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P03305

- POLG_FMDVO

UniProt

P03305 - POLG_FMDVO

Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O) (FMDV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    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.
    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.
    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 activity
    Active sitei148 – 1481For leader protease activity
    Active sitei163 – 1631For leader protease activity
    Sitei201 – 2022Cleavage; by leader proteaseSequence Analysis
    Sitei286 – 2872CleavageSequence Analysis
    Sitei504 – 5052Cleavage; by picornain 3CSequence Analysis
    Sitei724 – 7252Cleavage; by picornain 3CSequence Analysis
    Sitei935 – 9362Cleavage; by picornain 3CSequence Analysis
    Sitei953 – 9542Cleavage; by ribosomal skipSequence Analysis
    Sitei1107 – 11082Cleavage; by picornain 3CSequence Analysis
    Sitei1425 – 14262Cleavage; by picornain 3CSequence Analysis
    Sitei1578 – 15792Cleavage; by picornain 3CSequence Analysis
    Sitei1601 – 16022Cleavage; by picornain 3CSequence Analysis
    Sitei1625 – 16262Cleavage; by picornain 3CSequence Analysis
    Sitei1649 – 16502Cleavage; by picornain 3CSequence Analysis
    Active sitei1695 – 16951For picornain 3C activitySequence Analysis
    Active sitei1722 – 17221For picornain 3C activitySequence Analysis
    Active sitei1812 – 18121For picornain 3C activitySequence Analysis
    Sitei1862 – 18632Cleavage; by picornain 3CSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1217 – 12248ATPPROSITE-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- 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

    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/Germany/O1Kaufbeuren/1966 serotype O) (FMDV)
    Taxonomic identifieri73482 [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]
    ProteomesiUP000008765: 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_0000039872Add
    BLAST
    Chaini1 – 201201Leader proteasePRO_0000039873Add
    BLAST
    Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000374076Add
    BLAST
    Chaini202 – 28685Protein VP4Sequence AnalysisPRO_0000039876Add
    BLAST
    Chaini287 – 504218Protein VP2Sequence AnalysisPRO_0000039877Add
    BLAST
    Chaini505 – 724220Protein VP3Sequence AnalysisPRO_0000039878Add
    BLAST
    Chaini725 – 935211Protein VP1PRO_0000039879Add
    BLAST
    Chaini936 – 95318Protein 2ASequence AnalysisPRO_0000039880Add
    BLAST
    Chaini954 – 1107154Protein 2BSequence AnalysisPRO_0000310976Add
    BLAST
    Chaini1108 – 1425318Protein 2CSequence AnalysisPRO_0000039881Add
    BLAST
    Chaini1426 – 1578153Protein 3ASequence AnalysisPRO_0000039882Add
    BLAST
    Chaini1579 – 160123Protein 3B-1Sequence AnalysisPRO_0000039883Add
    BLAST
    Chaini1602 – 162524Protein 3B-2Sequence AnalysisPRO_0000310977Add
    BLAST
    Chaini1626 – 164924Protein 3B-3Sequence AnalysisPRO_0000310978Add
    BLAST
    Chaini1650 – 1862213Picornain 3CSequence AnalysisPRO_0000039884Add
    BLAST
    Chaini1863 – 2332470RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039885Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi202 – 2021N-myristoyl glycine; by hostBy similarity
    Disulfide bondi406 ↔ 858Interchain (between VP2 and VP1 chains)
    Disulfide bondi511 – 511Interchain; in VP3 dimer
    Modified residuei1581 – 15811O-(5'-phospho-RNA)-tyrosineBy similarity
    Modified residuei1604 – 16041O-(5'-phospho-RNA)-tyrosineBy similarity
    Modified residuei1628 – 16281O-(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.

    Structurei

    Secondary structure

    1
    2332
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 323
    Beta strandi38 – 403
    Beta strandi47 – 493
    Helixi51 – 6313
    Helixi66 – 683
    Helixi69 – 724
    Beta strandi73 – 764
    Helixi79 – 9012
    Helixi100 – 1078
    Helixi108 – 1103
    Beta strandi111 – 1133
    Beta strandi115 – 1206
    Beta strandi123 – 1264
    Beta strandi129 – 1313
    Helixi134 – 1363
    Beta strandi137 – 1448
    Turni145 – 1473
    Beta strandi148 – 1536
    Beta strandi158 – 1636
    Beta strandi166 – 1694
    Helixi174 – 1763
    Beta strandi177 – 1826
    Turni195 – 1973

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00573.
    ProteinModelPortaliP03305.
    SMRiP03305. Positions 29-201, 216-286, 291-934, 1656-1856, 1863-2332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03305.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 14801480CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1502 – 2332831CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1481 – 150121Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 201201Peptidase C28Add
    BLAST
    Domaini1189 – 1353165SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1652 – 1836185Peptidase C3Add
    BLAST
    Domaini2096 – 2214119RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

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

    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: P03305-1) [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

