Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 94 (23 Feb 2022)
Sequence version 1 (03 Mar 2009)
Previous versions | rss
Add a publicationFeedback
Protein

Genome polyprotein

Gene
N/A
Organism
Cosavirus A (isolate Human/Pakistan/0553/-) (HCoSV-A)
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>
-Protein inferred from homologyi <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

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.

By similarity

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.

By similarity

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.

By similarity

Lies on the inner surface of the capsid shell (By similarity).

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 (By similarity).

After genome has been released, the channel shrinks (By similarity).

By similarity

VP0 precursor is a component of immature procapsids.

By similarity

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).

By similarity

Affects membrane integrity and causes an increase in membrane permeability.

By similarity

Associates with and induces structural rearrangements of intracellular membranes (By similarity).

It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).

Interacts with IFIH1/MDA5 to inhibit the induction of the IFN-beta signal pathway (By similarity).

By similarity

Serves as membrane anchor via its hydrophobic domain.

By similarity

Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains.

By similarity

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).

Cleaves host TANK and disrupts the TANK-TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the IFN-beta signal pathway (By similarity).

By similarity

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%5Fsection">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%5Fsection">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 sitei1501For protease 3C activityPROSITE-ProRule annotation1
Active sitei1535For protease 3C activityPROSITE-ProRule annotation1
Active sitei1612For protease 3C activityPROSITE-ProRule annotation1
Active sitei1899For RdRp activityBy similarity1
Active sitei1997For RdRp activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi1130 – 1137ATPPROSITE-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, 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%5Fand%5Ftaxonomy%5Fsection">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 12 chains:
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
Alternative name(s):
G
Protein 2B
Short name:
I
Short name:
P2B
Protein 2C (EC:3.6.4.13)
Short name:
C
Short name:
P2C
Protein 3A
Short name:
P3A
VPg
Short name:
P3B
Alternative name(s):
H
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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiCosavirus A (isolate Human/Pakistan/0553/-) (HCoSV-A)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri1554483 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiVirusesRiboviriaOrthornaviraePisuviricotaPisoniviricetesPicornaviralesPicornaviridaeCosavirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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
  • UP000029753 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; by hostCurated
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004461932 – 2124Genome polyproteinAdd BLAST2123
ChainiPRO_00004461942 – 333Capsid protein VP0Add BLAST332
ChainiPRO_00004461952 – 68Capsid protein VP4Add BLAST67
ChainiPRO_000044619669 – 333Capsid protein VP2Add BLAST265
ChainiPRO_0000446197334 – 568Capsid protein VP3Add BLAST235
ChainiPRO_0000446198569 – 859Capsid protein VP1Add BLAST291
ChainiPRO_0000446199860 – 889Protein 2AAdd BLAST30
ChainiPRO_0000446200890 – 1010Protein 2BAdd BLAST121
ChainiPRO_00004462011011 – 1331Protein 2CAdd BLAST321
ChainiPRO_00004462021332 – 1434Protein 3AAdd BLAST103
ChainiPRO_00004462031435 – 1458VPgAdd BLAST24
ChainiPRO_00004462041459 – 1661Protease 3CAdd BLAST203
ChainiPRO_00004462051662 – 2123RNA-directed RNA polymeraseAdd BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Lipidationi2N-myristoyl glycine; by hostBy similarity1
<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 residuei1442O-(5'-phospho-RNA)-tyrosineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

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
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
Myristoylation is required during RNA encapsidation and formation of the mature virus particle.By similarity
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

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>Sitei68 – 69Cleavage2
Sitei333 – 334Cleavage; by protease 3CBy similarity2
Sitei568 – 569Cleavage; by protease 3CBy similarity2
Sitei859 – 860Cleavage; by protease 3CBy similarity2
Sitei889 – 890Cleavage; by ribosomal skipBy similarity2
Sitei1010 – 1011Cleavage; by protease 3CBy similarity2
Sitei1331 – 1332Cleavage; by protease 3CBy similarity2
Sitei1434 – 1435Cleavage; by protease 3CBy similarity2
Sitei1458 – 1459Cleavage; by protease 3CBy similarity2
Sitei1661 – 1662Cleavage; by protease 3CBy similarity2

Keywords - PTMi

Covalent protein-RNA linkage, 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with host EIF4E (By similarity).

By similarity

Interacts with host IFIH1/MDA5; this interaction inhibits the induction of the IFN-beta signal pathway (By similarity).

