Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - C0LJL5 (C0LJL5_HE71)

Entry version 88 (02 Dec 2020)
Sequence version 1 (05 May 2009)
Previous versions | rss
Add a publicationFeedback
Protein

Genome polyprotein

Gene
N/A
Organism
Human enterovirus 71 (EV71) (EV-71)
Status
Unreviewed-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

Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions.ARBA annotation
Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step.UniRule annotation
Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks.UniRule annotation
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.UniRule annotation
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.UniRule annotation
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.UniRule annotation
Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step.ARBA annotation
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.ARBA annotation
Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.ARBA annotation
Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome.ARBA annotation
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.ARBA annotation
Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.ARBA annotation
Protease 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins.UniRule annotation
Protease 3C: Major viral protease that mediates proteolytic processing of the polyprotein. Cleaves host EIF5B, contributing to host translation shutoff. Cleaves also host PABPC1, contributing to host translation shutoff.UniRule annotation
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.UniRule annotation
Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.UniRule annotation
Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface.UniRule annotation
Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.UniRule annotation
Protein 3CD: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome.UniRule annotation
RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated.UniRule annotation
Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.UniRule annotation

<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.UniRule annotation EC:3.4.22.28
  • Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.UniRule annotation EC:3.4.22.29
  • Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.ARBA annotation EC:3.4.22.29

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+ARBA annotation

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHelicaseUniRule annotationARBA annotation, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-bindingUniRule annotationARBA annotation, RNA-directed RNA polymeraseUniRule annotationARBA annotation, Thiol proteaseARBA annotation, Transferase, Viral ion channelUniRule annotationARBA annotation
Biological processActivation of host autophagy by virusUniRule annotationARBA annotation, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virusUniRule annotationARBA annotation, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host MDA5 by virusARBA annotation, Inhibition of host mRNA nuclear export by virusUniRule annotationARBA annotation, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cellUniRule annotationARBA annotation, Transport, Viral attachment to host cellUniRule annotationARBA annotation, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replicationUniRule annotationARBA annotation, Virus endocytosis by hostUniRule annotationARBA annotation, Virus entry into host cell
LigandATP-binding, MagnesiumARBA annotation, 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%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 polyproteinUniRule annotation
Cleaved into the following 17 chains:
P3UniRule annotation
Protein 3ABUniRule annotation
P2UniRule annotation
P1UniRule annotation
Capsid protein VP0UniRule annotation
Alternative name(s):
VP4-VP2UniRule annotation
Capsid protein VP4UniRule annotation
Alternative name(s):
P1AUniRule annotation
Virion protein 4UniRule annotation
Capsid protein VP2UniRule annotation
Alternative name(s):
P1BUniRule annotation
Virion protein 2UniRule annotation
Capsid protein VP3UniRule annotation
Alternative name(s):
P1CUniRule annotation
Virion protein 3UniRule annotation
Capsid protein VP1UniRule annotation
Alternative name(s):
P1DUniRule annotation
Virion protein 1UniRule annotation
Protease 2AUniRule annotation (EC:3.4.22.29UniRule annotation)
Short name:
P2AUniRule annotation
Alternative name(s):
Picornain 2AUniRule annotation
Protein 2AUniRule annotation
Protein 2BUniRule annotation
Short name:
P2BUniRule annotation
Protein 2CUniRule annotation (EC:3.6.1.15UniRule annotation)
Short name:
P2CUniRule annotation
Protein 3AUniRule annotation
Short name:
P3AUniRule annotation
Viral protein genome-linkedUniRule annotation
Short name:
VPgUniRule annotation
Alternative name(s):
Protein 3BUniRule annotation
Short name:
P3BUniRule annotation
Protein 3CDUniRule annotation (EC:3.4.22.28UniRule annotation)
Protease 3CUniRule annotation
Short name:
P3CUniRule annotation
RNA-directed RNA polymeraseUniRule annotation (EC:2.7.7.48UniRule annotation)
Short name:
RdRpUniRule annotation
Alternative name(s):
3D polymeraseUniRule annotation
Short name:
3DpolUniRule annotation
Protein 3DUniRule annotation
Short name:
3DUniRule annotation
<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>OrganismiHuman enterovirus 71 (EV71) (EV-71)Imported
<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 identifieri39054 [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 lineageiViruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Enterovirus › Enterovirus A
<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
  • UP000171212 <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

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Capsid protein, Host cytoplasmUniRule annotationARBA annotation, Host cytoplasmic vesicleUniRule annotationARBA annotation, Host membraneUniRule annotationARBA annotation, Host nucleusARBA annotation, Membrane, T=pseudo3 icosahedral capsid proteinUniRule annotationARBA annotation, 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

Keywords - PTMi

Covalent protein-RNA linkageUniRule annotationARBA annotation, Lipoprotein, MyristateUniRule annotationARBA annotation, PhosphoproteinARBA annotation

<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

Capsid protein VP1:

Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid.

Interacts with capsid protein VP2, capsid protein VP3 and capsid protein VP4 following cleavage of capsid protein VP0.

UniRule annotation

Homodimer.

