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P03308

- POLG_FMDVA

UniProt

P03308 - POLG_FMDVA

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Protein
Genome polyprotein
Gene
N/A
Organism
Foot-and-mouth disease virus (isolate Bovine/United Kingdom/A12Valle119/1932 serotype A) (FMDV)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei51 – 511For leader protease activity By similarity
Active sitei148 – 1481For leader protease activity By similarity
Active sitei163 – 1631For leader protease activity By similarity
Sitei201 – 2022Cleavage; by leader protease Reviewed prediction
Sitei286 – 2872Cleavage Reviewed prediction
Sitei504 – 5052Cleavage; by picornain 3C Reviewed prediction
Sitei725 – 7262Cleavage; by picornain 3C Reviewed prediction
Sitei936 – 9372Cleavage; by picornain 3C Reviewed prediction
Sitei954 – 9552Cleavage; by ribosomal skip Reviewed prediction
Sitei1108 – 11092Cleavage; by picornain 3C Reviewed prediction
Sitei1426 – 14272Cleavage; by picornain 3C Reviewed prediction
Sitei1579 – 15802Cleavage; by picornain 3C Reviewed prediction
Sitei1602 – 16032Cleavage; by picornain 3C Reviewed prediction
Sitei1626 – 16272Cleavage; by picornain 3C Reviewed prediction
Sitei1650 – 16512Cleavage; by picornain 3C Reviewed prediction
Active sitei1696 – 16961For picornain 3C activity Reviewed prediction
Active sitei1723 – 17231For picornain 3C activity Reviewed prediction
Active sitei1813 – 18131For picornain 3C activity Reviewed prediction
Sitei1863 – 18642Cleavage; by picornain 3C Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1218 – 12258ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB-KW
  3. RNA helicase activity Source: InterPro
  4. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  5. cysteine-type endopeptidase activity Source: InterPro
  6. ion channel activity Source: UniProtKB-KW
  7. structural molecule activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. RNA-protein covalent cross-linking Source: UniProtKB-KW
  2. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  3. induction by virus of host autophagy Source: UniProtKB
  4. modulation by virus of host chromatin organization Source: UniProtKB-KW
  5. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  6. protein oligomerization Source: UniProtKB-KW
  7. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  8. suppression by virus of host translation initiation factor activity Source: UniProtKB
  9. transcription, DNA-templated Source: InterPro
  10. viral RNA genome replication Source: InterPro
  11. viral protein processing Source: InterPro
  12. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

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

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 15 chains:
Leader protease (EC:3.4.22.46)
Short name:
Lpro
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Alternative name(s):
P52
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Protein 3B-1
Short name:
P3B-1
Alternative name(s):
Genome-linked protein VPg1
Protein 3B-2
Short name:
P3B-2
Alternative name(s):
Genome-linked protein VPg2
Protein 3B-3
Short name:
P3B-3
Alternative name(s):
Genome-linked protein VPg3
Alternative name(s):
Protease 3C
Short name:
P3C
Protease P20B
Alternative name(s):
P56A
OrganismiFoot-and-mouth disease virus (isolate Bovine/United Kingdom/A12Valle119/1932 serotype A) (FMDV)
Taxonomic identifieri12114 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeAphthovirus
Virus hostiBos 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]
ProteomesiUP000007707: Genome, UP000013587: Genome

