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Entry version 74 (07 Oct 2020)
Sequence version 1 (01 Sep 2009)
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Protein

Genome polyprotein

Gene
N/A
Organism
Human klassevirus 1 (HKV-1)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Required for viral RNA replication and viral RNA encapsidation (By similarity). Does not have any proteolytic activity (By similarity).By similarity
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity).By similarity
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity).By similarity
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP1 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity).By similarity
Required for viral RNA replication (By similarity). Does not have any proteolytic activity (By similarity).By similarity
Affects membrane integrity and causes an increase in membrane permeability.By similarity
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.By similarity
Serves as membrane anchor via its hydrophobic domain. Plays an essential role in viral RNA replication by recruiting PI4KB at the viral replication sites, thereby allowing the formation of rearranged membranous structures where viral replication takes place (By similarity).By similarity
Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains.By similarity
Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease (By similarity).By similarity
Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity). Performs VPg uridylylation (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1745For protease 3C activityPROSITE-ProRule annotation1
Active sitei1776For protease 3C activityPROSITE-ProRule annotation1
Active sitei1849For protease 3C activityPROSITE-ProRule annotation1
Active sitei2128For RdRp activityBy similarity1
Active sitei2225For RdRp activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1384 – 1391ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHelicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
Biological processEukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host mRNA nuclear export by virus, Ion transport, Transport, Viral attachment to host cell, Viral RNA replication, Virus entry into host cell
LigandATP-binding, Nucleotide-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 12 chains:
Leader protein
Short name:
L
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.4.13By similarity)
Short name:
P2C
Protein 3A
Short name:
P3A
VPg
Short name:
P3B
Alternative name(s):
Protein 3B
Protein 3CD (EC:3.4.22.28)
Protease 3CPROSITE-ProRule annotation (EC:3.4.22.28PROSITE-ProRule annotation)
Alternative name(s):
Picornain 3CPROSITE-ProRule annotation
Short name:
P3CPROSITE-ProRule annotation
RNA-directed RNA polymerase (EC:2.7.7.48PROSITE-ProRule annotation)
Short name:
RdRp
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHuman klassevirus 1 (HKV-1)
<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 identifieri655603 [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 lineageiVirusesRiboviriaOrthornaviraePisuviricotaPisoniviricetesPicornaviralesPicornaviridaeSalivirus
<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
  • UP000126165 <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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1646 – 1666HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host Golgi apparatus, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, Virion

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004480321 – 2370Genome polyproteinAdd BLAST2370
ChainiPRO_00004480331 – 111Leader proteinAdd BLAST111
ChainiPRO_0000448034112 – 479Capsid protein VP0Add BLAST368
ChainiPRO_0000448035480 – 702Capsid protein VP3Add BLAST223
ChainiPRO_0000448036703 – 952Capsid protein VP1Add BLAST250
ChainiPRO_0000448037953 – 1097Protein 2AAdd BLAST145
ChainiPRO_00004480381098 – 1250Protein 2BAdd BLAST153
ChainiPRO_00004480391251 – 1596Protein 2CAdd BLAST346
ChainiPRO_00004480401597 – 1673Protein 3AAdd BLAST77
ChainiPRO_00004480411674 – 1702VPgAdd BLAST29
ChainiPRO_00004480421703 – 2362Protein 3CDAdd BLAST660
ChainiPRO_00004480431703 – 1897Protease 3CAdd BLAST195
ChainiPRO_00004480441898 – 2362RNA-directed RNA polymeraseAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi112N-myristoyl glycine; by hostBy similarity1
Lipidationi1597N-myristoyl glycine; by host1 Publication1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1676O-(5'-phospho-RNA)-tyrosineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The leader protein-VP0 junction is cleaved by 3C proteinase (By similarity). The VP1/2A junction is cleaved by the protein 3CD in association with protein 2A (By similarity).By similarity
Uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei111 – 112Cleavage; by protease 3CCurated2
Sitei479 – 480Cleavage; by protease 3CBy similarity2
Sitei702 – 703Cleavage; by protease 3CBy similarity2
Sitei952 – 953Cleavage; by protein 3CDBy similarity2
Sitei1097 – 1098Cleavage; by protease 3CBy similarity2
Sitei1250 – 1251Cleavage; by protease 3CBy similarity2
Sitei1596 – 1597Cleavage; by protease 3CBy similarity2
Sitei1673 – 1674Cleavage; by protease 3CBy similarity2
Sitei1702 – 1703Cleavage; by protease 3CBy similarity2
Sitei1897 – 1898Cleavage; by protease 3CBy similarity2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
C6KEF6

