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P03307

- POLG_FMDV5

UniProt

P03307 - POLG_FMDV5

Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate -/Germany/A5Westerwald/1951 serotype A) (FMDV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (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
    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 -/Germany/A5Westerwald/1951 serotype A) (FMDV)
    Taxonomic identifieri12113 [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]
    ProteomesiUP000012669: 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 – 23312331Genome polyproteinBy similarityPRO_0000422477Add
    BLAST
    Chaini1 – 201201Leader proteaseBy similarityPRO_0000422478Add
    BLAST
    Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000422479Add
    BLAST
    Chaini202 – 28685Protein VP4Sequence AnalysisPRO_0000422480Add
    BLAST
    Chaini287 – 504218Protein VP2Sequence AnalysisPRO_0000422481Add
    BLAST
    Chaini505 – 725221Protein VP3Sequence AnalysisPRO_0000039830Add
    BLAST
    Chaini726 – 935210Protein VP1Sequence AnalysisPRO_0000039831Add
    BLAST
    Chaini936 – 95318Protein 2ASequence AnalysisPRO_0000039832Add
    BLAST
    Chaini954 – 1107154Protein 2BSequence AnalysisPRO_0000422482Add
    BLAST
    Chaini1108 – 1425318Protein 2CSequence AnalysisPRO_0000422483Add
    BLAST
    Chaini1426 – 1578153Protein 3ASequence AnalysisPRO_0000422484Add
    BLAST
    Chaini1579 – 160123Protein 3B-1Sequence AnalysisPRO_0000422485Add
    BLAST
    Chaini1602 – 162524Protein 3B-2Sequence AnalysisPRO_0000422486Add
    BLAST
    Chaini1626 – 164924Protein 3B-3Sequence AnalysisPRO_0000422487Add
    BLAST
    Chaini1650 – 1862213Picornain 3CSequence AnalysisPRO_0000422488Add
    BLAST
    Chaini1863 – 2332470RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000422489Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi202 – 2021N-myristoyl glycine; by hostBy similarity
    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.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP03307.
    SMRiP03307. Positions 29-201, 216-286, 298-933, 1656-1856, 1863-2332.
    ModBaseiSearch...
    MobiDBiSearch...

    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
    Motifi868 – 8703Cell 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: P03307-1) [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

