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Reviewed, UniProtKB/Swiss-Prot P03300 (POLG_POL1M)

Last modified June 16, 2009. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Genome polyprotein
Cleaved into the following 12 chains:
    1- Recommended name:
            Protein VP0
        Alternative name(s):
            VP4-VP2
    2- Recommended name:
            Protein VP4
        Alternative name(s):
            Virion protein 4
            P1A
    3- Recommended name:
            Protein VP2
        Alternative name(s):
            Virion protein 2
            P1B
    4- Recommended name:
            Protein VP3
        Alternative name(s):
            Virion protein 3
            P1C
    5- Recommended name:
            Protein VP1
        Alternative name(s):
            Virion protein 1
            P1D
    6- Recommended name:
            Picornain 2A
                Short name=Protein 2A
                Short name=P2A
              EC=3.4.22.29
    7- Recommended name:
            Protein 2B
                Short name=P2B
    8- Recommended name:
            Protein 2C
                Short name=P2C
              EC=3.6.1.15
    9- Recommended name:
            Protein 3A
                Short name=P3A
    10- Recommended name:
            Protein 3B
                Short name=P3B
        Alternative name(s):
            VPg
    11- Recommended name:
            Picornain 3C
              EC=3.4.22.28
        Alternative name(s):
            Protease 3C
              Short name=P3C
    12- Recommended name:
            RNA-directed RNA polymerase 3D-POL
                Short name=P3D-POL
              EC=2.7.7.48
OrganismPoliovirus type 1 (strain Mahoney) [Complete proteome]
Taxonomic identifier12081 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

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Protein attributes

Sequence length2209 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The interaction of five VP1 proteins in the fivefold axes results in a prominent protusion extending to about 25 Angstroms from the capsid shell. The resulting structure appears as a steep plateau encircled by a valley or cleft. This depression also termed canyon is the receptor binding site. The capsid interacts with human PVR at this site to provide virion attachment to target cell. Ref.8

VP0 precursor is a component of immature procapsids By similarity.

Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription. Ref.8

Protein 2B affects membrane integrity and cause an increase in membrane permeability By similarity.

Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities. Ref.8

Protein 3A, via its hydrophobic domain, serves as membrane anchor. It also inhibits endoplasmic reticulum-to-Golgi transport By similarity.

Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease By similarity.

RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals 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.

Subunit structure

P2C N-terminus interacts with human RTN3. This interaction is important for viral replication By similarity. Interacts with human PVR.

Subcellular location

Protein VP2: Virion. Host cytoplasm Potential.

Protein VP3: Virion. Host cytoplasm Potential.

Protein VP1: Virion. Host cytoplasm Potential.

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 By similarity.

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 By similarity.

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 By similarity.

Protein 3B: Virion Potential.

Picornain 3C: Host cytoplasm Potential.

RNA-directed RNA polymerase 3D-POL: 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 By similarity.

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.

Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Contains 2 peptidase C3 domains.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

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Ontologies

Keywords
   Biological processHost-virus interaction
RNA replication
   Cellular componentCapsid protein
Cytoplasm
Cytoplasmic vesicle
Membrane
Virion
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Thiol protease
Transferase
   PTMCovalent protein-RNA linkage
Lipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processRNA-protein covalent cross-linking

Inferred from electronic annotation. Source: UniProtKB-KW

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

transcription, RNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasmic vesicle

Inferred from electronic annotation. Source: UniProtKB-KW

host cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

structural molecule activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 341340Protein VP0 Potential
PRO_0000311078
Chain2 – 6968Protein VP4 Potential
PRO_0000040080
Chain70 – 341272Protein VP2 Potential
PRO_0000040081
Chain342 – 579238Protein VP3 Potential
PRO_0000040082
Chain580 – 881302Protein VP1 Potential
PRO_0000040083
Chain882 – 1030149Picornain 2A Potential
PRO_0000040084
Chain1031 – 112797Protein 2B Potential
PRO_0000040085
Chain1128 – 1456329Protein 2C Potential
PRO_0000040086
Chain1457 – 154387Protein 3A Potential
PRO_0000040087
Chain1544 – 156522Protein 3B Potential
PRO_0000040088
Chain1566 – 1747182Picornain 3C Potential
PRO_0000040089
Chain1748 – 2209462RNA-directed RNA polymerase 3D-POL Potential
PRO_0000040090

Regions

Topological domain2 – 15201519Cytoplasmic Potential
Topological domain1521 – 153616In membrane Potential
Topological domain1537 – 2209673Cytoplasmic Potential
Domain1232 – 1388157SF3 helicase
Domain1975 – 2090116RdRp catalytic
Nucleotide binding1256 – 12638ATP Potential

