Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9QEJ5 (POLG_PESV) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 7 chains:

  1. Protein p11
  2. Protein p28
  3. NTPase
    EC=3.6.1.15
    Alternative name(s):
    p35
  4. Protein p32
  5. Viral genome-linked protein
    Alternative name(s):
    VPg
    p14
  6. Protease-polymerase p70
    Short name=Pro-Pol
    EC=2.7.7.48
    EC=3.4.22.66
  7. Capsid protein
    Short name=CP
    Alternative name(s):
    VP1
    p60
Gene names
ORF Names:ORF1
OrganismPorcine enteric sapovirus (isolate Swine/United States/Cowden/1980) (Sw/SV/Cowden/1980/US)
Taxonomic identifier523795 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageCaliciviridaeSapovirus
Virus hostSus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length2254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity By similarity.

Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation By similarity.

Protease-polymerase p70 processes the polyprotein: Pro-Pol is first released by autocleavage, then all other proteins are cleaved By similarity. It is also an RNA-directed RNA polymerase which replicates genomic and antigenomic viral RNA by recognizing specific signals. Catalyzes the covalent attachment VPg with viral RNAs By similarity.

Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells, inducing endocytosis of the viral particle. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm By similarity.

Catalytic activity

NTP + H2O = NDP + phosphate.

Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Subunit structure

Capsid protein homodimerizes, then multimerizes By similarity.

Subcellular location

Capsid protein: Virion. Host cytoplasm.

Domain

Protease-polymerase is composed of two domains displaying two different catalytic activity. These activities may act independently.

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins. Pro-Pol is first autocatalytically cleaved, then processes the whole polyprotein.

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

Miscellaneous

Two differents RNAs lead the expression of the capsid protein. One arises from the cleavage of the polyprotein translated from the genomic RNA and the other from the translation of a subgenomic RNA derived from the (-)RNA template. Capsid protein expressed from the subgenomic mRNA is produced in much larger amounts than the cleaved one By similarity.

Sequence similarities

Contains 1 peptidase C24 domain.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Ontologies

Keywords
   Biological processDNA replication
Viral RNA replication
   Cellular componentCapsid protein
Host cytoplasm
Virion
   Coding sequence diversityAlternative promoter usage
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Thiol protease
Transferase
   PTMCovalent protein-RNA linkage
Phosphoprotein
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-protein covalent cross-linking

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

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

   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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: InterPro

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

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform Genome polyprotein (identifier: Q9QEJ5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced from the genomic RNA.
Isoform Subgenomic capsid protein (identifier: Q9QEJ5-2)

Also known as: VP1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1710: Missing.
Note: Produced from the subgenomic RNA.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22542254Genome polyprotein
PRO_0000341637
Chain1 – 5656Protein p11
PRO_0000341638
Chain57 – 310254Protein p28
PRO_0000341639
Chain311 – 650340NTPase
PRO_0000341640
Chain651 – 934284Protein p32
PRO_0000341641
Chain935 – 1048114Viral genome-linked protein
PRO_0000341642
Chain1049 – 1712664Protease-polymerase p70
PRO_0000341643
Chain1713 – 2254542Capsid protein
PRO_0000341644

Regions

Domain438 – 592155SF3 helicase
Domain1063 – 1169107Peptidase C24
Domain1434 – 1559126RdRp catalytic
Nucleotide binding464 – 4718ATP Potential

Sites

Active site10781For protease activity By similarity
Active site10991For protease activity By similarity
Active site11631For protease activity By similarity
Site56 – 572Cleavage; by Pro-Pol By similarity
Site310 – 3112Cleavage; by Pro-Pol By similarity
Site649 – 6502Cleavage; by Pro-Pol By similarity
Site934 – 9352Cleavage; by Pro-Pol By similarity
Site1047 – 10482Cleavage; by Pro-Pol By similarity
Site1712 – 17132Cleavage; by Pro-Pol By similarity

Amino acid modifications

Modified residue9561O-(5'-phospho-RNA)-tyrosine By similarity

Natural variations

Alternative sequence1 – 17101710Missing in isoform Subgenomic capsid protein.
VSP_034378

Sequences

Sequence LengthMass (Da)Tools
Isoform Genome polyprotein [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 90CA9F0314FAF739

