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P03306

- POLG_FMDV1

UniProt

P03306 - POLG_FMDV1

Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (strain A10-61) (Aphthovirus A) (FMDV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Feb 2005)
      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-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 (strain A10-61) (Aphthovirus A) (FMDV)
    Taxonomic identifieri12112 [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]
    ProteomesiUP000008764: 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_0000039816Add
    BLAST
    Chaini1 – 201201Leader proteaseSequence AnalysisPRO_0000039817Add
    BLAST
    Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000374073Add
    BLAST
    Chaini202 – 28685Protein VP4Sequence AnalysisPRO_0000039820Add
    BLAST
    Chaini287 – 504218Protein VP2Sequence AnalysisPRO_0000039821Add
    BLAST
    Chaini505 – 725221Protein VP3Sequence AnalysisPRO_0000039822Add
    BLAST
    Chaini726 – 935210Protein VP1Sequence AnalysisPRO_0000039823Add
    BLAST
    Chaini936 – 95318Protein 2ASequence AnalysisPRO_0000039824Add
    BLAST
    Chaini954 – 1107154Protein 2BSequence AnalysisPRO_0000310973Add
    BLAST
    Chaini1108 – 1425318Protein 2CSequence AnalysisPRO_0000310974Add
    BLAST
    Chaini1426 – 1578153Protein 3ASequence AnalysisPRO_0000310975Add
    BLAST
    Chaini1579 – 160123Protein 3B-1Sequence AnalysisPRO_0000039825Add
    BLAST
    Chaini1602 – 162524Protein 3B-2Sequence AnalysisPRO_0000039826Add
    BLAST
    Chaini1626 – 164924Protein 3B-3Sequence AnalysisPRO_0000039827Add
    BLAST
    Chaini1650 – 1862213Picornain 3CSequence AnalysisPRO_0000039828Add
    BLAST
    Chaini1863 – 2332470RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039829Add
    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 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

    Secondary structure

    1
    2332
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi229 – 2324
    Helixi268 – 2747
    Beta strandi301 – 3055
    Beta strandi308 – 3147
    Helixi332 – 3343
    Helixi342 – 3443
    Beta strandi348 – 3558
    Beta strandi364 – 3707
    Helixi376 – 3838
    Beta strandi384 – 39714
    Beta strandi404 – 41411
    Helixi422 – 4287
    Beta strandi429 – 4346
    Turni436 – 4383
    Beta strandi440 – 4467
    Beta strandi450 – 4556
    Turni457 – 4593
    Beta strandi463 – 47412
    Beta strandi477 – 4793
    Beta strandi483 – 49917
    Helixi548 – 5547
    Turni562 – 5643
    Beta strandi565 – 5695
    Beta strandi572 – 5743
    Beta strandi577 – 5837
    Helixi588 – 5903
    Helixi594 – 5996
    Beta strandi602 – 6076
    Beta strandi609 – 6157
    Beta strandi622 – 6309
    Beta strandi632 – 6365
    Helixi641 – 6444
    Beta strandi647 – 6537
    Beta strandi659 – 6646
    Beta strandi669 – 6713
    Beta strandi673 – 6764
    Beta strandi688 – 69811
    Beta strandi703 – 7108
    Beta strandi715 – 7195
    Helixi730 – 7323
    Helixi740 – 7434
    Helixi753 – 7553
    Helixi757 – 7615
    Beta strandi763 – 7675
    Beta strandi772 – 7754
    Helixi778 – 7803
    Helixi786 – 7927
    Beta strandi794 – 80916
    Beta strandi811 – 8144
    Helixi820 – 8245
    Beta strandi828 – 8314
    Beta strandi838 – 8425
    Beta strandi847 – 8537
    Beta strandi890 – 8923
    Beta strandi894 – 91118
    Beta strandi921 – 9233
    Beta strandi936 – 9383
    Helixi1657 – 16648
    Beta strandi1665 – 16728
    Beta strandi1675 – 168713
    Beta strandi1689 – 16935
    Helixi1694 – 16974
    Beta strandi1702 – 17065
    Beta strandi1709 – 17113
    Helixi1713 – 17153
    Beta strandi1716 – 17194
    Beta strandi1722 – 17254
    Beta strandi1726 – 17283
    Beta strandi1733 – 174210
    Helixi1749 – 17513
    Beta strandi1752 – 17554
    Beta strandi1763 – 17708
    Turni1771 – 17733
    Beta strandi1774 – 178411
    Beta strandi1800 – 18045
    Beta strandi1815 – 18206
    Beta strandi1823 – 183412
    Beta strandi1837 – 18426
    Helixi1845 – 18539

