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Q82122 (POLG_HRV16) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 137. 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 12 chains:

  1. Protein VP0
    Alternative name(s):
    VP4-VP2
  2. Protein VP4
    Alternative name(s):
    P1A
    Virion protein 4
  3. Protein VP2
    Alternative name(s):
    P1B
    Virion protein 2
  4. Protein VP3
    Alternative name(s):
    P1C
    Virion protein 3
  5. Protein VP1
    Alternative name(s):
    P1D
    Virion protein 1
  6. Protease 2A
    Short name=P2A
    EC=3.4.22.29
    Alternative name(s):
    Protein 2A
  7. Protein 2B
    Short name=P2B
  8. Protein 2C
    Short name=P2C
    EC=3.6.1.15
  9. Protein 3A
    Short name=P3A
  10. Protein 3B
    Short name=P3B
    Alternative name(s):
    VPg
  11. Protease 3C
    Short name=P3C
    EC=3.4.22.28
    Alternative name(s):
    Picornain 3C
  12. RNA-directed RNA polymerase 3D-POL
    Short name=P3D-POL
    EC=2.7.7.48
OrganismHuman rhinovirus 16 (HRV-16) [Complete proteome]
Taxonomic identifier31708 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusRhinovirus A
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length2153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein VP1: Forms, together with VP2 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Protein VP1 mainly forms the vertices of the capsid. VP1 interacts with host cell receptor ICAM1 to provide virion attachment to target cell. This attachment induces virion internalization through a cell-type specific entry mechanism. After binding to its receptor, the capsid undergoes conformational changes. VP1 N-terminus (that contains an amphipathic alpha-helix) is externalized, VP4 is released and together, they shape a virion-cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks By similarity. Ref.2

Protein VP2: Forms, together with VP1 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome By similarity. Ref.2

Protein VP3: Forms, together with VP1 and VP2, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome By similarity. Ref.2

Protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. VP4 is released, VP1 N-terminus is externalized, and together, they shape a virion-cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks By similarity. Ref.2

Protein VP0: Protein VP0: VP0 precursor is a component of immature procapsids, which gives rise to VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step By similarity. Ref.2

Protease 2A: 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 off the capped cellular mRNA transcription. Protease 2A also degrades host nucleoporins NUP62, NUP98 and NUP153 thereby blocking the nucleo-cytoplasmic trafficking, in particular the export of cellular mRNAs. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response By similarity. Ref.2

Protein 2B: Affects membrane integrity and cause an increase in membrane permeability By similarity. Ref.2

Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity. Ref.2

Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity. Ref.2

Protease 3C: 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 cooperatively to the protease By similarity. Cleaves Nup153, Nup214, and Nup358 thereby blocking the nucleo-cytoplasmic trafficking. Contributes to host cell shutoff in infected cells by localizing in the nucleus and facilitating nuclear pore breakdown. Ref.2

RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity. Ref.2

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

Capsid proteins interact with host ICAM1 By similarity.

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.

Protease 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 By similarity.

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.

Ontologies

Keywords
   Biological processActivation of host autophagy by virus
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
Virion
   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

endocytosis involved in viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

induction by virus of host autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

ion transmembrane transport

Inferred from electronic annotation. Source: GOC

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 mRNA export from nucleus

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

transcription, RNA-templated

Inferred from electronic annotation. Source: GOC

viral 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 – 330329Protein VP0 Potential
PRO_0000311075
Chain2 – 6968Protein VP4 Potential
PRO_0000040036
Chain70 – 330261Protein VP2 Potential
PRO_0000040037
Chain331 – 568238Protein VP3 Potential
PRO_0000040038
Chain569 – 853285Protein VP1 Potential
PRO_0000040039
Chain854 – 995142Protease 2A Potential
PRO_0000040040
Chain996 – 109095Protein 2B Potential
PRO_0000040041
Chain1091 – 1412322Protein 2C Potential
PRO_0000040042
Chain1413 – 148977Protein 3A Potential
PRO_0000040043
Chain1490 – 151021Protein 3B Potential
PRO_0000040044
Chain1511 – 1693183Protease 3C Potential
PRO_0000040045
Chain1694 – 2153460RNA-directed RNA polymerase 3D-POL Potential
PRO_0000040046

