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Entry version 154 (18 Sep 2019)
Sequence version 2 (29 May 2013)
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Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate -/Germany/C1Oberbayen/1960 serotype C) (FMDV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Leader protease: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Cleaves also the host translation initiation factors EIF4G1 and EIF4G3, in order to shutoff the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechanisms. Possesses a deubiquitinase activity acting on both 'Lys'-48 and 'Lys'-63-linked polyubiquitin chains. In turn, inhibits the ubiquitination and subsequent activation of key signaling molecules of type I IFN response such as host DDX58, TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by inducing a decrease in RELA mRNA levels. Cleaves a peptide bond in the C-terminus of host ISG15, resulting in the damaging of this mofidier that can no longer be attached to target proteins. Cleaves also host G3BP1 and G3BP2 in order to inhibit cytoplasmic stress granules assembly.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
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome.By similarity
Capsid protein V1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome. Mediates cell entry by attachment to an integrin receptor, usually host ITGAV/ITGB6, via a conserved arginine-glycine-aspartic acid (R-G-D) motif.By similarity
Capsid protein V3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome.By similarity
Protein 2A: Mediates self-processing of the polyprotein by a translational effect termed "ribosome skipping". Mechanistically, 2A-mediated cleavage occurs between the C-terminal glycine and the proline of the downstream protein 2B. In the case of foot-and-mouth disease virus, the 2A oligopeptide is post-translationally 'trimmed' from the C-terminus of the upstream protein 1D by 3C proteinase.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 cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.By similarity
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. Triggers host autophagy by interacting with host BECN1 and thereby promotes viral replication. Participates in viral replication and interacts with host DHX9. 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
Protein 3A: Plays important roles in virus replication, virulence and host range.By similarity
Protein 3B-1: Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.By similarity
Protein 3B-2: Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.By similarity
Protein 3B-3: Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.By similarity
Protease 3C: Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, binds to viral RNA and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease.By similarity
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. 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

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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-. EC:3.4.22.46
  • 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.PROSITE-ProRule annotation EC:3.4.22.28

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei51For leader protease activityBy similarity1
Active sitei148For leader protease activityBy similarity1
Active sitei163For leader protease activityBy similarity1
Active sitei1690For protease 3C activity; Proton donor/acceptorPROSITE-ProRule annotation1
Active sitei1728For protease 3C activityPROSITE-ProRule annotation1
Active sitei1807For protease 3C activityPROSITE-ProRule annotation1
Active sitei2195For RdRp activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1212 – 1219ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHelicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
Biological processClathrin- 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, Translation regulation, Transport, Viral attachment to host cell, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Nucleotide-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
Protease 3C (EC:3.4.22.28)
Alternative name(s):
Picornain 3C
Short name:
P3C
Protease P20B
RNA-directed RNA polymerase 3D-POL (EC:2.7.7.48)
Short name:
P3D-POL
Alternative name(s):
P56A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiFoot-and-mouth disease virus (isolate -/Germany/C1Oberbayen/1960 serotype C) (FMDV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri12121 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesRiboviriaPicornaviralesPicornaviridaeAphthovirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>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]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000012671 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Protein 2B :
Protein 2C :
Protein 3A :
RNA-directed RNA polymerase 3D-POL :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 1475CytoplasmicSequence analysisAdd BLAST1475
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1476 – 1496Sequence analysisAdd BLAST21
Topological domaini1497 – 2327CytoplasmicSequence analysisAdd BLAST831