Sites

Active site9011For picornain 2A activity By similarity
Active site9191For picornain 2A activity By similarity
Active site9901For picornain 2A activity By similarity
Active site16051For picornain 3C activity Potential
Active site16361For picornain 3C activity Potential
Active site17121For picornain 3C activity Potential
Site251Involved in the interaction with human RTN3 By similarity
Site69 – 702Cleavage Potential
Site341 – 3422Cleavage; by picornain 3C Potential
Site881 – 8822Cleavage; by picornain 2A Potential
Site1030 – 10312Cleavage; by picornain 3C Potential
Site1127 – 11282Cleavage; by picornain 3C Potential
Site1456 – 14572Cleavage; by picornain 3C Potential
Site1543 – 15442Cleavage; by picornain 3C Potential
Site1565 – 15662Cleavage; by picornain 3C Potential
Site1748 – 17492Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue15461O-(5'-phospho-RNA)-tyrosine
Lipidation21N-myristoyl glycine; by host Probable

Experimental info

Mutagenesis31A → D: 50% loss of myristoylation. Severe reduction in specific infectivity. Ref.6
Mutagenesis31A → G, L or V: No effect on myristoylation and virus growth. Ref.6
Mutagenesis31A → H: No effect on myristoylation. Severe reduction in specific infectivity. Ref.6
Sequence conflict242 – 26423RFCPV…FVFPH → SSARWITSLEMARCWGMPLC SA in CAA24446. Ref.2
Sequence conflict2871I → L in CAA24446. Ref.2
Sequence conflict3091A → V in CAA24446. Ref.2
Sequence conflict420 – 4223DDP → AAS in CAA24446. Ref.2
Sequence conflict4641F → S in CAA24446. Ref.2
Sequence conflict5151T → S in CAA24446. Ref.2
Sequence conflict855 – 8562AV → QL in CAA24446. Ref.2
Sequence conflict9721A → V in CAA24446. Ref.2
Sequence conflict9851A → E in CAA24446. Ref.2
Sequence conflict1140 – 11412NA → QR in CAA24446. Ref.2
Sequence conflict16191V → A in CAA24446. Ref.2
Sequence conflict1626 – 16272AL → VF in CAA24446. Ref.2
Sequence conflict16351L → F in CAA24446. Ref.2
Sequence conflict16821G → R in CAA24446. Ref.2
Sequence conflict1722 – 17309VIGMHVGGN → SSGCMLVD in CAA24446. Ref.2
Sequence conflict17431Y → L in CAA24446. Ref.2
Sequence conflict17521Q → P in CAA24446. Ref.2
Sequence conflict1759 – 17602EV → DA in CAA24446. Ref.2
Sequence conflict18401T → I in CAA24446. Ref.2

Secondary structure

1 ............................................................................................................................................................................................................................................................................ 2209
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P03300-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DF1754F87F2E97D6

FASTA2,209246,540
        10         20         30         40         50         60 
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP SKFTEPIKDV 

        70         80         90        100        110        120 
LIKTAPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEY LRDSEANPVD 

       130        140        150        160        170        180 
QPTEPDVAAC RFYTLDTVSW TKESRGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ 

       190        200        210        220        230        240 
CNASKFHQGA LGVFAVPEMC LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDNNQTSPA 

       250        260        270        280        290        300 
RRFCPVDYLL GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI 

       310        320        330        340        350        360 
LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG SNQYLTADNF 

       370        380        390        400        410        420 
QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA TKKNTMEMYR VRLSDKPHTD 

       430        440        450        460        470        480 
DPILCLSLSP ASDPRLSHTM LGEILNYYTH WAGSLKFTFL FCGFMMATGK LLVSYAPPGA 

       490        500        510        520        530        540 
DPPKKRKEAM LGTHVIWDIG LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV 

       550        560        570        580        590        600 
VPLSTPREMD ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA 

       610        620        630        640        650        660 
TSRDALPNTE ASGPTHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS RSESSIESFF 

       670        680        690        700        710        720 
ARGACVTIMT VDNPASTTNK DKLFAVWKIT YKDTVQLRRK LEFFTYSRFD MELTFVVTAN 

       730        740        750        760        770        780 
FTETNNGHAL NQVYQIMYVP PGAPVPEKWD DYTWQTSSNP SIFYTYGTAP ARISVPYVGI 

       790        800        810        820        830        840 
SNAYSHFYDG FSKVPLKDQS AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL 

       850        860        870        880        890        900 
KPKHIRVWCP RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY 

       910        920        930        940        950        960 
HLATQDDLQN AVNVMWSRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK YYPVSFVGPT 

       970        980        990       1000       1010       1020 
FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV IGIITAGGEG LVAFSDIRDL 

      1030       1040       1050       1060       1070       1080 
YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ ISDKITELTN MVTSTITEKL LKNLIKIISS 

      1090       1100       1110       1120       1130       1140 
LVIITRNYED TTTVLATLAL LGCDASPWQW LRKKACDVLE IPYVIKQGDS WLKKFTEACN 

