P2A
    EC=3.4.22.29
    Alternative name(s):
    Picornain 2A
    Protein 2A
  11. Protein 2B
    Short name=P2B
  12. Protein 2C
    Short name=P2C
    EC=3.6.1.15
  13. Protein 3A
    Short name=P3A
  14. Viral protein genome-linked
    Short name=VPg
    Alternative name(s):
    Protein 3B
    Short name=P3B
  15. Protein 3CD
    EC=3.4.22.28
  16. Protease 3C
    Short name=P3C
    EC=3.4.22.28
  17. RNA-directed RNA polymerase
    Short name=RdRp
    EC=2.7.7.48
    Alternative name(s):
    3D polymerase
    Short name=3Dpol
    Protein 3D
    Short name=3D
OrganismPoliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B) [Complete proteome]
Taxonomic identifier12088 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length2206 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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 regulation

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

Subunit structure

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.

Subcellular location

Capsid protein VP0: Virion By similarity. Host cytoplasm By similarity.

Capsid protein VP4: Virion By similarity.

Capsid protein VP2: Virion By similarity. Host cytoplasm By similarity.

Capsid protein VP3: Virion By similarity. Host cytoplasm By similarity.

Capsid protein VP1: Virion By similarity. Host cytoplasm By similarity.

Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Protein 3AB: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Viral protein genome-linked: Virion By similarity. Host cytoplasm By similarity.

Protease 3C: Host cytoplasm By similarity.

Protein 3CD: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

RNA-directed RNA polymerase: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Contains 1 peptidase C3 domain.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Ontologies

Keywords
   Biological processActivation of host autophagy by virus
Caveolin-mediated endocytosis of virus by host
Clathrin- and caveolin-independent endocytosis of virus by host
DNA replication
Host gene expression shutoff by virus
Host mRNA suppression by virus
Host transcription shutoff by virus
Host translation shutoff 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
Inhibition of host transcription initiation 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
   Cellular componentCapsid protein
Host cytoplasm
Host cytoplasmic vesicle
Host membrane
Membrane
T=pseudo3 icosahedral capsid protein
Virion
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
Ion channel
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Thiol protease
Transferase
Viral ion channel
   PTMCovalent protein-RNA linkage
Lipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processRNA-protein covalent cross-linking

Inferred from electronic annotation. Source: UniProtKB-KW

caveolin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

induction by virus of host autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

pore formation by virus in membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

pore-mediated entry of viral genome into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

protein oligomerization

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host RIG-I activity

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host transcription initiation from RNA polymerase II promoter

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 22062205Genome polyprotein By similarity
PRO_0000426656
Chain2 – 878877P1 By similarity
PRO_0000426657
Chain2 – 340339Capsid protein VP0 Potential
PRO_0000426658
Chain2 – 6968Capsid protein VP4 Potential
PRO_0000426659
Chain70 – 340271Capsid protein VP2 Potential
PRO_0000426660
Chain341 – 578238Capsid protein VP3 Potential
PRO_0000426661
Chain579 – 878300Capsid protein VP1 Potential
PRO_0000426662
Chain879 – 1453575P2 By similarity
PRO_0000426663
Chain879 – 1027149Protease 2A Potential
PRO_0000426664
Chain1028 – 112497Protein 2B Potential
PRO_0000040140
Chain1125 – 1453329Protein 2C Potential
PRO_0000040141
Chain1454 – 2206753P3 By similarity
PRO_0000426665
Chain1454 – 1562109Protein 3AB Potential
PRO_0000426666
Chain1454 – 154087Protein 3A Potential
PRO_0000040142
Chain1541 – 156222Viral protein genome-linked Potential
PRO_0000426667
Chain1563 – 2206644Protein 3CD Potential
PRO_0000426668
Chain1563 – 1744182Protease 3C Potential
PRO_0000426669
Chain1745 – 2206462RNA-directed RNA polymerase By similarity
PRO_0000426670

Regions

Topological domain2 – 15171516Cytoplasmic Potential
Intramembrane1518 – 153316 Potential
Topological domain1534 – 2206673Cytoplasmic Potential
Domain1229 – 1385157SF3 helicase
Domain1563 – 1728166Peptidase C3
Domain1972 – 2087116RdRp catalytic
Nucleotide binding1253 – 12608ATP Potential
Region579 – 60325Amphipatic alpha-helix Potential
Region1454 – 147623Disordered By similarity