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

3D structure databases

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

More...
SMRi
B8XTP8

Database of comparative protein structure models

More...
ModBasei
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%5Fand%5Fdomains%5Fsection">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>Domaini1102 – 1264SF3 helicasePROSITE-ProRule annotationAdd BLAST163
Domaini1459 – 1648Peptidase C3PROSITE-ProRule annotationAdd BLAST190
Domaini1893 – 2011RdRp 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>Regioni873 – 880Host EIF4E bindingBy similarity8
Regioni1415 – 1446DisorderedSequence analysisAdd BLAST32

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1415 – 1437Basic and acidic residuesSequence analysisAdd BLAST23

<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, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.10.10, 2 hits
2.60.120.20, 3 hits
3.30.70.270, 2 hits
4.10.90.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR037080, Capsid_VP4_sf_Picornavirus
IPR043502, DNA/RNA_pol_sf
IPR004004, Helic/Pol/Pept_Calicivir-typ
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
IPR044067, PCV_3C_PRO
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001676, Picornavirus_capsid
IPR043128, Rev_trsase/Diguanyl_cyclase
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

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
SSF56672, SSF56672, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

B8XTP8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGANNSKESV SSNGNEGTIV NNFYSNQYYA SIDASAQGVG TSTTPENGNV
60 70 80 90 100
SGFLGLAGSA FNALSLLASP RTETGMMMED RVLSRTAGNT SVNSQAAEGV
110 120 130 140 150
LQAYGTETDS NSPTSCGDDP SKGTHATDRA FVIQLLPWKQ TTNSYFAQWV
160 170 180 190 200
RLTQKLSNNL HGNVMAKNIK SHAFAKMGFE VMLQANTSPF HNGILGLFLV
210 220 230 240 250
PEFVRKGEIT DEWIDLTPTS SLVSNTELYN PQTYANFPFD AKHSFDYSDI
260 270 280 290 300
TPEQFMIFPH QLINPKDTNV ATVRVPYINI APTNDTTVHT VWTAVVMVLV
310 320 330 340 350
PLNFSSGASP TVSLTLTITP INSVFNGLHH TAQGPIPVRP FHNFQQFSTT
360 370 380 390 400
VPLRTEPCYG MTVTPPVDYM PLPITDLVEL AKVPSFVTVA NSDTTSERSF
410 420 430 440 450
PYFSVSNTEQ GRNLFKSSVV LSDLHYQHTL VANLARYFCN YRGSLQFDFI
460 470 480 490 500
AATTAMTRGK LLISYTPPGA GEPQSIDQAM MGTYAIWDLG LQSTFNFVVP
510 520 530 540 550
FISASDFRFN TSSVSNALNS DGWITVWLMN PLTYPPSTPP TQQILMLMSA
560 570 580 590 600
GSDFSYRLPI SPGFAEGETS EHPMDNAECG KIDDKDAGMF SGHSVGLPTP
610 620 630 640 650
HTSTSFFYDR YRFVGIVKSV VNNTPKPVNI YDDTGKVKNL QQVFPTSDTL
660 670 680 690 700
LPHSLMSLSP CASVCGQPIS SFLFAQRANP KKTLKLRSGD EFLYRCCPFS
710 720 730 740 750
YIKCDLEFTV VPPANSTRDY IVHWYPPGAT LDAGEVAVGN TSGSNGFDDN
760 770 780 790 800
GMNAGSSLFS YNPTFHARAP SKVSAVIPFC LPVSLLPLYF DGFPDYSTTK
810 820 830 840 850
GMYGCSPSFS FGTIYIESGL QETYSVYIRY KDFKGYAPRP LIRTPHIRLS
860 870 880 890 900
ERARYIMADS VLPRPLTRAE RDVARDLLLI AGDIESNPGP AFNPEYTAHG
910 920 930 940 950
PVTELIQLAR KPETVDNVNR LLTTLNTLMA KWNNLKDTVT DAVFLRDMVC
960 970 980 990 1000
LLVKLTSLMY LVHGQGPGAY FAAASILLAD GITFFDWYEK IKIFMARKLR
1010 1020 1030 1040 1050
VSPPFFPAAQ GPDLRDFVTF FNAARGAQWM IDSLKSLITC IKQWLELEEE
1060 1070 1080 1090 1100
NEAVQLEKML IDSPRHCKAI NDYNRGDSFQ RPTNSFEFMD RLVECATKLG
1110 1120 1130 1140 1150
KVQIATYFRN FTTADSDTSR PEPVVVVLRG KPGVGKSAAA TVMAAAVSKL
1160 1170 1180 1190 1200
LVGSQSVYTL SPDTEHMDGY HGQFVTLMDD LGQNPDGEDF RCFCQMVSCA
1210 1220 1230 1240 1250
QYRPAMADLK DKGILFTSRL LIATTNLPDF NPVTISDPRA LDRRITFDIL
1260 1270 1280 1290 1300
VTPGSAATKN GKLDLAAALK PDGPGEHPYT SDCPILHTTG LLLKNLRNNQ
1310 1320 1330 1340 1350
TMNLKDLVDM IVKRIKHKKE VGNMLDSLVA QGPTMIVGYT KDDDGIAIVD
1360 1370 1380 1390 1400
CLEEWNKIKD KKKKQLALEM VAQELKDKHE EHKGTIKLLK MFVTGLGVVA
1410 1420 1430 1440 1450
AVAGAYATMK YFTKDKPKEE EEEPEEKKEK KTEESKEAAG PYNGPTKKEI
1460 1470 1480 1490 1500
KTLKLKAQSP LMDMEKKIAQ NVMPFQIFYN GKRYTQSCLA IGKRVILVNK
1510 1520 1530 1540 1550
HAFESVEHKF VVDQKEYTLD QVTAISLDCG SGVTDVCAVC LPPGPDFKSI
1560 1570 1580 1590 1600
KKHFLPFNTT MFPGTRLTIL SNDHYPMSRE GSFLRFEDEV PTNVGNMPFV
1610 1620 1630 1640 1650
MLYKSTSYFG MCGSVVCSRF VDGGGIIGMH CAGGGGVSVG TRLTARMIES
1660 1670 1680 1690 1700
VFDYFYPPVA QGIIENTETG PRVHVPRTSK LKRTNATYPA TEKYGPAALS
1710 1720 1730 1740 1750
RYDPRLNEGV NLDEVIFSKH TQNTLVEKGS TFRSALDMAA EIYGEKFRGN
1760 1770 1780 1790 1800
DFSPLSVEDA ILGIPGLDRL DPNTASGLPY TKTRRQMIDF NTGQILDDTL
1810 1820 1830 1840 1850
KCRLGQWLAG RPPQEVHYQT FLKDEIRPIE KVKAGKTRII DVPPLDHVIA
1860 1870 1880 1890 1900
FRMLFGRFIA HYHLNFGFKT GSAIGCDPDV AWASFGFELS GFPYLYDFDY
1910 1920 1930 1940 1950
SNFDASHSTS IFEILEQKFF SPELGFDPRC SLLLKSLAVS THCYENKRLQ
1960 1970 1980 1990 2000
IAGGLPSGTA GTSVLNTVIN NIIFHGALYH TYTNFERDDI SMLAYGDDIV
2010 2020 2030 2040 2050
VASKFELDLV MVKAFMNRIG YKITPADKSD EFRPKCMDDI CFLKRRFVKV
2060 2070 2080 2090 2100
AGVWAPVMET ENLEAMLSWY KPGTLNEKLQ SVSRLAHFSG RDVYDHLFKP
2110 2120
FIRDGFDVTP WKQLHLEWLN KLSA
Length:2,124
Mass (Da):235,743
Last modified:March 3, 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:i3CCC63E880276B6F
GO

