Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website on Tuesday, June 28. Please explore and share your feedback. Take me to UniProt BETA

UniProtKB - P35956 (POL_VILVK)

Entry version 144 (23 Feb 2022)
Sequence version 2 (28 Feb 2018)
Previous versions | rss
Add a publicationFeedback
Protein

Gag-Pol polyprotein

Gene

pol

Organism
Maedi visna virus (strain KV1772) (MVV) (Visna lentivirus)
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

Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence.

By similarity

Targets the polyprotein to the plasma membrane.

By similarity

Forms the core that encapsulates the genomic RNA-nucleocapsid complex in the virion.

By similarity

Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearrangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination.

By similarity

The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell.

PROSITE-ProRule annotation

RT is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to perfom a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primers. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends.

PROSITE-ProRule annotation

Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions.

By similarity

Miscellaneous

The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template swiching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs.PROSITE-ProRule 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

  • 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. EC:3.1.13.2
  • Endonucleolytic cleavage to 5'-phosphomonoester.PROSITE-ProRule annotation EC:3.1.26.4

<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+PROSITE-ProRule annotationNote: The RT polymerase active site binds 2 magnesium ions.PROSITE-ProRule annotation

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 sitei464Protease; shared with dimeric partnerPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi652Magnesium 1; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi727Magnesium 1; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi728Magnesium 1; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi980Magnesium 2; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1012Magnesium 2; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1032Magnesium 2; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1085Magnesium 2; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1237ZincPROSITE-ProRule annotation1
Metal bindingi1241ZincPROSITE-ProRule annotation1
Metal bindingi1265ZincPROSITE-ProRule annotation1
Metal bindingi1268ZincPROSITE-ProRule annotation1
Metal bindingi1291Magnesium 3; catalytic; for integrase activityPROSITE-ProRule annotation1
Metal bindingi1343Magnesium 3; catalytic; for integrase activityPROSITE-ProRule annotation1
Metal bindingi1379Magnesium 3; catalytic; for integrase activityCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri385 – 402CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri404 – 421CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1228 – 1269Integrase-typePROSITE-ProRule annotationAdd BLAST42
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi1447 – 1499Integrase-typePROSITE-ProRule annotationAdd BLAST53

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionAspartyl protease, DNA-binding, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase
Biological processDNA integration, DNA recombination, Nucleotide metabolism, Viral genome integration, Virus entry into host cell
LigandMagnesium, Metal-binding, Zinc

Protein family/group databases

MEROPS protease database

More...MEROPSi		A02.006

<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:
Gag-Pol polyprotein
Cleaved into the following 7 chains:
Matrix protein p16
Capsid protein p25
Nucleocapsid protein p14
Protease (EC:3.4.23.-PROSITE-ProRule annotation)
Alternative name(s):
Retropepsin
Reverse transcriptase/ribonuclease H (EC:2.7.7.49PROSITE-ProRule annotation, EC:2.7.7.7PROSITE-ProRule annotation, EC:3.1.26.4PROSITE-ProRule annotation)
Short name:
RT
Alternative name(s):
Exoribonuclease H (EC:3.1.13.2)
Deoxyuridine 5'-triphosphate nucleotidohydrolase (EC:3.6.1.23Curated)
Short name:
dUTPase
Integrase (EC:2.7.7.-By similarity, EC:3.1.-.-By similarity)
Short name:
IN
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:pol
<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>OrganismiMaedi visna virus (strain KV1772) (MVV) (Visna lentivirus)
<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 identifieri36374 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiViruses › Riboviria › Pararnavirae › Artverviricota › Revtraviricetes › Ortervirales › Retroviridae › Orthoretrovirinae › Lentivirus ›
<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 hostiOvis aries (Sheep) [TaxID: 9940]

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

Keywords - Cellular componenti

Capsid protein, 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_00004433691 – 1506Gag-Pol polyproteinAdd BLAST1506
ChainiPRO_00004433701 – 143Matrix protein p16Add BLAST143
ChainiPRO_0000443371144 – 363Capsid protein p25Add BLAST220
ChainiPRO_0000443372364 – 442Nucleocapsid protein p14Add BLAST79
ChainiPRO_0000038869443 – 540ProteaseAdd BLAST98
ChainiPRO_0000038870541 – 1091Reverse transcriptase/ribonuclease HAdd BLAST551
ChainiPRO_00000388711092 – 1225Deoxyuridine 5'-triphosphate nucleotidohydrolaseAdd BLAST134
ChainiPRO_00000388721226 – 1506IntegraseAdd BLAST281

<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 yield mature proteins.Curated

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>Sitei363 – 364Cleavage; by viral proteaseBy similarity2

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P35956

<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

Homotetramer; further associates as a homohexadecamer.

