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P15072

- POLG_FMDVT

UniProt

P15072 - POLG_FMDVT

Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate -/Germany/C1Oberbayen/1960 serotype C) (FMDV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (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 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
    Protein VP0: VP0 precursor is a component of immature procapsids.By similarity

    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
    Sitei930 – 9312Cleavage; by picornain 3CSequence Analysis
    Sitei948 – 9492Cleavage; by ribosomal skipSequence Analysis
    Sitei1102 – 11032Cleavage; by picornain 3CSequence Analysis
    Sitei1420 – 14212Cleavage; by picornain 3CSequence Analysis
    Sitei1573 – 15742Cleavage; by picornain 3CSequence Analysis
    Sitei1596 – 15972Cleavage; by picornain 3CSequence Analysis
    Sitei1620 – 16212Cleavage; by picornain 3CSequence Analysis
    Sitei1644 – 16452Cleavage; by picornain 3CSequence Analysis
    Active sitei1690 – 16901For picornain 3C activitySequence Analysis
    Active sitei1717 – 17171For picornain 3C activitySequence Analysis
    Active sitei1807 – 18071For picornain 3C activitySequence Analysis
    Sitei1857 – 18582Cleavage; by picornain 3CSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1212 – 12198ATPPROSITE-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 8 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
    OrganismiFoot-and-mouth disease virus (isolate -/Germany/C1Oberbayen/1960 serotype C) (FMDV)
    Taxonomic identifieri12121 [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]
    ProteomesiUP000012671: 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 – 23272327Genome polyproteinBy similarityPRO_0000039891Add
    BLAST
    Chaini1 – 201201Leader proteasePRO_0000039892Add
    BLAST
    Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000374077Add
    BLAST
    Chaini202 – 28685Protein VP4Sequence AnalysisPRO_0000039895Add
    BLAST
    Chaini287 – 504218Protein VP2Sequence AnalysisPRO_0000039896Add
    BLAST
    Chaini505 – 723219Protein VP3Sequence AnalysisPRO_0000039897Add
    BLAST
    Chaini724 – 930207Protein VP1Sequence AnalysisPRO_0000039898Add
    BLAST
    Chaini931 – 94818Protein 2ASequence AnalysisPRO_0000039899Add
    BLAST
    Chaini949 – 1102154Protein 2BSequence AnalysisPRO_0000310980Add
    BLAST
    Chaini1103 – 1420318Protein 2CSequence AnalysisPRO_0000422519Add
    BLAST
    Chaini1421 – 1573153Protein 3ASequence AnalysisPRO_0000422520Add
    BLAST
    Chaini1574 – 159623Protein 3B-1Sequence AnalysisPRO_0000422521Add
    BLAST
    Chaini1597 – 162024Protein 3B-2Sequence AnalysisPRO_0000422522Add
    BLAST
    Chaini1621 – 164424Protein 3B-3Sequence AnalysisPRO_0000422523Add
    BLAST
    Chaini1645 – 1857213Picornain 3CSequence AnalysisPRO_0000422524Add
    BLAST
    Chaini1858 – 2327470RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000422525Add
    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 residuei1576 – 15761O-(5'-phospho-RNA)-tyrosineBy similarity
    Modified residuei1599 – 15991O-(5'-phospho-RNA)-tyrosineBy similarity
    Modified residuei1623 – 16231O-(5'-phospho-RNA)-tyrosineBy similarity

    Post-translational modificationi

    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
    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

    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
    2327
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi291 – 2933
    Beta strandi302 – 3054
    Beta strandi308 – 3114
    Helixi332 – 3343
    Turni342 – 3443
    Beta strandi348 – 3558
    Beta strandi364 – 3729
    Helixi375 – 3839
    Beta strandi384 – 39815
    Beta strandi404 – 41310
    Helixi421 – 4233
    Beta strandi429 – 4346
    Turni436 – 4383
    Beta strandi440 – 4467
    Beta strandi450 – 4556
    Helixi457 – 4593
    Beta strandi463 – 47412
    Turni476 – 4783
    Beta strandi483 – 49917
    Helixi548 – 5547
    Beta strandi561 – 5633
    Beta strandi571 – 5744
    Beta strandi576 – 5816
    Turni587 – 5915
    Helixi593 – 5986
    Beta strandi601 – 6055
    Beta strandi608 – 6147
    Beta strandi621 – 6299
    Beta strandi631 – 6333
    Helixi639 – 6424
    Beta strandi645 – 6517
    Beta strandi659 – 6624
    Beta strandi667 – 6693
    Beta strandi671 – 6744
    Beta strandi686 – 69611
    Beta strandi701 – 7088
    Beta strandi713 – 7175
    Beta strandi863 – 8653

