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P03305 (POLG_FMDVO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 15 chains:

  1. Leader protease
    Short name=Lpro
    EC=3.4.22.46
  2. Protein VP0
    Alternative name(s):
    VP4-VP2
  3. Protein VP4
    Alternative name(s):
    P1A
    Virion protein 4
  4. Protein VP2
    Alternative name(s):
    P1B
    Virion protein 2
  5. Protein VP3
    Alternative name(s):
    P1C
    Virion protein 3
  6. Protein VP1
    Alternative name(s):
    P1D
    Virion protein 1
  7. Protein 2A
    Short name=P2A
    Alternative name(s):
    P52
  8. Protein 2B
    Short name=P2B
  9. Protein 2C
    Short name=P2C
    EC=3.6.1.15
  10. Protein 3A
    Short name=P3A
  11. Protein 3B-1
    Short name=P3B-1
    Alternative name(s):
    Genome-linked protein VPg1
  12. Protein 3B-2
    Short name=P3B-2
    Alternative name(s):
    Genome-linked protein VPg2
  13. Protein 3B-3
    Short name=P3B-3
    Alternative name(s):
    Genome-linked protein VPg3
  14. Picornain 3C
    EC=3.4.22.28
    Alternative name(s):
    Protease 3C
    Short name=P3C
    Protease P20B
  15. RNA-directed RNA polymerase 3D-POL
    Short name=P3D-POL
    EC=2.7.7.48
    Alternative name(s):
    P56A
OrganismFoot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O) (FMDV) [Complete proteome]
Taxonomic identifier73482 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeAphthovirus
Virus hostBos taurus (Bovine) [TaxID: 9913]
Capra hircus (Goat) [TaxID: 9925]
Cervidae (deer) [TaxID: 9850]
Erinaceidae (hedgehogs) [TaxID: 9363]
Loxodonta africana (African elephant) [TaxID: 9785]
Ovis aries (Sheep) [TaxID: 9940]
Rattus norvegicus (Rat) [TaxID: 10116]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length2332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It also cleaves the host translation initiation factor EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription. Ref.5 Ref.6 Ref.8 Ref.10

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 host heparan sulfate and various integrins (alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis. In strains adapted to cell culture, attachment to heparan sulfate can also be used and induces virion internalization through clathrin- and caveolin-independent endocytosis. Ref.5 Ref.6 Ref.8 Ref.10

Protein VP0: VP0 precursor is a component of immature procapsids By similarity. Ref.5 Ref.6 Ref.8 Ref.10

Protein 2B: Affects membrane integrity and cause an increase in membrane permeability By similarity. Ref.5 Ref.6 Ref.8 Ref.10

Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity. Ref.5 Ref.6 Ref.8 Ref.10

Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity. Ref.5 Ref.6 Ref.8 Ref.10

Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. They acts as a genome-linked replication primer By similarity. Ref.5 Ref.6 Ref.8 Ref.10

Protease 3C: 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 cooperatively to the protease By similarity. Ref.5 Ref.6 Ref.8 Ref.10

RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity. Ref.5 Ref.6 Ref.8 Ref.10

Catalytic activity

Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.

NTP + H2O = NDP + phosphate.

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.

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

Subunit structure

VP1 interacts (via RGD) with integrins heterodimers alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8.

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-1: Virion Potential.

Protein 3B-2: Virion Potential.

Protein 3B-3: 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. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex By similarity. Ref.6 Ref.7 Ref.8

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

Protein 3B-1, 3B-2 and 3B-3 are uridylylated by the polymerase and are covalently linked to the 5'-end of genomic RNA. These uridylylated forms act as a nucleotide-peptide primer for the polymerase By similarity.

Miscellaneous

The capsid protein VP1 contains the main antigenic determinants of the virion; therefore, changes in its sequence must be responsible for the high antigenic variability of the virus.

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Contains 1 peptidase C28 domain.

Contains 1 peptidase C3 domain.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Ontologies

Keywords
   Biological processClathrin- and caveolin-independent endocytosis of virus by host
Clathrin-mediated endocytosis of virus by host
Host-virus interaction
Ion transport
Modulation of host chromatin by virus
Transport
Viral attachment to host cell
Viral penetration into host cytoplasm
Viral RNA replication
Virus endocytosis by host
Virus entry into host cell
   Cellular componentCapsid protein
Host cytoplasm
Host cytoplasmic vesicle
Host membrane
Membrane
Virion
   Coding sequence diversityAlternative initiation
   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
Disulfide bond
Lipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processRNA-protein covalent cross-linking

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

modulation by virus of host chromatin organization

Inferred from electronic annotation. Source: UniProtKB-KW

pore formation by virus in membrane of 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