    MNTTDCFIAL VQAIREIKAL FLSRTTGKME LTLYNGEKKT FYSRPNNHDN     50
    CWLNAILQLF RYVEEPFFDW VYSSPENLTL EAIKQLEDLT GLELHEGGPP 100
    ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV 150
    FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG EWKAKVQRKL 200
    KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
    GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 300
    LTTRNGHTTS TTQSSVGVTY GYATAEDFVS GPNTSGLETR VVQAERFFKT 350
    HLFDWVTSDS FGRCHLLELP TDHKGVYGSL TDSYAYMRNG WDVEVTAVGN 400
    QFNGGCLLVA MVPELYSIQK RELYQLTLFP HQFINPRTNM TAHITVPFVG 450
    VNRYDQYKVH KPWTLVVMVV APLTVNTEGA PQIKVYANIA PTNVHVAGEF 500
    PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVFNPPRNQ LPGRFTNLLD 550
    VAEACPTFLR FEGGVPYVTT KTDSDRVLAQ FDMSLAAKQM SNTFLAGLAQ 600
    YYTQYSGTIN LHFMFTGPTD AKARYMVAYA PPGMEPPKTP EAAAHCIHAE 650
    WDTGLNSKFT FSIPYLSAAD YAYTASGVAE TTNVQGWVCL FQITHGKADG 700
    DALVVLASAG KDFELRLPVD ARAETTSAGE SADPVTTTVE NYGGETQIQR 750
    RQHTDVSFIM DRFVKVTPQN QINILDLMQI PSHTLVGALL RASTYYFSDL 800
    EIAVKHEGDL TWVPNGAPEK ALDNTTNPTA YHKAPLTRLA LPYTAPHRVL 850
    ATVYNGECRY NRNAVPNLRG DLQVLAQKVA RTLPTSFNYG AIKATRVTEL 900
    LYRMKRAETY CPRPLLAIHP TEARHKQKIV APVKQTLNFD LLKLAGDVES 950
    NPGPFFFSDV RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAIGV 1000
    KAIRTGLDEA KPWYKLIKLL SRLSCMAAVA ARSKDPVLVA IMLADTGLEI 1050
    LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP VLLAGLVKVA SSFFRSTPED 1100
    LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW IASEEKFVTM 1150
    TDLVPGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA 1200
    PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP 1250
    DPDHFDGYNQ QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK 1300
    GKPFNSKVII ATTNLYSGFT PRTMVCPDAL NRRFHFDIDV SAKDGYKINS 1350
    KLDIIKALED THANPVAMFQ YDCALLNGMA VEMKRMQQDM FKPQPPLQNV 1400
    YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIE KGQHEAAIEF 1450
    FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM 1500
    IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKSPLE TSGASTVGFR 1550
    ERTLPGQKAC DDVNSEPAQP VEEQPQAEGP YAGPLERQKP LKVRAKLPQQ 1600
    EGPYAGPMER QKPLKVKAKA PVVKEGPYEG PVKKPVALKV KAKNLIVTES 1650
    GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC CATGVFGTAY LVPRHLFAEK 1700
    YDKIMVDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH RGNRVRDITK 1750
    HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL 1800
    FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK 1850
    MKAHIDPEPH HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA 1900
    LSNKDPRLNE GVVLDEVIFS KHKGDTKMSE EDKALFRRCA ADYASRLHSV 1950
    LGTANAPLSI YEAIKGVDGL DAMEPDTAPG LPWALQGKRR GALIDFENGT 2000
    VGPEVEAALK LMEKREYKFV CQTFLKDEIR PLEKVRAGKT RIVDVLPVEH 2050
    ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD 2100
    VDYSAFDANH CSDAMNIMFE EVFRTEFGFH PNAEWILKTL VNTEHAYENK 2150
    RITVGGGMPS GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD 2200
    DIVVASDYDL DFEALKPHFK SLGQTITPAD KSDKGFVLGH SITDVTFLKR 2250
    HFHMDYGTGF YKPVMASKTL EAILSFARRG TIQEKLISVA GLAVHSGPDE 2300
    YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA 2332
    Length:2,332
    Mass (Da):258,927
    Last modified:July 21, 1986 - v1
    Checksum:i4A83176F43447D68
    GO
    Isoform Lb (identifier: P03305-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,304
    Mass (Da):255,803
    Checksum:i5372D197CC761349
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti780 – 7801I → V in strain: Isolate O1BFS.
    Natural varianti808 – 8081G → R in strain: Isolate O1BFS.
    Natural varianti861 – 8611N → S in strain: Isolate O1BFS.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform Lb. CuratedVSP_018982Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00871 Genomic RNA. Translation: CAA25416.1.
    J02185 Genomic RNA. Translation: AAA42635.1.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Web resourcesi

    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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00871 Genomic RNA. Translation: CAA25416.1 .
    J02185 Genomic RNA. Translation: AAA42635.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QMY X-ray 1.90 A/B/C 29-195 [» ]
    1QOL X-ray 3.00 A/B/C/D/E/F/G/H 29-201 [» ]
    1QQP X-ray 1.90 1 725-937 [» ]
    2 287-504 [» ]
    3 505-724 [» ]
    4 202-286 [» ]
    2JQF NMR - R/S 29-201 [» ]
    2JQG NMR - R 29-195 [» ]
    DisProti DP00573.
    ProteinModelPortali P03305.
    SMRi P03305. Positions 29-201, 216-286, 291-934, 1656-1856, 1863-2332.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.008.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P03305.

    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 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.

    Entry informationi

    Entry nameiPOLG_FMDVO
    AccessioniPrimary (citable) accession number: P03305
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 155 of the entry and version 1 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.

    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