1 Publication

<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

Secondary structure

11506
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P35956

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P35956

<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>Domaini459 – 530Peptidase A2PROSITE-ProRule annotationAdd BLAST72
Domaini587 – 776Reverse transcriptasePROSITE-ProRule annotationAdd BLAST190
Domaini971 – 1093RNase H type-1PROSITE-ProRule annotationAdd BLAST123
Domaini1270 – 1430Integrase catalyticPROSITE-ProRule annotationAdd BLAST161

<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 retroviral Pol polyprotein family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri385 – 402CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri404 – 421CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1228 – 1269Integrase-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Conserved Domains Database

More...CDDi		cd07557, trimeric_dUTPase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.200, 1 hit
1.10.1200.30, 1 hit
1.10.375.10, 1 hit
2.30.30.10, 1 hit
2.40.70.10, 1 hit
2.70.40.10, 1 hit
3.30.420.10, 2 hits
3.30.70.270, 3 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001969, Aspartic_peptidase_AS
IPR043502, DNA/RNA_pol_sf
IPR029054, dUTPase-like
IPR036157, dUTPase-like_sf
IPR033704, dUTPase_trimeric
IPR045345, Gag_p24_C
IPR000721, Gag_p24_N
IPR017856, Integrase-like_N
IPR036862, Integrase_C_dom_sf_retrovir
IPR001037, Integrase_C_retrovir
IPR001584, Integrase_cat-core
IPR003308, Integrase_Zn-bd_dom_N
IPR001995, Peptidase_A2_cat
IPR021109, Peptidase_aspartic_dom_sf
IPR018061, Retropepsins
IPR008916, Retrov_capsid_C
IPR008919, Retrov_capsid_N
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR012337, RNaseH-like_sf
IPR002156, RNaseH_domain
IPR036397, RNaseH_sf
IPR000477, RT_dom
IPR010659, RVT_connect
IPR001878, Znf_CCHC
IPR036875, Znf_CCHC_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00692, dUTPase, 1 hit
PF00607, Gag_p24, 1 hit
PF19317, Gag_p24_C, 1 hit
PF02022, Integrase_Zn, 1 hit
PF00075, RNase_H, 1 hit
PF00665, rve, 1 hit
PF00077, RVP, 1 hit
PF00078, RVT_1, 1 hit
PF06815, RVT_connect, 1 hit
PF00098, zf-CCHC, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00343, ZnF_C2HC, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46919, SSF46919, 1 hit
SSF47943, SSF47943, 1 hit
SSF50122, SSF50122, 1 hit
SSF50630, SSF50630, 1 hit
SSF51283, SSF51283, 1 hit
SSF53098, SSF53098, 2 hits
SSF56672, SSF56672, 1 hit
SSF57756, SSF57756, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50175, ASP_PROT_RETROV, 1 hit
PS00141, ASP_PROTEASE, 1 hit
PS50994, INTEGRASE, 1 hit
PS51027, INTEGRASE_DBD, 1 hit
PS50879, RNASE_H_1, 1 hit
PS50878, RT_POL, 1 hit
PS50158, ZF_CCHC, 2 hits
PS50876, ZF_INTEGRASE, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
Isoform Gag-Pol polyprotein (identifier: P35956-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAKQGSKEKK GYPELKEVIK ATCKIRVGPG KETLTEGNCL WALKTIDFIF 
        60         70         80         90        100
EDLKTEPWTI TKMYTVWDRL KGLTPEETSK REFASLQATL ACIMCSQMGM 
