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P03308

- POLG_FMDVA

UniProt

P03308 - POLG_FMDVA

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
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (29 May 2013)
      Previous versions | rss
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    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.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.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.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.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.By similarity
    RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation

    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).PROSITE-ProRule annotation

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1218 – 12258ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    2. induction by virus of host autophagy Source: UniProtKB
    3. modulation by virus of host chromatin organization Source: UniProtKB-KW
    4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    5. protein oligomerization Source: UniProtKB-KW
    6. RNA-protein covalent cross-linking 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 protein processing Source: InterPro
    11. viral RNA genome replication Source: InterPro
    12. virion attachment to host cell Source: UniProtKB-KW

    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 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    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.By similarity
    Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    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.By similarity
    Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    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.By similarity
    Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    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.By similarity

    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

    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 polyproteinPRO_0000039833Add
    BLAST
    Chaini1 – 201201Leader proteasePRO_0000039834Add
    BLAST
    Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000374074Add
    BLAST
    Chaini202 – 28685Protein VP4Sequence AnalysisPRO_0000039837Add
    BLAST
    Chaini287 – 504218Protein VP2Sequence AnalysisPRO_0000039838Add
    BLAST
    Chaini505 – 725221Protein VP3Sequence AnalysisPRO_0000039839Add
    BLAST
    Chaini726 – 936211Protein VP1Sequence AnalysisPRO_0000039840Add
    BLAST
    Chaini937 – 95418Protein 2ASequence AnalysisPRO_0000039841Add
    BLAST
    Chaini955 – 1108154Protein 2BSequence AnalysisPRO_0000039842Add
    BLAST
    Chaini1109 – 1426318Protein 2CSequence AnalysisPRO_0000039843Add
    BLAST
    Chaini1427 – 1579153Protein 3ASequence AnalysisPRO_0000039844Add
    BLAST
    Chaini1580 – 160223Protein 3B-1Sequence AnalysisPRO_0000039845Add
    BLAST
    Chaini1603 – 162624Protein 3B-2Sequence AnalysisPRO_0000039846Add
    BLAST
    Chaini1627 – 165024Protein 3B-3Sequence AnalysisPRO_0000039847Add
    BLAST
    Chaini1651 – 1863213Picornain 3CSequence AnalysisPRO_0000039848Add
    BLAST
    Chaini1864 – 2333470RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039849Add
    BLAST

    Amino acid modifications

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

    1
    2333
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03308.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 14811481CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1503 – 2333831CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1482 – 150221Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 201201Peptidase C28Add
    BLAST
    Domaini1190 – 1354165SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1653 – 1837185Peptidase C3Add
    BLAST
    Domaini2097 – 2215119RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

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

    Sequence similaritiesi

    Belongs to the picornaviruses polyprotein family.Curated
    Contains 1 peptidase C28 domain.Curated
    Contains 1 peptidase C3 domain.Curated
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
    Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

    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. CuratedVSP_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...
    MobiDBi 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: October 1, 2014
    This is version 145 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