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O91734 (POLG_EC01F) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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. P2
  4. P1
  5. Capsid protein VP0
    Alternative name(s):
    VP4-VP2
  6. Capsid protein VP4
    Alternative name(s):
    P1A
    Virion protein 4
  7. Capsid protein VP2
    Alternative name(s):
    P1B
    Virion protein 2
  8. Capsid protein VP3
    Alternative name(s):
    P1C
    Virion protein 3
  9. Capsid protein VP1
    Alternative name(s):
    P1D
    Virion protein 1
  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
OrganismEchovirus 1 (strain Human/Egypt/Farouk/1951) (E-1) [Complete proteome]
Taxonomic identifier103908 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length2184 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 integrin ITGA2/ITGB1 to provide virion attachment to target host cells. This attachment induces virion internalization. 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. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Ref.5 Ref.6

Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 By similarity. Ref.5 Ref.6

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. Ref.5 Ref.6

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. Interact with host integrin ITGA2/ITGB1 heterodimer. 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. Ref.4

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.

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
DNA replication
Host gene expression shutoff by virus
Host mRNA suppression 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
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 translation

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 – 21842183Genome polyprotein By similarity
PRO_0000426356
Chain2 – 850849P1 By similarity
PRO_0000426357
Chain2 – 330329Capsid protein VP0 Potential
PRO_0000426358
Chain2 – 6968Capsid protein VP4 Potential
PRO_0000426359
Chain70 – 330261Capsid protein VP2 Potential
PRO_0000426360
Chain331 – 567237Capsid protein VP3 Potential
PRO_0000426361
Chain567 – 850284Capsid protein VP1 Potential
PRO_0000426362
Chain850 – 1428579P2 By similarity
PRO_0000426363
Chain850 – 1000151Protease 2A Potential
PRO_0000426364
Chain1001 – 109999Protein 2B Potential
PRO_0000039653
Chain1100 – 1428329Protein 2C Potential
PRO_0000039654
Chain1429 – 2184756P3 By similarity
PRO_0000426365
Chain1429 – 1539111Protein 3AB Potential
PRO_0000426366
Chain1429 – 151789Protein 3A Potential
PRO_0000039655
Chain1518 – 153922Viral protein genome-linked Potential
PRO_0000426367
Chain1540 – 2184645Protein 3CD Potential
PRO_0000426368
Chain1540 – 1721182Protease 3C Potential
PRO_0000426369
Chain1722 – 2184463RNA-directed RNA polymerase By similarity
PRO_0000426370

Regions

Topological domain2 – 14941493Cytoplasmic Potential
Intramembrane1495 – 151016 Potential
Topological domain1511 – 2184674Cytoplasmic Potential
Domain1204 – 1360157SF3 helicase
Domain1540 – 1705166Peptidase C3
Domain1949 – 2065117RdRp catalytic
Region567 – 58317Amphipatic alpha-helix Potential
Region1429 – 145224Disordered By similarity

Sites

Active site8711For Protease 2A activity By similarity
Active site8891For Protease 2A activity By similarity
Active site9601For Protease 2A activity By similarity
Active site15791For Protease 3C activity Potential
Active site16101For Protease 3C activity Potential
Active site16861For Protease 3C activity By similarity
Active site20511For RdRp activity By similarity
Site69 – 702Cleavage; by autolysis Potential
Site330 – 3312Cleavage; by Protease 3C Potential
Site1000 – 10012Cleavage; by Protease 3C Potential
Site1428 – 14292Cleavage; by Protease 3C Potential
Site1517 – 15182Cleavage; by Protease 3C Potential
Site1539 – 15402Cleavage; by Protease 3C Potential
Site1722 – 17232Cleavage; by Protease 3C Potential

Amino acid modifications

Modified residue15201O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation21N-myristoyl glycine; by host

Experimental info

Sequence conflict691N → M in CAA61710. Ref.2
Sequence conflict2381A → R in CAA61710. Ref.2
Sequence conflict6111A → V in AAD17718. Ref.3
Sequence conflict6451Y → F in AAD17718. Ref.3
Sequence conflict7241V → I in AAD17718. Ref.3
Sequence conflict7741A → T in AAD17718. Ref.3

Secondary structure

.............................................................................................................................................. 2184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O91734 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: CBBB937D0AC18EA9

FASTA2,184244,004
        10         20         30         40         50         60 
MGAQVSTQKT GAHETSLSAT GNSIIHYTNI NYYKDAASNS ANRQDFTQDP GKFTEPMKDV 