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
FJ438902 Genomic RNA Translation: ACL15185.1

NCBI Reference Sequences

More...
RefSeqi
YP_002956074.1, NC_012800.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7986820

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:7986820

<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
FJ438902 Genomic RNA Translation: ACL15185.1
RefSeqiYP_002956074.1, NC_012800.1

3D structure databases

SMRiB8XTP8
ModBaseiSearch...

Genome annotation databases

GeneIDi7986820
KEGGivg:7986820

Family and domain databases

CDDicd00205, rhv_like, 2 hits
Gene3Di2.40.10.10, 2 hits
2.60.120.20, 3 hits
3.30.70.270, 2 hits
4.10.90.10, 1 hit
InterProiView protein in InterPro
IPR037080, Capsid_VP4_sf_Picornavirus
IPR043502, DNA/RNA_pol_sf
IPR004004, Helic/Pol/Pept_Calicivir-typ
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
IPR044067, PCV_3C_PRO
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001676, Picornavirus_capsid
IPR043128, Rev_trsase/Diguanyl_cyclase
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
PRINTSiPR00918, CALICVIRUSNS
SUPFAMiSSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS51874, PCV_3C_PRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51218, SF3_HELICASE_2, 1 hit

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_COSAA
<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: B8XTP8
<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%5Fand%5Fisoforms">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: March 3, 2009
Last modified: February 23, 2022
This is version 94 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again