Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P12915

- POLG_BOVEV

UniProt

P12915 - POLG_BOVEV

Protein

Genome polyprotein

Gene
N/A
Organism
Bovine enterovirus (strain VG-5-27) (BEV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks By similarity.By similarity
    Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome By similarity.By similarity
    Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome By similarity.By similarity
    Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks By similarity.By similarity
    Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step By similarity.By similarity
    Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores By similarity.By similarity
    Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication By similarity.By similarity
    Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 By similarity.By similarity
    Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity By similarity.By similarity
    Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface By similarity.By similarity
    Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication By similarity.By similarity
    Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity By similarity.By similarity
    Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 By similarity.By similarity
    RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated By similarity.PROSITE-ProRule annotation

    Catalytic activityi

    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
    Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
    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.
    NTP + H2O = NDP + phosphate.

    Enzyme regulationi

    RNA-directed RNA polymerase: replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei317 – 3182Cleavage; by Protease 3CSequence Analysis
    Sitei840 – 8412Cleavage; by Protease 2ASequence Analysis
    Active sitei861 – 8611For Protease 2A activityBy similarity
    Active sitei879 – 8791For Protease 2A activityBy similarity
    Active sitei950 – 9501For Protease 2A activityBy similarity
    Sitei990 – 9912Cleavage; by Protease 3CSequence Analysis
    Sitei1419 – 14202Cleavage; by Protease 3CSequence Analysis
    Sitei1508 – 15092Cleavage; by Protease 3CSequence Analysis
    Sitei1531 – 15322Cleavage; by Protease 3CSequence Analysis
    Active sitei1571 – 15711For Protease 3C activitySequence Analysis
    Active sitei1602 – 16021For Protease 3C activitySequence Analysis
    Active sitei1678 – 16781For Protease 3C activitySequence Analysis
    Sitei1714 – 17152Cleavage; by Protease 3CSequence Analysis
    Active sitei2042 – 20421For RdRp activityBy similarity

    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. DNA replication Source: UniProtKB-KW
    2. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
    3. induction by virus of host autophagy Source: UniProtKB
    4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    5. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
    6. protein oligomerization Source: UniProtKB-KW
    7. RNA-protein covalent cross-linking Source: UniProtKB-KW
    8. suppression by virus of host gene expression Source: UniProtKB-KW
    9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
    10. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    11. suppression by virus of host translation initiation factor activity Source: UniProtKB
    12. transcription, DNA-templated Source: InterPro
    13. viral RNA genome replication Source: InterPro
    14. 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

    Activation of host autophagy by virus, DNA replication, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, Viral attachment to host cell, Viral immunoevasion, 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

    MEROPSiC03.020.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 17 chains:
    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
    Protease 2A (EC:3.4.22.29)
    Short name:
    P2A
    Alternative name(s):
    Picornain 2A
    Protein 2A
    Protein 2B
    Short name:
    P2B
    Protein 2C (EC:3.6.1.15)
    Short name:
    P2C
    Protein 3A
    Short name:
    P3A
    Alternative name(s):
    Protein 3B
    Short name:
    P3B
    Protease 3C (EC:3.4.22.28)
    Short name:
    P3C
    Alternative name(s):
    3D polymerase
    Short name:
    3Dpol
    Protein 3D
    Short name:
    3D
    OrganismiBovine enterovirus (strain VG-5-27) (BEV)
    Taxonomic identifieri12065 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirus
    Virus hostiBos taurus (Bovine) [TaxID: 9913]
    ProteomesiUP000006566: Genome

    Subcellular locationi

    Chain Capsid protein VP0 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP2 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP3 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP1 : Virion By similarity. Host cytoplasm By similarity
    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.
    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.
    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.
    Chain Protein 3AB : 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.
    Chain Protein 3CD : 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.
    Chain RNA-directed RNA polymerase : 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.

