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P03303 (POLG_HRV14) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 167. 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
OrganismHuman rhinovirus 14 (HRV-14) [Complete proteome]
Taxonomic identifier12131 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length2179 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 ICAM1 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.4

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.4

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.4

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.4

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.4

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.4

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.4

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.4

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.4

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.4

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.4

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.4

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.4

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.4

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 ICAM1. Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid By similarity. Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid By similarity. Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 By similarity. Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis By similarity. Protein 3AB: interacts with protein 3CD By similarity. Viral protein genome-linked: interacts with RNA-directed RNA polymerase By similarity. Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD By similarity.

Subcellular location

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

Capsid protein VP4: Virion By similarity.

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

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

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

Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

Protein 3AB: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

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

Protease 3C: Host cytoplasm By similarity.

Protein 3CD: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

RNA-directed RNA polymerase: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

Post-translational modification

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity.

VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.

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

Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion By similarity.

Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins By similarity.

Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion By similarity.

Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication By similarity.

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Contains 1 peptidase C3 domain.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Caution

The PDB data bank contains the 3D-structure coordinates of proteins VP1, VP2, VP3 and VP4.

Ontologies

Keywords
   Biological processActivation of host autophagy by virus
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 penetration via lysis of host organellar membrane
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

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

lysis of host organelle involved in viral entry into host cell

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 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

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 – 21792178Genome polyprotein By similarity
PRO_0000426536
Chain2 – 856855P1 By similarity
PRO_0000426537
Chain2 – 331330Capsid protein VP0 Potential
PRO_0000426538
Chain2 – 6968Capsid protein VP4 Potential
PRO_0000426539
Chain70 – 331262Capsid protein VP2 Potential
PRO_0000426540
Chain332 – 563232Capsid protein VP3 Potential
PRO_0000426541
Chain564 – 856293Capsid protein VP1 Potential
PRO_0000426542
Chain857 – 1429573P2 By similarity
PRO_0000426543
Chain857 – 1002146Protease 2A Potential
PRO_0000040029
Chain1003 – 109997Protein 2B Potential
PRO_0000040030
Chain1101 – 1429329Protein 2C Potential
PRO_0000426544
Chain1430 – 2179750P3 By similarity
PRO_0000426545
Chain1430 – 1537108Protein 3AB Potential
PRO_0000426546
Chain1430 – 151485Protein 3A Potential
PRO_0000040032
Chain1515 – 153723Viral protein genome-linked Potential
PRO_0000426547
Chain1538 – 2179642Protein 3CD Potential
PRO_0000426548
Chain1538 – 1718181Protease 3C Potential
PRO_0000426549
Chain1719 – 2179461RNA-directed RNA polymerase By similarity
PRO_0000426550

Regions

Topological domain2 – 14911490Cytoplasmic Potential
Intramembrane1492 – 150716 Potential
Topological domain1508 – 2179672Cytoplasmic Potential
Domain1205 – 1361157SF3 helicase
Domain1538 – 1702165Peptidase C3
Domain1946 – 2060115RdRp catalytic
Region564 – 58421Amphipatic alpha-helix Potential
Region1430 – 145122Disordered By similarity

Sites

Active site8761For Protease 2A activity By similarity
Active site8941For Protease 2A activity By similarity
Active site9651For Protease 2A activity By similarity
Active site15771For Protease 3C activity Potential
Active site16081For Protease 3C activity Potential
Active site16831For Protease 3C activity By similarity
Active site20461For RdRp activity By similarity
Site69 – 702Cleavage; by autolysis Potential
Site331 – 3322Cleavage; by Protease 3C Potential
Site856 – 8572Cleavage; by Protease 2A Potential
Site1002 – 10032Cleavage; by Protease 3C Potential
Site1429 – 14302Cleavage; by Protease 3C Potential
Site1514 – 15152Cleavage; by Protease 3C Potential
Site1537 – 15382Cleavage; by Protease 3C Potential
Site1719 – 17202Cleavage; by Protease 3C Potential