        70         80         90        100        110        120 
MIKTLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV VVGYGEWPEY LSDNEATAED 

       130        140        150        160        170        180 
QPTQPDVATC RFYTLDSVQW ENGSPGWWWK FPDALRDMGL FGQNMYYHYL GRAGYTIHVQ 

       190        200        210        220        230        240 
CNASKFHQGC ILVVCVPEAE MGSAQTSGVV NYEHISKGEI ASRFTTTTTA EDHGVQAAVW 

       250        260        270        280        290        300 
NAGMGVGVGN LTIFPHQWIN LRTNNSATIV MPYVNSVPMD NMYRHHNFTL MIIPFVPLDF 

       310        320        330        340        350        360 
SAGASTYVPI TVTVAPMCAE YNGLRLAGHQ GLPTMNTPGS NQFLTSDDFQ SPSAMPQFDV 

       370        380        390        400        410        420 
TPEMHIPGEV RNLMEIAEVD SVMPINNDSA AKVSSMEAYR VELSTNTNAG TQVFGFQLNP 

       430        440        450        460        470        480 
GAESVMNRTL MGEILNYYAH WSGSIKITFV FCGSAMTTGK FLLSYAPPGA GAPKTRKDAM 

       490        500        510        520        530        540 
LGTHVVWDVG LQSSCVLCIP WISQTHYRFV EKDPYTNAGF VTCWYQTSVV SPASNQPKCY 

       550        560        570        580        590        600 
MMCMVSACND FSVRMLRDTK FIEQTSFYQG DVQNAVEGAM VRVADTVQTS ATNSERVPNL 

       610        620        630        640        650        660 
TAVETGHTSQ AVPGDTMQTR HVINNHVRSE STIENFLARS ACVFYLEYKT GTKEDSNSFN 

       670        680        690        700        710        720 
NWVITTRRVA QLRRKLEMFT YLRFDMEITV VITSSQDQST SQNQNAPVLT HQIMYVPPGG 

       730        740        750        760        770        780 
PIPVSVDDYS WQTSTNPSIF WTEGNAPARM SIPFISIGNA YSNFYDGWSH FSQAGVYGFT 

       790        800        810        820        830        840 
TLNNMGQLFF RHVNKPNPAA ITSVARIYFK PKHVRAWVPR PPRLCPYINS TNVNFEPKPV 

       850        860        870        880        890        900 
TEVRTNIITT GAFGQQSGAV YVGNYRVVNR HLATHIDWQN CVWEDYNRDL LVSTTTAHGC 

       910        920        930        940        950        960 
DTIARCQCTT GVYFCLSRNK HYPVSFEGPG LVEVQESEYY PKRYQSHVLL AAGFSEPGDC 

       970        980        990       1000       1010       1020 
GGILRCEHGV IGIVTMGGEG VVGFADVRDL LWLEDDAMEQ GVKDYVEQLG NAFGSGFTNQ 

      1030       1040       1050       1060       1070       1080 
ICEQVNLLKE SLVGQDSILE KSLKALVKII SALVIVVRNH DDLITVTATL ALIGCTSSPW 

      1090       1100       1110       1120       1130       1140 
RWLKQKVSQY YGIPMAERQN NGWLKKFTEM TNACKGMEWI AIKIQKFIEW LKVKILPEVK 

      1150       1160       1170       1180       1190       1200 
EKHEFLNRLK QLPLLESQIA TIEQSAPSQG DQEQLFSNVQ YFAHYCRKYA PLYAAEAKRV 

      1210       1220       1230       1240       1250       1260 
FSLEKKMSNY IQFKSKCRIE PVCLLLHGSP GAGKSVATNL IGRSLAEKLN SSVYSLPPDP 

      1270       1280       1290       1300       1310       1320 
DHFDGYKQQA VVIMDDLCQN PDGKDVSLFC QMVSSVDFVP PMAALEEKGI LFTSPFVLAS 

      1330       1340       1350       1360       1370       1380 
TNAGSINAPT VSDSRALARR FHFDMNIEVI SMYSQNGKIN MPMSVKTCDE DCCPVNFKKC 

      1390       1400       1410       1420       1430       1440 
CPLVCGKAIQ FIDRKTQVRY SLDMLVTEMF REYNHRHSVG ATLEALFQGP PVYREIKISV 

      1450       1460       1470       1480       1490       1500 
APETPPPPAI ADLLKSVDSE AVREYCKEKG WLVPEISSTL QIEKHVSRAF ICLQALTTFV 

