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P03310

- POLG_FMDVI

UniProt

P03310 - POLG_FMDVI

Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate -/Brazil/C3Indaial/1971 serotype C) (FMDV)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 90 (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
    Sitei723 – 7242Cleavage; by picornain 3CSequence Analysis
    Sitei931 – 9322Cleavage; by picornain 3CSequence Analysis
    Sitei949 – 9502Cleavage; by ribosomal skipSequence Analysis
    Sitei1103 – 11042Cleavage; by picornain 3CSequence Analysis
    Sitei1421 – 14222Cleavage; by picornain 3CSequence Analysis
    Sitei1574 – 15752Cleavage; by picornain 3CSequence Analysis
    Sitei1597 – 15982Cleavage; by picornain 3CSequence Analysis
    Sitei1621 – 16222Cleavage; by picornain 3CSequence Analysis
    Sitei1645 – 16462Cleavage; by picornain 3CSequence Analysis
    Active sitei1691 – 16911For picornain 3C activitySequence Analysis
    Active sitei1718 – 17181For picornain 3C activitySequence Analysis
    Active sitei1808 – 18081For picornain 3C activitySequence Analysis
    Sitei1858 – 18592Cleavage; by picornain 3CSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1213 – 12208ATPPROSITE-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 -/Brazil/C3Indaial/1971 serotype C) (FMDV)
    Taxonomic identifieri12117 [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]
    ProteomesiUP000012668: 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 – 23282328Genome polyproteinBy similarityPRO_0000422504Add
    BLAST
    Chaini1 – 201201Leader proteaseBy similarityPRO_0000422505Add
    BLAST
    Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000422506Add
    BLAST
    Chaini202 – 28685Protein VP4Sequence AnalysisPRO_0000422507Add
    BLAST
    Chaini287 – 504218Protein VP2Sequence AnalysisPRO_0000422508Add
    BLAST
    Chaini505 – 723219Protein VP3Sequence AnalysisPRO_0000039869Add
    BLAST
    Chaini724 – 931208Protein VP1By similarityPRO_0000039870Add
    BLAST
    Chaini932 – 94918Protein 2ASequence AnalysisPRO_0000039871Add
    BLAST
    Chaini950 – 1103154Protein 2BSequence AnalysisPRO_0000422509Add
    BLAST
    Chaini1104 – 1421318Protein 2CSequence AnalysisPRO_0000422510Add
    BLAST
    Chaini1422 – 1574153Protein 3ASequence AnalysisPRO_0000422511Add
    BLAST
    Chaini1575 – 159723Protein 3B-1Sequence AnalysisPRO_0000422512Add
    BLAST
    Chaini1598 – 162124Protein 3B-2Sequence AnalysisPRO_0000422513Add
    BLAST
    Chaini1622 – 164524Protein 3B-3Sequence AnalysisPRO_0000422514Add
    BLAST
    Chaini1646 – 1858213Picornain 3CSequence AnalysisPRO_0000422515Add
    BLAST
    Chaini1859 – 2328470RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000422516Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi202 – 2021N-myristoyl glycine; by hostBy similarity
    Disulfide bondi511 – 511Interchain; in VP3 dimerBy similarity
    Modified residuei1577 – 15771O-(5'-phospho-RNA)-tyrosineBy similarity
    Modified residuei1600 – 16001O-(5'-phospho-RNA)-tyrosineBy similarity
    Modified residuei1624 – 16241O-(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

