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P12915 (POLG_BOVEV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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. Picornain 2A
    Short name=P2A
    Short name=Protein 2A
    EC=3.4.22.29
  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. Picornain 3C
    EC=3.4.22.28
    Alternative name(s):
    Protease 3C
    Short name=P3C
  12. RNA-directed RNA polymerase 3D-POL
    Short name=P3D-POL
    EC=2.7.7.48
OrganismBovine enterovirus (strain VG-5-27) (BEV) [Complete proteome]
Taxonomic identifier12065 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus ›
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length2175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 By similarity.

VP0 precursor is a component of immature procapsids By similarity.

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.

Protein 2B affects membrane integrity and cause an increase in membrane permeability By similarity.

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

Protein 3A, via its hydrophobic domain, serves as membrane anchor. It also inhibits endoplasmic reticulum-to-Golgi transport By similarity.

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.

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).

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.

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.

Picornain 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 uridylated 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-virus interaction
Inhibition of host IFN-mediated response initiation by virus
Inhibition of host RIG-I by virus
Inhibition of host innate immune response by virus
Ion transport
Transport
Viral RNA replication
Viral attachment to host cell
Viral immunoevasion
Virus entry into host cell
   Cellular componentHost cytoplasm
Host cytoplasmic vesicle
Host membrane
Membrane
Virion
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionCapsid protein
Helicase
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

induction by virus of host autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

ion transport

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 type I interferon production

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

viral attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular_componenthost cell cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

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 – 317316Protein VP0 Potential
PRO_0000311036
Chain2 – 6968Protein VP4 Potential
PRO_0000039459
Chain70 – 317248Protein VP2 Potential
PRO_0000039460
Chain318 – 559242Protein VP3 Potential
PRO_0000039461
Chain560 – 840281Protein VP1 Potential
PRO_0000039462
Chain841 – 990150Picornain 2A Potential
PRO_0000039463
Chain991 – 108999Protein 2B Potential
PRO_0000039464
Chain1090 – 1419330Protein 2C Potential
PRO_0000039465
Chain1420 – 150889Protein 3A Potential
PRO_0000039466
Chain1509 – 153123Protein 3B Potential
PRO_0000039467
Chain1532 – 1714183Picornain 3C Potential
PRO_0000039468
Chain1715 – 2175461RNA-directed RNA polymerase 3D-POL Potential
PRO_0000039469

Regions

Topological domain2 – 14851484Cytoplasmic Potential
Intramembrane1486 – 150116 Potential
Topological domain1502 – 2175674Cytoplasmic Potential
Domain1194 – 1352159SF3 helicase
Domain1941 – 2056116RdRp catalytic
Nucleotide binding1218 – 12258ATP Potential

Sites

Active site8611For picornain 2A activity By similarity
Active site8791For picornain 2A activity By similarity
Active site9501For picornain 2A activity By similarity
Active site15711For picornain 3C activity Potential
Active site16021For picornain 3C activity Potential
Active site16781For picornain 3C activity Potential
Site69 – 702Cleavage Potential
Site317 – 3182Cleavage; by picornain 3C Potential
Site840 – 8412Cleavage; by picornain 2A Potential
Site990 – 9912Cleavage; by picornain 3C Potential
Site1089 – 10902Cleavage; by picornain 3C Potential
Site1419 – 14202Cleavage; by picornain 3C Potential
Site1508 – 15092Cleavage; by picornain 3C Potential
Site1531 – 15322Cleavage; by picornain 3C Potential
Site1714 – 17152Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue15111O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Secondary structure

1 ............................................................................................................................................... 2175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12915 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 44FCADE8704E48FD

FASTA2,175242,504
        10         20         30         40         50         60 
MGAQLSRNTA GSHTTGTYAT GGSTINYNNI NYYSHAASAA QNKQDFTQDP SKFTQPIADV 

        70         80         90        100        110        120 
IKETAVPLKS PSAEACGYSD RVAQLTLGNS TITTQEAANI CVAYGCWPAK LSDTDATSVD 