ARBA annotation

Interacts with RNA-directed RNA polymerase.

ARBA annotation

Interacts with Viral protein genome-linked and with protein 3CD.

ARBA annotation

Interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity).

Interacts with capsid protein VP4 in the mature capsid (By similarity).

Interacts with protein 2C; this interaction may be important for virion morphogenesis.

ARBA annotation

Interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers.

ARBA annotation

Interacts with protein 3CD.

ARBA annotation

<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>Domaini1216 – 1374SF3 helicaseInterPro annotationAdd BLAST159
Domaini1549 – 1727Peptidase C3InterPro annotationAdd BLAST179
Domaini1958 – 2073RdRp catalyticInterPro annotationAdd BLAST116

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>Regioni1 – 21DisorderedSequence analysisAdd BLAST21

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili1164 – 1184Sequence analysisAdd BLAST21

<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.UniRule annotationARBA annotation

Keywords - Domaini

Coiled coilSequence analysis, RepeatUniRule annotationARBA annotation, Zinc-fingerARBA annotation

Family and domain databases

Conserved Domains Database

More...CDDi		cd00205, rhv_like, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.870, 1 hit
2.40.10.10, 4 hits
2.60.120.20, 3 hits
3.30.70.270, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003593, AAA+_ATPase
IPR043502, DNA/RNA_pol_sf
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
IPR014838, P3A
IPR036203, P3A_soluble_dom
IPR044067, PCV_3C_PRO
IPR000081, Peptidase_C3
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR003138, Pico_P1A
IPR002527, Pico_P2B
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
PF08727, P3A, 1 hit
PF00548, Peptidase_C3, 1 hit
PF02226, Pico_P1A, 1 hit
PF00947, Pico_P2A, 1 hit
PF01552, Pico_P2B, 1 hit
PF00680, RdRP_1, 1 hit
PF00073, Rhv, 3 hits
PF00910, RNA_helicase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00382, AAA, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494, SSF50494, 2 hits
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit
SSF89043, SSF89043, 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.

