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Protein

Genome polyprotein

Gene
N/A
Organism
Enterovirus D68
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

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. After genome has been released, the channel shrinks.UniRule annotation
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1.UniRule annotation
Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores.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 dissassembly 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: Is 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. The 3C domain in the context of protein 3CD may have an RNA binding activity.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. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.UniRule annotationSAAS annotation EC:3.4.22.28
  • Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.UniRule annotation EC:3.4.22.29

<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 annotationSAAS annotation, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-bindingUniRule annotationSAAS annotation, RNA-directed RNA polymeraseUniRule annotationSAAS annotation, Thiol proteaseSAAS annotation, Transferase, Viral ion channelUniRule annotationSAAS annotation
Biological processActivation of host autophagy by virusUniRule annotation, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virusUniRule 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 annotation, Inhibition of host RIG-I by virusUniRule annotation, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cellUniRule annotation, Transport, Viral attachment to host cellUniRule annotationSAAS annotation, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replicationUniRule annotationSAAS annotation, Virus endocytosis by hostUniRule annotation, Virus entry into host cell
LigandATP-binding, Nucleotide-binding

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_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome 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_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEnterovirus D68Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri42789 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus D
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000105171 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

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

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasmUniRule annotationSAAS annotation, Host cytoplasmic vesicleUniRule annotationSAAS annotation, Host membraneUniRule annotationSAAS annotation, Membrane, T=pseudo3 icosahedral capsid proteinUniRule 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 annotation, Lipoprotein, MyristateUniRule 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_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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 VP4 in the mature capsid (By similarity). Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid (By similarity). Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 (By similarity). Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity). Protein 3AB: interacts with protein 3CD (By similarity). Viral protein genome-linked: interacts with RNA-directed RNA polymerase (By similarity). Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD.UniRule 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

Select the link destinations:

Protein Data Bank Europe

More...
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
4WM7X-ray2.32B70-317[»]
C318-564[»]
4WM8X-ray2.00B70-317[»]
C318-564[»]
5BNNX-ray2.32A565-861[»]
B70-317[»]
C318-564[»]
D2-69[»]
5BNOX-ray2.15A565-861[»]
B70-317[»]
C318-564[»]
D2-69[»]
5BNPX-ray2.15A565-861[»]
B70-317[»]
C318-564[»]
D2-69[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q68T42

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

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SMRi
Q68T42

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1212 – 1370SF3 helicaseInterPro annotationAdd BLAST159
Domaini1954 – 2069RdRp catalyticInterPro annotationAdd BLAST116

<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 annotationSAAS annotation

Keywords - Domaini

RepeatUniRule annotation

Family and domain databases

Conserved Domains Database

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CDDi
cd00205 rhv_like, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.870, 1 hit
2.60.120.20, 3 hits
4.10.80.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
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
IPR003138 Pico_P1A
IPR036988 Pico_P1A_sf
IPR002527 Pico_P2B
IPR001676 Picornavirus_capsid
IPR033703 Rhv-like
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
IPR029053 Viral_coat

Pfam protein domain database

More...
Pfami
View protein in Pfam
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

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD001306 Peptidase_C3, 1 hit
PD649346 Pico_P2B, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00382 AAA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50494 SSF50494, 2 hits
SSF52540 SSF52540, 1 hit
SSF89043 SSF89043, 1 hit

