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UniProtKB/Swiss-Prot entry P07210


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name POLG_HRV89
Primary accession number P07210
Secondary accession numbers Q82096 Q82097 Q82098 Q82099 Q82100 Q82101 Q82102 Q82103 Q82104 Q82105
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 91)
Name and origin of the protein
Protein name Genome polyprotein
Synonyms None
Contains Protein VP0
     (VP4-VP2)
Protein VP4
     (Virion protein 4)
     (P1A)
Protein VP2
     (Virion protein 2)
     (P1B)
Protein VP3
     (Virion protein 3)
     (P1C)
Protein VP1
     (Virion protein 1)
     (P1D)
Picornain 2A
     (Protein 2A)
     (P2A)
     (EC 3.4.22.29)
Protein 2B
     (P2B)
Protein 2C
     (P2C)
     (EC 3.6.1.15)
Protein 3A
     (P3A)
Protein 3B
     (P3B)
     (VPg)
Picornain 3C
     (EC 3.4.22.28)
     (Protease 3C)
     (P3C)
RNA-directed RNA polymerase 3D-POL
     (P3D-POL)
     (EC 2.7.7.48)
Gene name None
From
Human rhinovirus 89 (HRV-89) [TaxID: 12132] 
Taxonomy Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; Picornaviridae; Rhinovirus.
Virus host Homo sapiens (Human) [TaxID: 9606]
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3033653 [NCBI, ExPASy, EBI, Israel, Japan]
Duechler M., Skern T., Sommergruber W., Neubauer C., Gruendler P., Fogy I., Blaas D., Kuechler E.;
"Evolutionary relationships within the human rhinovirus genus: comparison of serotypes 89, 2, and 14.";
Proc. Natl. Acad. Sci. U.S.A. 84:2605-2609(1987).
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 capsid interacts with human ICAM1 to provide virion attachment to target cell (By similarity).
  • FUNCTION: VP0 precursor is a component of immature procapsids (By similarity).
  • FUNCTION: 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 (By similarity).
  • FUNCTION: Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity).
  • FUNCTION: Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
  • FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).
  • FUNCTION: 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).
  • FUNCTION: 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).
  • CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
  • CATALYTIC ACTIVITY: 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.
  • CATALYTIC ACTIVITY: NTP + H2O = NDP + phosphate.
  • SUBUNIT: Capsid proteins interact with host ICAM1 (By similarity).
  • SUBCELLULAR LOCATION: Protein VP2: Virion. Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: Protein VP3: Virion. Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: Protein VP1: Virion. Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: Protein 2B: 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).
  • SUBCELLULAR LOCATION: Protein 2C: 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).
  • SUBCELLULAR LOCATION: Protein 3A: 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).
  • SUBCELLULAR LOCATION: Protein 3B: Virion (Potential).
  • SUBCELLULAR LOCATION: Picornain 3C: Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: 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).
  • PTM: 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).
  • PTM: VPg is covalently linked to the genomic RNA (By similarity).
  • PTM: Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle (By similarity).
  • SIMILARITY: Belongs to the picornaviruses polyprotein family.
  • SIMILARITY: Contains 2 peptidase C3 domains [view classification].
  • SIMILARITY: Contains 1 RdRp catalytic domain.
  • SIMILARITY: Contains 1 SF3 helicase domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M16248; AAA45762.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29862; GNNY89.
3D structure databases
ModBase P07210.
Protein family/group databases
MEROPS C03.007; -.
C03.021; -.
Ontologies
GO
GO:0031410; Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR003593; AAA+_ATPase_core.
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 of domain structure.
Pfam PF08727; P3A; 1.
PF00548; Peptidase_C3; 1.
PF02226; Pico_P1A; 1.
PF00947; Pico_P2A; 1.
PF01552; Pico_P2B; 1.
PF00680; RdRP_1; 1.
PF00073; Rhv; 3.
PF00910; RNA_helicase; 1.
Pfam graphical view of domain structure.
ProDom PD001125; Pept_C3_picorn; 1.
PD001306; Peptidase_C3_2; 1.
PD001274; Pico_P2B; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00382; AAA; 1.
SMART graphical view of domain structure.
PROSITE PS50507; RDRP_SSRNA_POS; 1.
PS51218; SF3_HELICASE_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P07210.
ProtoNet P07210.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Capsid protein; Complete proteome; Covalent protein-RNA linkage; Cytoplasm; Cytoplasmic vesicle; Helicase; Host-virus interaction; Hydrolase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease; RNA replication; RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase; Virion.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed; by host (By similarity). 
CHAIN   2    336  335     Protein VP0 (Potential). PRO_0000311076
CHAIN   2     69  68     Protein VP4 (Potential). PRO_0000040047
CHAIN   70    336  267     Protein VP2 (Potential). PRO_0000040048
CHAIN   337    574  238     Protein VP3 (Potential). PRO_0000040049
CHAIN   575    866  292     Protein VP1 (Potential). PRO_0000040050
CHAIN   867   1008  142     Picornain 2A (Potential). PRO_0000040051
CHAIN   1009   1103  95     Protein 2B (Potential). PRO_0000040052
CHAIN   1104   1424  321     Protein 2C (Potential). PRO_0000040053
CHAIN   1425   1500  76     Protein 3A (Potential). PRO_0000040054
CHAIN   1501   1521  21     Protein 3B (Potential). PRO_0000040055
CHAIN   1522   1704  183     Picornain 3C (Potential). PRO_0000040056
CHAIN   1705   2164  460     RNA-directed RNA polymerase 3D-POL (Potential). PRO_0000040057
TOPO_DOM   2   1477  1476     Cytoplasmic (Potential). 
TOPO_DOM   1478   1493  16     In membrane (Potential). 
TOPO_DOM   1494   2164  671     Cytoplasmic (Potential). 
DOMAIN   1197   1357  161     SF3 helicase. 
DOMAIN   1932   2045  114     RdRp catalytic. 
NP_BIND   1227   1234  8     ATP (Potential). 
ACT_SITE   884    884        For picornain 2A activity (By similarity). 
ACT_SITE   901    901        For picornain 2A activity (By similarity). 
ACT_SITE   972    972        For picornain 2A activity (By similarity). 
ACT_SITE   1561   1561        For picornain 3C activity (Potential). 
ACT_SITE   1592   1592        For picornain 3C activity (Potential). 
ACT_SITE   1668   1668        For picornain 3C activity (Potential). 
SITE   69     70  2     Cleavage (Potential). 
SITE   336    337  2     Cleavage; by picornain 3C (Potential). 
SITE   866    867  2     Cleavage; by picornain 2A (Potential). 
SITE   1008   1009  2     Cleavage; by picornain 3C (Potential). 
SITE   1103   1104  2     Cleavage; by picornain 3C (Potential). 
SITE   1424   1425  2     Cleavage; by picornain 3C (Potential). 
SITE   1500   1501  2     Cleavage; by picornain 3C (Potential). 
SITE   1521   1522  2     Cleavage; by picornain 3C (Potential). 
SITE   1704   1705  2     Cleavage; by picornain 3C (Potential). 
MOD_RES   1503   1503        O-(5'-phospho-RNA)-tyrosine (By similarity). 
LIPID   2      2        N-myristoyl glycine; by host (By similarity). 
Sequence information
Length: 2164 AA [This is the length of the unprocessed precursor] Molecular weight: 241065 Da [This is the MW of the unprocessed precursor] CRC64: F5D9C8F4FBEA7D54 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP SKFTDPVKDV 

