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Q9DUN3 (POLG_VESVA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 6 chains:

  1. Protein p16
  2. Protein p32
  3. NTPase
    EC=3.6.1.15
    Alternative name(s):
    p39
  4. Protein p30
  5. Viral genome-linked protein
    Alternative name(s):
    VPg
    p13
  6. Protease-polymerase p76
    Short name=Pro-Pol
    EC=2.7.7.48
    EC=3.4.22.66
Gene names
ORF Names:ORF1
OrganismVesicular exanthema of swine virus serotype A48 (isolate Swine/United States/A48/1948) (VESV) [Reference proteome]
Taxonomic identifier85617 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae › Vesivirus ›
Virus hostSus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length1881 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 p76 processes the polyprotein: Pro-Pol is first released by autocleavage, then all other proteins are cleaved. Cleaves host translation initiation factor eIF4G1 and eIF4G2 thereby inducing a shutdown of host protein synthesis. This shutdown may not prevent viral mRNA from being translated since viral Vpg replaces the cap. May cleave host polyadenylate-binding protein thereby inhibiting cellular translation. It is also a RNA-directed RNA polymerase which replicates genomic and antigenomic viral RNA by recognizing specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA encodes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs 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

Protein p32: homodimer, interacts with NTPase, protein p30 and Pro-Pol. Viral genome-linked protein interacts with capsid protein and Pro-Pol. Protease-polymerase p76: Homooligomers, interacts with Vpg, protein p32 and may interact with capsid protein By similarity.

Domain

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

Post-translational modification

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

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.

Sequence similarities

Contains 1 peptidase C24 domain.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18811881Genome polyprotein
PRO_0000402456
Chain1 – 148148Protein p16 By similarity
PRO_0000402457
Chain149 – 435287Protein p32 By similarity
PRO_0000402458
Chain436 – 791356NTPase By similarity
PRO_0000402459
Chain792 – 1070279Protein p30 By similarity
PRO_0000402460
Chain1071 – 1183113Viral genome-linked protein By similarity
PRO_0000402461
Chain1184 – 1881698Protease-polymerase p76 By similarity
PRO_0000402462

Regions

Domain564 – 720157SF3 helicase
Domain1207 – 1311105Peptidase C24
Domain1593 – 1718126RdRp catalytic
Nucleotide binding590 – 5978ATP Potential

Sites

Active site12221For protease activity By similarity
Active site12431For protease activity By similarity
Active site13051For protease activity By similarity
Site148 – 1492Cleavage; by Pro-Pol By similarity
Site435 – 4362Cleavage; by Pro-Pol By similarity
Site791 – 7922Cleavage; by Pro-Pol By similarity
Site1070 – 10712Cleavage; by Pro-Pol By similarity
Site1183 – 11842Cleavage; by Pro-Pol By similarity

Amino acid modifications

Modified residue10931O-(5'-phospho-RNA)-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DUN3 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 6E487A72523AFE4F

FASTA1,881208,813
        10         20         30         40         50         60 
MAQTLSKISN KENASSGLRP KRFKPHQPIP TWMVRCEPLD HDSRRGRDPV RASPQAKRVR 

        70         80         90        100        110        120 
TPTPYPRHLK PAASAVVRSG NNPSHLKPAS TDVVRSGPQP LCCEAKDGGV VRSCKTYNLK 

       130        140        150        160        170        180 
PAHESKAVAF SLPKTDGPTG NEPEFIAEAC PSCALYDTCP NCTSKVINDD GSTDGTIPSW 

       190        200        210        220        230        240 
DQIETTPAFL SLLSNTDEEM SADELTNLAA HLRKAFETGS HPANVDYSKD QLQGLLEMAE 

       250        260        270        280        290        300 
AAVPPARRQT LPFYQQRLEA RRTWREKIFN QPLEEINKIL TTSKDRFQRC AAWKVILEKA 

       310        320        330        340        350        360 
VLAKEYGEEA YAYAQQALKN INSFDVNLVL KMAAATFIDH IRMMTVDNPD LVSYIPKLIV 

       370        380        390        400        410        420 
KLKPLTLKMI IDNHENTKEG WLVTLTSLAE LYGMVEVAID FVPTVVGKLF DLLMKTTSKM 

       430        440        450        460        470        480 
YSMFKSVVLA TFTSESLDFT NPFWYAIAAI LCFLITGAIP HNGKMKIHKN ILSNATGIVA 

       490        500        510        520        530        540 
GIKAIQALAA MFSTWSNERL VNDLSSRTIA LTELNNPTIT ADIDAVINLQ RLAEVLRDEV 

       550        560        570        580        590        600 
KSHTLNPLMQ PYNPILRNLM SALDKVISCC TRRKAIATKR TAPVAVILTG PPGCGKTTAA 

       610        620        630        640        650        660 
FALAKRLSQQ KPSIISLDVD HHDTYTGNEV CIIDEFDSSD KVDYANFVVN MVNTNPMVLN 