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZBAX-ray2.001726-937[»]
    2287-504[»]
    3505-725[»]
    4202-286[»]
    1ZBEX-ray3.001726-937[»]
    2287-504[»]
    3505-725[»]
    4202-286[»]
    2BHGX-ray1.90A/B1650-1855[»]
    2J92X-ray2.20A/B1649-1855[»]
    2WV4X-ray2.50A/B1650-1862[»]
    C/D931-940[»]
    2WV5X-ray2.70A/B/C/D1650-1862[»]
    E/F/G/H936-940[»]
    ProteinModelPortaliP03306.
    SMRiP03306. Positions 29-201, 216-286, 298-933, 1656-1856, 1863-2332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03306.

    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 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

    Note: Both isoforms are able to cleave the L/VP0 junction and the host translation initiation factor EIF4G1.

    Isoform Lab (identifier: P03306-1) [UniParc]FASTAAdd to Basket

    Also known as: P20a

    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 VYLIREIKTL FRSRTKGKME FTLHNGEKKT FYSRPNNHDN     50
    CWLNTILQLF RYVDEPFFDW VYNSPENLTL DAIKQLENFT GLELHEGGPP 100
    ALVIWNIKHL LQTGIGTASR PSEVCMVDGT DMCLADFHAG IFMKGQEHAV 150
    FACVTSDGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG DWKTQVQKKL 200
    KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMSTQLG DNTISGGSNE 250
    GSTDTTSTHT TNTQNNDWFS KLASSAFTGL FGALLADKKT EETTLLEDRI 300
    LTTRNGHTTS TTQSSVGVTY GYSTEEDHVA GPNTSGLETR VVQAERFFKK 350
    FLFDWTTDKP FGYLTKLELP TDHHGVFGHL VDSYAYMRNG WDVEVSAVGN 400
    QFNGGCLLVA MVPEWKAFDT REKYQLTLFP HQFISPRTNM TAHITVPYLG 450
    VNRYDQYKKH KPWTLVVMVL SPLTVSNTAA PQIKVYANIA PTYVHVAGEL 500
    PSKEGIFPVA CADGYGGLVT TDPKTADPVY GKVYNPPKTN YPGRFTNLLD 550
    VAEACPTFLR FDDGKPYVVT RADDTRLLAK FDVSLAAKHM SNTYLSGIAQ 600
    YYTQYSGTIN LHFMFTGSTD SKARYMVAYI PPGVETPPDT PEEAAHCIHA 650
    EWDTGLNSKF TFSIPYVSAA DYAYTASDTA ETTNVQGWVC VYQITHGKAE 700
    NDTLLVSASA GKDFELRLPI DPRTQTTTTG ESADPVTTTV ENYGGDTQVQ 750
    RRHHTDVGFI MDRFVKINSL SPTHVIDLMQ THKHGIVGAL LRAATYYFSD 800
    LEIVVRHDGN LTWVPNGAPE AALSNTSNPT AYNKAPFTRL ALPYTAPHRV 850
    LATVYDGTNK YSASDSRSGD LGSIAARVAT QLPASFNYGA IQAQAIHELL 900
    VRMKRAELYC PRPLLAIKVT SQDRYKQKII APAKQLLNFD LLKLAGDVES 950
    NLGPFFFADV RSNFSKLVDT INQMQEDMST KHGPDFNRLV SAFEELATGV 1000
    KAIRTGLDEA KPWYKLIKLL SRLSCMAAVA ARSKDPVLVA IMLADTGLEI 1050
    LDSTFVVKKS SDSLSSLFHV PAPAFSFGAP VLLAGLVKVA SSFFRSTPED 1100
    LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW IASEEKFVTM 1150
    TDLVPGILEK QRDLNDPGKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA 1200
    PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP 1250
    DPDHFDGYNQ QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK 1300
    GKPFNSKVII ATTNLYSGFT PRTMVCPDAL NRRFHFDIDV SAKDGYKINN 1350
    KLDIIKALED THTNPVAMFQ YDCALLNGMA VEMKRLQQDM FKPQPPLQNV 1400
    YQLVQEVIER VELHEKVSSH PIFKQISIPS QKSVLYFLIE KGQHEAAIEF 1450
    FEGMVHDSVK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM 1500
    IRETRKRQKM VDDAVNEYIE RANITTDDKT LDEAEKNPLE TSGASTVGFR 1550
    ERSLTGQKVR DDVSSEPAQP AEDQPQAEGP YSGPLERQKP LKVRAKLPQQ 1600
    EGPYAGPMER QKPLKVKVKA PVVKEGPYEG PVKKPVALKV KARNLIVTES 1650
    GAPPTDLQKM VMGNTKPVEL NLDGKTVAIC CATGVFGTAY LVPRHLFAEK 1700
    YDKIMLDGRA MTDSDYRVFE FEIKVKGQDM LSDAALIVLH RGNCVRDITK 1750
    HFRDTARMKK GTPVVGVVNN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL 1800
    FAYKAATRAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLQK 1850
    MKAHVDPEPH HEGLIVDTRD VEERVHVMRK TKLAPTVAYG VFNPEFGPAA 1900
    LSNKDPRLNE GVVLDDVIFS KHKGDAKMTE EDKALFRRCA ADYASRLHSV 1950
    LGTANAPLSI YEAIKGVDGL DAMEPDTAPG LPWALQGKRR GALIDFENGT 2000
    VGPEVEAALK LMEKREYKFA CQTFLKDEIR PMEKVRAGKT RIVDVLPVEH 2050
    ILYTKMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD 2100
    VDYSAFDANH CSDAMNIMFE EVFRTDFGFH PNAEWILKTL VNTEHAYENK 2150
    RITVEGGMPS GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD 2200
    DIVVASDYDL DFEALKPHFK SLGQTITPAD KSDKGFVLGQ SITDVTFLKR 2250
    HFHMDYGTGF YKPVMASKTL EAILSFARRG TIQEKLISVA GLAVHSGPDE 2300
    YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA 2332
    Length:2,332
    Mass (Da):259,319
    Last modified:February 1, 2005 - v2
    Checksum:iFE8A553569F1A6DD
    GO
    Isoform Lb (identifier: P03306-2) [UniParc]FASTAAdd to Basket