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with capsid protein VP1 (By similarity).

Interacts with capsid protein VP3 (By similarity).

By similarity

Interacts with capsid protein VP0 (By similarity).

Interacts with capsid protein VP3 (By similarity).

By similarity

Interacts with capsid protein VP0 (By similarity).

Interacts with capsid protein VP1 (By similarity).

By similarity

Homodimer.

Interacts with protein 2B (By similarity).

Interacts with protein 2C (By similarity).

By similarity

Homodimer.

Interacts with host ABCD3.

Interacts with protein 2A (By similarity).

Interacts with host ACBD3 (By similarity).

By similarity

Homodimer.

Interacts with host ABCD3 (By similarity).

Interacts with protein 2A (By similarity).

Interacts with protein 3A (By similarity).

Interacts with protein 3C (By similarity).

Interacts with host ACBD3 (By similarity).

By similarity

Homodimer (By similarity).

Interacts with host ABCD3 (via GOLD domain) and PI4KB; these interactions allow the formation of a viral protein/ACBD3/PI4KB complex in order to synthesize PI4P at the viral RNA replication sites (Probable).

Interacts with protein 2C (By similarity).

Interacts with protein 3C (By similarity). Protein 3C:

Interacts with protein 2A (By similarity). Protein 3C:

Interacts with protein 2C (By similarity).

By similarity1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
C6KEF6, 1 interactor

<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
C6KEF6

Database of comparative protein structure models

More...
ModBasei
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1358 – 1522SF3 helicasePROSITE-ProRule annotationAdd BLAST165
Domaini1697 – 1886Peptidase C3PROSITE-ProRule annotationAdd BLAST190
Domaini2122 – 2239RdRp catalyticPROSITE-ProRule annotationAdd BLAST118

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00205, rhv_like, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.10.10, 2 hits
2.60.120.20, 4 hits
3.30.70.270, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR043502, DNA/RNA_pol_sf
IPR004004, Helic/Pol/Pept_Calicivir-typ
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001676, Picornavirus_capsid
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR033703, Rhv-like
IPR001205, RNA-dir_pol_C
IPR007094, RNA-dir_pol_PSvirus
IPR029053, Viral_coat

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00680, RdRP_1, 1 hit
PF00073, Rhv, 2 hits
PF00910, RNA_helicase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00918, CALICVIRUSNS

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51874, PCV_3C_PRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51218, SF3_HELICASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

