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Entry version 136 (07 Oct 2020)
Sequence version 1 (01 Mar 2002)
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Protein

Genome polyprotein

Gene
N/A
Organism
Echovirus E18
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>
-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

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
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
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
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.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
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.ARBA 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

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 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, DNA replicationARBA 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 mRNA nuclear export by virusUniRule annotationARBA annotation, Inhibition of host RIG-I by virusARBA 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

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C03.011

<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>OrganismiEchovirus E18Imported
<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 identifieri47506 [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 lineageiVirusesRiboviriaOrthornaviraePisuviricotaPisoniviricetesPicornaviralesPicornaviridaeEnterovirusEnterovirus B
<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
  • UP000326240 <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

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

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi497 ↔ 547Combined sources

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

Homohexamer; forms a hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases (By similarity).

Interacts (via N-terminus) with host RTN3 (via reticulon domain); this interaction is important for viral replication (By similarity).

Interacts with capsid protein VP3; this interaction may be important for virion morphogenesis.

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 VP1 and capsid protein VP3 to form heterotrimeric protomers.

ARBA annotation

Interacts with protein 3AB and with RNA-directed RNA polymerase.

ARBA annotation

Interacts with protein 3CD.

ARBA annotation

<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
Q8V635

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%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>Domaini1209 – 1365SF3 helicaseInterPro annotationAdd BLAST157
Domaini1954 – 2070RdRp catalyticInterPro annotationAdd BLAST117

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>Regioni563 – 589DisorderedSequence analysisAdd BLAST27

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi568 – 589PolarSequence analysisAdd BLAST22

<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

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
4.10.80.10, 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
IPR000081, Peptidase_C3
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR003138, Pico_P1A
IPR036988, Pico_P1A_sf
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
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.

Q8V635-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGAQVSTQKT GAHETSLSAK GNSIIHYTNI NFYKDAASSA SNRQDIQQDP
60 70 80 90 100
GKFTDPVKDL MIKTLPALNS PSAEECGYSD RVRSMTLGNS TITTQESANV
110 120 130 140 150
VVGYGEWPSY LSDREATAED QPTQPDVATC RFYTLESVQW EKTSPGWWWK
160 170 180 190 200
FPEALKNMGL FGQNMHYHYL GRAGYTIHVQ CNASKFHQGC LLVVCVPEAE
210 220 230 240 250
MGCADTDTTF PATELTTEDT PHVFTSDSIT GKKVQAAVCN AGMGVGVGNL
260 270 280 290 300
TIFPHQWINL RTNNSATIVI PYINSVPMDN MFRHYNFTLM IIPFAPLNFT
310 320 330 340 350
DGATAYVPIT VTIAPMYAEY NGLRLASTQG VPVLNTPGSN QFLTSDDYQS
360 370 380 390 400
PSAMPQFDET PEMHIPGEVR NLMEIAEVDS VVPVNNVTGK TKSMDAYQIP
410 420 430 440 450
VGTGNTDKTK PIFSFQMDPG YSSVLKRTLL GEMLNYYAHW SGSVKLTFLF
460 470 480 490 500
CGSAMATGKL LISYSPPGAS VPTSRKDAML GTHIVWDIGL QSSCVLCVPW
510 520 530 540 550
ISQSHYRMVQ QDPYTSAGYI TCWYQTNIVV PPGAPTSCDV LCFASACNDF
560 570 580 590 600
SVRLLRDTPF MAQPGKLQGD NQDRTVANTQ PSGPSNSTEI PALTAVETGH
610 620 630 640 650
TSQVDPSDTI QTRHVVNFHS RSESTIENFM GRAACVFMDQ YKINGEETST
660 670 680 690 700
DRFAVWTINI REMAQLRRKC EMFTYMRFDI EMTMVITSCQ DQGTILDQDM
710 720 730 740 750
PVLTHQIMYV PPGGPIPAKV DGYEWQTSTN PSVFWTEGNA PPRISIPFIS
760 770 780 790 800
VGNAYSSFYD GWSHFTQDGT YGYTTLNAMG KLYIRHVNRS SPHQITSTIR
810 820 830 840 850
VYFKPKHIKA WVPRPPRLCP YINKRDVNFV VTEITDSRTS ITDTPHPEHS
860 870 880 890 900
VLATHGAFGQ QSGAVYVGNY RVVNRHLATH ADWQNCVWED YNRDLLVSTT
910 920 930 940 950
TAHGCDTIAR CQCTAGVYFC SSRNKHYPVS FEGPGLVEVQ ESEYYPRRYQ
960 970 980 990 1000
SHVLLAAGFS EPGDCGGILR CEHGVIGLVT MGGEGVVGFA DVRDLLWLED
1010 1020 1030 1040 1050
DAMEQGVKDY VEQLGNAFGS GFTNQICEQV SLLKESLVGQ DSILEKSLKA
1060 1070 1080 1090 1100
LVKIISALVI VVKNHDDLIT VTATLALIGC TSSPWRWLKQ KVSQYYGIPM
1110 1120 1130 1140 1150
AERQNNGWLK KFTEMTNACK GMEWIAIKIQ KFIEWLKVKI LPEVKEKHEF
1160 1170 1180 1190 1200
LNRLKQLPLL ESQIATIEQS APSQSDQEQL FSNVQYFAHY CRKYAPLYAA
1210 1220 1230 1240 1250
EAKRVFSLEK KMSNYIQFKS KCRIEPVCLL LHGSPGAGKS VATNLIGRSL
1260 1270 1280 1290 1300
AEKLNSSVYS LPPDPDHFDG YKQQAVVIMD DLCQNPDGKD VSLFCQMVSS
1310 1320 1330 1340 1350
VDFVPPMAAL EEKGILFTSP FVLASTNAGS INAPTVSDSR ALARRFHFDM
1360 1370 1380 1390 1400
NIEVISMYSQ NGKVNMPMSV KTCDEECCPV NFKKCCPLVC GKAIQFIDRR
1410 1420 1430 1440 1450
TQVRYSLDML VTEMFREYNH RHSVGATLEA LFQGPPIYKE IKISVAPETP
1460 1470 1480 1490 1500
PPPAIADLLK SVDSEAVRDY CKEKGWLVPE VNSSLQIEKH VSRAFICLQA
1510 1520 1530 1540 1550
LTTFVSVAGI IYIIYKLFAG FQGAYTGMPN QKPRVPTLRQ AKVQGPAFEF
1560 1570 1580 1590 1600
AVAMMKRNSS TVKTEYGEFT MLGIYDRWAV LPRHAKPGPT ILMNDQEVGV
1610 1620 1630 1640 1650
SDAKELVDKD GTNLELTLLK LNRNEKFRDI RGFLAKEEVE VNEAVLAINT
1660 1670 1680 1690 1700
SKFPNMYIPV GQVTDYGFLN LGGTPTKRML MYNFPTRAGQ CGGVLMSTGK
1710 1720 1730 1740 1750
VLGIHVGGNG HQGFSAALLK HYFNDEQGEI EFIESSKEAG FPVINTPSKT
1760 1770 1780 1790 1800
KLEPSVFHQV FEGNKEPAVL RNGDPRLKAN FEEAIFSKYI GNVNTHVDEY
1810 1820 1830 1840 1850
MLEAVDHYAG QLATLDISTE PMRLEDAVYG TEGLEALDLT TSAGYPYVAL
1860 1870 1880 1890 1900
GIKKRDILSK KTRDLTRLKE CMDKYGLNLP MVTYVKDELR SAEKVAKGKS
1910 1920 1930 1940 1950
RLIEASSLND SVAMRQTFGN LYKTFHLNPG IVTGSAVGCD PDLFWSKIPV
1960 1970 1980 1990 2000
MLDGHLIAFD YSGYDASLSP VWFACLKLLL EKLGYSHKET NYIDYLCNSH
2010 2020 2030 2040 2050
HLYRDKHYFV RGGMPSGCSG TSIFNSMINN IIIRTLMLKV YKGIDLDQFR
2060 2070 2080 2090 2100
MIAYGDDVIA SYPWPIDASL LAEAGKGYGL IMTPADKGEC FNEVTWTNVT
2110 2120 2130 2140 2150
FLKRYFRADE QYPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCLLAW
2160 2170 2180
HNGEHEYEEF IRKIRSIPVG RCLTLPAFST LRRKWLDSF
Length:2,189
Mass (Da):244,421
Last modified:March 1, 2002 - 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:i95765355147B846A
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
AF317694 Genomic RNA Translation: AAL37163.1