       670        680        690        700        710        720 
CDLIENKGKT FTSKYVIMTS NTETPVKPTS RRAGAFYRRV MIVDVTNNAV DKWKSDNPGK 

       730        740        750        760        770        780 
AVPKWCFNKD FSHLSLSLRG TEPYSKEYVL DPTGRNHQSR RAPPPQQITL EQLAQKMVVQ 

       790        800        810        820        830        840 
HTTNTSEFVT QAGDVPVFGF VCQNNEIDTV YNLLAAVKAR YGANFNLYKG MVRTAHENSG 

       850        860        870        880        890        900 
CGAHVHVISR EDNFRGKAFT VNRSRLESVP HLEGDSFRRS LGVVMSDKDV TTMFYYIKGK 

       910        920        930        940        950        960 
VINDQVSLTE LPANQHVVTV HTVYDMAWAL RRHLKWSGQW QLIKAAYEIM CYPDTAACAL 

       970        980        990       1000       1010       1020 
RNWMDSTDFS EEHVVTQFIA PGGTIILESC YGARMWATGQ RLIRAGGLTE AGGPQGGVRF 

      1030       1040       1050       1060       1070       1080 
AGLGARNVPW SEILREFMTL ISHIWSQIKG ATVVLTALTF YLKRFRPRVE AKGKNKNKGP 

      1090       1100       1110       1120       1130       1140 
RKNTGVALTD DEYNDWKQSK AEKNLDLTVK DFLQLRHRAA MGADNTDAVK FRYWYSKKQK 

      1150       1160       1170       1180       1190       1200 
IYHDLENFPI IGRGGLKREL IRKGPLRPRG NDFYDEPDDW YSEGVIDGVT HKNAIVSVDD 

      1210       1220       1230       1240       1250       1260 
VDGMHKGYAI HIGHGVYISL KHVLTGNARI LSEEPKGITI SGELATFRLN NILPTAVPVG 

      1270       1280       1290       1300       1310       1320 
TNKPIKDPWG NPVSTDWQFK NYNTTSGNIY GACGSSCSLT RQGDCGLPYV DDHGVVVGLH 

      1330       1340       1350       1360       1370       1380 
AGSGGDKCPS RKLIVPYVKV DMRIRDTCTK ESPTKTHKPT FSYRGLLGKE TGEPRTIMKG 

      1390       1400       1410       1420       1430       1440 
TRLHVSPAHV DDYEECTHQP ASLGAGDPRC PISLTGIMVN NLQPYTEASP GPDTATLNRV 

      1450       1460       1470       1480       1490       1500 
SKMLTSHMEG YVPKVHKTEE DSISAFYMLN HDTLCGPYIG ARKKDHVKDG VLDKNLLDLL 

      1510       1520       1530       1540       1550       1560 
SSKWNRAKLG LALPHEYALG LKDELRPKDK VAVGKRRLIW GCDVGVSTVC AAAFKRVSES 

      1570       1580       1590       1600       1610       1620 
IMANHALGFI QVGINMDGPA VEDLFKRLER PKHDRYCVDY SKWDSTQPPK VTSQSIDILR 

      1630       1640       1650       1660       1670       1680 
HFTDKSPIVD SACATLKSNP IGIFNGVAFK VAGGLPSGMP LTSIINSLNH CLMVGSAVVK 

      1690       1700       1710       1720       1730       1740 
ALEDSGVRVT WNIFDSMDLF TYGDDGVYIV PPLISSVMPK VFANLRQFGL KPTRTDKSDA 

      1750       1760       1770       1780       1790       1800 
EITPIPADEP VEFLKRTIVR TENGVRALLD RSSIIRQFYY IKAENTENWT VPPKRIDTPS 

      1810       1820       1830       1840       1850       1860 
RGQQLYNACL YASQHGEEFY TSKIVPLIER AVKLEGLHIE VPEFHQAVAA YNGYFNGTEG 

      1870       1880 
QPNQIAHASG GLGLSGEVFE N

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References

[1]"The capsid protein of vesicular exanthema of swine virus serotype A48: relationship to the capsid protein of other animal caliciviruses."
Neill J.D., Meyer R.F., Seal B.S.
Virus Res. 54:39-50(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Complete nucleotide sequence of the genomic RNA of vesicular exanthema of swine virus A48."
Neill J.D., Seal B.S., Ridpath J.F.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U76874 Genomic RNA. Translation: AAG13641.1.
RefSeqNP_066255.1. NC_002551.1.

3D structure databases

HSSPHSSP built from PDB template 1KHV based on UniProtKB P27410.
ProteinModelPortalQ9DUN3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR003593. AAA+_ATPase.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR000317. Peptidase_C24.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF03510. Peptidase_C24. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
PRINTSPR00916. 2CENDOPTASE.
PR00918. CALICVIRUSNS.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_VESVA
AccessionPrimary (citable) accession number: Q9DUN3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents