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P03308 (POLG_FMDVA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. 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·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/United Kingdom/A12Valle119/1932 serotype A) (FMDV) [Complete proteome]
Taxonomic identifier12114 [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 length2333 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 cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription By similarity.

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 (alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta6, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis By similarity.

Protein VP0: VP0 precursor is a component of immature procapsids 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 By similarity.

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.

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.

RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.

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 By similarity.

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.

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 By similarity.

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-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: P03308-1)

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: P03308-2)

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_0000039833
Chain1 – 201201Leader protease
PRO_0000039834
Chain202 – 504303Protein VP0 Potential
PRO_0000374074
Chain202 – 28685Protein VP4 Potential
PRO_0000039837
Chain287 – 504218Protein VP2 Potential
PRO_0000039838
Chain505 – 725221Protein VP3 Potential
PRO_0000039839
Chain726 – 936211Protein VP1 Potential
PRO_0000039840
Chain937 – 95418Protein 2A Potential
PRO_0000039841
Chain955 – 1108154Protein 2B Potential
PRO_0000039842
Chain1109 – 1426318Protein 2C Potential
PRO_0000039843
Chain1427 – 1579153Protein 3A Potential
PRO_0000039844
Chain1580 – 160223Protein 3B-1 Potential
PRO_0000039845
Chain1603 – 162624Protein 3B-2 Potential
PRO_0000039846
Chain1627 – 165024Protein 3B-3 Potential
PRO_0000039847
Chain1651 – 1863213Picornain 3C Potential
PRO_0000039848
Chain1864 – 2333470RNA-directed RNA polymerase 3D-POL Potential
PRO_0000039849

Regions

Topological domain1 – 14811481Cytoplasmic Potential
Intramembrane1482 – 150221 Potential
Topological domain1503 – 2333831Cytoplasmic Potential
Domain1 – 201201Peptidase C28
Domain1190 – 1354165SF3 helicase
Domain1653 – 1837185Peptidase C3
Domain2097 – 2215119RdRp catalytic
Nucleotide binding1218 – 12258ATP Potential
Motif869 – 8713Cell attachment site

Sites

Active site511For leader protease activity By similarity
Active site1481For leader protease activity By similarity
Active site1631For leader protease activity By similarity
Active site16961For picornain 3C activity Potential
Active site17231For picornain 3C activity Potential
Active site18131For picornain 3C activity Potential
Site201 – 2022Cleavage; by leader protease Potential
Site286 – 2872Cleavage Potential
Site504 – 5052Cleavage; by picornain 3C Potential
Site725 – 7262Cleavage; by picornain 3C Potential
Site936 – 9372Cleavage; by picornain 3C Potential
Site954 – 9552Cleavage; by ribosomal skip Potential
Site1108 – 11092Cleavage; by picornain 3C Potential
Site1426 – 14272Cleavage; by picornain 3C Potential
Site1579 – 15802Cleavage; by picornain 3C Potential
Site1602 – 16032Cleavage; by picornain 3C Potential
Site1626 – 16272Cleavage; by picornain 3C Potential
Site1650 – 16512Cleavage; by picornain 3C Potential
Site1863 – 18642Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue15821O-(5'-phospho-RNA)-tyrosine By similarity
Modified residue16051O-(5'-phospho-RNA)-tyrosine By similarity
Modified residue16291O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation2021N-myristoyl glycine; by host By similarity
Disulfide bond511Interchain; in VP3 dimer

Natural variations

Alternative sequence1 – 2828Missing in isoform Lb.
VSP_018980
Natural variant122 – 1243SEV → AR in 119ab variant.
Natural variant1311D → N in 119ab variant.
Natural variant1451G → E in 119ab variant.
Natural variant3571T → P in 119ab variant.
Natural variant364 – 3652LE → RT in 119ab variant.
Natural variant4171E → T in 119ab variant.
Natural variant4201K → T in 119ab variant.
Natural variant4231K → E in 119ab variant.
Natural variant4701V → L in 119ab variant.
Natural variant5041E → V in 119ab variant.
Natural variant5331V → E in 119ab variant.
Natural variant5381R → K in 119ab variant.
Natural variant5431G → R in 119ab variant.
Natural variant7011G → D in 119ab variant.
Natural variant8721S → F in 119ab variant.
Natural variant9541G → R in 119ab variant.
Natural variant10341S → T in 119ab variant.
Natural variant10951F → L in 119ab variant.
Natural variant11511T → M in 119ab variant.
Natural variant11561P → L in 119ab variant.
Natural variant13561I → V in 119ab variant.
Natural variant18001G → S in 119ab variant.
Natural variant18461R → K in 119ab variant.
Natural variant18611H → Q in 119ab variant.
Natural variant19391R → A in 119ab variant.
Natural variant20211A → V in 119ab variant.
Natural variant21091A → T in 119ab variant.
Natural variant21621G → D in 119ab variant.
Natural variant21671S → G in 119ab variant.