    3D structure databases

    ProteinModelPortaliP03310.
    SMRiP03310. Positions 29-201, 216-931, 1652-1852, 1859-2328.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 14761476CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1498 – 2328831CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1477 – 149721Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 201201Peptidase C28Add
    BLAST
    Domaini1185 – 1349165SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1648 – 1832185Peptidase C3Add
    BLAST
    Domaini2092 – 2210119RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi865 – 8673Cell 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: P03310-1) [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 VHAIREIKTH FFSRYTGRME FTLHNGEKKI FYSRPNNHDN     50
    CWLNTILQLF RYVDEPFFDW VYNSPENLTL SAIEQLEKLT GLELREGGPP 100
    ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV 150
    FACVTSDGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG GWKANVQRKL 200
    KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
    GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 300
    LTTRNGHTTS TTQSSVGVTY GYATTEDSTS GPNTSGLETR VHQAERFFKM 350
    TLFEWVPSQS FGHMHKVVLP SEPKGVYGGL VKSYAYMRNG WDVEVTAVGN 400
    QFNGGCLLVA LVPEMGDISD REKYQLTLYP HQFINPRTNM TAHITVPYVG 450
    VNRYDQYNQH KPWTLVVMVV APLTVNTSGA QQIKVYANIA PTNVHVAGEL 500
    PSKEGIFPVA CADGYGNMVT TDPKTADPAY GKVYNPPRTA LPGRFTNYLD 550
    VAEACPTLLT FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY 600
    YTQYAGTINL HFMFTGPTDA KARYMVAYVP PGMEAPDNPE EAAHCIHAEW 650
    DTGLNSKFTF SIPYISAADY AYTASSEAET TSVQGWVCVY QITHGKADAD 700
    ALVVSASAGK DFELRLPVDA RQQTTTTGES ADPVTTTVEN YGGETQTQRR 750
    HHTDVAFVLD RFVKVQVSGN QHTLDVMQVH KDSIVGALLR AATYYFSDLE 800
    IAVTHTGKLT WVPNGAPVSA LDNTTNPTAY HKGPLTRLAL PYTAPHRVLA 850
    TAYTGTTAYT TGVRRGDLAH LAAAHARHLP TSFNFGAVKA ETITELLVRM 900
    KRAELYCPRP VLPVQPAGDR HKQPLIAPAK QLLNFDLLKL AGDVESNPGP 950
    FFFSDVRSNF SKLVETINQM QEDMSTKHGP DFNRLVSAFE ELATGVKAIR 1000
    TGLDEAKPWY KLIKLLSRLS CMAAVAARSK DPVLVAIMLA DTGLEILDST 1050
    FVVKKISDSL SSLFHVPAPV FSFGAPILLA GLVKVASSFF RSTPEDLERA 1100
    EKQLKARDIN DIFAILKNGE WLVKLILAIR DWIKAWIASE EKFVTMTDLV 1150
    PGILEKQRDL NDPSKYKEAK EWLDNARQAC LKNGNTHIAN LCKVVAPAPS 1200
    KSRPEPVVVC LRGKSGQGKS FLANVLAQAI STHFTGRTDS VWYCPPDPDH 1250
    FDGYNQQTVV VMDDLGQNPD GKDFKYFAQM VSTTGFIPPM ASLEDKGKPF 1300
    NSKVIIATTN LYSGFTPRTM VCPDALNRRF HFDIDVSAKD GYKINNKLDI 1350
    IKALEDTHTN PVAMFQYDCA LLNGMAVEMK RMQQDMFKPQ PPLQNVYQLV 1400
    QEVIERVELH EKVSSHPIFK QISIPSQKSV LYFLIEKGQH EAAIEFFEGM 1450
    VHDSIKEELR PLIQQTSFVK RAFKRLKENF EIVALCLTLL ANIVIMIRET 1500
    RKRQQMVDDA VNEYIEKANI TTDDKTLDEA EKNPLETSGA STVGFRERTL 1550
    PGHKARDDVN SEPAQPVEEQ PQAEGPYAGP LERQKPLKVR AKLPQQEGPY 1600
    AGPMERQKPL KVKAKAPVVK EGPYEGPVKK PVALKVKAKN LIVTESGAPP 1650
    TDLQKMVMGN TKPVELILDG KTVAICCATG VFGTAYLVPR HLFAEKYDKI 1700
    MLDGRAMTDS DYRVFEFEIK VKGQDMLSDA ALMVLHRGNR VRDITKHFRD 1750
    TARMKKGTPV VGVINNADVG RLIFSGEALT YKDIVVCMDG DTMPGLFAYR 1800
    AATKAGYCGG AVLAKDGADT FIVGTHSAGG NGVGYCSCVS RSMLLKMKAH 1850