Sites

Active site8981For Protease 2A activity By similarity
Active site9161For Protease 2A activity By similarity
Active site9871For Protease 2A activity By similarity
Active site16021For Protease 3C activity Potential
Active site16331For Protease 3C activity Potential
Active site17091For Protease 3C activity Potential
Active site20731For RdRp activity By similarity
Site69 – 702Cleavage; by autolysis Potential
Site340 – 3412Cleavage; by Protease 3C Potential
Site878 – 8792Cleavage; by Protease 2A Potential
Site1027 – 10282Cleavage; by Protease 3C Potential
Site1124 – 11252Cleavage; by Protease 3C Potential
Site1453 – 14542Cleavage; by Protease 3C Potential
Site1540 – 15412Cleavage; by Protease 3C Potential
Site1562 – 15632Cleavage; by Protease 3C Potential
Site1745 – 17462Cleavage; by Protease 3C Potential

Amino acid modifications

Modified residue15431O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation21N-myristoyl glycine; by host

Natural variations

Natural variant4311S → F in strain: P3/Leon 12a[1]b.
Natural variant8641K → R in strain: P3/Leon 12a[1]b.
Natural variant9081T → A in strain: P3/Leon 12a[1]b.

Secondary structure

.................................................................................................................................................. 2206
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03302 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4766B15C861F66D3

FASTA2,206246,165
        10         20         30         40         50         60 
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYKDSASNA ASKQDYSQDP SKFTEPLKDV 

        70         80         90        100        110        120 
LIKTAPALNS PNVEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEF IRDDEANPVD 

       130        140        150        160        170        180 
QPTEPDVATC RFYTLDTVMW GKESKGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ 

       190        200        210        220        230        240 
CNASKFHQGA LGVFAIPEYC LAGDSDKQRY TSYANANPGE RGGKFYSQFN KDNAVTSPKR 

       250        260        270        280        290        300 
EFCPVDYLLG CGVLLGNAFV YPHQIINLRT NNSATIVLPY VNALAIDSMV KHNNWGIAIL 

       310        320        330        340        350        360 
PLSPLDFAQD SSVEIPITVT IAPMCSEFNG LRNVTAPKFQ GLPVLNTPGS NQYLTSDNHQ 

       370        380        390        400        410        420 
SPCAIPEFDV TPPIDIPGEV KNMMELAEID TMIPLNLEST KRNTMDMYRV TLSDSADLSQ 

       430        440        450        460        470        480 
PILCLSLSPA SDPRLSHTML GEVLNYYTHW AGSLKFTFLF CGSMMATGKI LVAYAPPGAQ 

       490        500        510        520        530        540 
PPTSRKEAML GTHVIWDLGL QSSCTMVVPW ISNVTYRQTT QDSFTEGGYI SMFYQTRIVV 

       550        560        570        580        590        600 
PLSTPKSMSM LGFVSACNDF SVRLLRDTTH ISQSALPQGI EDLISEVAQG ALTLSLPKQQ 

       610        620        630        640        650        660 
DSLPDTKASG PAHSKEVPAL TAVETGATNP LAPSDTVQTR HVVQRRSRSE STIESFFARG 

       670        680        690        700        710        720 
ACVAIIEVDN EQPTTRAQKL FAMWRITYKD TVQLRRKLEF FTYSRFDMEF TFVVTANFTN 

       730        740        750        760        770        780 
ANNGHALNQV YQIMYIPPGA PTPKSWDDYT WQTSSNPSIF YTYGAAPARI SVPYVGLANA 

       790        800        810        820        830        840 
YSHFYDGFAK VPLKTDANDQ IGDSLYSAMT VDDFGVLAVR VVNDHNPTKV TSKVRIYMKP 

       850        860        870        880        890        900 
KHVRVWCPRP PRAVPYYGPG VDYKNNLDPL SEKGLTTYGF GHQNKAVYTA GYKICNYHLA 

       910        920        930        940        950        960 
TKEDLQNTVS IMWNRDLLVV ESKAQGTDSI ARCNCNAGVY YCESRRKYYP VSFVGPTFQY 

       970        980        990       1000       1010       1020 
MEANDYYPAR YQSHMLIGHG FASPGDCGGI LRCQHGVIGI VTAGGEGLVA FSDIRDLYAY 

      1030       1040       1050       1060       1070       1080 
EEEAMEQGIS NYIESLGAAF GSGFTQQIGD KISELTSMVT STITEKLLKN LIKIISSLVI 