    GO - Cellular componenti

    1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    2. integral to membrane of host cell Source: UniProtKB-KW
    3. membrane Source: UniProtKB-KW
    4. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 21752174Genome polyproteinBy similarityPRO_0000426107Add
    BLAST
    Chaini2 – 840839P1By similarityPRO_0000426108Add
    BLAST
    Chaini2 – 317316Capsid protein VP0Sequence AnalysisPRO_0000426109Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426110Add
    BLAST
    Chaini70 – 317248Capsid protein VP2Sequence AnalysisPRO_0000426111Add
    BLAST
    Chaini318 – 557240Capsid protein VP3Sequence AnalysisPRO_0000426112Add
    BLAST
    Chaini557 – 840284Capsid protein VP1Sequence AnalysisPRO_0000426113Add
    BLAST
    Chaini841 – 1419579P2By similarityPRO_0000426114Add
    BLAST
    Chaini841 – 990150Protease 2ASequence AnalysisPRO_0000039463Add
    BLAST
    Chaini991 – 108999Protein 2BSequence AnalysisPRO_0000039464Add
    BLAST
    Chaini1090 – 1419330Protein 2CSequence AnalysisPRO_0000039465Add
    BLAST
    Chaini1420 – 2175756P3By similarityPRO_0000426115Add
    BLAST
    Chaini1420 – 1531112Protein 3ABSequence AnalysisPRO_0000426116Add
    BLAST
    Chaini1420 – 150889Protein 3ASequence AnalysisPRO_0000039466Add
    BLAST
    Chaini1509 – 153123Viral protein genome-linkedSequence AnalysisPRO_0000426117Add
    BLAST
    Chaini1532 – 2175644Protein 3CDSequence AnalysisPRO_0000426118Add
    BLAST
    Chaini1532 – 1713182Protease 3CSequence AnalysisPRO_0000426119Add
    BLAST
    Chaini1714 – 2175462RNA-directed RNA polymeraseBy similarityPRO_0000426120Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei1511 – 15111O-(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 By similarity.By similarity
    VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylated form acts as a nucleotide-peptide primer for the polymerase By similarity.By similarity
    Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
    Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion By similarity.By similarity
    Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.By similarity
    Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion By similarity.By similarity
    Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication By similarity.By similarity

    Keywords - PTMi

    Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    PRIDEiP12915.

    Interactioni

    Subunit structurei

    Capsid protein VP1: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid By similarity. Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid By similarity. Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid By similarity. Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 By similarity. Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis By similarity. Protein 3AB: interacts with protein 3CD By similarity. Viral protein genome-linked: interacts with RNA-directed RNA polymerase By similarity. Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD By similarity.By similarity

    Structurei

    Secondary structure

    1
    2175
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 353
    Helixi36 – 383
    Helixi51 – 544
    Beta strandi57 – 593
    Beta strandi78 – 814
    Beta strandi83 – 875
    Beta strandi90 – 967
    Helixi103 – 1053
    Turni113 – 1153
    Helixi126 – 1283
    Beta strandi147 – 1515
    Helixi153 – 1553
    Helixi159 – 1679
    Beta strandi168 – 18013
    Beta strandi187 – 19711
    Beta strandi203 – 2053
    Helixi209 – 2124
    Helixi215 – 2173
    Helixi224 – 2263
    Turni227 – 2304
    Helixi234 – 2385
    Beta strandi239 – 2457
    Turni246 – 2483
    Beta strandi250 – 2567
    Beta strandi261 – 2633
    Turni267 – 2693
    Beta strandi273 – 28917
    Beta strandi294 – 30916
    Turni325 – 3284
    Beta strandi340 – 3423
    Beta strandi356 – 3594
    Helixi361 – 3644
    Helixi382 – 3843
    Beta strandi386 – 3894
    Beta strandi397 – 4026
    Helixi410 – 4134
    Helixi415 – 4206
    Beta strandi423 – 4286
    Beta strandi430 – 4367
    Beta strandi445 – 4517
    Beta strandi453 – 4553
    Helixi461 – 4644
    Beta strandi467 – 4737
    Beta strandi475 – 4773
    Beta strandi479 – 4846
    Beta strandi489 – 4913
    Beta strandi493 – 4953
    Turni499 – 5024
    Helixi503 – 5064
    Beta strandi510 – 5178
    Beta strandi527 – 53711
    Beta strandi542 – 5465
    Helixi600 – 6023
    Helixi610 – 6134
    Helixi626 – 6283
    Helixi630 – 6345
    Beta strandi638 – 6414
    Turni647 – 6493
    Beta strandi651 – 6555
    Helixi662 – 6687
    Beta strandi671 – 68515
    Beta strandi699 – 7057
    Beta strandi714 – 7163
    Helixi718 – 7214
    Beta strandi723 – 7253
    Beta strandi727 – 7315
    Beta strandi737 – 7415
    Beta strandi746 – 7527
    Beta strandi756 – 7594
    Helixi765 – 7673
    Helixi772 – 7743
    Beta strandi778 – 7858
    Beta strandi792 – 80716
    Beta strandi818 – 8203