      1150       1160       1170       1180       1190       1200 
AAKGLEWVSN KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ 

      1210       1220       1230       1240       1250       1260 
EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV CLLVHGSPGT 

      1270       1280       1290       1300       1310       1320 
GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV IMDDLNQNPD GADMKLFCQM 

      1330       1340       1350       1360       1370       1380 
VSTVEFIPPM ASLEEKGILF TSNYVLASTN SSRISPPTVA HSDALARRFA FDMDIQVMNE 

      1390       1400       1410       1420       1430       1440 
YSRDGKLNMA MATEMCKNCH QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE 

      1450       1460       1470       1480       1490       1500 
RNRRSNIGNC MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV 

      1510       1520       1530       1540       1550       1560 
NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP NKKPNVPTIR 

      1570       1580       1590       1600       1610       1620 
TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA ILPTHASPGE SIVIDGKEVE 

      1630       1640       1650       1660       1670       1680 
ILDAKALEDQ AGTNLEITII TLKRNEKFRD IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP 

      1690       1700       1710       1720       1730       1740 
VGAVTEQGYL NLGGRQTART LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK 

      1750       1760       1770       1780       1790       1800 
RSYFTQSQGE IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT 

      1810       1820       1830       1840       1850       1860 
DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY GTDGLEALDL 

      1870       1880       1890       1900       1910       1920 
STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL PLVTYVKDEL RSKTKVEQGK 

      1930       1940       1950       1960       1970       1980 
SRLIEASSLN DSVAMRMAFG NLYAAFHKNP GVITGSAVGC DPDLFWSKIP VLMEEKLFAF 

      1990       2000       2010       2020       2030       2040 
DYTGYDASLS PAWFEALKMV LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG 

      2050       2060       2070       2080       2090       2100 
TSIFNSMINN LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL 

      2110       2120       2130       2140       2150       2160 
TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR WTKDPRNTQD 

      2170       2180       2190       2200 
HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST LYRRWLDSF

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References

[1]"Primary structure, gene organization and polypeptide expression of poliovirus RNA."
Kitamura N., Semler B.L., Rothberg P.G., Larsen G.R., Adler C.J., Dorner A.J., Emini E.A., Hanecak R., Lee J.J., van der Werf S., Anderson C.W., Wimmer E.
Nature 291:547-553(1981) [PubMed: 6264310] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genome."
Racaniello V.R., Baltimore D.
Proc. Natl. Acad. Sci. U.S.A. 78:4887-4891(1981) [PubMed: 6272282] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Identification of the initiation site of poliovirus polyprotein synthesis."
Dorner A.J., Dorner L.F., Larsen G.R., Wimmer E., Anderson C.W.
J. Virol. 42:1017-1028(1982) [PubMed: 6284987] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-69.
[4]"The genome-linked protein of picornaviruses. VII. Genetic mapping of poliovirus VPg by protein and RNA sequence studies."
Kitamura N., Adler C.J., Rothberg P.G., Martinko J., Nathenson S.G., Wimmer E.
Cell 21:295-302(1980) [PubMed: 6250717] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1539-1574, COVALENT RNA-LINKAGE OF VPG.
[5]"Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine."
Ambros V., Baltimore D.
J. Biol. Chem. 253:5263-5266(1978) [PubMed: 209034] [Abstract]
Cited for: COVALENT RNA-LINKAGE OF VPG.
[6]"Myristoylation is important at multiple stages in poliovirus assembly."
Moscufo N., Simons J., Chow M.
J. Virol. 65:2372-2380(1991) [PubMed: 1850017] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2, MUTAGENESIS OF ALA-3.
[7]"Poliovirus protein 2C has ATPase and GTPase activities."
Rodriguez P.L., Carrasco L.
J. Biol. Chem. 268:8105-8110(1993) [PubMed: 8385138] [Abstract]
Cited for: CHARACTERIZATION OF PROTEIN 2C.
[8]"Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F complex."
Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.
FEBS Lett. 435:79-83(1998) [PubMed: 9755863] [Abstract]
Cited for: FUNCTION OF PICORNAIN 2A.
[9]"Biochemical and genetic studies of the VPg uridylylation reaction catalyzed by the RNA polymerase of poliovirus."
Paul A.V., Peters J., Mugavero J., Yin J., van Boom J.H., Wimmer E.
J. Virol. 77:891-904(2003) [PubMed: 12502805] [Abstract]
Cited for: COVALENT RNA-LINKAGE OF VPG, URIDYLYLATION AT TYR-1546.
[10]"Intramolecular and intermolecular uridylylation by poliovirus RNA-dependent RNA polymerase."
Richards O.C., Spagnolo J.F., Lyle J.M., Vleck S.E., Kuchta R.D., Kirkegaard K.
J. Virol. 80:7405-7415(2006) [PubMed: 16840321] [Abstract]
Cited for: COVALENT RNA-LINKAGE OF VPG, URIDYLYLATION AT TYR-1546.
[11]"Reticulon 3 binds the 2C protein of enterovirus 71 and is required for viral replication."
Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H., Lin K.-H., Lai H.-C., Tang P., Horng J.-T.
J. Biol. Chem. 282:5888-5898(2007) [PubMed: 17182608] [Abstract]
Cited for: INTERACTION WITH HUMAN RTN3.
[12]"Membrane topography of the hydrophobic anchor sequence of poliovirus 3A and 3AB proteins and the functional effect of 3A/3AB membrane association upon RNA replication."
Fujita K., Krishnakumar S.S., Franco D., Paul A.V., London E., Wimmer E.
Biochemistry 46:5185-5199(2007) [PubMed: 17417822] [Abstract]
Cited for: TOPOLOGY.
[13]"Three-dimensional structure of poliovirus at 2.9-A resolution."
Hogle J.M., Chow M., Filman D.J.
Science 229:1358-1365(1985) [PubMed: 2994218] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881.
[14]"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: 7820548] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881.
[15]"Interaction of the poliovirus receptor with poliovirus."
He Y., Bowman V.D., Mueller S., Bator C.M., Bella J., Peng X., Baker T.S., Wimmer E., Kuhn R.J., Rossmann M.G.
Proc. Natl. Acad. Sci. U.S.A. 97:79-84(2000) [PubMed: 10618374] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.0 ANGSTROMS) OF 1-881.
+Additional computationally mapped references.