Subcellular locationi

Chain Protein VP2 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP3 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP1 : Virion. Host cytoplasm Reviewed prediction
Chain Protein 2B : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 2C : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3A : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3B-1 : Virion Reviewed prediction
Chain Protein 3B-2 : Virion Reviewed prediction
Chain Protein 3B-3 : Virion Reviewed prediction
Chain Picornain 3C : Host cytoplasm Reviewed prediction
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 14811481Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1482 – 150221 Reviewed prediction
Add
BLAST
Topological domaini1503 – 2333831Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. icosahedral viral capsid Source: InterPro
  3. integral to membrane of host cell Source: UniProtKB-KW
  4. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23322332Genome polyprotein
PRO_0000039833Add
BLAST
Chaini1 – 201201Leader protease
PRO_0000039834Add
BLAST
Chaini202 – 504303Protein VP0 Reviewed prediction
PRO_0000374074Add
BLAST
Chaini202 – 28685Protein VP4 Reviewed prediction
PRO_0000039837Add
BLAST
Chaini287 – 504218Protein VP2 Reviewed prediction
PRO_0000039838Add
BLAST
Chaini505 – 725221Protein VP3 Reviewed prediction
PRO_0000039839Add
BLAST
Chaini726 – 936211Protein VP1 Reviewed prediction
PRO_0000039840Add
BLAST
Chaini937 – 95418Protein 2A Reviewed prediction
PRO_0000039841Add
BLAST
Chaini955 – 1108154Protein 2B Reviewed prediction
PRO_0000039842Add
BLAST
Chaini1109 – 1426318Protein 2C Reviewed prediction
PRO_0000039843Add
BLAST
Chaini1427 – 1579153Protein 3A Reviewed prediction
PRO_0000039844Add
BLAST
Chaini1580 – 160223Protein 3B-1 Reviewed prediction
PRO_0000039845Add
BLAST
Chaini1603 – 162624Protein 3B-2 Reviewed prediction
PRO_0000039846Add
BLAST
Chaini1627 – 165024Protein 3B-3 Reviewed prediction
PRO_0000039847Add
BLAST
Chaini1651 – 1863213Picornain 3C Reviewed prediction
PRO_0000039848Add
BLAST
Chaini1864 – 2333470RNA-directed RNA polymerase 3D-POL Reviewed prediction
PRO_0000039849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi202 – 2021N-myristoyl glycine; by host By similarity
Disulfide bondi511 – 511Interchain; in VP3 dimer
Modified residuei1582 – 15821O-(5'-phospho-RNA)-tyrosine By similarity
Modified residuei1605 – 16051O-(5'-phospho-RNA)-tyrosine By similarity
Modified residuei1629 – 16291O-(5'-phospho-RNA)-tyrosine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Covalent protein-RNA linkage, Disulfide bond, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi880 – 8823

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCVNMR-A865-883[»]
ProteinModelPortaliP03308.
SMRiP03308. Positions 29-201, 216-286, 298-934, 1657-1857, 1864-2333.

Miscellaneous databases

EvolutionaryTraceiP03308.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 201201Peptidase C28
Add
BLAST
Domaini1190 – 1354165SF3 helicase
Add
BLAST
Domaini1653 – 1837185Peptidase C3
Add
BLAST
Domaini2097 – 2215119RdRp catalytic
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi869 – 8713Cell attachment site