C6KEF6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMEGSNGFSS SLAGLSSSRS SLRLLTHLLS LPPPNRDARR HSGWYRSPPT
60 70 80 90 100
LPVNVYLNEQ FDNLCLAALR YPGCKLYPSV YTLFPDVSPF KIPQSIPAFA
110 120 130 140 150
HLVQRQGLRR QGNPTTNIYG NGNEVTTDVG ANGMSLPIAV GDMPTASSSE
160 170 180 190 200
APLGSNKGGS STSPKSTSNG NVVRGSRYSK WWEPAAARAL DRALDHAVDA
210 220 230 240 250
TDAVAGAASK GIKAGATKLS NKLAGSQTTA LLALPGNIAG GAPSATVNAN
260 270 280 290 300
NTSISSQALL PSVNPYPSTP AVSLPNPDAP TQVGPAADRQ WLVDTIPWSE
310 320 330 340 350
TTPPLTVFSG PKALTPGTYP PTIEPNTGVY PLPAALCVSH PESVFTTAYN
360 370 380 390 400
AHAYFNCGFD VTVVVNASQF HGGSLIVLAM AEGLGDITPA DSSTWFNFPH
410 420 430 440 450
AIINLANSNS ATLKLPYIGV TPNTSTEGLH NYWTILFAPL TPLAVPTGSP
460 470 480 490 500
TSVKVSLFVS PIDSAFYGLR FPIPFPTPQH WKTRAVPGAG SYGSVVAGQE
510 520 530 540 550
IPLVGYAPAA PPRDYLPGRV RNWLEYAARH SWERNLPWTA ADEVGDQLVS
560 570 580 590 600
YPIQPETLAN TQTNTAFVLS LFSQWRGSLQ ISLIFTGPAQ CYGRLLLAYT
610 620 630 640 650
PPSANPPTTI EEANNGTYDV WDVNGDSTYT FTIPFCSQAY WKTVDIGTSS
660 670 680 690 700
GLVSNNGYFT IFVMNPLVTP GPSPPSATVA AFLHVADDFD VRLPQCPALG
710 720 730 740 750
FQSGADGAEV QPAPTSDLSD GNPTTDPAPR DNFDYPHHPV DPSTDLAFYF
760 770 780 790 800
SQYRWFGLNE DLTPLNVTGG LFYHVSLNPV NFQQNSLLSV LGAFTYVYAN
810 820 830 840 850
LSLNINVSAP LQACTFYIFY APPGASVPST QTLAELSFFT HTATPLNLAA
860 870 880 890 900
PTNITVSIPY ASPQSVLCTS FGGFGLQNGG DPGNLHSNTW GTLILYVDLP
910 920 930 940 950
QSDSVSVSAY ISFRDFEAYV PRQTPGVGPI PTSTSIVRVA RPTPKPRTVR
960 970 980 990 1000
RQGGTLADLI LTPESRCFIV AHTTAPYYSI LLVNPDEEYA ISMFTHGDES
1010 1020 1030 1040 1050
ILRYSSRGGT RLAPTAPAFF LCAAASVDTI LPYPISQSHL WLSDLTGIPL
1060 1070 1080 1090 1100
RAVPPLTLFL SAGAALCAGA QTLIAVAQGG SAPDTPPTPN RALFRRQGLG
1110 1120 1130 1140 1150
DLPDAAKGLS AALENVAKVA GDADIATSSQ AIASSINSLS NSIDGATTFM
1160 1170 1180 1190 1200
QNFFSGLAPK NPTSPLQHLF AKLIKWVTKI IGSLIIICNN PTPSALIGVS
1210 1220 1230 1240 1250
LMLCGDLAED ITEFFSNLGN PLAAVFYRCA RALGLSPTPQ SAAQAAGGRQ
1260 1270 1280 1290 1300
GVRDYNDIMS ALRNTDWFFE KIMSHIKNLL EWLGVLVKDD PRTKLNSQHE
1310 1320 1330 1340 1350
KILELYTDSV TASSTPPSEL SADAIRSNLD LAKQLLTLSH AANSVTHIQL
1360 1370 1380 1390 1400
CTRAITNYST ALSAISLVGT PGTRPEPLVV YLYGPPGTGK SLLASLLAST
1410 1420 1430 1440 1450
LAQALSGDPN NYYSPSSPDC KFYDGYSGQP VHYIDDIGQD PDGADWADFV
1460 1470 1480 1490 1500
NIVSSAPFIV PMADVNDKGR FYTSRVVIVT SNFPGPNPRS ARCVAALERR
1510 1520 1530 1540 1550
LHIRLNVTAR DGAAFSAAAA LKPSEPLAAT RYCKFSNPLT QFSMFNLAVD
1560 1570 1580 1590 1600
YKSIVLPNTP LSCFDELIDF ILGSLRDRAS VNSLLSGMVR TDVARQGGNA
1610 1620 1630 1640 1650
DAPAPSAAPL PSVLPSVPSQ DPFVRAVNEN RPVSFLSKIW SWRAPIFAAS
1660 1670 1680 1690 1700
SFLSLIAATL TIVRCLRDLR STQGAYSGTP VPKPRKKDLP KQPVYSGPVR
1710 1720 1730 1740 1750
RQGFDPAVMK IMGNVDSFVT LSGSKPIWTM SCLWIGGRNL IAPSHAFVSD
1760 1770 1780 1790 1800
DYEITHIRVG SRTLDVSRVT RVDDGELSLI SVPDGPEHKS LIRYIRSASP
1810 1820 1830 1840 1850
KSGILASKFS DTPVFVSFWN GKPHSTPLPG VVDEKDSFTY RCSSFQGLCG
1860 1870 1880 1890 1900
SPMIATDPGG LGILGIHVAG VAGYNGFSAR LTPERVQAFL SNLATPQSVL
1910 1920 1930 1940 1950
HFHPPMGPPA HVSRRSRLHP SPAFGAFPIT KEPAALSRKD PRLPEGTDLD
1960 1970 1980 1990 2000
AITLAKHDKG DIATPWPCME EAADWYFSQL PDSLPVLSQE DAIRGLDHMD
2010 2020 2030 2040 2050
AIDLSQSPGY PWTTQGRSRR SLFDEDGNPV PELQKAIDSV WDGGSYIYQS
2060 2070 2080 2090 2100
FLKDELRPTA KARAGKTRIV EAAPIQAIVV GRRLLGSLIN HLQGNPLQYG
2110 2120 2130 2140 2150
SAVGCNPDIH WTQIFHSLTP FSNVWSIDYS CFDATIPSVL LSAIASRIAS
2160 2170 2180 2190 2200
RSDQPGRVLD YLSYTTTSYH VYDSLWYTMV GGNPSGCVGT SILNTIANNI
2210 2220 2230 2240 2250
AIISAMMYCN KFDPRDPPVL YCYGDDLIWG SNQDFHPREL QAFYQKFTNF
2260 2270 2280 2290 2300
VVTPADKASD FPDSSSIYDI TFLKRYFVPD DIHPHLIHPV MDEATLTNSI
2310 2320 2330 2340 2350
MWLRGGEFEE VLRSLETLAF HSGPNNYSTW CEKIKAKIRE NGCDATFTPY
2360 2370
SVLQRGWVST CMTGPYPLTG
Length:2,370
Mass (Da):255,138
Last modified:September 1, 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:iD8B0F432F127C715
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
GQ184145 Genomic RNA Translation: ACS91540.1