Regions

Topological domain2 – 14661465Cytoplasmic Potential
Intramembrane1467 – 148216 Potential
Topological domain1483 – 2153671Cytoplasmic Potential
Domain1186 – 1346161SF3 helicase
Domain1921 – 2034114RdRp catalytic
Nucleotide binding1214 – 12218ATP Potential

Sites

Active site8711For protease 2A activity By similarity
Active site8881For protease 2A activity By similarity
Active site9591For protease 2A activity By similarity
Active site15501For protease 3C activity Potential
Active site15811For protease 3C activity Potential
Active site16571For protease 3C activity By similarity
Site69 – 702Cleavage Potential
Site330 – 3312Cleavage; by protease 3C Potential
Site853 – 8542Cleavage; by protease 2A Potential
Site995 – 9962Cleavage; by protease 3C Potential
Site1412 – 14132Cleavage; by protease 3C Potential
Site1489 – 14902Cleavage; by protease 3C Potential
Site1510 – 15112Cleavage; by protease 3C Potential
Site1693 – 16942Cleavage; by protease 3C Potential

Amino acid modifications

Modified residue14921O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Experimental info

Sequence conflict547 – 5482KD → NH in AAA69862. Ref.1

Secondary structure

................................................................................................................................................................................................................................. 2153
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q82122 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 6B11D0D93DF11C04

FASTA2,153242,244
        10         20         30         40         50         60 
MGAQVSRQNV GTHSTQNMVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP SKFTDPVKDV 

        70         80         90        100        110        120 
LEKGIPTLQS PSVEACGYSD RIIQITRGDS TITSQDVANA VVGYGVWPHY LTPQDATAID 

       130        140        150        160        170        180 
KPTQPDTSSN RFYTLDSKMW NSTSKGWWWK LPDALKDMGI FGENMFYHFL GRSGYTVHVQ 

       190        200        210        220        230        240 
CNASKFHQGT LLVVMIPEHQ LATVNKGNVN AGYKYTHPGE AGREVGTQVE NEKQPSDDNW 

       250        260        270        280        290        300 
LNFDGTLLGN LLIFPHQFIN LRSNNSATLI VPYVNAVPMD SMVRHNNWSL VIIPVCQLQS 

       310        320        330        340        350        360 
NNISNIVPIT VSISPMCAEF SGARAKTVVQ GLPVYVTPGS GQFMTTDDMQ SPCALPWYHP 

       370        380        390        400        410        420 
TKEIFIPGEV KNLIEMCQVD TLIPINSTQS NIGNVSMYTV TLSPQTKLAE EIFAIKVDIA 

       430        440        450        460        470        480 
SHPLATTLIG EIASYFTHWT GSLRFSFMFC GTANTTLKVL LAYTPPGIGK PRSRKEAMLG 

       490        500        510        520        530        540 
THVVWDVGLQ STVSLVVPWI SASQYRFTTP DTYSSAGYIT CWYQTNFVVP PNTPNTAEML 

       550        560        570        580        590        600 
CFVSGCKDFC LRMARDTDLH KQTGPITQNP VERYVDEVLN EVLVVPNINQ SHPTTSNAAP 

       610        620        630        640        650        660 
VLDAAETGHT NKIQPEDTIE TRYVQSSQTL DEMSVESFLG RSGCIHESVL DIVDNYNDQS 

       670        680        690        700        710        720 
FTKWNINLQE MAQIRRKFEM FTYARFDSEI TMVPSVAAKD GHIGHIVMQY MYVPPGAPIP 

       730        740        750        760        770        780 
TTRDDYAWQS GTNASVFWQH GQPFPRFSLP FLSIASAYYM FYDGYDGDTY KSRYGTVVTN 