    MHTTDCFIAL VHAIREIRAL FLPRTTGKME LTLHNGEKKT FYSRPNNHDN     50
    CWLNTILQLF RYVDEPFFDW VYNSPENLTL EAINQLEELT GLELHEGGPP 100
    ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV 150
    FACVTSNGWY AIDDEEFYPW TPDPSDVLVF VPYDQEPLNG DWKAMVQRKL 200
    KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
    GSTDTTSTHT TNTQNNDWFS KLASSAFTGL FGALLADKKT EETTLLEDRI 300
    LTTRNGHTIS TTQSSVGVTY GYSTGEDHVA GPNTSGLETR VVQAERFFKK 350
    FLFDWTTDKP FGHLEKLELP ADHHGVFGHL VESYAYMRNG WDVEVSAVGN 400
    QFNGGCLLVA MVPEWKEFEQ REKYQLTLFP HQFISPRTNM TAHITVPYLG 450
    VNRYDQYKKH KPWTLVVMVV SPLTVSDTAA AQIKVYANIA PTYVHVAGEL 500
    PSKEGIFPVA CSDGYGGLVT TDPKTADPAY GKVYNPPRTN YPGRFTNLLD 550
    VAEACPTFLC FDDGKPYVVT RTDDTRLLAK FDVSLAAKHM SNTYLSGIAQ 600
    YYAQYSGTIN LHFMFTGSTD SKARYMVAYI PPGVEVPPDT PERAAHCIHA 650
    EWDTGLNSKF TFSIPYVSAA DYAYTASDTA ETTNVQGWVC IYQITHGKAE 700
    NDTLVVSASA GKDFELRLPI DPRQQTTAVG ESADPVTTTV ENYGGETQTQ 750
    RRHHTDVGFI MDRFVKINSL SPTHVIDLMQ THQHGLVGAL LRAATYYFSD 800
    LEIVVRHDGN LTWVPNGAPE AALSNTSNPT AYNKAPFTRL ALPYTAPHRV 850
    LATVYNGTNK YSTGGPRRGD TGSPAARAAK QLPASFNYGA IRAVTIHELL 900
    VRMKRAELYC PRPLLAIEVS SQDRHKQKII APARQLLNFD LLKLAGDVES 950
    NPGPFFFSDV RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAAGV 1000
    KAIRTGLDEA KPWYKLIKLL SRLSCMAAVA ARSKDPVLVA IMLADTGLEI 1050
    LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP ILLAGLVKVA SSFFRSTPED 1100
    LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW IASEEKFVTM 1150
    TDLVPGILEK QHDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA 1200
    PAPSKPRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RTDSVWYCPP 1250
    DPDHFDGYNQ QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK 1300
    GKPFNSKVII ATTNLYSGFT PRTMVCPDAL NRRFHFDIDV SAKDGYKINN 1350
    KLDITKALED THTNPVAMFQ YDCALLNGMA VEMKRMQQDM FKPQPPLQNV 1400
    YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIK KGQHEAAIEF 1450
    FEGMVHDSVK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM 1500
    IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKNPLE TSGASTVGFR 1550
    ERTLPGQKAR DDVNSEPAQP AEEQPQAEGP YAGPLERQRP LKVRAKLPQQ 1600
    EGPYAGPMER QKPLKVKAKA PVVKEGPYEG PVKKPVALKV RAKNLIVTES 1650
    GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC CATGVFGTAY LVPRHLFAEK 1700
    YDKIMLDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH RGNRVRDITK 1750
    HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL 1800
    FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK 1850
    MKAHIDPEPH HEGLIVDTRD AEERVHVMRK TKLAPTVAHG VFNPEFGPAA 1900
    LSNKDPRLNE GVVLDEVIFS KHKGDTKMSE EDKALFRRCA ADYASRLHSV 1950
    LGTANAPLSI YEAIKGVDGL DAMEPDTAPG LPWALQGKRR GALIDFENGT 2000
    VGPEVEAALK LMEKREYKFV CQTFLKDEIR PMEKVRAGKT RIVDVLPVEH 2050
    ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD 2100
    VDYSAFDANH CSDAMNIMFE EVFRTDFGFH PNAEWILKTL VNTEHAYENK 2150
    RHTVEGGMPS 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):259,336
    Last modified:May 29, 2013 - v2
    Checksum:iCD295048EBAA0EFC
    GO
    Isoform Lb (identifier: P03307-2) [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):256,143
    Checksum:i1EEAD5368F43ABE1
    GO

    Sequence cautioni

    The sequence CAA24365.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti746 – 7461E → D.
    Natural varianti753 – 7553HHT → YYM.
    Natural varianti871 – 8711T → M.
    Natural varianti874 – 8741P → A.
    Natural varianti894 – 8941V → I.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform Lb. CuratedVSP_046529Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY593781 Genomic RNA. Translation: AAT01724.1.
    V01135 Genomic RNA. Translation: CAA24365.1. Different initiation.
    V01135 Genomic RNA. Translation: CAA24366.1. Sequence problems.
    PIRiA03909.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY593781 Genomic RNA. Translation: AAT01724.1 .
    V01135 Genomic RNA. Translation: CAA24365.1 . Different initiation.
    V01135 Genomic RNA. Translation: CAA24366.1 . Sequence problems.
    PIRi A03909.

    3D structure databases

    ProteinModelPortali P03307.
    SMRi P03307. Positions 29-201, 216-286, 298-933, 1656-1856, 1863-2332.
    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. "The molecular basis of the antigenic variation of foot-and-mouth disease virus."
      Beck E., Feil G., Strohmaier K.
      EMBO J. 2:555-559(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiPOLG_FMDV5
    AccessioniPrimary (citable) accession number: P03307
    Secondary accession number(s): Q6PN05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: May 29, 2013
    Last modified: October 1, 2014
    This is version 92 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

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