    Also known as: P16

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

    Show »
    Length:2,304
    Mass (Da):256,019
    Checksum:i77C9C2F0CE91C454
    GO

    Sequence cautioni

    The sequence CAA25127.1 differs from that shown. Reason: Frameshift at positions 1727 and 1739.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti396 – 3961S → C in CAA24361. (PubMed:6282711)Curated
    Sequence conflicti632 – 6321P → L in CAA24361. (PubMed:6282711)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform Lb. CuratedVSP_018979Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00429 Genomic RNA. Translation: CAA25127.1. Frameshift.
    V01130 Genomic RNA. Translation: CAA24361.1.
    PIRiA93508. GNNY2F.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00429 Genomic RNA. Translation: CAA25127.1 . Frameshift.
    V01130 Genomic RNA. Translation: CAA24361.1 .
    PIRi A93508. GNNY2F.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZBA X-ray 2.00 1 726-937 [» ]
    2 287-504 [» ]
    3 505-725 [» ]
    4 202-286 [» ]
    1ZBE X-ray 3.00 1 726-937 [» ]
    2 287-504 [» ]
    3 505-725 [» ]
    4 202-286 [» ]
    2BHG X-ray 1.90 A/B 1650-1855 [» ]
    2J92 X-ray 2.20 A/B 1649-1855 [» ]
    2WV4 X-ray 2.50 A/B 1650-1862 [» ]
    C/D 931-940 [» ]
    2WV5 X-ray 2.70 A/B/C/D 1650-1862 [» ]
    E/F/G/H 936-940 [» ]
    ProteinModelPortali P03306.
    SMRi P03306. 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...

    Miscellaneous databases

    EvolutionaryTracei P03306.

    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 complete nucleotide sequence of the RNA coding for the primary translation product of foot and mouth disease virus."
      Carroll A.R., Rowlands D.J., Clarke B.E.
      Nucleic Acids Res. 12:2461-2472(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "The nucleotide sequence of cDNA coding for the structural proteins of foot-and-mouth disease virus."
      Boothroyd J.C., Harris T.J.R., Rowlands D.J., Lowe P.A.
      Gene 17:153-161(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 115-1048.
    3. "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_FMDV1
    AccessioniPrimary (citable) accession number: P03306
    Secondary accession number(s): Q64768
    , Q84750, Q84751, Q84752, Q84753, Q84754, Q84760, Q84761, Q84762, Q84763, Q84764, Q84765, Q84766, Q84767, Q84768, Q84769, Q89824
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 151 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