C0LJL5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSQVSTQRS GSHENSNSAT EGSTINYTTI NYYKVSYAAT AGKQGLKQDP 
        60         70         80         90        100
DKFANPVKDI FTEMAAPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI 
       110        120        130        140        150
IVGYGEWPSY CSDSDATAVD KPTRPDVSVN RFYTLDTKLW EKSSKGWYWK 
       160        170        180        190        200
FPDVLTETGV FGQNAQFHYL YRSGFCIHVQ CNASKFHQGV LLVAVLPEYV 
       210        220        230        240        250
IGTVAGGTGT EDSHPPYKQT QPGADGFELQ HPYVLDAGIP ISQLTVCPHQ 
       260        270        280        290        300
WINLRTNNCA TIIVPYINAL PFDSALNHCN FGLLVVPISP LDYDQGATPV 
       310        320        330        340        350
IPITITLAPM CSEFAGLRQA VTQGFPTELK PGTNQFLTTD DGVSAPILPN 
       360        370        380        390        400
FHPTPCIHIP GEVRNLLELC QVETILEVNN VPTNATSLME RLRFPVSAQA 
       410        420        430        440        450
GKGELCAVFR ADPGRNGPWQ STLLGQLCGY YTQWSGSLEV TFMFTGSFMA 
       460        470        480        490        500
IGKMLIAYTP PGGPLPKDRA TAMLGTHVIW DFWLQSSVTL VIPWISNTHY 
       510        520        530        540        550
RAHARDGVFD YYTTGLVSIW YQTNYVVPIG APNTAYIIAL AAAQKNFTMK 
       560        570        580        590        600
LCKDASDILQ TGTIQGDRVA DVIESSIGDS VSRALTHALP APTGQNTQVS 
       610        620        630        640        650
SHRLDTGKVP ALQAAEIGAS SNASDESMIE TRCVLNSHST AETTLDSFFS 
       660        670        680        690        700
RAGLVGEIDL PLEGTTNPNG YANWDIDITG YAQMRRKVEL FTYMRFDAEF 
       710        720        730        740        750
TFVACTPTGE VVPQLLQYMF VPPGAPKPDS RESLAWQTAT NPSVFVKLSD 
       760        770        780        790        800
PPAQVSVPFM SPASAYQWFY DGYPTFGEHK QEKDLEYGAC PNNMMGTFSV 
       810        820        830        840        850
RTVGTSKSKY PLVVRIYMRM KHVRAWIPRP MRNQNYLFKA NPNYAGNSIK 
       860        870        880        890        900
PTGASRTAIT TLGKFGQQSG AIYVGNFRVV NRHLATHNDW ANLVWEDSSR 
       910        920        930        940        950
DLLVSSTTAQ GCDTIARCDC QTGVYYCNSR RKHYPVSFSK PSLIYVEASE 
       960        970        980        990       1000
YYPARYQSHL MLAQGHSEPG DCGGILRCQH GVVGIVSTGG NGLVGFADVR 
      1010       1020       1030       1040       1050
DLLWLDEEAM EQGVSDYIKG LGDAFGTGFT DAVSREVEAL KNYLIGSEGA 
      1060       1070       1080       1090       1100
VEKILKNLVK LISALVIVIR SDYDMVTLTA TLALIGCHGS PWAWIKAKTA 
      1110       1120       1130       1140       1150
SILGIPIAQK QSASWLKKFN DMANAAKGLE WVSNKISKFI DWLKEKIVPA 
      1160       1170       1180       1190       1200
AKEKVEFLNN LKQLPLLENQ ISNLEQSAAS QEDLEVMFGN VSYLAHFCRK 
      1210       1220       1230       1240       1250
FQPLYATEAK RVYALEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT 
      1260       1270       1280       1290       1300
GIIARAIADK YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL 
      1310       1320       1330       1340       1350
FCQMVSTVDF IPPMASLEEK GVSFTSKFVI ASTNASNIIV PTVSDSDAIR 
      1360       1370       1380       1390       1400
RRFYMDCDIE VTDSYKTDLG RLDAGRAAKL CSENNTANFK RCSPLVCGKA 
      1410       1420       1430       1440       1450
IQLRDRKSKV RYSVDTVVSE LIREYSNRSA IGNTIEALFQ GPPKFRPIRI 
      1460       1470       1480       1490       1500
SLEEKPAPDA ISDLLASVDS EEVRQYCRDQ GWIIPETPTN VERHLNRAVL 
      1510       1520       1530       1540       1550
VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKQVLKKP ALRTATVQGP 
      1560       1570       1580       1590       1600
SLDFALSLLR RNVRQVQTDQ GHFTMLGVRD RLAVLPRHSQ PGKTIWIEHK 
      1610       1620       1630       1640       1650
LVNVLDAVEL VDEQGVNLEL TLITLDTNEK FRDITKFIPE SISTASDATL 
      1660       1670       1680       1690       1700
VINTEHMPSM FVPVGDVVQY GFLNLSGKPT HRTMMYNFPT KAGQCGGVVT 
      1710       1720       1730       1740       1750
SVGKVIGIHI GGNGRQGFCA GLKRSYFASE QGEIQWVKPN KETGRLNING 
      1760       1770       1780       1790       1800
PTRTKLEPSV FHDVFEGSRE PAVLHSKDPR LEVDFEQALF SKYVGNTLHE 
      1810       1820       1830       1840       1850
PDEYIKEAAL HYANQLKQLE INTSQMSMEE ACYGTENLEA IDLHTSAGYP 
      1860       1870       1880       1890       1900
YGALGIKKRD ILDPTTRDVS KMKLYMDKYG LDLPYSTYVK DELRSVDKIK 
      1910       1920       1930       1940       1950
KGKSRLIEAS SLNDSVCLRM AFGHLYEAFH ANPRTITGSA VGCNPDTFWS 
      1960       1970       1980       1990       2000
KLPILLPGSL FAFDYSGYDA SLSPVWFRAL ELVLREIGYS EGAVSLIEGI 
      2010       2020       2030       2040       2050
NHTHHVYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRAL LIKTFKGIDL 
      2060       2070       2080       2090       2100
DELNMVAYGD DVLASYPFPI DCLELAKTGK EYGLTMTPAD KSPCFNEVNW 
      2110       2120       2130       2140       2150
GNATFLKRGF LPDEQFPFLI HPTMPMREIH ESIRWTKDAR NTQDHVRSLC 
      2160       2170       2180       2190 
LLAWHNGKQE YEKFVSTIRS VPVGRALAIP NYENLRRNWL ELF
Length:2,193
Mass (Da):242,752
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:iABFC6A67D0B37DB1
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
FJ713137 Genomic RNA Translation: ACN59569.1

<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
FJ713137 Genomic RNA Translation: ACN59569.1

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

Family and domain databases

CDDicd00205, rhv_like, 3 hits
Gene3Di1.10.10.870, 1 hit
2.40.10.10, 4 hits
2.60.120.20, 3 hits
3.30.70.270, 1 hit
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR043502, DNA/RNA_pol_sf
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
IPR014838, P3A
IPR036203, P3A_soluble_dom
IPR044067, PCV_3C_PRO
IPR000081, Peptidase_C3
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR003138, Pico_P1A
IPR002527, Pico_P2B
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
PF08727, P3A, 1 hit
PF00548, Peptidase_C3, 1 hit
PF02226, Pico_P1A, 1 hit
PF00947, Pico_P2A, 1 hit
PF01552, Pico_P2B, 1 hit
PF00680, RdRP_1, 1 hit
PF00073, Rhv, 3 hits
PF00910, RNA_helicase, 1 hit
SMARTiView protein in SMART
SM00382, AAA, 1 hit
SUPFAMiSSF50494, SSF50494, 2 hits
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit
SSF89043, SSF89043, 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

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 nameiC0LJL5_HE71
<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: C0LJL5
<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/TrEMBL: May 5, 2009
Last sequence update: May 5, 2009
Last modified: December 2, 2020
This is version 88 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 statusiUnreviewed (UniProtKB/TrEMBL)
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