       790        800        810        820        830        840 
DMGTLCSRIV TSEQLHKVKV VTRIYHKAKH TKAWCPRPPR AVQYSHTHTT NYKLSSEVHN 

       850        860        870        880        890        900 
DVAIRPRTNL TTVGPSDMYV HVGNLIYRNL HLFNSDIHDS ILVSYSSDLI IYRTSTQGDG 

       910        920        930        940        950        960 
YIPTCNCTEA TYYCKHKNRY YPINVTPHDW YEIQESEYYP KHIQYNLLIG EGPCEPGDCG 

       970        980        990       1000       1010       1020 
GKLLCKHGVI GIITAGGEGH VAFIDLRHFH CAEEQGITDY IHMLGEAFGS GFVDSVKDQI 

      1030       1040       1050       1060       1070       1080 
NSINPINNIS SKMVKWMLRI ISAMVIIIRN SSDPQTIIAT LTLIGCNGSP WRFLKEKFCK 

      1090       1100       1110       1120       1130       1140 
WTQLTYIHKE SDSWLKKFTE MCNAARGLEW IGNKISKFID WMKSMLPQAQ LKVKYLSELK 

      1150       1160       1170       1180       1190       1200 
KLNFLEKQVE NLRAADTNTQ EKIKCEIDTL HDLSCKFLPL YASEAKRIKV LYHKCTNIIK 

      1210       1220       1230       1240       1250       1260 
QKKRSEPVAV MIHGPPGTGK SITTSFLARM ITNESDIYSL PPDPKYFDGY DNQSVVIMDD 

      1270       1280       1290       1300       1310       1320 
IMQNPGGEDM TLFCQMVSSV TFIPPMADLP DKGKPFDSRF VLCSTNHSLL APPTISSLPA 

      1330       1340       1350       1360       1370       1380 
MNRRFYLDLD ILVHDNYKDN QGKLDVSRAF RLCDVDSKIG NAKCCPFVCG KAVTFKDRNT 

      1390       1400       1410       1420       1430       1440 
CRTYSLSQIY NQILEEDKRR RQVVDVMSAI FQGPISMDKP PPPAITDLLR SVRTPEVIKY 

      1450       1460       1470       1480       1490       1500 
CQDNKWIVPA DCQIERDLNI ANSIITIIAN IISIAGIIYI IYKLFCSLQG PYSGEPKPKT 

      1510       1520       1530       1540       1550       1560 
KVPERRVVAQ GPEEEFGMSI IKNNTCVVTT TNGKFTGLGI YDRILILPTH ADPGSEIQVN 

      1570       1580       1590       1600       1610       1620 
GIHTKVLDSY DLFNKEGVKL EITVLKLDRN EKFRDIRKYI PESEDDYPEC NLALVANQTE 

      1630       1640       1650       1660       1670       1680 
PTIIKVGDVV SYGNILLSGT QTARMLKYNY PTKSGYCGGV LYKIGQILGI HVGGNGRDGF 

      1690       1700       1710       1720       1730       1740 
SSMLLRSYFT EQQGQIQISK HVKDVGLPSI HTPTKTKLQP SVFYDIFPGS KEPAVLTEKD 

      1750       1760       1770       1780       1790       1800 
PRLKVDFDSA LFSKYKGNTE CSLNEHIQVA VAHYSAQLAT LDIDPQPIAM EDSVFGMDGL 

      1810       1820       1830       1840       1850       1860 
EALDLNTSAG YPYVTLGIKK KDLINNKTKD ISKLKLALDK YDVDLPMITF LKDELRKKDK 

      1870       1880       1890       1900       1910       1920 
IAAGKTRVIE ASSINDTILF RTVYGNLFSK FHLNPGVVTG CAVGCDPETF WSKIPLMLDG 