       130        140        150        160        170        180 
KPTEPGVSAD AFYTLRSKPW QADSKGWYWK LPDALNNTGM FGQNAQFHYI YRGGWAVHVQ 

       190        200        210        220        230        240 
CNATKFHQGT LLVLAIPEHQ IATQEQPAFD RTMPGSEGGT FQEPFWLEDG TSLGNSLIYP 

       250        260        270        280        290        300 
HQWINLRTNN SATLILPYVN AIPMDSAIRH SNWTLAIIPV APLKYAAETT PLVPITVTIA 

       310        320        330        340        350        360 
PMETEYNGLR RAIASNQGLP TKPGPGSYQF MTTDEDCSPC ILPDFQPTLE IFIPGKVNNL 

       370        380        390        400        410        420 
LEIAQVESIL EANNREGVEG VERYVIPVSV QDALDAQIYA LRLELGGSGP LSSSLLGTLA 

       430        440        450        460        470        480 
KHYTQWSGSV EITCMFTGTF MTTGKVLLAY TPPGGDMPRN REEAMLGTHV VWDFGLQSSI 

       490        500        510        520        530        540 
TLVIPWISAS HFRGVSNDDV LNYQYYAAGH VTIWYQTNMV IPPGFPNTAG IIMMIAAQPN 

       550        560        570        580        590        600 
FSFRIQKDRE DMTQTAILQN DPGKMLKDAI DKQVAGALVA GTTTSTHSVA TDSTPALQAA 

       610        620        630        640        650        660 
ETGATSTARD ESMIETRTIV PTHGIHETSV ESFFGRSSLV GMPLLATGTS ITNWRIDFRE 

       670        680        690        700        710        720 
FVQLRAKMSW FTYMRFDVEF TIIATSSTGQ NVTTEQHTTY QVMYVPPGAP VPSNQDSFQW 

       730        740        750        760        770        780 
QSGCNPSVFA DTDGPPAQFS VPFMSSANAY STVYDGYARF MDTDPDRYGI LPSNFLGFMY 

       790        800        810        820        830        840 
FRTLEDAAHQ VRFRICAKIK HTSCWIPRAP RQAPYKKRYN LVFSGDSDRI CSNRASLTSY 

       850        860        870        880        890        900 
GPFGQQQGAA YVGSYKILNR HLATYADWEN EVWQSYQRDL LVTRVDAHGC DTIARCNCRS 

       910        920        930        940        950        960 
GIYYCKSTAK HYPIVVTPPS IYKIEANDYY PERMQTHILL GIGFAEPGDC GGLLRCEHGV 

       970        980        990       1000       1010       1020 
MGILTVGGGD HVGFADVRDL LWIEDDAMEQ GITDYVQQLG NAFGAGFTAE IANYTNQLRD 

      1030       1040       1050       1060       1070       1080 
MLMGSDSVVE KIIRSLVRLV SALVIVVRNH QDLITVGATL ALLGCEGSPW KWLKRKVCQI 

      1090       1100       1110       1120       1130       1140 
LGINMAERQS DNWMKKFTEM CNAFRGLDWI AAKISKFIDW LKQKILPELK ERAEFVKKLK 

      1150       1160       1170       1180       1190       1200 
QLPLLEAQVN TLEHSSASQE RQEQLFGNVQ YLAHHCRKNA PLYAAEAKRV YHLEKRVLGA 

      1210       1220       1230       1240       1250       1260 
MQFKTKNRIE PVCALIHGSP GTGQSLATMI VGRKLAEYEG SDVYSLPPDP DHFDGYQQQA 

      1270       1280       1290       1300       1310       1320 
VVVMDDLLQN PDGKDMTLFC QMVSTAPFTV PMAALEDKGK LFTSKFVLAS TNAGQVTPPT 

      1330       1340       1350       1360       1370       1380 
VADYKALQRR FFFDCDIEVQ KEYKRDGVTL DVAKATETCE DCSPANFKKC MPLICGKALQ 

