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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: 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)DescriptionActionsGraphical viewLength
Active sitei898For Protease 2A activityBy similarity1
Active sitei916For Protease 2A activityBy similarity1
Active sitei987For Protease 2A activityBy similarity1
Active sitei1602For Protease 3C activitySequence analysis1
Active sitei1633For Protease 3C activitySequence analysis1
Active sitei1709For Protease 3C activitySequence analysis1
Active sitei2073For RdRp activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1253 – 1260ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

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 virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008995 Componenti: Genome
  • UP000008147 Componenti: Genome

Subcellular locationi

Capsid protein VP0 :
Capsid protein VP4 :
Capsid protein VP2 :
Capsid protein VP3 :
Capsid protein VP1 :
Protein 2B :
Protein 2C :
Protein 3A :
Protein 3AB :
Protease 3C :
Protein 3CD :
RNA-directed RNA polymerase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 1517CytoplasmicSequence analysisAdd BLAST1516
Intramembranei1518 – 1533Sequence analysisAdd BLAST16
Topological domaini1534 – 2206CytoplasmicSequence analysisAdd BLAST673

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00004266562 – 2206Genome polyproteinBy similarityAdd BLAST2205
ChainiPRO_00004266572 – 878P1By similarityAdd BLAST877
ChainiPRO_00004266582 – 340Capsid protein VP0Sequence analysisAdd BLAST339
ChainiPRO_00004266592 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042666070 – 340Capsid protein VP2Sequence analysisAdd BLAST271
ChainiPRO_0000426661341 – 578Capsid protein VP3Sequence analysisAdd BLAST238
ChainiPRO_0000426662579 – 878Capsid protein VP1Sequence analysisAdd BLAST300
ChainiPRO_0000426663879 – 1453P2By similarityAdd BLAST575
ChainiPRO_0000426664879 – 1027Protease 2ASequence analysisAdd BLAST149
ChainiPRO_00000401401028 – 1124Protein 2BSequence analysisAdd BLAST97
ChainiPRO_00000401411125 – 1453Protein 2CSequence analysisAdd BLAST329
ChainiPRO_00004266651454 – 2206P3By similarityAdd BLAST753
ChainiPRO_00004266661454 – 1562Protein 3ABSequence analysisAdd BLAST109
ChainiPRO_00000401421454 – 1540Protein 3ASequence analysisAdd BLAST87
ChainiPRO_00004266671541 – 1562Viral protein genome-linkedSequence analysisAdd BLAST22
ChainiPRO_00004266681563 – 2206Protein 3CDSequence analysisAdd BLAST644
ChainiPRO_00004266691563 – 1744Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00004266701745 – 2206RNA-directed RNA polymeraseBy similarityAdd BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei1543O-(5'-phospho-RNA)-tyrosineBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei69 – 70Cleavage; by autolysisSequence analysis2
Sitei340 – 341Cleavage; by Protease 3CSequence analysis2
Sitei878 – 879Cleavage; by Protease 2ASequence analysis2
Sitei1027 – 1028Cleavage; by Protease 3CSequence analysis2
Sitei1124 – 1125Cleavage; by Protease 3CSequence analysis2
Sitei1453 – 1454Cleavage; by Protease 3CSequence analysis2
Sitei1540 – 1541Cleavage; by Protease 3CSequence analysis2
Sitei1562 – 1563Cleavage; by Protease 3CSequence analysis2
Sitei1745 – 1746Cleavage; by Protease 3CSequence analysis2