       110        120        130        140        150
KPETVQAAKG IISMKEGLHE NKEAKGEKVE QLYPNLEKHR EVYPIVNLQA 
       160        170        180        190        200
GGRSWKAVES VVFQQLQTVA MQHGLVSEDF ERQLAYYATT WTSKDILEVL 
       210        220        230        240        250
AMMPGNRAQK ELIQGKLNEE AERWVRQNPP GPNVLTVDQI MGVGQTNQQA 
       260        270        280        290        300
SQANMDQARQ ICLQWVITAL RSVRHMSHRP GNPMLVKQKN TESYEDFIAR 
       310        320        330        340        350
LLEAIDAEPV TDPIKTYLKV TLSYTNASTD CQKQMDRTLG TRVQQATVEE 
       360        370        380        390        400
KMQACRDVGS EGFKMQLLAQ ALRPQGKAGQ KGVNQKCYNC GKPGHLARQC 
       410        420        430        440        450
RQGIICHHCG KRGHMQKDCR QKKQQGKQQE GATCGAVRAP YVVTEAPPKI 
       460        470        480        490        500
EIKVGTRWKK LLVDTGADKT IVTSHDMSGI PKGRIILQGI GGIIEGEKWE 
       510        520        530        540        550
QVHLQYKDKI IRGTIVVLAT SPVEVLGRDN MRELGIGLIM ANLEEKKIPS 
       560        570        580        590        600
TRVRLKEGCK GPHIAQWPLT QEKLEGLKEI VDRLEKEGKV GRAPPHWTCN 
       610        620        630        640        650
TPIFCIKKKS GKWRMLIDFR ELNKQTEDLA EAQLGLPHPG GLQRKKHVTI 
       660        670        680        690        700
LDIGDAYFTI PLYEPYRQYT CFTMLSPNNL GPCVRYYWKV LPQGWKLSPA 
       710        720        730        740        750
VYQFTMQKIL RGWIEEHPMI QFGIYMDDIY IGSDLGLEEH RGIVNELASY 
       760        770        780        790        800
IAQYGFMLPE DKRQEGYPAK WLGFELHPEK WKFQKHTLPE ITEGPITLNK 
       810        820        830        840        850
LQKLVGDLVW RQSLIGKSIP NILKLMEGDR ALQSERYIES IHVREWEACR 
       860        870        880        890        900
QKLKEMEGNY YDEEKDIYGQ LDWGNKAIEY IVFQEKGKPL WVNVVHSIKN 
       910        920        930        940        950
LSQAQQIIKA AQKLTQEVII RTGKIPWILL PGREEDWILE LQMGNINWMP 
       960        970        980        990       1000
SFWSCYKGSV RWKKRNVIAE VVPGPTYYTD GGKKNGRGSL GYITSTGEKF 
      1010       1020       1030       1040       1050
RIHEEGTNQQ LELRAIEEAC KQGPEKMNIV TDSRYAYEFM LRNWDEEVIR 
      1060       1070       1080       1090       1100
NPIQARIMEL VHNKEKIGVH WVPGHKGIPQ NEEIDRYISE IFLAKEGRGI 
      1110       1120       1130       1140       1150
LQKRAEDAGY DLICPQEISI PAGQVKRIAI DLKINLKKDQ WAMIGTKSSF 
      1160       1170       1180       1190       1200
ANKGVFVQGG IIDSGYQGTI QVVIYNSNNK EVVIPQGRKF AQLILMPLIH 
      1210       1220       1230       1240       1250
EELEPWGETR KTERGEQGFG STGMYWIENI PLAEEEHNKW HQDAVSLHLE 
      1260       1270       1280       1290       1300
FGIPRTAAED IVQQCDVCQE NKMPSTLRGS NKRGIDHWQV DYTHYEDKII 
      1310       1320       1330       1340       1350
LVWVETNSGL IYAERVKGET GQEFRVQTMK WYAMFAPKSL QSDNGPAFVA 
      1360       1370       1380       1390       1400
ESTQLLMKYL GIEHTTGIPW NPQSQALVER THQTLKNTLE KLIPMFNAFE 
      1410       1420       1430       1440       1450
SALAGTLITL NIKRKGGLGT SPMDIFIFNK EQQRIQQQSK SKQEKIRFCY 
      1460       1470       1480       1490       1500
YRTRKRGHPG EWQGPTQVLW GGDGAIVVKD RGTDRYLVIA NKDVKFIPPP 