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EJOX-ray2.30P859-873[»]
    1FMDX-ray3.502287-504[»]
    3505-723[»]
    1QGCelectron microscopy30.002287-504[»]
    3505-723[»]
    ProteinModelPortaliP15072.
    SMRiP15072. Positions 29-201, 216-930, 1651-1851, 1858-2327.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15072.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 14751475CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1497 – 2327831CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1476 – 149621Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 201201Peptidase C28Add
    BLAST
    Domaini1184 – 1348165SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1647 – 1831185Peptidase C3Add
    BLAST
    Domaini2091 – 2209119RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi864 – 8663Cell attachment site

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di2.60.120.20. 3 hits.
    4.10.90.10. 1 hit.
    InterProiIPR015031. Capsid_VP4_Picornavir.
    IPR004080. FMDV_VP1_coat.
    IPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR008739. Peptidase_C28.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF05408. Peptidase_C28. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 3 hits.
    PF00910. RNA_helicase. 1 hit.
    PF08935. VP4_2. 1 hit.
    [Graphical view]
    PRINTSiPR00918. CALICVIRUSNS.
    PR01542. FMDVP1COAT.
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform Lab (identifier: P15072-1) [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

    MNTTDCFIAV VNAIREIRAL FLPRTTGKME FTLHDGEKKV FYSRPNNHDN     50
    CWLNTILQLF RYVDEPFFDW VYNSPENLTL EAIKQLEELT GLELREGGPP 100
    ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFMKGQEHAV 150
    FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNE GWKANVQRKL 200
    KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
    GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 300
    LTTRNGHTTS TTQSSVGVTF GYATAEDSTS GPNTSGLETR VHQAERFFKM 350
    ALFDWVPSQN FGHMHKVVLP HEPKGVYGGL VKSYAYMRNG WDVEVTAVGN 400
    QFNGGCLLVA LVPEMGDISD REKYQLTLYP HQFINPRTNM TAHITVPYVG 450
    VNRYDQYKQH RPWTLVVMVV APLTTNTAGA QQIKVYANIA PTNVHVAGEL 500
    PSKEGIFPVA CSDGYGNMVT TDPKTADPAY GKVYNPPRTA LPGRFTNYLD 550
    VAEACPTFLM FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY 600
    YTQYTGTINL HFMFTGPTDA KARYMVAYVP PGMDAPDNPE EAAHCIHAEW 650
    DTGLNSKFTF SIPYISAADY AYTASHEAET TCVQGWVCVY QITHGKADAD 700
    ALVVSASAGK DFELRLPVDA RQQTTATGES ADPVTTTVEN YGGETQVQRR 750
    HHTDVAFVLD RFVKVTVSGN QHTLDVMQAH KDNIVGALLR AATYYFSDLE 800
    IAVTHTGKLT WVPNGAPVSA LDNTTNPTAY HKGPLTRLAL PYTAPHRVLA 850
    TAYTGTTTYT ASTRGDSAHL TATRARHLPT SFNFGAVKAE TITELLVRMK 900
    RAELYCPRPI LPIQPTGDRH KQPLVAPAKQ LLNFDLLKLA GDVESNPGPF 950
    FFSDVRSNFS KLVETINQMQ EDMSTKHGPD FNRLVSAFEE LASGVKAIRT 1000
    GLDEAKPWYK LIKLLSRLSC MAAVAARSKD PVLVAIMLAD TGLEILDSTF 1050
    VVKKISDSLS SLFHVPAPAF SFGAPILLAG LVKVASSFFR STPEDLERAE 1100
    KQLKARDIND IFAILKNGEW LVKLILAIRD WIKAWIASEE KFVTMTDLVP 1150
    GILEKQRDLN DPSKYKDAKE WLDNTRQACL KSGNVHIANL CKVVAPAPSK 1200
    SRPEPVVVCL RGKSGQGKSF LANVLAQAIS THLTGRTDSV WYCPPDPDHF 1250
    DGYNQQTVVV MDDLGQNPDG KDFKYFAQMV STTGFIPPMA SLEDKGKPFS 1300
    SKVIIATTNL YSGFTPKTMV CPDALNRRFH FDIDVSAKDG YKINNKLDII 1350
    KALEDTHTNP VAMFQYDCAL LNGMAVEMKR LQQDMFKPQP PLQNVYQLVQ 1400
    EVIERVELHE KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE AAIEFFEGMV 1450