      1930       1940       1950       1960       1970       1980 
DCIMAFDYTN YDGSIHPIWF KALGMVLDNL SFNPTLINRL CNSKHIFKST YYEVEGGVPS 

      1990       2000       2010       2020       2030       2040 
GCSGTSIFNS MINNIIIRTL VLDAYKHIDL DKLKIIAYGD DVIFSYKYKL DMEAIAKEGQ 

      2050       2060       2070       2080       2090       2100 
KYGLTITPAD KSSEFKELDY GNVTFLKRGF RQDDKYKFLI HPTFPVEEIY ESIRWTKKPS 

      2110       2120       2130       2140       2150 
QMQEHVLSLC HLMWHNGPEI YKDFETKIRS VSAGRALYIP PYELLRHEWY EKF 

« Hide

References

[1]"Complete sequence of the RNA genome of human rhinovirus 16, a clinically useful common cold virus belonging to the ICAM-1 receptor group."
Lee W.M., Wang W., Rueckert R.R.
Virus Genes 9:177-181(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Rhinovirus 3C protease can localize in the nucleus and alter active and passive nucleocytoplasmic transport."
Ghildyal R., Jordan B., Li D., Dagher H., Bardin P.G., Gern J.E., Jans D.A.
J. Virol. 83:7349-7352(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF PROTEASE 3C.
[3]"Productive entry pathways of human rhinoviruses."
Fuchs R., Blaas D.
Adv. Virol. 2012:826301-826301(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[4]"The structure of human rhinovirus 16."
Oliveira M.A., Zhao R., Lee W.M., Kremer M.J., Minor I., Rueckert R.R., Diana G.D., Pevear D.C., Dutko F.J., McKinlay M.A., Rossmann M.G.
Structure 1:51-68(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-853.
[5]"The refined structure of human rhinovirus 16 at 2.15-A resolution: implications for the viral life cycle."
Hadfield A.T., Lee W.M., Zhao R., Oliveira M.A., Minor I., Rueckert R.R., Rossmann M.G.
Structure 5:427-441(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-853, SEQUENCE REVISION TO 547-548.
+Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure at high resolution

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral drug VP63843 (pleconaril)

Virus Particle ExploreR db

Icosahedral capsid structure in complex with a two-domain fragment of its cellular receptor ICAM1

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound pleconaril

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound pleconaril

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound VP61209

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound WIN68934

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound VP65099

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L24917 Genomic RNA. Translation: AAA69862.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYMX-ray2.151569-853[»]
270-330[»]
3331-568[»]
1AYNX-ray2.901569-853[»]
270-330[»]
3331-568[»]
1C8MX-ray2.801569-852[»]
279-329[»]
3331-567[»]
42-77[»]
1D3Eelectron microscopy28.001574-853[»]
279-329[»]
3331-567[»]
42-68[»]
1NCRX-ray2.70A569-853[»]
B70-330[»]
C331-568[»]
D2-69[»]
1ND2X-ray2.50A569-853[»]
B70-330[»]
C331-568[»]
D2-69[»]
1ND3X-ray2.80A569-853[»]
B70-330[»]
C331-568[»]
D2-69[»]
1QJUX-ray2.801569-853[»]
270-330[»]
3331-568[»]
42-69[»]
1QJXX-ray2.801569-853[»]
270-330[»]
3331-568[»]
42-69[»]
1QJYX-ray2.801569-853[»]
270-330[»]
3331-568[»]
42-69[»]
1TP7X-ray2.40A/B/C/D1694-2153[»]
1XR7X-ray2.30A/B1694-2153[»]
4K50X-ray2.93A/E/I/M1694-2153[»]
ProteinModelPortalQ82122.
SMRQ82122. Positions 2-69, 79-992, 1511-1690, 1694-2153.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ82122.
ChEMBLCHEMBL5296.

Protein family/group databases

MEROPSC03.007.

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

EvolutionaryTraceQ82122.

Entry information

Entry namePOLG_HRV16
AccessionPrimary (citable) accession number: Q82122
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 137 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