        70         80         90        100        110        120 
LEKGIPTLQS PTVEACGYSD RLIQITRGDS TITSQDTANA VVAYGVWPSY LTPDDATAID 

       130        140        150        160        170        180 
KPTQPDTSSN RFYTLDSRSW TSASSGWWWK LPDALKNMGI FGENMFYHFL GRSGYTIHVQ 

       190        200        210        220        230        240 
CNSSKFHQGL LIVAAIPEHQ LASATSGNVS VGYNHTHPGE QGREVVPSRT SSDNKRPSDD 

       250        260        270        280        290        300 
SWLNFDGTLL GNLPIYPHQY INLRTNNSAT LILPYVNAVP MDSMLRHNNW SLVIIPICPL 

       310        320        330        340        350        360 
QVQPGGTQSI PITVSISPMF SEFSGPRSKV VFSTTQGLPV MLTPGSGQFL TTDDTQSPSA 

       370        380        390        400        410        420 
FPYFHPTKEI FIPGQVRNLI EMCQVDTLIP VNNTQENVRS VNMYTVDLRT QVDLAKEVFS 

       430        440        450        460        470        480 
IPVDIASQPL ATTLIGELAS YYTHWTGSLR FSFMFCGSAS STLKLLIAYT PPGVGKPKSR 

       490        500        510        520        530        540 
REAMLGTHLV WDVGLQSTAS LVVPWVSASH FRFTTPDTYS SAGYITCWYQ TNFVVPDSTP 

       550        560        570        580        590        600 
DNAKMVCMVS ACKDFCLRLA RDTNLHTQEG VLTQNPVENY IDSVLNEVLV VPNIQPSTSV 

       610        620        630        640        650        660 
SSHAAPALDA AETGHTSSVQ PEDMIETRYV ITDQTRDETS IESFLGRSGC IAMIEFNTSS 

       670        680        690        700        710        720 
DKTEHDKIGK GFKTWKVSLQ EMAQIRRKYE LFTYTRFDSE ITIVTAAAAQ GNDSGHIVLQ 