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

12206
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi25 – 29Combined sources5
Helixi36 – 38Combined sources3
Helixi51 – 54Combined sources4
Beta strandi57 – 59Combined sources3
Beta strandi83 – 87Combined sources5
Beta strandi90 – 96Combined sources7
Helixi103 – 105Combined sources3
Turni113 – 115Combined sources3
Helixi126 – 128Combined sources3
Beta strandi138 – 141Combined sources4
Beta strandi147 – 151Combined sources5
Helixi153 – 155Combined sources3
Helixi159 – 167Combined sources9
Beta strandi168 – 180Combined sources13
Beta strandi187 – 197Combined sources11
Beta strandi203 – 207Combined sources5
Helixi213 – 216Combined sources4
Helixi219 – 221Combined sources3
Beta strandi226 – 228Combined sources3
Helixi246 – 248Combined sources3
Turni249 – 252Combined sources4
Helixi255 – 260Combined sources6
Beta strandi261 – 267Combined sources7
Turni268 – 270Combined sources3
Beta strandi272 – 278Combined sources7
Beta strandi282 – 287Combined sources6
Turni289 – 291Combined sources3
Beta strandi295 – 307Combined sources13
Beta strandi314 – 331Combined sources18
Turni348 – 351Combined sources4
Beta strandi363 – 365Combined sources3
Beta strandi379 – 382Combined sources4
Helixi384 – 387Combined sources4
Turni399 – 403Combined sources5
Helixi405 – 408Combined sources4
Beta strandi410 – 413Combined sources4
Beta strandi422 – 427Combined sources6
Turni429 – 431Combined sources3
Turni433 – 437Combined sources5
Helixi439 – 444Combined sources6
Beta strandi447 – 452Combined sources6
Beta strandi454 – 460Combined sources7
Beta strandi469 – 475Combined sources7
Beta strandi477 – 479Combined sources3
Helixi485 – 488Combined sources4
Beta strandi491 – 497Combined sources7
Beta strandi499 – 501Combined sources3
Beta strandi503 – 508Combined sources6
Beta strandi513 – 520Combined sources8
Helixi523 – 525Combined sources3
Beta strandi529 – 536Combined sources8
Beta strandi546 – 556Combined sources11
Beta strandi561 – 565Combined sources5
Helixi623 – 625Combined sources3
Helixi633 – 635Combined sources3
Helixi649 – 651Combined sources3
Helixi653 – 657Combined sources5
Beta strandi661 – 671Combined sources11
Beta strandi675 – 677Combined sources3
Beta strandi680 – 685Combined sources6
Beta strandi690 – 692Combined sources3
Helixi693 – 698Combined sources6
Beta strandi701 – 718Combined sources18
Beta strandi730 – 736Combined sources7
Helixi749 – 752Combined sources4
Beta strandi754 – 756Combined sources3
Beta strandi758 – 762Combined sources5
Beta strandi768 – 772Combined sources5
Beta strandi777 – 783Combined sources7
Turni799 – 802Combined sources4
Beta strandi810 – 812Combined sources3
Beta strandi816 – 821Combined sources6
Beta strandi830 – 848Combined sources19
Beta strandi858 – 861Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03302.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1229 – 1385SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1563 – 1728Peptidase C3Add BLAST166
Domaini1972 – 2087RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni579 – 603Amphipatic alpha-helixSequence analysisAdd BLAST25
Regioni1454 – 1476DisorderedBy similarityAdd BLAST23

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

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
4.10.80.10. 2 hits.
InterProiIPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
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]
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