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BEVX-ray3.001560-840[»]
    270-317[»]
    3318-559[»]
    42-69[»]
    ProteinModelPortaliP12915.
    SMRiP12915. Positions 23-62, 74-559, 573-990, 1419-1480, 1532-2175.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12915.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 14851484CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1502 – 2175674CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1486 – 150116Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1194 – 1352159SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1532 – 1697166Peptidase C3Add
    BLAST
    Domaini1941 – 2056116RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni557 – 57418Amphipatic alpha-helixSequence AnalysisAdd
    BLAST
    Regioni1420 – 144324DisorderedBy similarityAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di2.60.120.20. 3 hits.
    4.10.80.10. 2 hits.
    InterProiIPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR014838. P3A.
    IPR000081. Peptidase_C3.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR003138. Pico_P1A.
    IPR002527. Pico_P2B.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF08727. P3A. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF02226. Pico_P1A. 1 hit.
    PF00947. Pico_P2A. 1 hit.
    PF01552. Pico_P2B. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 3 hits.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view]
    PRINTSiPR00918. CALICVIRUSNS.
    ProDomiPD001306. Peptidase_C3. 1 hit.
    PD649346. Pico_P2B. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF50494. SSF50494. 2 hits.
    SSF52540. SSF52540. 1 hit.
    SSF89043. SSF89043. 1 hit.
    PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P12915-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAQLSRNTA GSHTTGTYAT GGSTINYNNI NYYSHAASAA QNKQDFTQDP     50
    SKFTQPIADV IKETAVPLKS PSAEACGYSD RVAQLTLGNS TITTQEAANI 100
    CVAYGCWPAK LSDTDATSVD KPTEPGVSAD AFYTLRSKPW QADSKGWYWK 150
    LPDALNNTGM FGQNAQFHYI YRGGWAVHVQ CNATKFHQGT LLVLAIPEHQ 200
    IATQEQPAFD RTMPGSEGGT FQEPFWLEDG TSLGNSLIYP HQWINLRTNN 250
    SATLILPYVN AIPMDSAIRH SNWTLAIIPV APLKYAAETT PLVPITVTIA 300
    PMETEYNGLR RAIASNQGLP TKPGPGSYQF MTTDEDCSPC ILPDFQPTLE 350
    IFIPGKVNNL LEIAQVESIL EANNREGVEG VERYVIPVSV QDALDAQIYA 400
    LRLELGGSGP LSSSLLGTLA KHYTQWSGSV EITCMFTGTF MTTGKVLLAY 450
    TPPGGDMPRN REEAMLGTHV VWDFGLQSSI TLVIPWISAS HFRGVSNDDV 500
    LNYQYYAAGH VTIWYQTNMV IPPGFPNTAG IIMMIAAQPN FSFRIQKDRE 550
    DMTQTAILQN DPGKMLKDAI DKQVAGALVA GTTTSTHSVA TDSTPALQAA 600
    ETGATSTARD ESMIETRTIV PTHGIHETSV ESFFGRSSLV GMPLLATGTS 650
    ITNWRIDFRE FVQLRAKMSW FTYMRFDVEF TIIATSSTGQ NVTTEQHTTY 700
    QVMYVPPGAP VPSNQDSFQW QSGCNPSVFA DTDGPPAQFS VPFMSSANAY 750
    STVYDGYARF MDTDPDRYGI LPSNFLGFMY FRTLEDAAHQ VRFRICAKIK 800
    HTSCWIPRAP RQAPYKKRYN LVFSGDSDRI CSNRASLTSY GPFGQQQGAA 850
    YVGSYKILNR HLATYADWEN EVWQSYQRDL LVTRVDAHGC DTIARCNCRS 900
    GIYYCKSTAK HYPIVVTPPS IYKIEANDYY PERMQTHILL GIGFAEPGDC 950
    GGLLRCEHGV MGILTVGGGD HVGFADVRDL LWIEDDAMEQ GITDYVQQLG 1000
    NAFGAGFTAE IANYTNQLRD MLMGSDSVVE KIIRSLVRLV SALVIVVRNH 1050
    QDLITVGATL ALLGCEGSPW KWLKRKVCQI LGINMAERQS DNWMKKFTEM 1100
    CNAFRGLDWI AAKISKFIDW LKQKILPELK ERAEFVKKLK QLPLLEAQVN 1150
    TLEHSSASQE RQEQLFGNVQ YLAHHCRKNA PLYAAEAKRV YHLEKRVLGA 1200
    MQFKTKNRIE PVCALIHGSP GTGQSLATMI VGRKLAEYEG SDVYSLPPDP 1250
    DHFDGYQQQA VVVMDDLLQN PDGKDMTLFC QMVSTAPFTV PMAALEDKGK 1300
    LFTSKFVLAS TNAGQVTPPT VADYKALQRR FFFDCDIEVQ KEYKRDGVTL 1350
    DVAKATETCE DCSPANFKKC MPLICGKALQ LKSRKGDGMR YSLDTLISEL 1400
    RRESNRRYNI GNVLEALFQG PVCYKPLRIE VHEEEPAPSA ISDLLQAVDS 1450
    EEVREYCRSK GWIVEERVTE LKLERNVNRA LAVIQSVSLI AAVAGTIYIV 1500
    YRLFSGMQGP YSGIGTNYAT KKPVVRQVQT QGPLFDFGVS LLKKNIRTVK 1550
    TGAGEFTALG VYDTVVVLPR HAMPGKTIEM NGKDIEVLDA YDLNDKTDTS 1600
    LELTIVKLKM NEKFRDIRAM VPDQITDYNE AVVVVNTSYY PQLFTCVGRV 1650
    KDYGFLNLAG RPTHRVLMYE FPTKAGQCGG VVISMGKIVG VHVGGNGAQG 1700
    FAASLLRRYF TAEQGQIEYI EKSKDAGYPV INAPTQTKLE PSVFFDVFPG 1750
    VKEPAVLHKK DKRLETNFEE ALFSKYIGNV QRDMPEELLI AIDHYSEQLK 1800
    MLNIDPRPIS MEDAIYGTEG LEALDLGTSA SYPYVAMGIK KRDILNKETR 1850
    DVTKMQECID KYGLNLPMVT YVKDELRAPD KIRKGKSRLI EASSLNDSVA 1900
    MRCYFGNLYK VFHTNPGTIS GCAVGCDPET FWSKIPVMMD GELFGFDYTA 1950
    YDASLSPMWF HALAEVLRRI GFVECKHFID QLCCSHHLYM DKHYYVVGGM 2000
    PSGCSGTSIF NSMINNLIIR TLVLTVYKNI DLDDLKIIAY GDDVLASYPY 2050
    EIDASLLAEA GKSFGLIMTP PDKSAEFVKL TWDNVTFLKR KFVRDARYPF 2100
    LVHPVMDMSN IHESIRWTKD PRHTEDHVRS LCLLAWHCGE EEYNEFVTKI 2150
    RSVPVGRALH LPSFKALERK WYDSF 2175
    Length:2,175
    Mass (Da):242,504
    Last modified:January 23, 2007 - v3
    Checksum:i44FCADE8704E48FD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00214 Genomic RNA. Translation: BAA24003.1. Sequence problems.
    PIRiA29824. GNNYBE.
    RefSeqiNP_045756.1. NC_001859.1.