GO - Cellular componenti

Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000398911 – 2327Genome polyproteinBy similarityAdd BLAST2327
ChainiPRO_00000398921 – 201Leader proteaseAdd BLAST201
ChainiPRO_0000374077202 – 504Protein VP0Sequence analysisAdd BLAST303
ChainiPRO_0000039895202 – 286Protein VP4Sequence analysisAdd BLAST85
ChainiPRO_0000039896287 – 504Protein VP2Sequence analysisAdd BLAST218
ChainiPRO_0000039897505 – 723Protein VP3Sequence analysisAdd BLAST219
ChainiPRO_0000039898724 – 930Protein VP1Sequence analysisAdd BLAST207
ChainiPRO_0000039899931 – 948Protein 2ASequence analysisAdd BLAST18
ChainiPRO_0000310980949 – 1102Protein 2BSequence analysisAdd BLAST154
ChainiPRO_00004225191103 – 1420Protein 2CSequence analysisAdd BLAST318
ChainiPRO_00004225201421 – 1573Protein 3ASequence analysisAdd BLAST153
ChainiPRO_00004225211574 – 1596Protein 3B-1Sequence analysisAdd BLAST23
ChainiPRO_00004225221597 – 1620Protein 3B-2Sequence analysisAdd BLAST24
ChainiPRO_00004225231621 – 1644Protein 3B-3Sequence analysisAdd BLAST24
ChainiPRO_00004225241645 – 1857Protease 3CSequence analysisAdd BLAST213
ChainiPRO_00004225251858 – 2327RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi202N-myristoyl glycine; by hostBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi511Interchain; in VP3 dimerBy similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1576O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1599O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1623O-(5'-phospho-RNA)-tyrosineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei201 – 202Cleavage; by leader proteaseSequence analysis2
Sitei286 – 287CleavageSequence analysis2
Sitei504 – 505Cleavage; by picornain 3CSequence analysis2
Sitei723 – 724Cleavage; by picornain 3CSequence analysis2
Sitei930 – 931Cleavage; by picornain 3CSequence analysis2
Sitei948 – 949Cleavage; by ribosomal skipSequence analysis2
Sitei1102 – 1103Cleavage; by picornain 3CSequence analysis2
Sitei1420 – 1421Cleavage; by picornain 3CSequence analysis2
Sitei1573 – 1574Cleavage; by picornain 3CSequence analysis2
Sitei1596 – 1597Cleavage; by picornain 3CSequence analysis2
Sitei1620 – 1621Cleavage; by picornain 3CSequence analysis2
Sitei1644 – 1645Cleavage; by picornain 3CSequence analysis2
Sitei1857 – 1858Cleavage; by picornain 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Disulfide bond, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P15072

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Leader protease:

Interacts with host ISG15. Capsid protein VP1:

Interacts (via R-G-D motif) with host ITGAV/ITGB6. Protein 2B: Forms homooligomers. Protein 2C:

Interacts with host VIM.

Interacts with host BECN1. Protein 3A:

Interacts with host DCTN3.

By similarity

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P15072

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P15072

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 201Peptidase C28Add BLAST201
Domaini1184 – 1348SF3 helicasePROSITE-ProRule annotationAdd BLAST165
Domaini1647 – 1843Peptidase C3PROSITE-ProRule annotationAdd BLAST197
Domaini2091 – 2209RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi864 – 866Cell attachment site3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00205 rhv_like, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.20, 3 hits
4.10.90.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015031 Capsid_VP4_Picornavir
IPR037080 Capsid_VP4_sf_Picornavirus
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
IPR038765 Papain-like_cys_pep_sf
IPR008739 Peptidase_C28
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR001676 Picornavirus_capsid
IPR033703 Rhv-like
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
IPR029053 Viral_coat

Pfam protein domain database

More...
Pfami
View protein in Pfam
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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00918 CALICVIRUSNS
PR01542 FMDVP1COAT