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProiIPR015031. 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.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF05408. 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]
PRINTSiPR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform Lab (identifier: P03308-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MNTTNCFIAL VHAIREIRAF FLSRATGKME FTLYNGERKT FYSRPNNHDN     50
CWLNTILQLF RYVDEPFFDW VYNSPENLTL AAIKQLEELT GLELHEGGPP 100
ALVIWNIKHL LQTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV 150
FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG GWKANVQRKL 200
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
GSTDTTSTHT TNTQNNDWFS KLASSAFTGL FGALLADKKT EETTLLEDRI 300
LTTRNGHTTS TTQSSVGVTY GYSTEEDHVA GPNTSGLETR VVQAERFFKK 350
FLFDWTTDKP FGHLEKLELP TDHHGVFGHL VDSYAYMRNG WDVEVSAVGN 400
QFNGGCLLVA MVPEWKEFDK REKYQLTLFP HQFISPRTNM TAHITVPYLG 450
VNRYDQYKKH KPWTLVIMVV SPLTVSNTAA TQIKVYANIA PTYVHVAGEL 500
PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVYNPPRTN YPGRFTNLLD 550
VAEACPTFLC FDDGKPYVVT RTDDTRLLAK FDVSLAAKHM SNTYLSGIAQ 600
YYTQYSGTIN LHFMFTGSTD SKARYMVAYI PPGVETPPET PEGAAHCIHA 650
EWDTGLNSKF TFSIPYVSAA DYAYTASDTA ETTNVQGWVC IYQITHGKAE 700
GDTLVVSASA GKDFELRLPI DPRSQTTATG ESADPVTTTV ENYGGETQVQ 750
RRHHTDVSFI MDRFVKIKSL NPTHVIDLMQ THQHGLVGAL LRAATYYFSD 800
LEIVVRHDGN LTWVPNGAPE AALSNTGNPT AYNKAPFTRL ALPYTAPHRV 850
LATVYNGTNK YSASGSGVRG DSGSLAPRVA RQLPASFNYG AIKAETIHEL 900
LVRMKRAELY CPRPLLAIEV SSQDRHKQKI IAPGKQLLNF DLLKLAGDVE 950
SNPGPFFFAD VRSNFSKLVD TINQMQEDMS TKHGPDFNRL VSAFEELATG 1000
VKAIRTGLDE AKPWYKLIKL LSRLSCMAAV AARSKDPVLV AIMLADTGLE 1050
ILDSTFVVKK ISDSLSSLFH VPAPVFSFGA PVLLAGLVKV ASSFFRSTPE 1100
DLERAEKQLK ARDINDIFAI LKNGEWLVKL ILAIRDWIKA WIASEEKFVT 1150
TTDLVPGILE KQRDLNDPSK YKEAKEWLDN ARQACLKSGN VHIANLCKVV 1200
APAPSKSRPE PVVVCLRGKS GQGKSFLANV LAQAISTHFT GRTDSVWYCP 1250
PDPDHFDGYN QQTVVVMDDL GQNPDGKDFK YFAQMVSTTG FIPPMASLED 1300
KGKPFNSKVI IATTNLYSGF TPRTMVCPDA LNRRFHFDID VSAKDGYKIN 1350
NKLDIIKALE DTHTNPVAMF QYDCALLNGM AVEMKRMQQD MFKPQPPLQN 1400
VYQLVQEVIE RVELHEKVSS HPIFKQISIP SQKSVLYFLI EKGQHEAAIE 1450
FFEGMVHDSI KEELRPLIQQ TSFVKRAFKR LKENFEIVAL CLTLLANIVI 1500
MIRETRKRQK MVDDAVNEYI EKANITTDDT TLDEAEKNPL ETSGASTVGF 1550
RERTLTGQRA CNDVNSEPAR PAEEQPQAEG PYTGPLERQR PLKVRAKLPQ 1600
QEGPYAGPLE RQKPLKVKAK APVVKEGPYE GPVKKPVALK VKAKNLIVTE 1650
SGAPPTDLQK MVMGNTKPVE LILDGKTVAI CCATGVFGTA YLVPRHLFAE 1700
KYDKIMLDGR AMTDSDYRVF EFEIKVKGQD MLSDAALMVL HRGNRVRDIT 1750
KHFRDTARMK KGTPVVGVVN NADVGRLIFS GEALTYKDIV VCMDGDTMPG 1800
LFAYKAATKA GYCGGAVLAK DGADTFIVGT HSAGGNGVGY CSCVSRSMLL 1850
RMKAHVDPEP HHEGLIVDTR DVEERVHVMR KTKLAPTVAH GVFNPEFGPA 1900
ALSNKDPRLN EGVVLDEVIF SKHKGDTKMS AEDKALFRRC AADYASRLHS 1950
VLGTANAPLS IYEAIKGVDG LDAMESDTAP GLPWAFQGKR RGALIDFENG 2000
TVGPEVEAAL KLMEKREYKF ACQTFLKDEI RPMEKVRAGK TRIVDVLPVE 2050
HILYTRMMIG RFCAQMHSNN GPQIGSAVGC NPDVDWQRFG THFAQYRNVW 2100
DVDYSAFDAN HCSDAMNIMF EEVFRTDFGF HPNAEWILKT LVNTEHAYEN 2150
KRITVEGGMP SGCSATSIIN TILNNIYVLY ALRRHYEGVE LDTYTMISYG 2200
DDIVVASDYD LDFEALKPHF KSLGQTITPA DKSDKGFVLG HSITDVTFLK 2250
RHFHIDYGTG FYKPVMASKT LEAILSFARR GTIQEKLTSV AGLAVHSGPD 2300
EYRRLFEPFQ GLFEIPSYRS LYLRWVNAVC GDA 2333