Amino acid modifications

Modified residue15171O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Experimental info

Sequence conflict3681P → L in AAA45756. Ref.3
Sequence conflict4591I → T in AAA45756. Ref.3
Sequence conflict7221P → H in AAA45756. Ref.3
Sequence conflict726 – 7272NP → KS Ref.3
Sequence conflict729 – 7313EWD → RVG Ref.3
Sequence conflict9131C → R in AAA45756. Ref.3
Sequence conflict9421N → S in AAA45756. Ref.3
Sequence conflict9621P → L in AAA45756. Ref.3
Sequence conflict9821G → E in AAA45756. Ref.3
Sequence conflict11931L → F in AAA45756. Ref.3
Sequence conflict11931L → H in AAA45758. Ref.2
Sequence conflict12201I → T Ref.2
Sequence conflict12201I → T Ref.3
Sequence conflict13991I → V Ref.2
Sequence conflict13991I → V Ref.3
Sequence conflict14461P → S in AAA45756. Ref.3
Sequence conflict17391P → A in AAA45756. Ref.3

Secondary structure

.................................................................................................................................................................................................................................................................... 2179
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03303 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 827201A3032F0285

FASTA2,179242,991
        10         20         30         40         50         60 
MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASTS SAGQSLSMDP SKFTEPVKDL 

        70         80         90        100        110        120 
MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA VVCYAEWPEY LPDVDASDVN 

       130        140        150        160        170        180 
KTSKPDTSVC RFYTLDSKTW TTGSKGWCWK LPDALKDMGV FGQNMFFHSL GRSGYTVHVQ 

       190        200        210        220        230        240 
CNATKFHSGC LLVVVIPEHQ LASHEGGNVS VKYTFTHPGE RGIDLSSANE VGGPVKDVIY 

       250        260        270        280        290        300 
NMNGTLLGNL LIFPHQFINL RTNNTATIVI PYINSVPIDS MTRHNNVSLM VIPIAPLTVP 

       310        320        330        340        350        360 
TGATPSLPIT VTIAPMCTEF SGIRSKSIVP QGLPTTTLPG SGQFLTTDDR QSPSALPNYE 

       370        380        390        400        410        420 
PTPRIHIPGK VHNLLEIIQV DTLIPMNNTH TKDEVNSYLI PLNANRQNEQ VFGTNLFIGD 

       430        440        450        460        470        480 
GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG PALSSAKLIL AYTPPGARGP QDRREAMLGT 

       490        500        510        520        530        540 
HVVWDIGLQS TIVMTIPWTS GVQFRYTDPD TYTSAGFLSC WYQTSLILPP ETTGQVYLLS 

       550        560        570        580        590        600 
FISACPDFKL RLMKDTQTIS QTVALTEGLG DELEEVIVEK TKQTVASISS GPKHTQKVPI 

       610        620        630        640        650        660 
LTANETGATM PVLPSDSIET RTTYMHFNGS ETDVECFLGR AACVHVTEIQ NKDATGIDNH 

       670        680        690        700        710        720 
REAKLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT ASQPDSANYS SNLVVQAMYV 

       730        740        750        760        770        780 
PPGAPNPKEW DDYTWQSASN PSVFFKVGDT SRFSVPYVGL ASAYNCFYDG YSHDDAETQY 

       790        800        810        820        830        840 
GITVLNHMGS MAFRIVNEHD EHKTLVKIRV YHRAKHVEAW IPRAPRALPY TSIGRTNYPK 

       850        860        870        880        890        900 
NTEPVIKKRK GDIKSYGLGP RYGGIYTSNV KIMNYHLMTP EDHHNLIAPY PNRDLAIVST 

       910        920        930        940        950        960 
GGHGAETIPH CNCTSGVYYS TYYRKYYPII CEKPTNIWIE GNPYYPSRFQ AGVMKGVGPA 