Secondary structure

... 2333
Helix Strand Turn

Details...

Sequences

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

Last modified May 29, 2013. Version 2.
Checksum: 3B61837F593073BD

FASTA2,333259,162
        10         20         30         40         50         60 
MNTTNCFIAL VHAIREIRAF FLSRATGKME FTLYNGERKT FYSRPNNHDN CWLNTILQLF 

        70         80         90        100        110        120 
RYVDEPFFDW VYNSPENLTL AAIKQLEELT GLELHEGGPP ALVIWNIKHL LQTGIGTASR 

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

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

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

       310        320        330        340        350        360 
LTTRNGHTTS TTQSSVGVTY GYSTEEDHVA GPNTSGLETR VVQAERFFKK FLFDWTTDKP 

       370        380        390        400        410        420 
FGHLEKLELP TDHHGVFGHL VDSYAYMRNG WDVEVSAVGN QFNGGCLLVA MVPEWKEFDK 

       430        440        450        460        470        480 
REKYQLTLFP HQFISPRTNM TAHITVPYLG VNRYDQYKKH KPWTLVIMVV SPLTVSNTAA 

       490        500        510        520        530        540 
TQIKVYANIA PTYVHVAGEL PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVYNPPRTN 

       550        560        570        580        590        600 
YPGRFTNLLD VAEACPTFLC FDDGKPYVVT RTDDTRLLAK FDVSLAAKHM SNTYLSGIAQ 

       610        620        630        640        650        660 
YYTQYSGTIN LHFMFTGSTD SKARYMVAYI PPGVETPPET PEGAAHCIHA EWDTGLNSKF 

       670        680        690        700        710        720 
TFSIPYVSAA DYAYTASDTA ETTNVQGWVC IYQITHGKAE GDTLVVSASA GKDFELRLPI 

       730        740        750        760        770        780 
DPRSQTTATG ESADPVTTTV ENYGGETQVQ RRHHTDVSFI MDRFVKIKSL NPTHVIDLMQ 

       790        800        810        820        830        840 
THQHGLVGAL LRAATYYFSD LEIVVRHDGN LTWVPNGAPE AALSNTGNPT AYNKAPFTRL 

       850        860        870        880        890        900 
ALPYTAPHRV LATVYNGTNK YSASGSGVRG DSGSLAPRVA RQLPASFNYG AIKAETIHEL 

       910        920        930        940        950        960 
LVRMKRAELY CPRPLLAIEV SSQDRHKQKI IAPGKQLLNF DLLKLAGDVE SNPGPFFFAD 

       970        980        990       1000       1010       1020 
VRSNFSKLVD TINQMQEDMS TKHGPDFNRL VSAFEELATG VKAIRTGLDE AKPWYKLIKL 

      1030       1040       1050       1060       1070       1080 
LSRLSCMAAV AARSKDPVLV AIMLADTGLE ILDSTFVVKK ISDSLSSLFH VPAPVFSFGA 

      1090       1100       1110       1120       1130       1140 
PVLLAGLVKV ASSFFRSTPE DLERAEKQLK ARDINDIFAI LKNGEWLVKL ILAIRDWIKA 

      1150       1160       1170       1180       1190       1200 
WIASEEKFVT TTDLVPGILE KQRDLNDPSK YKEAKEWLDN ARQACLKSGN VHIANLCKVV 

      1210       1220       1230       1240       1250       1260 
APAPSKSRPE PVVVCLRGKS GQGKSFLANV LAQAISTHFT GRTDSVWYCP PDPDHFDGYN 

      1270       1280       1290       1300       1310       1320 
QQTVVVMDDL GQNPDGKDFK YFAQMVSTTG FIPPMASLED KGKPFNSKVI IATTNLYSGF 

      1330       1340       1350       1360       1370       1380 
TPRTMVCPDA LNRRFHFDID VSAKDGYKIN NKLDIIKALE DTHTNPVAMF QYDCALLNGM 

      1390       1400       1410       1420       1430       1440 
AVEMKRMQQD MFKPQPPLQN VYQLVQEVIE RVELHEKVSS HPIFKQISIP SQKSVLYFLI 

      1450       1460       1470       1480       1490       1500 
EKGQHEAAIE FFEGMVHDSI KEELRPLIQQ TSFVKRAFKR LKENFEIVAL CLTLLANIVI 

      1510       1520       1530       1540       1550       1560 
MIRETRKRQK MVDDAVNEYI EKANITTDDT TLDEAEKNPL ETSGASTVGF RERTLTGQRA 