FASTA2,254247,170
        10         20         30         40         50         60 
MANCRPLPIG QLPNRIFDTP RLTPGWVWAC TSEATFKLEW LQDPVVIRPP DVFVAQGVVD 

        70         80         90        100        110        120 
DFFRPKRVLQ GDPQLIAQVL LGDANGPLVG PVSMQQLTSL LHEVSQALSD HKHPLANRYT 

       130        140        150        160        170        180 
RASLQRYADT LSNYIPLVDI LTGPKDLTPR DVLEQLAAGR EWECVPDSAL KKVFRDMWQY 

       190        200        210        220        230        240 
ICEGCDSVYI KLQDVKRKMP HIDTTVLKQF IITLTDTISM ATALDTKTWL AHILGWLKPT 

       250        260        270        280        290        300 
CLVMIMQQHV NSPQGWAATL TALAELYYGI MPLTETLGSV ASWVTDKFAD MATSTWGKFK 

       310        320        330        340        350        360 
SWWDSLYTPQ AGNDLIILGG VVGLVYFMVF GDAPTQMFTK KLMRVCGFIT STVAAIKAAM 

       370        380        390        400        410        420 
WIVDYFKQRE HEHQVRITLA RWAALQEVIK QNRCAGLSEV TKLKECCEVL LNEVTELMYK 

       430        440        450        460        470        480 
LGASPLAGLI RSTSDVIQTT INELAQLMAY DTQRKPPAMV VFGGPPGIGK TRLVEALAKQ 

       490        500        510        520        530        540 
LGEVSHFTMT VDHYDTYTGN TVAIWDEFDV DSKQAFIEAT IGIVNCAPYP LNCDRPEAKG 

       550        560        570        580        590        600 
RVFTSKYVLA TTNCPTPVMP DHPRAMAFWR RITFIDVTAP TIEQWLVDNP GRKAPTSLFK 

       610        620        630        640        650        660 
DDFSHLQCSV RGYTAYDEKG NTLSGKVARA RYVSVNNLLD LIKEKYNSEA ADVKHLWFTV 

       670        680        690        700        710        720 
PQAIHKQARD IILGWLRFHS YPNTVADNIP LSEVRDPTCF GYVVISDVDP PRHVAEHVAH 

       730        740        750        760        770        780 
IEVESILRTD IVGLLREGGG GLFRALKVKS APRNCIINKV MMQAHHTTLQ VLTSQEPHPP 

       790        800        810        820        830        840 
NLPRPRRLVF VESPIDIISA LRHHVGFCTI PGIVKLITSG VGLGVENLGN FLQSIAGNVR 

       850        860        870        880        890        900 
FPLQSECSLL RTPSGDVLFY TSGQAAVWAT PARFPIVTPG EASVGKEVCS ESSWWDILKA 

       910        920        930        940        950        960 
LFSTLVVAFG PIATLVLTAH NLAYLNTREN TLSEAKGKNK RGRGARRAIA LRDDEYDEWQ 

       970        980        990       1000       1010       1020 
DIIRDWRKEM TVQQFLDLKE RALSGASDPD SQRYNAWLEL RAKRLSAGAY QHAVVDIIGK 

      1030       1040       1050       1060       1070       1080 
SGHRREVIRT QVMRAPREPK GDTYDSEGRG YVVPMTAQEK HTGWAVHIGN GRLVTCTHVA 

      1090       1100       1110       1120       1130       1140 
NMCDRVAEVE FKVAETDRDT CIITAPLGHL PSVALGNGPP AFYTTNFHPI RVLDEGSWDT 

      1150       1160       1170       1180       1190       1200 
TTTRVTGWRV VINNGTTTAP GDCGQPYLNA RRQLVGVHAA TSTCGVKKLV SRVQTKKTAK 

      1210       1220       1230       1240       1250       1260 
ATFPWKGLPV TTMPDAGGLP TGTRYHRSIA WPKLLPEETH APAPYGVNDP RHPFSQHQMI 

      1270       1280       1290       1300       1310       1320 
ANNLQPYINT PVALDQTLLQ RAVKHTKGYL DQIIGTHRSP NLTYAAAVES MAHDTACGPN 

      1330       1340       1350       1360       1370       1380 
LPGRKKDYMT DQGEPIGPLK QMLEEAWDMA HRGVPRRHEY KLALKDELRP IEKNDQGKKR 