Length:2,333
Mass (Da):259,162
Last modified:May 29, 2013 - v2
Checksum:i3B61837F593073BD
GO
Isoform Lb (identifier: P03308-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,305
Mass (Da):255,998
Checksum:i469A19C57B5F5E8B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti122 – 1243SEV → AR in 119ab variant.
Natural varianti131 – 1311D → N in 119ab variant.
Natural varianti145 – 1451G → E in 119ab variant.
Natural varianti357 – 3571T → P in 119ab variant.
Natural varianti364 – 3652LE → RT in 119ab variant.
Natural varianti417 – 4171E → T in 119ab variant.
Natural varianti420 – 4201K → T in 119ab variant.
Natural varianti423 – 4231K → E in 119ab variant.
Natural varianti470 – 4701V → L in 119ab variant.
Natural varianti504 – 5041E → V in 119ab variant.
Natural varianti533 – 5331V → E in 119ab variant.
Natural varianti538 – 5381R → K in 119ab variant.
Natural varianti543 – 5431G → R in 119ab variant.
Natural varianti701 – 7011G → D in 119ab variant.
Natural varianti872 – 8721S → F in 119ab variant.
Natural varianti954 – 9541G → R in 119ab variant.
Natural varianti1034 – 10341S → T in 119ab variant.
Natural varianti1095 – 10951F → L in 119ab variant.
Natural varianti1151 – 11511T → M in 119ab variant.
Natural varianti1156 – 11561P → L in 119ab variant.
Natural varianti1356 – 13561I → V in 119ab variant.
Natural varianti1800 – 18001G → S in 119ab variant.
Natural varianti1846 – 18461R → K in 119ab variant.
Natural varianti1861 – 18611H → Q in 119ab variant.
Natural varianti1939 – 19391R → A in 119ab variant.
Natural varianti2021 – 20211A → V in 119ab variant.
Natural varianti2109 – 21091A → T in 119ab variant.
Natural varianti2162 – 21621G → D in 119ab variant.
Natural varianti2167 – 21671S → G in 119ab variant.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform Lb.
VSP_018980Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10975 Genomic RNA. Translation: AAA42593.1.
AY593752 Genomic RNA. Translation: AAT01695.1.
J02187 Genomic RNA. Translation: AAA42670.1.
PIRiA25794. GNNY4F.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10975 Genomic RNA. Translation: AAA42593.1 .
AY593752 Genomic RNA. Translation: AAT01695.1 .
J02187 Genomic RNA. Translation: AAA42670.1 .
PIRi A25794. GNNY4F.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BCV NMR - A 865-883 [» ]
ProteinModelPortali P03308.
SMRi P03308. Positions 29-201, 216-286, 298-934, 1657-1857, 1864-2333.
ModBasei Search...

Protein family/group databases

MEROPSi C03.008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03308.

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProi IPR015031. 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.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF05408. 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 ]
PRINTSi PR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiPOLG_FMDVA
AccessioniPrimary (citable) accession number: P03308
Secondary accession number(s): P03312
, Q65038, Q65039, Q65040, Q65041, Q65042, Q65043, Q65044, Q65045, Q65046, Q65047, Q6PN34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 29, 2013
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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