PROSITE; a protein domain and family database

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

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

Q68T42-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGAQVTRQQT GTHENANIAT NGSHITYNQI NFYKDSYAAS ASKQDFSQDP
60 70 80 90 100
SKFTEPVVEG LKAGAPVLKS PSAEACGYSD RVLQLKLGNS AIVTQEAANY
110 120 130 140 150
CCAYGEWPNY LPDHEAVAID KPTQPETSTD RFYTLRSVKW ESNSTGWWWK
160 170 180 190 200
LPDALNNIGM FGQNVQYHYL YRSGFLIHVQ CNATKFHQGA LLVVAIPEHQ
210 220 230 240 250
RGAHDTTTSP GFNDIMKGER GGTFNHPYVL DDGTSIACAT IFPHQWINLR
260 270 280 290 300
TNNSATIVLP WMNVAPMDFP LRHNQWTLAV IPVVPLGTRT MSSVVPITVS
310 320 330 340 350
IAPMCCEFNG LRHAITQGVP TYLLPGSGQF LTTDDHSSAP VLPCFNPTPE
360 370 380 390 400
MHIPGQIRNM LEMIQVESMM EINNTDGANG MERLRVDISV QADLDQLLFN
410 420 430 440 450
IPLDIQLDGP LRNTLVGNIS RYYTHWSGSL EMTFMFCGSF MATGKLILCY
460 470 480 490 500
TPPGGSCPTT RETAMLGTHI VWDFGLQSSI TLIIPWISGS HYRMFNSDAK
510 520 530 540 550
STNANVGYVT CFMQTNLIVP SESSDTCSLI GFIAAKDDFS LRLMRDSPDI
560 570 580 590 600
GQSNHLHGAE AAYQVESIIK TATDTVKSEI NAELGVVPSL NAVETGATSN
610 620 630 640 650
TEPEEAIQTR TVINQHGVSE TLVENFLGRA ALVSKKSFEY KNHASSSAGT
660 670 680 690 700
HKNFFKWTIN TKSFVQLRRK LELFTYLRFD AEITILTTVA VNGNNDSTYM
710 720 730 740 750
GLPDLTLQAM FVPTGALTPK EQDSFHWQSG SNASVFFKIS DPPARMTIPF
760 770 780 790 800
MCINSAYSVF YDGFAGFEKN GLYGINPADT IGNLCVRIVN EHQPVGFTVT
810 820 830 840 850
VRVYMKPKHI KAWAPRPPRT MPYMSIANAN YKGRDTAPNT LNAIIGNRAS
860 870 880 890 900
VTTMPHNIVT TGPGFGGVFV GSFKIINYHL ATIEERQSAI YVDWQSDVLV
910 920 930 940 950
TPIAAHGRHQ IARCKCNTGV YYCRHRDRSY PICFEGPGIQ WIEQNEYYPA
960 970 980 990 1000
RYQTNVLLAA GPAEAGDCGG LLVCPHGVIG LLTAGGGGIV AFTDIRNLLW
1010 1020 1030 1040 1050
LDTDVMEQGI TDYIQNLGNA FGAGFTETIS NKAKEVQDML IGESSLLEKL
1060 1070 1080 1090 1100
LKALIKIISA LVIVIRNSED LITVTATLAL LGCHDSPWSY LKQKVCSYLG
1110 1120 1130 1140 1150
IPYVPRQSES WLKKFTEACN ALRGLDWLSQ KIDKFINWLK TKILPEAREK
1160 1170 1180 1190 1200
YEFVQRLKQL PVIEKQVSTI EHSCPTTERQ QALFNNVQYY SHYCRKYAPL
1210 1220 1230 1240 1250
YAVESKRVAA LEKKINNYIQ FKSKSRIEPV CLIIHGSPGT GKSVASNLIA
1260 1270 1280 1290 1300
RAITEKLGGD IYSLPPDPKY FDGYKQQTVV LMDDLMQNPD GNDISMFCQM
1310 1320 1330 1340 1350
VSTVDFIPPM ASLEEKGTLY TSPFLIATTN AGSIHAPTVS DSKALSRRFK
1360 1370 1380 1390 1400
FDVDIEVTDS YKDSNKLDMS RAVEMCKPDN CTPTNYKRCC PLICGKAIQF
1410 1420 1430 1440 1450
RDRRTNARST VDMLVTDIIK EYRTRNSTQD KLEALFQGPP QFKEIKISVA
1460 1470 1480 1490 1500
PDTPAPDAIN DLLRSVDSQE VRDYCQKKGW IVIHPSNELV VEKHISRAFI
1510 1520 1530 1540 1550
TLQAIATFVS IAGVVYVIYK LFAGIQGPYT GIPNPKPKVP SLRTAKVQGP
1560 1570 1580 1590 1600
GFDFAQAIMK KNTVIARTEK GEFTMLGVYD RVAVIPTHAS VGEIIYINDV
1610 1620 1630 1640 1650
ETRVLDACAL RDLTDTNLEI TIVKLDRNQK FRDIRHFLPR CEDDYNDAVL
1660 1670 1680 1690 1700
SVHTSKFPNM YIPVGQVTNY GFLNLGGTPT HRILMYNFPT RAGQCGGVVT
1710 1720 1730 1740 1750
TTGKVIGIHV GGNGAQGFAA MLLHSYFTDT QGEIVSNEKS GMCINAPAKT
1760 1770 1780 1790 1800
KLQPSVFHQV FEGSKEPAVL NSKDPRLKTD FEEAIFSKYT GNKIMLMDEY
1810 1820 1830 1840 1850
MEEAVDHYVG CLEPLDISVD PIPLENAMYG MEGLEALDLT TSAGFPYLLQ
1860 1870 1880 1890 1900
GKKKRDIFNR QTRDTSEMTK MLEKYGVDLP FVTFVKDELR SREKVEKGKS
1910 1920 1930 1940 1950
RLIEASSLND SVAMRVAFGN LYATFHNNPG TATGSAVGCD PDIFWSKIPI
1960 1970 1980 1990 2000
LLDGEIFAFD YTGYDASLSP VWFACLKKVL IKLGYTHQTS FIDYLCHSVH
2010 2020 2030 2040 2050
LYKDRKYVIN GGMPSGSSGT SIFNTMINNI IIRTLLIKVY KGIDLDQFKM
2060 2070 2080 2090 2100
IAYGDDVIAS YPHKIDPGLL AEAGKHYGLV MTPADKGTSF IDTNWENVTF
2110 2120 2130 2140 2150
LKRYFRADDQ YPFLIHPVMP MKEIHESIRW TKDPRNTQDH VRSLCYLAWH
2160 2170 2180
NGEEAYNEFC RKIRSVPVGR ALTLPAYSSL RRKWLDSF
Length:2,188
Mass (Da):243,800
Last modified:October 11, 2004 - 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:i185C5A05E971727E
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
AY426531 Genomic RNA Translation: AAR98503.1

<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
AY426531 Genomic RNA Translation: AAR98503.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WM7X-ray2.32B70-317[»]
C318-564[»]
4WM8X-ray2.00B70-317[»]
C318-564[»]
5BNNX-ray2.32A565-861[»]
B70-317[»]
C318-564[»]
D2-69[»]
5BNOX-ray2.15A565-861[»]
B70-317[»]
C318-564[»]
D2-69[»]
5BNPX-ray2.15A565-861[»]
B70-317[»]
C318-564[»]
D2-69[»]
ProteinModelPortaliQ68T42
SMRiQ68T42
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC03.011

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00205 rhv_like, 3 hits
Gene3Di1.10.10.870, 1 hit
2.60.120.20, 3 hits
4.10.80.10, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
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
IPR003138 Pico_P1A
IPR036988 Pico_P1A_sf
IPR002527 Pico_P2B
IPR001676 Picornavirus_capsid
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
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001306 Peptidase_C3, 1 hit
PD649346 Pico_P2B, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF50494 SSF50494, 2 hits
SSF52540 SSF52540, 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

More...
ProtoNeti
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 nameiQ68T42_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: Q68T42
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/TrEMBL: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 16, 2019
This is version 124 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, Complete proteomeImported
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