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P49303

- POLG_FMDVZ

UniProt

P49303 - POLG_FMDVZ

Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate -/Azerbaijan/A22-550/1965 serotype A) (FMDV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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
    Sitei936 – 9372Cleavage; by picornain 3CSequence Analysis
    Sitei954 – 9552Cleavage; by ribosomal skipSequence Analysis
    Sitei1108 – 11092Cleavage; by picornain 3CSequence Analysis
    Sitei1426 – 14272Cleavage; by picornain 3CSequence Analysis
    Sitei1579 – 15802Cleavage; by picornain 3CSequence Analysis
    Sitei1602 – 16032Cleavage; by picornain 3CSequence Analysis
    Sitei1626 – 16272Cleavage; by picornain 3CSequence Analysis
    Sitei1650 – 16512Cleavage; by picornain 3CSequence Analysis
    Active sitei1696 – 16961For picornain 3C activitySequence Analysis
    Active sitei1723 – 17231For picornain 3C activitySequence Analysis
    Active sitei1813 – 18131For picornain 3C activitySequence Analysis
    Sitei1863 – 18642Cleavage; by picornain 3CSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1218 – 12258ATPPROSITE-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 (isolate -/Azerbaijan/A22-550/1965 serotype A) (FMDV)
    Taxonomic identifieri73481 [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]
    ProteomesiUP000008621: 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 – 23362336Genome polyproteinPRO_0000039850Add
    BLAST
    Chaini1 – 201201Leader proteasePRO_0000039851Add
    BLAST
    Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000374075Add
    BLAST
    Chaini202 – 28685Protein VP4Sequence AnalysisPRO_0000039854Add
    BLAST
    Chaini287 – 504218Protein VP2Sequence AnalysisPRO_0000039855Add
    BLAST
    Chaini505 – 725221Protein VP3Sequence AnalysisPRO_0000039856Add
    BLAST
    Chaini726 – 936211Protein VP1Sequence AnalysisPRO_0000039857Add
    BLAST
    Chaini937 – 95418Protein 2ASequence AnalysisPRO_0000039858Add
    BLAST
    Chaini955 – 1108154Protein 2BSequence AnalysisPRO_0000039859Add
    BLAST
    Chaini1109 – 1426318Protein 2CSequence AnalysisPRO_0000039860Add
    BLAST
    Chaini1427 – 1579153Protein 3ASequence AnalysisPRO_0000039861Add
    BLAST
    Chaini1580 – 160223Protein 3B-1Sequence AnalysisPRO_0000039862Add
    BLAST
    Chaini1603 – 162624Protein 3B-2Sequence AnalysisPRO_0000039863Add
    BLAST
    Chaini1627 – 165024Protein 3B-3Sequence AnalysisPRO_0000039864Add
    BLAST
    Chaini1651 – 1863213Picornain 3CSequence AnalysisPRO_0000039865Add
    BLAST
    Chaini1864 – 2336473RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039866Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi202 – 2021N-myristoyl glycine; by hostBy similarity
    Disulfide bondi511 – 511Interchain; in VP3 dimer
    Modified residuei1582 – 15821O-(5'-phospho-RNA)-tyrosineBy similarity
    Modified residuei1605 – 16051O-(5'-phospho-RNA)-tyrosineBy similarity
    Modified residuei1629 – 16291O-(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
    2336
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi229 – 2324
    Helixi269 – 2746