       730        740        750        760        770        780 
FMYVPPGAPV PEKRDDYTWQ SGTNASVFWQ EGQPYPRFTI PFMSIASAYY MFYDGYDGDS 

       790        800        810        820        830        840 
AASKYGSVVT NDMGTICVRI VTSNQKHDSN IVCRIYHKAK HIKAWCPRPP RAVAYQHTHS 

       850        860        870        880        890        900 
TNYIPSNGEA TTQIKTRPDV FTVTNVGPSS MFVHVGNLIY RNLHLFNSDL DDSILVSYSS 

       910        920        930        940        950        960 
DLIIYRTNTE GNDVIPNCDC TECTYYCHHK DRYFPIRVTA HDWYEIQESE YYPKHIQYNL 

       970        980        990       1000       1010       1020 
LIGEGPCEPG DCGGKLLCKH GVIGMITAGG EGHVAFIDLR KFQCAEEQGL SDYVEHLGQV 

      1030       1040       1050       1060       1070       1080 
FGVGFVDSIK QQVNFINPTS KIGSKVIKWL LRIVSAMIIM VRNSSDPQTV IATLTLLGCS 

      1090       1100       1110       1120       1130       1140 
GSPWRFLKEK LCAWLQLSYV HKQSDSWLKK FTEACNAARG LEWIGQKISK FIDWIKSMLP 

      1150       1160       1170       1180       1190       1200 
QAQLKIDYLT KLKQLNLLEK QIETIRLAPA SVQEKIFIEI NTLHDLSLKF LPLYASEARR 

      1210       1220       1230       1240       1250       1260 
IKNLYIKCSN VIKGGKRNEP VAVLIHGSPG TGKSLATSVL ARMLTVETDI YSLPPDPKYF 

      1270       1280       1290       1300       1310       1320 
DGYDQQSVVI MDDIMQNPSG EDMTLFCQMV SSVPFIPPMA DLPDKGKPFT SKFVLASTNH 

      1330       1340       1350       1360       1370       1380 
TLLTPPTVSS LPAMARRFYF DLDIQVKKEY LLDGKLDIAK SFRPCDVNIK IGNAKCCPFI 

      1390       1400       1410       1420       1430       1440 
CGKAVEFKDR NSCTTLSLSQ LYSHIKEEDR RRSSAAQAME AIFQGIDLQS PPPPAIADLL 

      1450       1460       1470       1480       1490       1500 
RSVKTPEIIK YCQDNNWIVP AECSIERDLG IANMTIGIIA NVVSIVGVIY IIYKLFCTLQ 

      1510       1520       1530       1540       1550       1560 
GPYSGEPKPK SRAPERRVVT QGPEEEFGRS LLKHNCCVVT TDKGKFTGLG IYDQVMVLPT 

      1570       1580       1590       1600       1610       1620 
HSDPGSEILV DGVKVKVSDS YDLHNHEGVK LEITVVKLIR NEKFKDIRKY LPSREDDYPA 

      1630       1640       1650       1660       1670       1680 
CNLALLANQD EPTIISVGDA VSYGNILLSG TNTARMIKYH YPTKAGYCGG VLYKVGSILG 

      1690       1700       1710       1720       1730       1740 
IHVGGNGRDG FSAMLLKSYF GETQGLITKE LPVSVKNLPS VHVSSKTRLQ PSVFHDVFPG 

      1750       1760       1770       1780       1790       1800 
TKEPAVLSSN DPRLETDFDS ALFSKYKGNP ACQVTPHMKI AVAHYAAQLS TLDINPQPLS 

      1810       1820       1830       1840       1850       1860 
LEESVFGIEG LEALDLNTSA GFPYVSLGIK KKDLIDKKTK DITKLRKAID EYGIDLPMVT 

      1870       1880       1890       1900       1910       1920 
FLKDELRKKE KIKDGKTRVI EANSVNDTVL FRSVFGNLFS AFHKNPGIVT GSAVGCDPEV 

      1930       1940       1950       1960       1970       1980 
FWSTIPLMLD GECLMAFDYS NYDGSLHPVW FKCLSMLLED IGFSSQLINQ ICNSKHIYKS 

      1990       2000       2010       2020       2030       2040 
KYYEVEGGMP SGCAGTSIFN TIINNIIIRT LVLDAYKNID LDKLKILAYG DDVIFSYNFK 

      2050       2060       2070       2080       2090       2100 
LDMAVLAKEG EKYGLTITPA DKSDVFQELT YKNVTFLKRG FRADERHSFL IHPTFPVAEI 

      2110       2120       2130       2140       2150       2160 
HDSIRWTKNP SCMQEHVLSL CHLMWHNGRH AYQEFIKGIR SVSAGRALYI PAYEVLEHEW 


YEKF 

P07210 in FASTA format

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