      1390       1400       1410       1420       1430       1440 
LLWGCDAGVS MIANAVFKPV TERLVDTVPM HPVAVGICMD SPQIEQMNQA LTGRVLYCLD 

      1450       1460       1470       1480       1490       1500 
YSKWDSTQNP AVTCASVDIL ASYAEDTPLS SAAIATLCSP AVGRLDDIGL TVTSGLPSGM 

      1510       1520       1530       1540       1550       1560 
PFTSVINSVN HMIYFAMAVL EAYEEFKVPY MGNIFDNETI YTYGDDCVYG LTPATASIMP 

      1570       1580       1590       1600       1610       1620 
VVVKNLTSYG LVPTAADKSQ SIEPTDTPVF LKRTFSQTPF GLRALLDETS LARQCYWVKA 

      1630       1640       1650       1660       1670       1680 
NRTTDLFEPA AVDVDIRKNQ LEVMLAYASQ HPRSVFDKLA GMAEVTASAE GYQLVNVNWA 

      1690       1700       1710       1720       1730       1740 
NAVATYNAWY GGTDGGRAPT NEDEEPEVFV MEAPAPTRSV ASNPEGTQNS NESRPVQPAG 

      1750       1760       1770       1780       1790       1800 
PMPVAAAQAL EMAVATGQIN DTIPSVVRET FSTYTNVTWT TRQPTGTLLA RMSLGPGLNP 

      1810       1820       1830       1840       1850       1860 
YTLHLSAMWA GWGGSFEIKV IISGSGMYAG KLLCALIPPG VDPSAVDQPG AFPHALVDAR 

      1870       1880       1890       1900       1910       1920 
ITDGVTFTLG DVRAVDYHET GVGGAIASLA LYVYQPLINP FETAVSAAMV TIETRPGPDF 

      1930       1940       1950       1960       1970       1980 
GFTLLKPPNQ AMEVGFDPRS LLPRTARTLR GNRFGRPITA VVIVGVAQQI NRHFSAEGTT 

      1990       2000       2010       2020       2030       2040 
LGWSTAPIGP CVARVNGKHT DNTGRAVFQL GPLSNGPLYP NIINHYPDVA ASTIFNTGTA 

      2050       2060       2070       2080       2090       2100 
VNDNTTGGGG PMVIFNDVGD VVEDVAYQMR FIASHATSQS PTLIDQINAT SMAVCSFGNS 

      2110       2120       2130       2140       2150       2160 
RADLNQNQLN VGIELTYTCG NTAINGIVTS FMDRQYTFGP QGPNNIMLWV ESVLGTHTGN 

      2170       2180       2190       2200       2210       2220 
NTVYSSQPDT VSAALQGQPF NIPDGYMAVW NVNADSADFQ IGLRRDGYFV TNGAIGTRMV 

      2230       2240       2250 
ISEDTTFSFN GMYTLTTPLI GPSGTSGRSI HSSR 

« Hide

Isoform Subgenomic capsid protein (VP1) [UniParc].

Checksum: 15FA9B93FA05D946
Show »

FASTA54457,615

References

[1]"Molecular characterization of a porcine enteric calicivirus genetically related to Sapporo-like human caliciviruses."
Guo M., Chang K.O., Hardy M.E., Zhang Q., Parwani A.V., Saif L.J.
J. Virol. 73:9625-9631(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Expression and self-assembly in baculovirus of porcine enteric calicivirus capsids into virus-like particles and their use in an enzyme-linked immunosorbent assay for antibody detection in swine."
Guo M., Qian Y., Chang K.O., Saif L.J.
J. Clin. Microbiol. 39:1487-1493(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF CAPSID PROTEIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF182760 Genomic RNA. Translation: AAF04560.1.
RefSeqNP_051035.1. NC_000940.1.

3D structure databases

ProteinModelPortalQ9QEJ5.
SMRQ9QEJ5. Positions 1202-1693.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC24.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1457802.

Family and domain databases

InterProIPR004005. Calicivirus_coat.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR000317. Peptidase_C24.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00915. Calici_coat. 1 hit.
PF03510. Peptidase_C24. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
PRINTSPR00916. 2CENDOPTASE.
PR00918. CALICVIRUSNS.
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_PESV
AccessionPrimary (citable) accession number: Q9QEJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: May 1, 2000
Last modified: March 19, 2014
This is version 70 of the entry and version 1 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