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 1 hit
SSF54001 SSF54001, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51887 APHTHOVIRUS_LPRO, 1 hit
PS51874 PCV_3C_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51218 SF3_HELICASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform Lab (identifier: P15072-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
        10         20         30         40         50
MNTTDCFIAV VNAIREIRAL FLPRTTGKME FTLHDGEKKV FYSRPNNHDN
60 70 80 90 100
CWLNTILQLF RYVDEPFFDW VYNSPENLTL EAIKQLEELT GLELREGGPP
110 120 130 140 150
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFMKGQEHAV
160 170 180 190 200
FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNE GWKANVQRKL
210 220 230 240 250
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE
260 270 280 290 300
GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
310 320 330 340 350
LTTRNGHTTS TTQSSVGVTF GYATAEDSTS GPNTSGLETR VHQAERFFKM
360 370 380 390 400
ALFDWVPSQN FGHMHKVVLP HEPKGVYGGL VKSYAYMRNG WDVEVTAVGN
410 420 430 440 450
QFNGGCLLVA LVPEMGDISD REKYQLTLYP HQFINPRTNM TAHITVPYVG
460 470 480 490 500
VNRYDQYKQH RPWTLVVMVV APLTTNTAGA QQIKVYANIA PTNVHVAGEL
510 520 530 540 550
PSKEGIFPVA CSDGYGNMVT TDPKTADPAY GKVYNPPRTA LPGRFTNYLD
560 570 580 590 600
VAEACPTFLM FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY
610 620 630 640 650
YTQYTGTINL HFMFTGPTDA KARYMVAYVP PGMDAPDNPE EAAHCIHAEW
660 670 680 690 700
DTGLNSKFTF SIPYISAADY AYTASHEAET TCVQGWVCVY QITHGKADAD
710 720 730 740 750
ALVVSASAGK DFELRLPVDA RQQTTATGES ADPVTTTVEN YGGETQVQRR
760 770 780 790 800
HHTDVAFVLD RFVKVTVSGN QHTLDVMQAH KDNIVGALLR AATYYFSDLE
810 820 830 840 850
IAVTHTGKLT WVPNGAPVSA LDNTTNPTAY HKGPLTRLAL PYTAPHRVLA
860 870 880 890 900
TAYTGTTTYT ASTRGDSAHL TATRARHLPT SFNFGAVKAE TITELLVRMK
910 920 930 940 950
RAELYCPRPI LPIQPTGDRH KQPLVAPAKQ LLNFDLLKLA GDVESNPGPF
960 970 980 990 1000
FFSDVRSNFS KLVETINQMQ EDMSTKHGPD FNRLVSAFEE LASGVKAIRT
1010 1020 1030 1040 1050
GLDEAKPWYK LIKLLSRLSC MAAVAARSKD PVLVAIMLAD TGLEILDSTF
1060 1070 1080 1090 1100
VVKKISDSLS SLFHVPAPAF SFGAPILLAG LVKVASSFFR STPEDLERAE
1110 1120 1130 1140 1150
KQLKARDIND IFAILKNGEW LVKLILAIRD WIKAWIASEE KFVTMTDLVP
1160 1170 1180 1190 1200
GILEKQRDLN DPSKYKDAKE WLDNTRQACL KSGNVHIANL CKVVAPAPSK
1210 1220 1230 1240 1250
SRPEPVVVCL RGKSGQGKSF LANVLAQAIS THLTGRTDSV WYCPPDPDHF
1260 1270 1280 1290 1300
DGYNQQTVVV MDDLGQNPDG KDFKYFAQMV STTGFIPPMA SLEDKGKPFS
1310 1320 1330 1340 1350
SKVIIATTNL YSGFTPKTMV CPDALNRRFH FDIDVSAKDG YKINNKLDII
1360 1370 1380 1390 1400
KALEDTHTNP VAMFQYDCAL LNGMAVEMKR LQQDMFKPQP PLQNVYQLVQ
1410 1420 1430 1440 1450
EVIERVELHE KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE AAIEFFEGMV
1460 1470 1480 1490 1500
HDSIKEELRP LIQQTSFVKR AFKRLKENFE IVALCLTLLA NIVIMIRETH
1510 1520 1530 1540 1550
KRQKMVDDAV NEYIEKANIT TDDKTLDEAE KNPLETSGAS TVGFRERTLP
1560 1570 1580 1590 1600
GQKARDDVNS EPAQPTEEQP QAEGPYAGPL ERQRPLKVRA KLPQQEGPYA
1610 1620 1630 1640 1650
GPMERQKPLK VKARAPVVKE GPYEGPVKKP VALKVKAKNL IVTESGAPPT
1660 1670 1680 1690 1700
DLQKMVMGNT KPVELILDGK TVAICCATGV FGTAYLVPRH LFAEKYDKIM
1710 1720 1730 1740 1750
LDGRALTDSD YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV RDITKHFRDV
1760 1770 1780 1790 1800
ARMKKGTPVV GVINNADVGR LIFSGEALTY KDIVVCMDGD TMPGLFAYKA
1810 1820 1830 1840 1850
ATKAGYCGGA VLAKDGADTF IVGTHSAGGN GVGYCSCVSR SMLLKMKAHI
1860 1870 1880 1890 1900
DPEPHHEGLI VDTRDVEERV HVMRKTKLAP TVAHGVFNPE FGPAALSNKD
1910 1920 1930 1940 1950
PRLNEGVVLD EVIFSKHKGD TKMSEEDKAL FRRCAADYAS RLHSVLGTAN
1960 1970 1980 1990 2000
APLSIYEAIK GVDGLDAMEP DTAPGLPWAL QGKRRGALID FENGTVGPEV
2010 2020 2030 2040 2050
EAALKLMEKR EYKFACQTFL KDEIRPMEKV RAGKTRIVDV LPVEHILYTR
2060 2070 2080 2090 2100
MMIGRFCAQM HSNNGPQIGS AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA
2110 2120 2130 2140 2150
FDANHCSDAM NIMFEEVFRT EFGFHPNAEW ILKTLVNTEH AYENKRITVE
2160 2170 2180 2190 2200
GGMPSGCSAT SIINTILNNI YVLYALRRHY EGVELDTYTM ISYGDDIVVA
2210 2220 2230 2240 2250
SDYDLDFEAL KPHFKSLGQT ITPADKSDKG FVLGHSITDV TFLKRHFHMD
2260 2270 2280 2290 2300
YGTGFYKPVM ASKTLEAILS FARRGTIQEK LISVAGLAVH SGPDEYRRLF
2310 2320
EPFQGLFEIP SYRSLYLRWV NAVCGDA
Length:2,327
Mass (Da):258,119
Last modified:May 29, 2013 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti8I → T. 1
Natural varianti48H → Q. 1
Natural varianti307H → Q. 1
Natural varianti408 – 409LV → QA. 2
Natural varianti726A → T. 1
Natural varianti852A → G. 1
Natural varianti867S → L. 1
Natural varianti876R → G. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0189831 – 28Missing in isoform Lb. CuratedAdd BLAST28