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FMDX-ray3.504202-286[»]
    ProteinModelPortaliP49303.
    SMRiP49303. Positions 29-201, 216-286, 298-934, 1657-1857, 1864-2333.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 14811481CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1503 – 2336834CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1482 – 150221Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 201201Peptidase C28Add
    BLAST
    Domaini1190 – 1354165SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1653 – 1837185Peptidase C3Add
    BLAST
    Domaini2097 – 2215119RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi869 – 8713Cell 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: P49303-1) [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 LYALREIKAF LLSRTQGKME LTLYNGEKKT FYSRPNNHDN     50
    CWLNTILQLF RYVDEPFFDW VYDSPENLTC EAIRQLEEIT GLELHEGGPP 100
    ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV 150
    FACVTSDGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG EWKAKVQKRL 200
    KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
    GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 300
    LTTRNGHTTS TTQSSVGVTY GYSTQEDHVS GPNTSGLETR VVQAERFFKK 350
    YLFDWTPDKA FGHLEKLELP TDHKGVYGHL VDSFAYMRNG WDVEVSAVGN 400
    QFNGGCLLVA MVPEWKELTP REKYQLTLFP HQFISPRTNM TAHIVVPYLG 450
    VNRYDQYKKH KPWTLVVMVV SPLTTNTVSA GQIKVYANIA PTHVHVAGEL 500
    PSKEGIVPVA CSDGYGGLVT TDPKTADPVY GMVYNPPRTN YPGRFTNLLD 550
    VAEACPTFLC FDDGKPYVVT RTDEQRLLAK FDLSLAAKHM SNTYLSGIAQ 600
    YYAQYSGTIN LHFMFTGSTD SKARYMVAYV PPGVETPPDT PEKAAHCIHA 650
    EWDTGLNSKF TFSIPYVSAA DYAYTASDVA ETTNVQGWVC IYQITHGKAE 700
    QDTLVVSVSA GKDFELRLPI DPRSQTTSTG ESADPVTTTV ENYGGETQVQ 750
    RRQHTDVTFI MDRFVKIQNL NPIHVIDLMQ THQHGLVGAL LRAATYYFSD 800
    LEIVVRHDGN LTWVPNGAPE AALSNMGNPT AYPKAPFTRL ALPYTAPHRV 850
    LATVYNGTGK YSAGGMGRRG DLEPLAARVA AQLPTSFNFG AIQATTIHEL 900
    LVRMKRAELY CPRPLLAVEV SSQDRHKQKI IAPAKQLLNF DLLKLAGDVE 950
    SNPGPFFFSD VRSNFSKLVE TINQMQEDMS TKHGPDFNRL VSAFEELATG 1000
    VKAIRTGLDE AKPWYKLIKL LSRLSCMAAV AARSKDPVLV AIMLADTGLE 1050
    ILDSTFVVKK ISDSLSSLFH VPAPVFSFGA PILLAGLVKV ASSFFRSTPE 1100
    DLERAEKQLK ARDINDIFAI LKNGEWLVKL ILAIRDWIKA WIASEEKFVT 1150
    MTDLVPGILE KQRDLNDPSK YKEAKEWLDS ARQACLKNGN VHIANLCKVV 1200
    TPAPSKSRPE PVVVCLRGKS GQGKSFLANV LAQAISTHFT GRIDSVWYCP 1250
    PDPDHFDGYN QQTVVVMDDL GQNPDGKDFK YFAQMVSTTG FIPPMASLED 1300
    KGKPFNSKVI ITTTNLYSGF TPRTMVCPDA LNRRFHFDID VSAKDGYKVN 1350
    NKLDITKALE DTHTNPVAMF KYDCALLNGM AVEMKRMQQD MFKPQPPLQN 1400
    VYQLVQEVIE RVELHEKVSS HQIFKQISIP SQKSVLYFLI EKGQHEAAIE 1450
    FFEGLVHDSI KEELRPLIQQ TSFVKRAFKR LKENFEIVAL CLTLLANIVI 1500
    MIRETRKRQQ MVDDAVNEYI EKANITTDDK TLDEAEKNPL ETSGVSIVGF 1550
    RERTLPGHRA SDDVNSEPAR PVEEQPQAEG PYTGPLERQK PLKVKAKLPQ 1600
    QEGPYAGPME RQKPLKVKVK APVVKEGPYE GPVKKPVALK VKAKNLIVTE 1650
    SGAPPTDLQK MVMGNTKPVE LILDGKTVAI CCATGVFGTA YLVPRHLFAE 1700
    KYDKIMLDGR AMTDSDYRVF EFEIKVKGQD MLSDAALMVL HRGNRVRDIT 1750
    KHFRDTARMK KGTPVVGVIN NADVGRLIFS GEALTYKDIV VCMDGDTMPG 1800
    LFAYKAATKA GYCGGAVLAK DGADTFIVGT HSAGGNGVGY CSCVSRSMLL 1850
    KMKAHIDPEP HHEGLIVDTR DVEERVHVMR KTKLAPTVAH GVFNPEFGPA 1900
    ALSNKDPRLN EGVVLDEVIF SKHKGDTKMT EEDKALFRRC AADYASRLHN 1950
    VLGTANAPLS IYEAIKGVDG LDAMEPDTAP GLPWALQGKR RGTLIDFENG 2000
    TVGPEVASAL ELMEKRQYKF TCQTFLKDEV RPMEKVRAGK TRIVDVLPVE 2050
    HILYTRMMIG RFCAQMHSNN GPQIGSAVGC NPDVDWQRFG THFAQYKNVW 2100
    DVDYSAFDAN HCSDAMNIMF EEVFRTEFGF HPNAEWILKT LVNTEHAYEN 2150
    KRITVEGGMP SGCSATSIIN TILNNIYVLY ALRRHYEGVE LDTYTMISYG 2200
    DDIVVASDYD LDFEALKPHF KSLGQTITPA DKSDKGFVLG QSITDVTFLK 2250
    RHFRMDYGTG FYKPVMASKT LEAILSFARR GTIQEKLISV AGLAVHSGPD 2300
    EYRRLFEPFQ GLFEIPSYRS LYLRWVNAVC GDAQSL 2336
    Length:2,336
    Mass (Da):259,985
    Last modified:February 1, 1996 - v1
    Checksum:i15AC2AB022B5B954
    GO
    Isoform Lb (identifier: P49303-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,308
    Mass (Da):256,785
    Checksum:iFD33D0633D64D309
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti726 – 7283TTS → NTT.
    Natural varianti804 – 8041V → L.
    Natural varianti859 – 8591G → S.
    Natural varianti919 – 9191E → V.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform Lb. CuratedVSP_018981Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74812 Genomic RNA. Translation: CAA52812.1.
    M38362 Genomic RNA. Translation: AAA42664.1.
    PIRiS37077.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74812 Genomic RNA. Translation: CAA52812.1 .
    M38362 Genomic RNA. Translation: AAA42664.1 .
    PIRi S37077.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FMD X-ray 3.50 4 202-286 [» ]
    ProteinModelPortali P49303.
    SMRi P49303. Positions 29-201, 216-286, 298-934, 1657-1857, 1864-2333.
    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. "Primary structure of the DNA copy of the protein VP1 gene of the foot-and-mouth disease virus A22."
      Onishchenko A.M., Petrov N.A., Blinov V.M., Vassilenko S.K., Sandakhchiev L.S., Burdov A.N., Ivanyushchenkov V.N., Perevozchikova N.A.
      Bioorg. Khim. 12:416-419(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 702-955.

    Entry informationi

    Entry nameiPOLG_FMDVZ
    AccessioniPrimary (citable) accession number: P49303
    Secondary accession number(s): Q65094
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The capsid protein VP1 contains the main antigenic determinants of the virion; therefore, changes in its sequence must be responsible for the high antigenic variability of the virus.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