    HDSIKEELRP LIQQTSFVKR AFKRLKENFE IVALCLTLLA NIVIMIRETH 1500
    KRQKMVDDAV NEYIEKANIT TDDKTLDEAE KNPLETSGAS TVGFRERTLP 1550
    GQKARDDVNS EPAQPTEEQP QAEGPYAGPL ERQRPLKVRA KLPQQEGPYA 1600
    GPMERQKPLK VKARAPVVKE GPYEGPVKKP VALKVKAKNL IVTESGAPPT 1650
    DLQKMVMGNT KPVELILDGK TVAICCATGV FGTAYLVPRH LFAEKYDKIM 1700
    LDGRALTDSD YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV RDITKHFRDV 1750
    ARMKKGTPVV GVINNADVGR LIFSGEALTY KDIVVCMDGD TMPGLFAYKA 1800
    ATKAGYCGGA VLAKDGADTF IVGTHSAGGN GVGYCSCVSR SMLLKMKAHI 1850
    DPEPHHEGLI VDTRDVEERV HVMRKTKLAP TVAHGVFNPE FGPAALSNKD 1900
    PRLNEGVVLD EVIFSKHKGD TKMSEEDKAL FRRCAADYAS RLHSVLGTAN 1950
    APLSIYEAIK GVDGLDAMEP DTAPGLPWAL QGKRRGALID FENGTVGPEV 2000
    EAALKLMEKR EYKFACQTFL KDEIRPMEKV RAGKTRIVDV LPVEHILYTR 2050
    MMIGRFCAQM HSNNGPQIGS AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA 2100
    FDANHCSDAM NIMFEEVFRT EFGFHPNAEW ILKTLVNTEH AYENKRITVE 2150
    GGMPSGCSAT SIINTILNNI YVLYALRRHY EGVELDTYTM ISYGDDIVVA 2200
    SDYDLDFEAL KPHFKSLGQT ITPADKSDKG FVLGHSITDV TFLKRHFHMD 2250
    YGTGFYKPVM ASKTLEAILS FARRGTIQEK LISVAGLAVH SGPDEYRRLF 2300
    EPFQGLFEIP SYRSLYLRWV NAVCGDA 2327
    Length:2,327
    Mass (Da):258,119
    Last modified:May 29, 2013 - v2
    Checksum:iA81AB150E79617DD
    GO
    Isoform Lb (identifier: P15072-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,299
    Mass (Da):254,985
    Checksum:iA0B0C0DD67DE5BA2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81I → T.
    Natural varianti48 – 481H → Q.
    Natural varianti307 – 3071H → Q.
    Natural varianti408 – 4092LV → QA.
    Natural varianti726 – 7261A → T.
    Natural varianti852 – 8521A → G.
    Natural varianti867 – 8671S → L.
    Natural varianti876 – 8761R → G.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform Lb. CuratedVSP_018983Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY593805 Genomic RNA. Translation: AAT01748.1.
    X00130 Genomic RNA. Translation: CAA24960.2.
    PIRiA20288. GNNYC1.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with a fab fragment of a neutralizing antibody

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY593805 Genomic RNA. Translation: AAT01748.1 .
    X00130 Genomic RNA. Translation: CAA24960.2 .
    PIRi A20288. GNNYC1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EJO X-ray 2.30 P 859-873 [» ]
    1FMD X-ray 3.50 2 287-504 [» ]
    3 505-723 [» ]
    1QGC electron microscopy 30.00 2 287-504 [» ]
    3 505-723 [» ]
    ProteinModelPortali P15072.
    SMRi P15072. Positions 29-201, 216-930, 1651-1851, 1858-2327.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.008.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P15072.

    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. "Structure of the FMDV translation initiation site and of the structural proteins."
      Beck E., Forss S., Strebel K., Cattaneo R., Feil G.
      Nucleic Acids Res. 11:7873-7885(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1011.
    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_FMDVT
    AccessioniPrimary (citable) accession number: P15072
    Secondary accession number(s): Q6PMY1
    , Q84755, Q84756, Q84757, Q84758
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: May 29, 2013
    Last modified: October 1, 2014
    This is version 124 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.

    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