    Genome annotation databases

    GeneIDi1493914.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00214 Genomic RNA. Translation: BAA24003.1 . Sequence problems.
    PIRi A29824. GNNYBE.
    RefSeqi NP_045756.1. NC_001859.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BEV X-ray 3.00 1 560-840 [» ]
    2 70-317 [» ]
    3 318-559 [» ]
    4 2-69 [» ]
    ProteinModelPortali P12915.
    SMRi P12915. Positions 23-62, 74-559, 573-990, 1419-1480, 1532-2175.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.020.

    Proteomic databases

    PRIDEi P12915.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1493914.

    Miscellaneous databases

    EvolutionaryTracei P12915.

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    4.10.80.10. 2 hits.
    InterProi IPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR014838. P3A.
    IPR000081. Peptidase_C3.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR003138. Pico_P1A.
    IPR002527. Pico_P2B.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF08727. P3A. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF02226. Pico_P1A. 1 hit.
    PF00947. Pico_P2A. 1 hit.
    PF01552. Pico_P2B. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 3 hits.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view ]
    PRINTSi PR00918. CALICVIRUSNS.
    ProDomi PD001306. Peptidase_C3. 1 hit.
    PD649346. Pico_P2B. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF50494. SSF50494. 2 hits.
    SSF52540. SSF52540. 1 hit.
    SSF89043. SSF89043. 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 a bovine enterovirus."
      Earle J.A.P., Skuce R.A., Fleming C.S., Hoey E.M., Martin S.J.
      J. Gen. Virol. 69:253-263(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Implications for viral uncoating from the structure of bovine enterovirus."
      Smyth M., Tate J., Hoey E.M., Lyons C., Martin S.J., Stuart D.
      Nat. Struct. Biol. 2:224-231(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-840.

    Entry informationi

    Entry nameiPOLG_BOVEV
    AccessioniPrimary (citable) accession number: P12915
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    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