      1090       1100       1110       1120       1130       1140 
ITRNYEDTTT VLATLALLGC DVSPWQWLKK KACDTLEIPY VIRQGDSWLK KFTEACNAAK 

      1150       1160       1170       1180       1190       1200 
GLEWVSNKIS KFIDWLRERI IPQARDKLEF VTKLKQLEML ENQISTIHQS CPSQEHQEIL 

      1210       1220       1230       1240       1250       1260 
FNNVRWLSIQ SKRFAPLYAL EAKRIQKLEH TINNYIQFKS KHRIEPVCLL VHGSPGTGKS 

      1270       1280       1290       1300       1310       1320 
VATNLIARAI AEKENTSTYS LPPDPSHFDG YKQQGVVIMD DLNQNPDGAD MKLFCQMVST 

      1330       1340       1350       1360       1370       1380 
VEFIPPMASL EEKGILFTSN YVLASTNSSR ITPPTVAHSD ALARRFAFDM DIQVMGEYSR 

      1390       1400       1410       1420       1430       1440 
DGKLNMAMAT ETCKDCHQPA NFKRCCPLVC GKAIQLMDKS SRVRYSVDQI TTMIINERNR 

      1450       1460       1470       1480       1490       1500 
RSNIGNCMEA LFQGPLQYKD LKIDIKTRPP PECINDLLQA VDSQEVRDYC EKKGWIVNIT 

      1510       1520       1530       1540       1550       1560 
SQVQTERNIN RAMTILQAVT TFAAVAGVVY VMYKLFAGHQ GAYTGLPNKR PNVPTIRAAK 

      1570       1580       1590       1600       1610       1620 
VQGPGFDYAV AMAKRNIVTA TTSKGEFTML GVHDNVAILP THASPGESIV IDGKEVEILD 

      1630       1640       1650       1660       1670       1680 
AKALEDQAGT NLEITIITLK RNEKFRDIRQ HIPTQITETN DGVLIVNTSK YPNMYVPVGA 

      1690       1700       1710       1720       1730       1740 
VTEQGYLNLG GRQTARILMY NFPTRAGQCG GVITCTGKVI GMHVGGNGSH GFAAALKRSY 

      1750       1760       1770       1780       1790       1800 
FTQSQGEIQW MRPSKEAGYP IINAPTKTKL EPSAFHYVFE GVKEPAVLTK NDPRLKTDFE 

      1810       1820       1830       1840       1850       1860 
EAIFSKYVGN KITEVDEYMK EAVDHYAGQL MSLDISTEQM CLEDAMYGTD GLEALDLSTS 

      1870       1880       1890       1900       1910       1920 
AGYPYVAMGK KKRDILNKQT RDTKEMQRLL DAYGINLPLV TYVKDELRSK TKVEQGKSRL 

      1930       1940       1950       1960       1970       1980 
IEASSLNDSV AMRMAFGNLY AAFHRNPGVV TGSAVGCDPD LFWSKIPVLM EEKLFAFDYT 

      1990       2000       2010       2020       2030       2040 
GYDASLSPAW FEALKMVLEK IGFGDRVDYI DYLNHSHHLY KNKIYCVKGG MPSGCSGTSI 

      2050       2060       2070       2080       2090       2100 
FNSMINNLII RTLLLKTYKG IDLDHLKMIA YGDDVIASYP HEVDASLLAQ SGKDYGLTMT 

      2110       2120       2130       2140       2150       2160 
PADKSATFET VTWENVTFLK RFFRADEKYP FLIHPVMPMK EIHESIRWTK DPRNTQDHVR 

      2170       2180       2190       2200 
SLCLLAWHNG EEEYNKFLAK IRSVPIGRAL LLPEYSTLYR RWLDSF 

« Hide

References

[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.
+Additional computationally mapped references.

Web resources

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01392 Genomic RNA. Translation: AAA46914.1.
X00925 Genomic RNA. Translation: CAA25444.1.
PIRGNNY4P. A93987.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP03302.
SMRP03302. Positions 2-575, 600-1027, 1454-1512, 1563-2206.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC03.020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D4.10.80.10. 2 hits.
InterProIPR003593. 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.
[Graphical view]
PfamPF08727. 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]
ProDomPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03302.

Entry information

Entry namePOLG_POL3L
AccessionPrimary (citable) accession number: P03302
Secondary accession number(s): Q84783 expand/collapse secondary AC list , Q84784, Q84785, Q84786, Q84787, Q84788, Q84789, Q84790, Q98592, Q98593, Q98594
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references