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Web resources

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure in complex with R80633, an inhibitor of viral replication

Virus Particle ExploreR db

Icosahedral capsid structure in complex with R77975, an inhibitor of viral replication

Virus Particle ExploreR db

Icosahedral empty capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with R78206

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure of 135S cell entry intermediate

Virus Particle ExploreR db

Icosahedral capsid structure

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Cross-references

Sequence databases

V01149 Genomic RNA. Translation: CAA24461.1.
V01148 Genomic RNA. Translation: CAA24446.1.
PIRGNNY2P. A03898.
GNNY1P. A93258.
RefSeqNP_041277.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AL2X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR6X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR7X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR8X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR9X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1ASJX-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1DGIelectron microscopy22.001599-881[»]
274-341[»]
3342-576[»]
42-69[»]
1FPTX-ray3.00P665-682[»]
1HXSX-ray2.201580-881[»]
270-341[»]
3342-578[»]
42-69[»]
1L1NX-ray2.10A/B1566-1748[»]
1NG7NMR-A/B1457-1515[»]
1NN8electron microscopy15.001580-881[»]
270-341[»]
3342-576[»]
41-69[»]
1PO1X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1PO2X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1POVX-ray2.80025-341[»]
1580-881[»]
3342-579[»]
1RA6X-ray2.00A1749-2209[»]
1RA7X-ray2.35A1749-2209[»]
1RAJX-ray2.50A1817-2209[»]
1RDRX-ray2.40A1749-2209[»]
1TQLX-ray2.30A1750-2209[»]
1VBDX-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1XYRelectron microscopy11.001650-881[»]
297-333[»]
3391-572[»]
5342-353[»]
6355-390[»]
782-95[»]
8621-631[»]
2BBLNMR-A1544-1565[»]
2BBPNMR-A1544-1565[»]
2IJDX-ray3.401/21566-2209[»]
2IJFX-ray3.00A1749-2209[»]
2ILYX-ray2.60A1749-2209[»]
2ILZX-ray2.50A1749-2209[»]
2IM0X-ray2.25A1749-2209[»]
2IM1X-ray2.50A1749-2209[»]
2IM2X-ray2.35A1749-2209[»]
2IM3X-ray2.60A1749-2209[»]
2PLVX-ray2.881580-881[»]
270-341[»]
3342-579[»]
42-69[»]
3EPCelectron microscopy8.001599-881[»]
274-341[»]
3342-576[»]
42-69[»]
SMRP03300. Positions 1566-2209.
ModBaseSearch...

Genome annotation databases

GeneID919920.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR004004. Helicase/Pol/Pept_Calicivir.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR014838. P3A.
IPR000199. Pept_C3_picorn.
IPR000081. Peptidase_C3.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA_pol_P3D.
IPR007094. RNA_pol_PSvir.
[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]
PRINTSPR00918. CALICVIRUSNS.
ProDomPD001125. Pept_C3_picorn. 1 hit.
PD001306. Peptidase_C3_2. 1 hit.
PD001274. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePOLG_POL1M
AccessionPrimary (citable) accession number: P03300
Secondary accession number(s): P03299 expand/collapse secondary AC list , Q84879, Q84880, Q89679
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents