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Entry version 85 (18 Sep 2019)
Sequence version 1 (05 May 2009)
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Protein

Genome polyprotein

Gene
N/A
Organism
Saffold virus (SafV) (Human TMEV-like virus-Saffold)
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 protein: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (Probable). Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).By similarity1 Publication
Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.1 Publication
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.1 Publication
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.1 Publication
Capsid protein VP4: Lies on the inner surface of the capsid shell (PubMed:27279624). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). 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 similarity1 Publication
Capsid protein VP0: VP0 precursor is a component of immature procapsids.By similarity
Protein 2A: Involved in host translation shutoff by inhibiting cap-dependent mRNA translation (By similarity). Nuclear localization is required for this function (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). Inhibits the phosphorylation of the leader protein (PubMed:25210192).By similarity1 Publication
Protein 2B: Affects membrane integrity and causes an increase in membrane permeability.By similarity
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes (By similarity). It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).By similarity
Protein 3A: Serves as membrane anchor via its hydrophobic domain.By similarity
VpG: Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains.By similarity
Protease 3C: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease. Cleaves host PABP1, this cleavage is important for viral replication (By similarity).By similarity
RNA-directed RNA polymerase: Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity). Performs VPg uridylylation (By similarity).By similarity

<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

  • 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 sitei1672For protease 3C activityPROSITE-ProRule annotation1
Active sitei1706For protease 3C activityPROSITE-ProRule annotation1
Active sitei1785For protease 3C activityPROSITE-ProRule annotation1
Active sitei2069For RdRp activityBy similarity1
Active sitei2167For 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 specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri3 – 14By similarityAdd BLAST12
<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 bindingi1307 – 1314ATPPROSITE-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 processHost-virus interaction, Ion transport, Transport, Viral attachment to host cell, Viral RNA replication, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

<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 13 chains:
Leader protein
Short name:
L
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Rho
Virion protein 4
Alternative name(s):
Beta
P1B
Virion protein 2
Alternative name(s):
Gamma
P1C
Virion protein 3
Alternative name(s):
Alpha
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.4.13)
Short name:
P2C
Protein 3A
Short name:
P3A
VPg
Short name:
P3B
Alternative name(s):
Protein 3B
Protease 3C (EC:3.4.22.28By similarity)
Short name:
P3C
Alternative name(s):
Picornain 3C
p22
RNA-directed RNA polymerase (EC:2.7.7.48PROSITE-ProRule annotation)
Short name:
RdRp
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
<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>OrganismiSaffold virus (SafV) (Human TMEV-like virus-Saffold)
<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 identifieri434309 [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 lineageiVirusesRiboviriaPicornaviralesPicornaviridaeCardiovirus
<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 hostiHomo sapiens (Human) [TaxID: 9606]
<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
  • UP000174252 <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

Capsid protein VP2 :
Capsid protein VP3 :
Capsid protein VP1 :
Protein 2A :
Protein 2B :
Protein 2C :
Protein 3A :
VPg :
RNA-directed RNA polymerase :

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, 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_00004462061 – 2295Genome polyproteinAdd BLAST2295
ChainiPRO_00004462071 – 71Leader proteinAdd BLAST71
ChainiPRO_000044620872 – 414Capsid protein VP0Add BLAST343
ChainiPRO_000044620972 – 143Capsid protein VP4Add BLAST72
ChainiPRO_0000446210144 – 414Capsid protein VP2Add BLAST271
ChainiPRO_0000446211415 – 646Capsid protein VP3Add BLAST232
ChainiPRO_0000446212647 – 917Capsid protein VP1Add BLAST271
ChainiPRO_0000446213918 – 1050Protein 2AAdd BLAST133
ChainiPRO_00004462141051 – 1186Protein 2BAdd BLAST136
ChainiPRO_00004462151187 – 1511Protein 2CAdd BLAST325
ChainiPRO_00004462161512 – 1597Protein 3AAdd BLAST86
ChainiPRO_00004462171598 – 1617VPgAdd BLAST20
ChainiPRO_00004462181618 – 1834Protease 3CAdd BLAST217
ChainiPRO_00004462191835 – 2295RNA-directed RNA polymeraseAdd BLAST461

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>Lipidationi72N-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 bondi501 ↔ 5031 Publication
<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 residuei1600O-(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

Leader protein: Phosphorylated.By similarity
Genome polyprotein: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). 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 (By similarity). This process would release the P1-2A peptide from the translational complex (By similarity).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 is followed by a conformational change of the particle.By similarity
VPg: Uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase.By similarity
Capsid protein VP4: Myristoylation 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>Sitei143 – 144CleavageSequence analysis2
Sitei414 – 415Cleavage; by protease 3CBy similarity2
Sitei646 – 647Cleavage; by protease 3CBy similarity2
Sitei917 – 918Cleavage; by protease 3CBy similarity2
Sitei1050 – 1051Cleavage; by ribosomal skipBy similarity2
Sitei1186 – 1187Cleavage; by protease 3CBy similarity2
Sitei1511 – 1512Cleavage; by protease 3CBy similarity2
Sitei1597 – 1598Cleavage; by protease 3CBy similarity2
Sitei1617 – 1618Cleavage; by protease 3CBy similarity2
Sitei1834 – 1835Cleavage; by protease 3CBy similarity2

Keywords - PTMi

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

<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

Protein 2A:

Interacts with host EIF4E (By similarity). Leader protein:

Interacts with host RAN; the complex L-RAN recruits cellular kinases responsible for the L-induced nucleocytoplasmic trafficking inhibition (By similarity). The complex L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS (By similarity). Leader protein:

Interacts with the protein 2A (PubMed:25210192). Protein 2A:

Interacts with the leader protein (PubMed:25210192). Leader protein:

Interacts with host RNASEL; this interaction prevents RNASEL activation by its substrate 2'-5' oligoadenylates (By similarity).

By similarity1 Publication

<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

12295
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
C0MHL9

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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>Domaini1278 – 1443SF3 helicasePROSITE-ProRule annotationAdd BLAST166
Domaini1628 – 1821Peptidase C3PROSITE-ProRule annotationAdd BLAST194
Domaini2063 – 2181RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni30 – 46AcidicCuratedAdd BLAST17
Regioni55 – 68TheiloBy similarityAdd BLAST14
Regioni1036 – 1042Host EIF4E bindingBy similarity7

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Leader protein: The Theilo and zinc-finger regions may both play a role in the inhibition of host nucleocytoplasmic trafficking and IRF-3 dimerization antagonism by the L protein.By similarity

<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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri3 – 14By similarityAdd BLAST12

Keywords - Domaini

Coiled coil, Zinc-finger

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
IPR004004 Helic/Pol/Pept_Calicivir-typ
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR014759 Helicase_SF3_ssRNA_vir
IPR027417 P-loop_NTPase
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
PF00548 Peptidase_C3, 1 hit
PF00680 RdRP_1, 1 hit
PF00073 Rhv, 2 hits
PF00910 RNA_helicase, 1 hit
PF08935 VP4_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00918 CALICVIRUSNS

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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>Sequencei

<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.

C0MHL9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MACKHGYPLL CPLCTALDIT PDGSFTLLFD NEWYPTDLLT VNLDDDVFYP
60 70 80 90 100
LDTNMDWTDL PLIQDIVMEP QGNSNSSDKN NSQSSGNEGV IINNYYSNQY
110 120 130 140 150
QNSIDLSANA NGVGKENSKP QGQLMNILGS AADAFKNIAP LLMDQNTEEM
160 170 180 190 200
TNLSDRVSSD TAGNTATNTQ STVGRLFGFG QRHKGKHPAS CADTATDKVL
210 220 230 240 250
AAERYYTIKL ASWTKTQESF DHIRVPLPHA LAGENGGVFS STLRRHYLCK
260 270 280 290 300
CGWRIQVQCN ASQFHAGSLL VFMAPEFDTS NHSTEVEPRA DTAFKVDANW
310 320 330 340 350
QKHAQILTGH AYVNTTTKVN VPLALNHQNF WQWTTYPHQI LNLRTNTTCD
360 370 380 390 400
LEVPYVNVCP TSSWTQHANW TLVIAVLTPL QYSQGSATTI EITASIQPVK
410 420 430 440 450
PVFNGLRHTV VNPQSPFPVT VREHAGTFFS TTPDTTVPVY GNTISTPFDY
460 470 480 490 500
MCGEFTDLLS LCKIPTFLGN LDSNKKRIPY FSATNSTPAT PLVTYQVTLS
510 520 530 540 550
CSCMANSMLA AVARNFNQYR GSLNYLFVFT GSAMTKGKFL ISYTPPGAGE
560 570 580 590 600
PKTLDQAMQA TYAIWDLGLN SSYNFTVPFI SPTHYRQTSY NTPTITSVDG
610 620 630 640 650
WLTVWQLTPL TYPLGVPNDS HILTLVSGGD DFTLRMPVTF TKYVPQGVDN
660 670 680 690 700
AEKGKVSDDN ASTDFVAEPV KLPENQTRVS FVYDRSTLSS VLQSTSDVSS
710 720 730 740 750
KFTPSTAKNL QNSILLTPLP SDIVNNSVLP EQERWISFAS PTTQKPPYKT
760 770 780 790 800
KQDWNFIMFS PFTYYKCDLE VTLSKNDRET ISSVVRYVPC GAPSDLSDQT
810 820 830 840 850
MPQTPSLADT RDPHMWVVGQ GTTNQISFVI PYTSPLSVLP SVWFNGFSNF
860 870 880 890 900
DNSSRFGVAP NADFGRLLLQ GQGTFSVHYR YKKMRVFCPR PTVFIPWPNP
910 920 930 940 950
QDTKIKSVRP TPTLELQNPI SIYRVDLFIN FSDEIIQFTY KVHGRTVCQY
960 970 980 990 1000
EIPGFGLSRS GRLLVCMGEK PCQLPISTPK CFYHIVFTGS RNSFGVSIYK
1010 1020 1030 1040 1050
ARYRPWKQPL HDELHDYGFS TFTDFFKAVR DYHASYYKQR LQHDIETNPG
1060 1070 1080 1090 1100
PVQSVFQLQG GVLTKSQAPM SGLQSMLLRA IGIEADCTEF TRAVNLITDL
1110 1120 1130 1140 1150
CNTWESAKTT LSSPEFWTKM VMRIVKMFAA SVLYLHNPDL TTTVCLSLMA
1160 1170 1180 1190 1200
GIDILTNDSV FNWLSTKLSK FFHTPAPPIV PLLQQQSPIR EANDSFNLAK
1210 1220 1230 1240 1250
NIEWAIKTIK RIVEWITSWF KQEETSPQAK LDKMLTDFPE HCNSILAMRN
1260 1270 1280 1290 1300
GRKAYTDCAS AFKYFEQLYN LAVQCKRIPL ATLCEKFKNK HDHAVARPEP
1310 1320 1330 1340 1350
VVVVLRGNAG QGKSVTSQII AQAVSKLSFG RQSVYSLPPD SDYLDGYENQ
1360 1370 1380 1390 1400
YSVIMDDLGQ NPDGEDFKVF CQMVSSTNFL PNMAHLEKKG TPFTSNFIIA
1410 1420 1430 1440 1450
TTNLPKFRPV TVAHYPAVDR RITFDLTVEA GDECVTHNGM LDVEKAFEEI
1460 1470 1480 1490 1500
PGKPQLDCFN TDCRLLHKRG VRFVCNRTKN IYNLQQVVKM VKSTIDNKVE
1510 1520 1530 1540 1550
NLKKMNTLVA QSPGNDMDYV LTCLRQTNAA LQDQIDELQE AFNQAQERQN
1560 1570 1580 1590 1600
FLSDWLKVSA IVFASIASLS AVCKLVSRFK NLVCPAPVQI QLSEGEQAAY
1610 1620 1630 1640 1650
SGGKKGEKQT LQVLDVQGGG KIVAQAGNPV MDYEVNIAKN MVNPITFFYA