      1390       1400       1410       1420       1430       1440 
LKSRKGDGMR YSLDTLISEL RRESNRRYNI GNVLEALFQG PVCYKPLRIE VHEEEPAPSA 

      1450       1460       1470       1480       1490       1500 
ISDLLQAVDS EEVREYCRSK GWIVEERVTE LKLERNVNRA LAVIQSVSLI AAVAGTIYIV 

      1510       1520       1530       1540       1550       1560 
YRLFSGMQGP YSGIGTNYAT KKPVVRQVQT QGPLFDFGVS LLKKNIRTVK TGAGEFTALG 

      1570       1580       1590       1600       1610       1620 
VYDTVVVLPR HAMPGKTIEM NGKDIEVLDA YDLNDKTDTS LELTIVKLKM NEKFRDIRAM 

      1630       1640       1650       1660       1670       1680 
VPDQITDYNE AVVVVNTSYY PQLFTCVGRV KDYGFLNLAG RPTHRVLMYE FPTKAGQCGG 

      1690       1700       1710       1720       1730       1740 
VVISMGKIVG VHVGGNGAQG FAASLLRRYF TAEQGQIEYI EKSKDAGYPV INAPTQTKLE 

      1750       1760       1770       1780       1790       1800 
PSVFFDVFPG VKEPAVLHKK DKRLETNFEE ALFSKYIGNV QRDMPEELLI AIDHYSEQLK 

      1810       1820       1830       1840       1850       1860 
MLNIDPRPIS MEDAIYGTEG LEALDLGTSA SYPYVAMGIK KRDILNKETR DVTKMQECID 

      1870       1880       1890       1900       1910       1920 
KYGLNLPMVT YVKDELRAPD KIRKGKSRLI EASSLNDSVA MRCYFGNLYK VFHTNPGTIS 

      1930       1940       1950       1960       1970       1980 
GCAVGCDPET FWSKIPVMMD GELFGFDYTA YDASLSPMWF HALAEVLRRI GFVECKHFID 

      1990       2000       2010       2020       2030       2040 
QLCCSHHLYM DKHYYVVGGM PSGCSGTSIF NSMINNLIIR TLVLTVYKNI DLDDLKIIAY 

      2050       2060       2070       2080       2090       2100 
GDDVLASYPY EIDASLLAEA GKSFGLIMTP PDKSAEFVKL TWDNVTFLKR KFVRDARYPF 

      2110       2120       2130       2140       2150       2160 
LVHPVMDMSN IHESIRWTKD PRHTEDHVRS LCLLAWHCGE EEYNEFVTKI RSVPVGRALH 

      2170 
LPSFKALERK WYDSF

« Hide

References

[1]"The complete nucleotide sequence of a bovine enterovirus."
Earle J.A.P., Skuce R.A., Fleming C.S., Hoey E.M., Martin S.J.
J. Gen. Virol. 69:253-263(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Implications for viral uncoating from the structure of bovine enterovirus."
Smyth M., Tate J., Hoey E.M., Lyons C., Martin S.J., Stuart D.
Nat. Struct. Biol. 2:224-231(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-840.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D00214 Genomic RNA. Translation: BAA24003.1. Sequence problems.
PIRGNNYBE. A29824.
RefSeqNP_045756.1. NC_001859.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BEVX-ray3.001560-840[»]
270-317[»]
3318-559[»]
42-69[»]
ProteinModelPortalP12915.
SMRP12915. Positions 23-62, 74-559, 573-990, 1419-1480, 1532-2175.
ModBaseSearch...

Protein family/group databases

MEROPSC03.014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1493914.

Family and domain databases

Gene3D4.10.80.10. 2 hits.
InterProIPR004004. Helic/Pol/Pept_Calicivir-typ.
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]
PRINTSPR00918. CALICVIRUSNS.
ProDomPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF89043. P3A. 1 hit.
SSF50494. Pept_Ser_Cys. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12915.

Entry information

Entry namePOLG_BOVEV
AccessionPrimary (citable) accession number: P12915
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 138 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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