NCBI Reference Sequences

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RefSeqi
YP_003065643.1, NC_012986.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
8187145

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
vg:8187145

<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
GQ184145 Genomic RNA Translation: ACS91540.1
RefSeqiYP_003065643.1, NC_012986.1

3D structure databases

SMRiC6KEF6
ModBaseiSearch...

Protein-protein interaction databases

IntActiC6KEF6, 1 interactor

PTM databases

iPTMnetiC6KEF6

Genome annotation databases

GeneIDi8187145
KEGGivg:8187145

Family and domain databases

CDDicd00205, rhv_like, 3 hits
Gene3Di2.40.10.10, 2 hits
2.60.120.20, 4 hits
3.30.70.270, 2 hits
InterProiView protein in InterPro
IPR043502, DNA/RNA_pol_sf
IPR004004, Helic/Pol/Pept_Calicivir-typ
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001676, Picornavirus_capsid
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR033703, Rhv-like
IPR001205, RNA-dir_pol_C
IPR007094, RNA-dir_pol_PSvirus
IPR029053, Viral_coat
PfamiView protein in Pfam
PF00680, RdRP_1, 1 hit
PF00073, Rhv, 2 hits
PF00910, RNA_helicase, 1 hit
PRINTSiPR00918, CALICVIRUSNS
SUPFAMiSSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS51874, PCV_3C_PRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51218, SF3_HELICASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_HKV1
<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: C6KEF6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 16, 2019
Last sequence update: September 1, 2009
Last modified: October 7, 2020
This is version 74 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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