KEIQKE
Note: Produced by a -1 ribosomal frameshifting between gag and pol.1 Publication
Length:1,506
Mass (Da):171,957
Last modified:February 28, 2018 - v2
<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:iA51F80B2AEB4952A
GO
Isoform Gag polyprotein (identifier: P35955-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P35955.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:442
Mass (Da):49,857
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA48359 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAB25460 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L06906 Genomic RNA Translation: AAA48359.1 Sequence problems.
S55323 Genomic DNA Translation: AAB25460.1 Sequence problems.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

<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
L06906 Genomic RNA Translation: AAA48359.1 Sequence problems.
S55323 Genomic DNA Translation: AAB25460.1 Sequence problems.

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HPGX-ray3.28A/B/C/D/E/F1228-1445[»]
3HPHX-ray2.64A/B/C/D1228-1445[»]
5LLJX-ray1.78A/B1444-1501[»]
5M0Qelectron microscopy4.91A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1228-1506[»]
5M0Relectron microscopy8.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1228-1506[»]
5T3AX-ray2.50A1285-1506[»]
SMRiP35956
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiA02.006

Proteomic databases

PRIDEiP35956

Miscellaneous databases

EvolutionaryTraceiP35956

Family and domain databases

CDDicd07557, trimeric_dUTPase, 1 hit
Gene3Di1.10.10.200, 1 hit
1.10.1200.30, 1 hit
1.10.375.10, 1 hit
2.30.30.10, 1 hit
2.40.70.10, 1 hit
2.70.40.10, 1 hit
3.30.420.10, 2 hits
3.30.70.270, 3 hits
InterProiView protein in InterPro
IPR001969, Aspartic_peptidase_AS
IPR043502, DNA/RNA_pol_sf
IPR029054, dUTPase-like
IPR036157, dUTPase-like_sf
IPR033704, dUTPase_trimeric
IPR045345, Gag_p24_C
IPR000721, Gag_p24_N
IPR017856, Integrase-like_N
IPR036862, Integrase_C_dom_sf_retrovir
IPR001037, Integrase_C_retrovir
IPR001584, Integrase_cat-core
IPR003308, Integrase_Zn-bd_dom_N
IPR001995, Peptidase_A2_cat
IPR021109, Peptidase_aspartic_dom_sf
IPR018061, Retropepsins
IPR008916, Retrov_capsid_C
IPR008919, Retrov_capsid_N
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR012337, RNaseH-like_sf
IPR002156, RNaseH_domain
IPR036397, RNaseH_sf
IPR000477, RT_dom
IPR010659, RVT_connect
IPR001878, Znf_CCHC
IPR036875, Znf_CCHC_sf
PfamiView protein in Pfam
PF00692, dUTPase, 1 hit
PF00607, Gag_p24, 1 hit
PF19317, Gag_p24_C, 1 hit
PF02022, Integrase_Zn, 1 hit
PF00075, RNase_H, 1 hit
PF00665, rve, 1 hit
PF00077, RVP, 1 hit
PF00078, RVT_1, 1 hit
PF06815, RVT_connect, 1 hit
PF00098, zf-CCHC, 2 hits
SMARTiView protein in SMART
SM00343, ZnF_C2HC, 2 hits
SUPFAMiSSF46919, SSF46919, 1 hit
SSF47943, SSF47943, 1 hit
SSF50122, SSF50122, 1 hit
SSF50630, SSF50630, 1 hit
SSF51283, SSF51283, 1 hit
SSF53098, SSF53098, 2 hits
SSF56672, SSF56672, 1 hit
SSF57756, SSF57756, 1 hit
PROSITEiView protein in PROSITE
PS50175, ASP_PROT_RETROV, 1 hit
PS00141, ASP_PROTEASE, 1 hit
PS50994, INTEGRASE, 1 hit
PS51027, INTEGRASE_DBD, 1 hit
PS50879, RNASE_H_1, 1 hit
PS50878, RT_POL, 1 hit
PS50158, ZF_CCHC, 2 hits
PS50876, ZF_INTEGRASE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOL_VILVK
<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: P35956
<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: June 1, 1994
Last sequence update: February 28, 2018
Last modified: February 23, 2022
This is version 144 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again