    IDPEPHHEGL IVDTRDVEER VHVMRKTKLA PTVAHGVFNP DFGPAALSNR 1900
    DPRLNEGVVL DEVIFSKHKG DTKMSEEDKA LFRRCAADYA SRLHSVLGTA 1950
    NAPLSIYEAI KGVDGLDAME PDTAPGLPWA LQGKRRGALI DFENGTVGPE 2000
    VEAALKLMEK REYKFACQTF LKDEIRPMEK VRAGKTRIVD VLPVEHILYT 2050
    RMMIGRFCAQ MHSNNGPQIG SAVGCNPDVD WQRFGTHFAQ YRNVWDVDYS 2100
    AFDANHCSDA MNIMFEEVFR TEFGFHPNAE WILKTLVNTE HAYENKRITV 2150
    EGGMPSGCSA TSIINTILNN IYVLYALRRH YEGVELDTYT MISYGDDIVV 2200
    ASDYDLDFEA LKPHFKSIGQ TITPADKSDK GFVLGHSITD VTFLKRHFHM 2250
    DYGTGFYKPV MASKTLEAIL SFARRGTIQE KLISVAGLAV HSGPDEYRRL 2300
    FEPFQGLFEI PSYRSLYLRW VNAVCGDA 2328
    Length:2,328
    Mass (Da):258,282
    Last modified:May 29, 2013 - v2
    Checksum:iB2D0CE9A4BA94622
    GO
    Isoform Lb (identifier: P03310-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,300
    Mass (Da):254,971
    Checksum:i5D457B8195EFF8C8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti330 – 3301S → A.
    Natural varianti376 – 3761V → A.
    Natural varianti420 – 4201D → E.
    Natural varianti458 – 4581N → K.
    Natural varianti515 – 5151Y → F.
    Natural varianti560 – 5601T → M.
    Natural varianti638 – 6381N → S.
    Natural varianti677 – 6771E → D.
    Natural varianti722 – 7221Q → L.
    Natural varianti747 – 7471T → I.
    Natural varianti766 – 7661Q → H.
    Natural varianti805 – 8051H → Q.
    Natural varianti825 – 8251T → A.
    Natural varianti852 – 8521A → T.
    Natural varianti861 – 8633TGV → ASA.
    Natural varianti917 – 9171A → T.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform Lb. CuratedVSP_046531Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY593806 Genomic RNA. Translation: AAT01749.1.
    M90376 Genomic RNA. Translation: AAA91492.1.
    J02184 Genomic RNA. Translation: AAA42618.1.
    PIRiA03912.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY593806 Genomic RNA. Translation: AAT01749.1 .
    M90376 Genomic RNA. Translation: AAA91492.1 .
    J02184 Genomic RNA. Translation: AAA42618.1 .
    PIRi A03912.

    3D structure databases

    ProteinModelPortali P03310.
    SMRi P03310. Positions 29-201, 216-931, 1652-1852, 1859-2328.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.008.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Evolution of the capsid protein genes of foot-and-mouth disease virus: antigenic variation without accumulation of amino acid substitutions over six decades."
      Martinez M.A., Dopazo J., Hernandez J., Mateu M.G., Sobrino F., Domingo E., Knowles N.J.
      J. Virol. 66:3557-3565(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 202-933.
    3. "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] OF 714-947.

    Entry informationi

    Entry nameiPOLG_FMDVI
    AccessioniPrimary (citable) accession number: P03310
    Secondary accession number(s): Q65066, Q6PMY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: May 29, 2013
    Last modified: October 1, 2014
    This is version 90 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

    Complete proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3