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY593805 Genomic RNA Translation: AAT01748.1
X00130 Genomic RNA Translation: CAA24960.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A20288 GNNYC1

Keywords - Coding sequence diversityi

Alternative initiation

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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:
EMBLi
GenBanki
DDBJi
Links Updated
AY593805 Genomic RNA Translation: AAT01748.1
X00130 Genomic RNA Translation: CAA24960.2
PIRiA20288 GNNYC1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJOX-ray2.30P859-873[»]
1FMDX-ray3.502287-504[»]
3505-723[»]
1QGCelectron microscopy30.002287-504[»]
3505-723[»]
SMRiP15072
ModBaseiSearch...

Proteomic databases

PRIDEiP15072

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P15072
Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP15072

Family and domain databases

CDDicd00205 rhv_like, 3 hits
Gene3Di2.60.120.20, 3 hits
4.10.90.10, 1 hit
InterProiView protein in InterPro
IPR015031 Capsid_VP4_Picornavir
IPR037080 Capsid_VP4_sf_Picornavirus
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
IPR038765 Papain-like_cys_pep_sf
IPR008739 Peptidase_C28
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR001676 Picornavirus_capsid
IPR033703 Rhv-like
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
IPR029053 Viral_coat
PfamiView protein in Pfam
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
PRINTSiPR00918 CALICVIRUSNS
PR01542 FMDVP1COAT
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 1 hit
SSF54001 SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS51887 APHTHOVIRUS_LPRO, 1 hit
PS51874 PCV_3C_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51218 SF3_HELICASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_FMDVT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P15072
Secondary accession number(s): Q6PMY1
, Q84755, Q84756, Q84757, Q84758
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 29, 2013
Last modified: September 18, 2019
This is version 154 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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