      1510       1520       1530       1540       1550       1560 
SVAGIIYIIY KLFAGFQGAY TGMPNQKPKV PTLRQAKVQG PAFEFAVAMM KRNASTVKTE 

      1570       1580       1590       1600       1610       1620 
YGEFTMLGIY DRWAVLPRHA KPGPTILMND QEVGVLDAKE LVDKDGTNLE LTLLKLNRNE 

      1630       1640       1650       1660       1670       1680 
KFRDIRGFLA REEAEVNEAV LAINTSKFPN MYIPVGQVTD YGFLNLGGTP TKRMLMYNFP 

      1690       1700       1710       1720       1730       1740 
TRAGQCGGVL MSTGKVLGIH VGGNGHQGFS AALLRHYFNE EQGEIEFIES SKDAGFPVIN 

      1750       1760       1770       1780       1790       1800 
TPSKTKLEPS VFHQVFEGNK EPAVLRNGDP RLKVNFEEAI FSKYIGNVNT HVDEYMQEAV 

      1810       1820       1830       1840       1850       1860 
DHYAGQLATL DISTEPMKLE DAVYGTEGLE ALDLTTSAGY PYVALGIKKR DILSKKTKDL 

      1870       1880       1890       1900       1910       1920 
TKLKECMDKY GLNLPMVTYV KDELRSAEKV AKGKSRLIEA SSLNDSVAMR QTFGNLYKTF 

      1930       1940       1950       1960       1970       1980 
HLNPGIVTGS AVGCDPDVFW SKIPVMLDGH LIAFDYSGYD ASLSPVWFAC LKLLLEKLGY 

      1990       2000       2010       2020       2030       2040 
TNKETNYIDY LCNSHHLYRD KHYFVRGGMP SGCSGTSIFN SMINNIIIRT LMLKVYKGID 

      2050       2060       2070       2080       2090       2100 
LDQFRMIAYG DDVIASYPWP IDASLLAEAG KDYGLIMTPA DKGECFNEVT WTNVTFLKRY 

      2110       2120       2130       2140       2150       2160 
FRADEQYPFL VHPVMPMKDI HESIRWTKDP KNTQDHVRSL CLLAWHNGEH EYEEFIRKIR 

      2170       2180 
SVPVGRCLTL PAFSTLRRKW LDSF 

« Hide

References

[1]"Receptor interactions, infectious cDNA, and nucleotide sequences of echovirus 1/8."
Bergelson J.M.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"The major echovirus group is genetically coherent and related to coxsackie B viruses."
Huttunen P., Santti J., Pulli T., Hyypiae T.
J. Gen. Virol. 77:715-725(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 69-330.
[3]"Molecular evolution of the human enteroviruses: correlation of serotype with VP1 sequence and application to picornavirus classification."
Oberste M.S., Maher K., Kilpatrick D.R., Pallansch M.A.
J. Virol. 73:1941-1948(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 570-853.
[4]"Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of human VLA-2."
Bergelson J.M., St John N., Kawaguchi S., Chan M., Stubdal H., Modlin J., Finberg R.W.
J. Virol. 67:6847-6852(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ITGA2/ITGB1 INTEGRIN.
[5]"Internalization of echovirus 1 in caveolae."
Marjomaki V., Pietiainen V., Matilainen H., Upla P., Ivaska J., Nissinen L., Reunanen H., Huttunen P., Hyypia T., Heino J.
J. Virol. 76:1856-1865(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF CAPSID PROTEINS.
[6]"Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events."
Pietiainen V., Marjomaki V., Upla P., Pelkmans L., Helenius A., Hyypia T.
Mol. Biol. Cell 15:4911-4925(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF CAPSID PROTEINS.
[7]"Structure determination of echovirus 1."
Filman D.J., Wien M.W., Cunningham J.A., Bergelson J.M., Hogle J.M.
Acta Crystallogr. D 54:1261-1272(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.55 ANGSTROMS) OF 1-850.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF029859 Genomic RNA. Translation: AAC63944.2.
X89531 Genomic RNA. Translation: CAA61710.1.
AF081314 Genomic RNA. Translation: AAD17718.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EV1X-ray3.551570-850[»]
277-330[»]
3331-569[»]
42-69[»]
ProteinModelPortalO91734.
SMRO91734. Positions 2-69, 77-1000, 1540-2184.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC03.011.

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

EvolutionaryTraceO91734.

Entry information

Entry namePOLG_EC01F
AccessionPrimary (citable) accession number: O91734
Secondary accession number(s): Q66795, Q9YID6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 133 of the entry and version 4 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