<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
AF317694 Genomic RNA Translation: AAL37163.1

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
6HBGelectron microscopy3.16A569-855[»]
B70-329[»]
C330-568[»]
D1-69[»]
6HBHelectron microscopy3.36A569-855[»]
B70-329[»]
C330-568[»]
6HBJelectron microscopy3.16A569-855[»]
B70-329[»]
C330-568[»]
6HBKelectron microscopy3.80A/D/G/J/M/P/S/V/Y/b/e569-855[»]
B/E/H/K/N/Q/T/W/Z/c/f70-328[»]
C/F/I/L/O/R/U/X/a/d/g330-568[»]
6HBLelectron microscopy3.70A/D/G/J/M/P/S/V/Y/b/e/h/k/n/q569-855[»]
B/E/H/K/N/Q/T/W/Z/c/f/i/l/o/r70-329[»]
C/F/I/L/O/R/U/X/a/d/g/j/m/p/s330-568[»]
6HHTelectron microscopy4.05A1/A2/D1/D2/G1/G2/J1/J2/M1/M2/P1/P2/S1/S2/V1/V2/Y2/b2/e2/h2/k2/n2/q2/t2/w2569-855[»]
B1/B2/E1/E2/H1/H2/K1/K2/N1/N2/Q1/Q2/T1/T2/W1/W2/Z2/c2/f2/i2/l2/o2/r2/u2/x270-329[»]
SMRiQ8V635
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiC03.011

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
4.10.80.10, 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
IPR000081, Peptidase_C3
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR003138, Pico_P1A
IPR036988, Pico_P1A_sf
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
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 nameiQ8V635_9ENTO
<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: Q8V635
<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: March 1, 2002
Last sequence update: March 1, 2002
Last modified: October 7, 2020
This is version 136 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)

<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-structureCombined sources
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