       970        980        990       1000       1010       1020 
EPGDCGGILR CIHGPIGLLT AGGSGYVCFA DIRQLECIAE EQGLSDYITG LGRAFGVGFT 

      1030       1040       1050       1060       1070       1080 
DQISTKVTEL QEVAKDFLTT KVLSKVVKMV SALVIICRNH DDLVTVTATL ALLGCDGSPW 

      1090       1100       1110       1120       1130       1140 
RFLKMYISKH FQVPYIERQA NDGWFRKFND ACNAAKGLEW IANKISKLIE WIKNKVLPQA 

      1150       1160       1170       1180       1190       1200 
KEKLEFCSKL KQLDILERQI TTMHISNPTQ EKREQLFNNV LWLEQMSQKF APLYAVESKR 

      1210       1220       1230       1240       1250       1260 
IRELKNKMVN YMQFKSKQRI EPVCVLIHGT PGSGKSLTTS IVGRAIAEHF NSAVYSLPPD 

      1270       1280       1290       1300       1310       1320 
PKHFDGYQQQ EVVIMDDLNQ NPDGQDISMF CQMVSSVDFL PPMASLDNKG MLFTSNFVLA 

      1330       1340       1350       1360       1370       1380 
STNSNTLSPP TILNPEALVR RFGFDLDICL HTTYTKNGKL NAGMSTKTCK DCHQPSNFKK 

      1390       1400       1410       1420       1430       1440 
CCPLVCGKAI SLVDRTTNIR YSVDQLVTAI ISDFKSKMQI TDSLETLFQG PVYKDLEIDV 

      1450       1460       1470       1480       1490       1500 
CNTPPPECIN DLLKSVDSEE IREYCKKKKW IIPEIPTNIE RAMNQASMII NTILMFVSTL 

      1510       1520       1530       1540       1550       1560 
GIVYVIYKLF AQTQGPYSGN PPHNKLKAPT LRPVVVQGPN TEFALSLLRK NIMTITTSKG 

      1570       1580       1590       1600       1610       1620 
EFTGLGIHDR VCVIPTHAQP GDDVLVNGQK IRVKDKYKLV DPENINLELT VLTLDRNEKF 

      1630       1640       1650       1660       1670       1680 
RDIRGFISED LEGVDATLVV HSNNFTNTIL EVGPVTMAGL INLSSTPTNR MIRYDYATKT 

      1690       1700       1710       1720       1730       1740 
GQCGGVLCAT GKIFGIHVGG NGRQGFSAQL KKQYFVEKQG QVIARHKVRE FNINPVNTPT 

      1750       1760       1770       1780       1790       1800 
KSKLHPSVFY DVFPGDKEPA VLSDNDPRLE VKLTESLFSK YKGNVNTEPT ENMLVAVDHY 

      1810       1820       1830       1840       1850       1860 
AGQLLSLDIP TSELTLKEAL YGVDGLEPID ITTSAGFPYV SLGIKKRDIL NKETQDTEKM 

      1870       1880       1890       1900       1910       1920 
KFYLDKYGID LPLVTYIKDE LRSVDKVRLG KSRLIEASSL NDSVNMRMKL GNLYKAFHQN 

      1930       1940       1950       1960       1970       1980 
PGVLTGSAVG CDPDVFWSVI PCLMDGHLMA FDYSNFDASL SPVWFVCLEK VLTKLGFAGS 

      1990       2000       2010       2020       2030       2040 
SLIQSICNTH HIFRDEIYVV EGGMPSGCSG TSIFNSMINN IIIRTLILDA YKGIDLDKLK 

      2050       2060       2070       2080       2090       2100 
ILAYGDDLIV SYPYELDPQV LATLGKNYGL TITPPDKSET FTKMTWENLT FLKRYFKPDQ 

      2110       2120       2130       2140       2150       2160 
QFPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCMLAW HSGEKEYNEF IQKIRTTDIG 