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

viral protein processing

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

icosahedral viral capsid

Inferred from electronic annotation. Source: InterPro

integral to membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

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...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Lab (identifier: P03305-1)

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.
Isoform Lb (identifier: P03305-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23322332Genome polyprotein
PRO_0000039872
Chain1 – 201201Leader protease
PRO_0000039873
Chain202 – 504303Protein VP0 Potential
PRO_0000374076
Chain202 – 28685Protein VP4 Potential
PRO_0000039876
Chain287 – 504218Protein VP2 Potential
PRO_0000039877
Chain505 – 724220Protein VP3 Potential
PRO_0000039878
Chain725 – 935211Protein VP1
PRO_0000039879
Chain936 – 95318Protein 2A Potential
PRO_0000039880
Chain954 – 1107154Protein 2B Potential
PRO_0000310976
Chain1108 – 1425318Protein 2C Potential
PRO_0000039881
Chain1426 – 1578153Protein 3A Potential
PRO_0000039882
Chain1579 – 160123Protein 3B-1 Potential
PRO_0000039883
Chain1602 – 162524Protein 3B-2 Potential
PRO_0000310977
Chain1626 – 164924Protein 3B-3 Potential
PRO_0000310978
Chain1650 – 1862213Picornain 3C Potential
PRO_0000039884
Chain1863 – 2332470RNA-directed RNA polymerase 3D-POL Potential
PRO_0000039885

Regions

Topological domain1 – 14801480Cytoplasmic Potential
Intramembrane1481 – 150121 Potential
Topological domain1502 – 2332831Cytoplasmic Potential
Domain1 – 201201Peptidase C28
Domain1189 – 1353165SF3 helicase
Domain1652 – 1836185Peptidase C3
Domain2096 – 2214119RdRp catalytic
Nucleotide binding1217 – 12248ATP Potential
Motif869 – 8713Cell attachment site By similarity

Sites

Active site511For leader protease activity
Active site1481For leader protease activity
Active site1631For leader protease activity
Active site16951For picornain 3C activity Potential
Active site17221For picornain 3C activity Potential
Active site18121For picornain 3C activity Potential
Site201 – 2022Cleavage; by leader protease Potential
Site286 – 2872Cleavage Potential
Site504 – 5052Cleavage; by picornain 3C Potential
Site724 – 7252Cleavage; by picornain 3C Potential
Site935 – 9362Cleavage; by picornain 3C Potential
Site953 – 9542Cleavage; by ribosomal skip Potential
Site1107 – 11082Cleavage; by picornain 3C Potential
Site1425 – 14262Cleavage; by picornain 3C Potential
Site1578 – 15792Cleavage; by picornain 3C Potential
Site1601 – 16022Cleavage; by picornain 3C Potential
Site1625 – 16262Cleavage; by picornain 3C Potential
Site1649 – 16502Cleavage; by picornain 3C Potential
Site1862 – 18632Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue15811O-(5'-phospho-RNA)-tyrosine By similarity
Modified residue16041O-(5'-phospho-RNA)-tyrosine By similarity
Modified residue16281O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation2021N-myristoyl glycine; by host
Disulfide bond406 ↔ 858Interchain (between VP2 and VP1 chains)
Disulfide bond511Interchain; in VP3 dimer

Natural variations

Alternative sequence1 – 2828Missing in isoform Lb.
VSP_018982
Natural variant7801I → V in strain: Isolate O1BFS.
Natural variant8081G → R in strain: Isolate O1BFS.
Natural variant8611N → S in strain: Isolate O1BFS.

Secondary structure

....................................... 2332
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Lab [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 4A83176F43447D68

FASTA2,332258,927
        10         20         30         40         50         60 
MNTTDCFIAL VQAIREIKAL FLSRTTGKME LTLYNGEKKT FYSRPNNHDN CWLNAILQLF 

        70         80         90        100        110        120 
RYVEEPFFDW VYSSPENLTL EAIKQLEDLT GLELHEGGPP ALVIWNIKHL LHTGIGTASR 

       130        140        150        160        170        180 
PSEVCMVDGT DMCLADFHAG IFLKGQEHAV FACVTSNGWY AIDDEDFYPW TPDPSDVLVF 

       190        200        210        220        230        240 
VPYDQEPLNG EWKAKVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG 

       250        260        270        280        290        300 
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 

       310        320        330        340        350        360 
LTTRNGHTTS TTQSSVGVTY GYATAEDFVS GPNTSGLETR VVQAERFFKT HLFDWVTSDS 