      1570       1580       1590       1600       1610       1620 
CNDVNSEPAR PAEEQPQAEG PYTGPLERQR PLKVRAKLPQ QEGPYAGPLE RQKPLKVKAK 

      1630       1640       1650       1660       1670       1680 
APVVKEGPYE GPVKKPVALK VKAKNLIVTE SGAPPTDLQK MVMGNTKPVE LILDGKTVAI 

      1690       1700       1710       1720       1730       1740 
CCATGVFGTA YLVPRHLFAE KYDKIMLDGR AMTDSDYRVF EFEIKVKGQD MLSDAALMVL 

      1750       1760       1770       1780       1790       1800 
HRGNRVRDIT KHFRDTARMK KGTPVVGVVN NADVGRLIFS GEALTYKDIV VCMDGDTMPG 

      1810       1820       1830       1840       1850       1860 
LFAYKAATKA GYCGGAVLAK DGADTFIVGT HSAGGNGVGY CSCVSRSMLL RMKAHVDPEP 

      1870       1880       1890       1900       1910       1920 
HHEGLIVDTR DVEERVHVMR KTKLAPTVAH GVFNPEFGPA ALSNKDPRLN EGVVLDEVIF 

      1930       1940       1950       1960       1970       1980 
SKHKGDTKMS AEDKALFRRC AADYASRLHS VLGTANAPLS IYEAIKGVDG LDAMESDTAP 

      1990       2000       2010       2020       2030       2040 
GLPWAFQGKR RGALIDFENG TVGPEVEAAL KLMEKREYKF ACQTFLKDEI RPMEKVRAGK 

      2050       2060       2070       2080       2090       2100 
TRIVDVLPVE HILYTRMMIG RFCAQMHSNN GPQIGSAVGC NPDVDWQRFG THFAQYRNVW 

      2110       2120       2130       2140       2150       2160 
DVDYSAFDAN HCSDAMNIMF EEVFRTDFGF HPNAEWILKT LVNTEHAYEN KRITVEGGMP 

      2170       2180       2190       2200       2210       2220 
SGCSATSIIN TILNNIYVLY ALRRHYEGVE LDTYTMISYG DDIVVASDYD LDFEALKPHF 

      2230       2240       2250       2260       2270       2280 
KSLGQTITPA DKSDKGFVLG HSITDVTFLK RHFHIDYGTG FYKPVMASKT LEAILSFARR 

      2290       2300       2310       2320       2330 
GTIQEKLTSV AGLAVHSGPD EYRRLFEPFQ GLFEIPSYRS LYLRWVNAVC GDA 

« Hide

Isoform Lb [UniParc].

Checksum: 469A19C57B5F5E8B
Show »

FASTA2,305255,998

References

[1]"Nucleotide and amino acid sequence coding for polypeptides of foot-and-mouth disease virus type A12."
Robertson B.H., Grubman M.J., Weddell G.N., Moore D.M., Welsh J.D., Fischer T., Dowbenko D.J., Yansura D.G., Small B., Kleid D.G.
J. Virol. 54:651-660(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: 119ab variant.
[2]"Comparative genomics of foot-and-mouth disease virus."
Carrillo C., Tulman E.R., Delhon G., Lu Z., Carreno A., Vagnozzi A., Kutish G.F., Rock D.L.
J. Virol. 79:6487-6504(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Identification of amino acid and nucleotide sequence of the foot-and-mouth disease virus RNA polymerase."
Robertson B.H., Morgan D.O., Moore D.M., Grubman M.J., Card J., Fischer T., Weddell G.N., Dowbenko D.J., Yansura D.G.
Virology 126:614-623(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1863-2332.
[4]"Cloned viral protein vaccine for foot-and-mouth disease: responses in cattle and swine."
Kleid D.G., Yansura D.G., Small B., Dowbenko D.J., Moore D.M., Grubman M.J., McKercher P.D., Morgan D.O., Robertson B.H., Bachrach H.L.
Science 214:1125-1129(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 715-955.
[5]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10975 Genomic RNA. Translation: AAA42593.1.
AY593752 Genomic RNA. Translation: AAT01695.1.
J02187 Genomic RNA. Translation: AAA42670.1.
PIRGNNY4F. A25794.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCVNMR-A865-883[»]
ProteinModelPortalP03308.
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

EvolutionaryTraceP03308.

Entry information

Entry namePOLG_FMDVA
AccessionPrimary (citable) accession number: P03308
Secondary accession number(s): P03312 expand/collapse secondary AC list , Q65038, Q65039, Q65040, Q65041, Q65042, Q65043, Q65044, Q65045, Q65046, Q65047, Q6PN34
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 29, 2013
Last modified: April 16, 2014
This is version 141 of the entry and version 2 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