      2170 
KCLILPEYSV LRRRWLDLF 

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References

[1]"The complete nucleotide sequence of a common cold virus: human rhinovirus 14."
Stanway G., Hughes P.J., Mountford R.C., Minor P.D., Almond J.W.
Nucleic Acids Res. 12:7859-7875(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Role of maturation cleavage in infectivity of picornaviruses: activation of an infectosome."
Lee W.M., Monroe S., Rueckert R.R.
J. Virol. 67:2110-2122(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Molecular cloning and complete sequence determination of RNA genome of human rhinovirus type 14."
Callahan P.L., Mizutani S., Colonno R.J.
Proc. Natl. Acad. Sci. U.S.A. 82:732-736(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[4]"Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus."
Gustin K.E., Sarnow P.
J. Virol. 76:8787-8796(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF PROTEASE 2A.
[5]"Uncoating of human rhinoviruses."
Fuchs R., Blaas D.
Rev. Med. Virol. 20:281-297(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[6]"Productive entry pathways of human rhinoviruses."
Fuchs R., Blaas D.
Adv. Virol. 2012:826301-826301(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[7]"Structure of a human common cold virus and functional relationship to other picornaviruses."
Rossman M.G., Arnold E., Erickson J.W., Frankenberger E.A., Griffith J.P., Hecht H.-J., Johnson J.E., Kamer G., Luo M., Mosser A.G., Rueckert R.R., Sherry B., Vriend G.
Nature 317:145-153(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[8]"The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure."
Arnold E., Rossman M.G.
Acta Crystallogr. A 44:270-282(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[9]"Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor."
Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., Rossmann M.G.
EMBO J. 18:6249-6259(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF 70-856 IN COMPLEX WITH ICAM1.
[10]"Analysis of the structure of a common cold virus, human rhinovirus 14, refined at a resolution of 3.0 A."
Arnold E., Rossman M.G.
J. Mol. Biol. 211:763-801(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with antiviral compound SCH 38057

Virus Particle ExploreR db

Icosahedral capsid structure complexed with antiviral compound SDZ 35-682

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01087 Genomic RNA. Translation: CAA25565.1.
L05355 Genomic RNA. Translation: AAA45758.1.
K02121 Genomic RNA. Translation: AAA45756.1.
PIRGNNYH4. A03901.
RefSeqNP_041009.1. NC_001490.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3Ielectron microscopy26.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1HRIX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1HRVX-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1K5MX-ray2.70A568-856[»]
C332-567[»]
D2-69[»]
1NA1X-ray3.30A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1NCQX-ray2.50A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1R08X-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1R09X-ray2.901568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1RMUX-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1RUCX-ray3.101568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1RUDX-ray2.901568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1RUEX-ray2.901568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1RUFX-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUGX-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1RUHX-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1RUIX-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1RUJX-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1RVFX-ray4.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1VRHX-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
1XR5X-ray2.80A1720-2179[»]
2B0FNMR-A1538-1719[»]
2HWBX-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
2HWCX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2IN2NMR-A1538-1719[»]
2R04X-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
2R06X-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
2R07X-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
2RM2X-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
2RMUX-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
2RR1X-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
2RS1X-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
2RS3X-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
2RS5X-ray3.001568-855[»]
270-330[»]
3332-566[»]
42-68[»]
4RHVX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
ProteinModelPortalP03303.
SMRP03303. Positions 2-69, 77-567, 574-856, 1429-1486, 1538-2179.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC03.013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1461213.

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

EvolutionaryTraceP03303.

Entry information

Entry namePOLG_HRV14
AccessionPrimary (citable) accession number: P03303
Secondary accession number(s): Q82083 expand/collapse secondary AC list , Q82123, Q84736, Q84737, Q84738, Q84739, Q84740, Q84741, Q84774, Q84775, Q84776, Q84777, Q84778, Q84779, Q89441, Q89649, Q89763, Q89883
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 167 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references