       370        380        390        400        410        420 
FGRCHLLELP TDHKGVYGSL TDSYAYMRNG WDVEVTAVGN QFNGGCLLVA MVPELYSIQK 

       430        440        450        460        470        480 
RELYQLTLFP HQFINPRTNM TAHITVPFVG VNRYDQYKVH KPWTLVVMVV APLTVNTEGA 

       490        500        510        520        530        540 
PQIKVYANIA PTNVHVAGEF PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVFNPPRNQ 

       550        560        570        580        590        600 
LPGRFTNLLD VAEACPTFLR FEGGVPYVTT KTDSDRVLAQ FDMSLAAKQM SNTFLAGLAQ 

       610        620        630        640        650        660 
YYTQYSGTIN LHFMFTGPTD AKARYMVAYA PPGMEPPKTP EAAAHCIHAE WDTGLNSKFT 

       670        680        690        700        710        720 
FSIPYLSAAD YAYTASGVAE TTNVQGWVCL FQITHGKADG DALVVLASAG KDFELRLPVD 

       730        740        750        760        770        780 
ARAETTSAGE SADPVTTTVE NYGGETQIQR RQHTDVSFIM DRFVKVTPQN QINILDLMQI 

       790        800        810        820        830        840 
PSHTLVGALL RASTYYFSDL EIAVKHEGDL TWVPNGAPEK ALDNTTNPTA YHKAPLTRLA 

       850        860        870        880        890        900 
LPYTAPHRVL ATVYNGECRY NRNAVPNLRG DLQVLAQKVA RTLPTSFNYG AIKATRVTEL 

       910        920        930        940        950        960 
LYRMKRAETY CPRPLLAIHP TEARHKQKIV APVKQTLNFD LLKLAGDVES NPGPFFFSDV 

       970        980        990       1000       1010       1020 
RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAIGV KAIRTGLDEA KPWYKLIKLL 

      1030       1040       1050       1060       1070       1080 
SRLSCMAAVA ARSKDPVLVA IMLADTGLEI LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP 

      1090       1100       1110       1120       1130       1140 
VLLAGLVKVA SSFFRSTPED LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW 

      1150       1160       1170       1180       1190       1200 
IASEEKFVTM TDLVPGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA 

      1210       1220       1230       1240       1250       1260 
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP DPDHFDGYNQ 

      1270       1280       1290       1300       1310       1320 
QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK GKPFNSKVII ATTNLYSGFT 

      1330       1340       1350       1360       1370       1380 
PRTMVCPDAL NRRFHFDIDV SAKDGYKINS KLDIIKALED THANPVAMFQ YDCALLNGMA 

      1390       1400       1410       1420       1430       1440 
VEMKRMQQDM FKPQPPLQNV YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIE 

      1450       1460       1470       1480       1490       1500 
KGQHEAAIEF FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM 

      1510       1520       1530       1540       1550       1560 
IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKSPLE TSGASTVGFR ERTLPGQKAC 

      1570       1580       1590       1600       1610       1620 
DDVNSEPAQP VEEQPQAEGP YAGPLERQKP LKVRAKLPQQ EGPYAGPMER QKPLKVKAKA 

      1630       1640       1650       1660       1670       1680 
PVVKEGPYEG PVKKPVALKV KAKNLIVTES GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC 

      1690       1700       1710       1720       1730       1740 
CATGVFGTAY LVPRHLFAEK YDKIMVDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH 

      1750       1760       1770       1780       1790       1800 
RGNRVRDITK HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL 

      1810       1820       1830       1840       1850       1860 
FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK MKAHIDPEPH 

      1870       1880       1890       1900       1910       1920 
HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA LSNKDPRLNE GVVLDEVIFS 

      1930       1940       1950       1960       1970       1980 
KHKGDTKMSE EDKALFRRCA ADYASRLHSV LGTANAPLSI YEAIKGVDGL DAMEPDTAPG 

      1990       2000       2010       2020       2030       2040 
LPWALQGKRR GALIDFENGT VGPEVEAALK LMEKREYKFV CQTFLKDEIR PLEKVRAGKT 

      2050       2060       2070       2080       2090       2100 
RIVDVLPVEH ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD 

      2110       2120       2130       2140       2150       2160 
VDYSAFDANH CSDAMNIMFE EVFRTEFGFH PNAEWILKTL VNTEHAYENK RITVGGGMPS 

      2170       2180       2190       2200       2210       2220 
GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD DIVVASDYDL DFEALKPHFK 

      2230       2240       2250       2260       2270       2280 
SLGQTITPAD KSDKGFVLGH SITDVTFLKR HFHMDYGTGF YKPVMASKTL EAILSFARRG 

      2290       2300       2310       2320       2330 
TIQEKLISVA GLAVHSGPDE YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA 

« Hide

Isoform Lb [UniParc].