1660 1670 1680 1690 1700
DKAQVTQSCL LIKGHLFVVN RHVAETDWCA FELKGTRHER DSVQMRSVNK
1710 1720 1730 1740 1750
SGMEVDLTFV KVVKGPLFKD NSKKFCSKDD DFPARNETVT GIMNTGVPFV
1760 1770 1780 1790 1800
FTGKFLIGNQ PVNTTTGACF NHCIHYRATT HRGWCGSALI CHVNGKKAVY
1810 1820 1830 1840 1850
AMHSAGGGGM AAATIITQEM IEAAEKALDC LTPQGAIVEI GIDTVVHVPR
1860 1870 1880 1890 1900
KTKLRRTVAH PCFQPKFEPA VLSRYDPRTT KDVDQVAFSK HTTNLEELPS
1910 1920 1930 1940 1950
VFSMVAREYA TRVFTTIGKE NKILTPEQAI LGLPGMDPME KDTSPGLPYT
1960 1970 1980 1990 2000
QQGLKRAQLV NFEQGTMVQN LKEAHTKLTE GNYEDILYQS FLKDEIRPIE
2010 2020 2030 2040 2050
KIHEAKTRIV DVPPFHHCIW GRQLLGRFAS RFQTNPGLDL GSAIGTDPDT
2060 2070 2080 2090 2100
DWTAFAFQLL QYKYVYDVDY SNFDASHSTA MFEVLIENFF TTENGFDERI
2110 2120 2130 2140 2150
GDYLRSLAVS RHAFEERRVL VRGGLPSGCA ATSMLNTIIN NIVIRAALHL
2160 2170 2180 2190 2200
TYSNFEFDDI KVLSYGDDLL IATNYQINFN LVKQRLAPFN YKITPANKTV
2210 2220 2230 2240 2250
EFPEISNLYE VTFLKRKFVR YNSCLFKPQM DTENLKAMVS YCRPGTLKEK
2260 2270 2280 2290
LNSIALLAVH SGKSVYDEIF DPFRRIGIII PEHGTMLYRW LNLFR
Length:2,295
Mass (Da):257,300
Last modified:May 5, 2009 - v1
<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:i508AA51941DD7718
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
FM207487 Genomic RNA Translation: CAR62533.1

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM207487 Genomic RNA Translation: CAR62533.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5A8Felectron microscopy10.60A680-898[»]
C154-411[»]
5CFCX-ray2.50A647-898[»]
C154-411[»]
5CFDX-ray2.50A647-898[»]
B415-646[»]
C154-411[»]
SMRiC0MHL9
ModBaseiSearch...
PDBe-KBiSearch...

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
IPR004004 Helic/Pol/Pept_Calicivir-typ
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR014759 Helicase_SF3_ssRNA_vir
IPR027417 P-loop_NTPase
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
PF00548 Peptidase_C3, 1 hit
PF00680 RdRP_1, 1 hit
PF00073 Rhv, 2 hits
PF00910 RNA_helicase, 1 hit
PF08935 VP4_2, 1 hit
PRINTSiPR00918 CALICVIRUSNS
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51874 PCV_3C_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51218 SF3_HELICASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_SAFV
<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: C0MHL9
<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: January 16, 2019
Last sequence update: May 5, 2009
Last modified: September 18, 2019
This is version 85 of the entry and version 1 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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