« Hide

        10         20         30         40         50
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYKDSASNA ASKQDYSQDP
60 70 80 90 100
SKFTEPLKDV LIKTAPALNS PNVEACGYSD RVLQLTLGNS TITTQEAANS
110 120 130 140 150
VVAYGRWPEF IRDDEANPVD QPTEPDVATC RFYTLDTVMW GKESKGWWWK
160 170 180 190 200
LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAIPEYC
210 220 230 240 250
LAGDSDKQRY TSYANANPGE RGGKFYSQFN KDNAVTSPKR EFCPVDYLLG
260 270 280 290 300
CGVLLGNAFV YPHQIINLRT NNSATIVLPY VNALAIDSMV KHNNWGIAIL
310 320 330 340 350
PLSPLDFAQD SSVEIPITVT IAPMCSEFNG LRNVTAPKFQ GLPVLNTPGS
360 370 380 390 400
NQYLTSDNHQ SPCAIPEFDV TPPIDIPGEV KNMMELAEID TMIPLNLEST
410 420 430 440 450
KRNTMDMYRV TLSDSADLSQ PILCLSLSPA SDPRLSHTML GEVLNYYTHW
460 470 480 490 500
AGSLKFTFLF CGSMMATGKI LVAYAPPGAQ PPTSRKEAML GTHVIWDLGL
510 520 530 540 550
QSSCTMVVPW ISNVTYRQTT QDSFTEGGYI SMFYQTRIVV PLSTPKSMSM
560 570 580 590 600
LGFVSACNDF SVRLLRDTTH ISQSALPQGI EDLISEVAQG ALTLSLPKQQ
610 620 630 640 650
DSLPDTKASG PAHSKEVPAL TAVETGATNP LAPSDTVQTR HVVQRRSRSE
660 670 680 690 700
STIESFFARG ACVAIIEVDN EQPTTRAQKL FAMWRITYKD TVQLRRKLEF
710 720 730 740 750
FTYSRFDMEF TFVVTANFTN ANNGHALNQV YQIMYIPPGA PTPKSWDDYT
760 770 780 790 800
WQTSSNPSIF YTYGAAPARI SVPYVGLANA YSHFYDGFAK VPLKTDANDQ
810 820 830 840 850
IGDSLYSAMT VDDFGVLAVR VVNDHNPTKV TSKVRIYMKP KHVRVWCPRP
860 870 880 890 900
PRAVPYYGPG VDYKNNLDPL SEKGLTTYGF GHQNKAVYTA GYKICNYHLA
910 920 930 940 950
TKEDLQNTVS IMWNRDLLVV ESKAQGTDSI ARCNCNAGVY YCESRRKYYP
960 970 980 990 1000
VSFVGPTFQY MEANDYYPAR YQSHMLIGHG FASPGDCGGI LRCQHGVIGI
1010 1020 1030 1040 1050
VTAGGEGLVA FSDIRDLYAY EEEAMEQGIS NYIESLGAAF GSGFTQQIGD
1060 1070 1080 1090 1100
KISELTSMVT STITEKLLKN LIKIISSLVI ITRNYEDTTT VLATLALLGC
1110 1120 1130 1140 1150
DVSPWQWLKK KACDTLEIPY VIRQGDSWLK KFTEACNAAK GLEWVSNKIS
1160 1170 1180 1190 1200
KFIDWLRERI IPQARDKLEF VTKLKQLEML ENQISTIHQS CPSQEHQEIL
1210 1220 1230 1240 1250
FNNVRWLSIQ SKRFAPLYAL EAKRIQKLEH TINNYIQFKS KHRIEPVCLL
1260 1270 1280 1290 1300
VHGSPGTGKS VATNLIARAI AEKENTSTYS LPPDPSHFDG YKQQGVVIMD
1310 1320 1330 1340 1350
DLNQNPDGAD MKLFCQMVST VEFIPPMASL EEKGILFTSN YVLASTNSSR
1360 1370 1380 1390 1400
ITPPTVAHSD ALARRFAFDM DIQVMGEYSR DGKLNMAMAT ETCKDCHQPA
1410 1420 1430 1440 1450
NFKRCCPLVC GKAIQLMDKS SRVRYSVDQI TTMIINERNR RSNIGNCMEA
1460 1470 1480 1490 1500
LFQGPLQYKD LKIDIKTRPP PECINDLLQA VDSQEVRDYC EKKGWIVNIT
1510 1520 1530 1540 1550
SQVQTERNIN RAMTILQAVT TFAAVAGVVY VMYKLFAGHQ GAYTGLPNKR
1560 1570 1580 1590 1600
PNVPTIRAAK VQGPGFDYAV AMAKRNIVTA TTSKGEFTML GVHDNVAILP
1610 1620 1630 1640 1650
THASPGESIV IDGKEVEILD AKALEDQAGT NLEITIITLK RNEKFRDIRQ
1660 1670 1680 1690 1700
HIPTQITETN DGVLIVNTSK YPNMYVPVGA VTEQGYLNLG GRQTARILMY
1710 1720 1730 1740 1750
NFPTRAGQCG GVITCTGKVI GMHVGGNGSH GFAAALKRSY FTQSQGEIQW
1760 1770 1780 1790 1800
MRPSKEAGYP IINAPTKTKL EPSAFHYVFE GVKEPAVLTK NDPRLKTDFE
1810 1820 1830 1840 1850
EAIFSKYVGN KITEVDEYMK EAVDHYAGQL MSLDISTEQM CLEDAMYGTD
1860 1870 1880 1890 1900
GLEALDLSTS AGYPYVAMGK KKRDILNKQT RDTKEMQRLL DAYGINLPLV
1910 1920 1930 1940 1950
TYVKDELRSK TKVEQGKSRL IEASSLNDSV AMRMAFGNLY AAFHRNPGVV
1960 1970 1980 1990 2000
TGSAVGCDPD LFWSKIPVLM EEKLFAFDYT GYDASLSPAW FEALKMVLEK
2010 2020 2030 2040 2050
IGFGDRVDYI DYLNHSHHLY KNKIYCVKGG MPSGCSGTSI FNSMINNLII
2060 2070 2080 2090 2100
RTLLLKTYKG IDLDHLKMIA YGDDVIASYP HEVDASLLAQ SGKDYGLTMT
2110 2120 2130 2140 2150
PADKSATFET VTWENVTFLK RFFRADEKYP FLIHPVMPMK EIHESIRWTK
2160 2170 2180 2190 2200
DPRNTQDHVR SLCLLAWHNG EEEYNKFLAK IRSVPIGRAL LLPEYSTLYR

RWLDSF
Length:2,206
Mass (Da):246,165
Last modified:January 23, 2007 - v3
Checksum:i4766B15C861F66D3
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti431S → F in strain: P3/Leon 12a[1]b. 1
Natural varianti864K → R in strain: P3/Leon 12a[1]b. 1
Natural varianti908T → A in strain: P3/Leon 12a[1]b. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
K01392 Genomic RNA. Translation: AAA46914.1.
X00925 Genomic RNA. Translation: CAA25444.1.
PIRiA93987. GNNY4P.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC03.020.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03302.

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
4.10.80.10. 2 hits.
InterProiIPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
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]
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 174 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.