Checksum: 5372D197CC761349
Show »

FASTA2,304255,803

References

[1]"Nucleotide sequence and genome organization of foot-and-mouth disease virus."
Forss S., Strebel K., Beck E., Schaller H.
Nucleic Acids Res. 12:6587-6601(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Comparison of the amino acid sequence of the major immunogen from three serotypes of foot and mouth disease virus."
Makoff A.J., Paynter C.A., Rowlands D.J., Boothroyd J.C.
Nucleic Acids Res. 10:8285-8295(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate O1BFS/Britain/1968.
[3]"Foot-and-mouth disease virus leader proteinase: specificity at the P2 and P3 positions and comparison with other papain-like enzymes."
Kuehnel E., Cencic R., Foeger N., Skern T.
Biochemistry 43:11482-11490(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"All foot and mouth disease virus serotypes initiate protein synthesis at two separate AUGs."
Sangar D.V., Newton S.E., Rowlands D.J., Clarke B.E.
Nucleic Acids Res. 15:3305-3315(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION.
[5]"The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities."
Medina M., Domingo E., Brangwyn J.K., Belsham G.J.
Virology 194:355-359(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE LEADER PROTEASE.
[6]"Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro."
Glaser W., Skern T.
FEBS Lett. 480:151-155(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE LEADER PROTEASE, CLEAVAGE OF HOST EIF4G1.
Strain: Isolate O1k.
[7]"Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: a putative ribosomal 'skip'."
Donnelly M.L.L., Luke G., Mehrotra A., Li X., Hughes L.E., Gani D., Ryan M.D.
J. Gen. Virol. 82:1013-1025(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYPROTEIN PROCESSING.
[8]"Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro."
Gradi A., Foeger N., Strong R., Svitkin Y.V., Sonenberg N., Skern T., Belsham G.J.
J. Virol. 78:3271-3278(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE LEADER PROTEASE, CLEAVAGE OF HOST EIF4G3.
[9]"Factors required for the uridylylation of the foot-and-mouth disease virus 3B1, 3B2, and 3B3 peptides by the RNA-dependent RNA polymerase (3Dpol) in vitro."
Nayak A., Goodfellow I.G., Belsham G.J.
J. Virol. 79:7698-7706(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: COVALENT RNA-LINKAGE OF 3B PROTEINS, URIDYLYLATION.
[10]"Heparan sulfate-binding foot-and-mouth disease virus enters cells via caveola-mediated endocytosis."
O'Donnell V., Larocco M., Baxt B.
J. Virol. 82:9075-9085(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF CAPSID PROTEINS.
[11]"Cellular receptors for foot and mouth disease virus."
Ruiz-Saenz J., Goez Y., Tabares W., Lopez-Herrera A.
Intervirology 52:201-212(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"The three-dimensional structure of foot-and-mouth disease virus at 2.9-A resolution."
Acharya R., Fry E., Stuart D., Fox G., Rowlands D., Brown F.
Nature 337:709-716(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[13]"Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition."
Guarne A., Tormo J., Kirchweger R., Pfistermueller D., Fita I., Skern T.
EMBO J. 17:7469-7479(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 29-201 OF MUTANT ALA-51.
[14]"Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes."
Guarne A., Hampoelz B., Glaser W., Carpena X., Tormo J., Fita I., Skern T.
J. Mol. Biol. 302:1227-1240(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-195 OF MUTANT ALA-51/SER-133.
+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 complexed with oligosaccharide receptor

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00871 Genomic RNA. Translation: CAA25416.1.
J02185 Genomic RNA. Translation: AAA42635.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QMYX-ray1.90A/B/C29-195[»]
1QOLX-ray3.00A/B/C/D/E/F/G/H29-201[»]
1QQPX-ray1.901725-937[»]
2287-504[»]
3505-724[»]
4202-286[»]
2JQFNMR-R/S29-201[»]
2JQGNMR-R29-195[»]
DisProtDP00573.
ProteinModelPortalP03305.
SMRP03305. Positions 29-201, 216-286, 291-934, 1656-1856, 1863-2332.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC03.008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D4.10.90.10. 1 hit.
InterProIPR015031. Capsid_VP4_Picornavir.
IPR004080. FMDV_VP1_coat.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR008739. Peptidase_C28.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF05408. Peptidase_C28. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
[Graphical view]
PRINTSPR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03305.

Entry information

Entry namePOLG_FMDVO
AccessionPrimary (citable) accession number: P03305
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 151 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references