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Entry version 90 (08 May 2019)
Sequence version 2 (31 Jan 2018)
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Protein

Gag-Pol polyprotein

Gene

pol

Organism
Woolly monkey sarcoma virus (WMSV) (Smian sarcoma-associated virus)
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>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

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

Gag-Pol polyprotein: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release.By similarity
Matrix protein p15: Targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the pre-integration complex.By similarity
RNA-binding phosphoprotein p12: Constituent of the pre-integration complex (PIC) which tethers the latter to mitotic chromosomes. This allows the integration of the viral genome into the host DNA.By similarity
Capsid protein p30: Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.By similarity
Nucleocapsid protein p10-Pol: Involved in the packaging and encapsidation of two copies of the genome (By similarity). Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome (By similarity). This binding is dependent on genome dimerization (By similarity). Acts as a nucleic acid chaperone which is involved in rearrangement of nucleic acid secondary structures during gRNA retrotranscription (By similarity).By similarity
Protease: 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
Reverse transcriptase/ribonuclease H: 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 perform 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 perform 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.Sequence analysis
Integrase: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step that requires cell division, the PIC enters cell nucleus. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The last step is viral DNA integration into host chromosome.By similarity

Miscellaneous

Gag-Pol polyprotein: This protein is translated as a gag-pol fusion protein by episodic readthrough of the gag protein termination codon. Readthrough of the terminator codon TAG occurs between the codons for 521-Asp and 523-Gly.By similarity
Nucleocapsid protein p10-Pol: Nucleocapsid protein p10-Pol released from Pol polyprotein (NC-pol) is a few amino acids shorter than the nucleocapsid protein p10 released from Gag polyprotein (NC-gag).By similarity
Reverse transcriptase/ribonuclease H: 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_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

<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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Protease: Most efficiently inhibited by Amprenavir, which is able to block Gag-Pol processing in infected cells.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei549Protease; shared with dimeric partnerPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi789Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi863Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi864Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1180Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1200Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1221Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1291MagnesiumPROSITE-ProRule annotation1
Metal bindingi1405Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation1
Metal bindingi1464Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 fingeri490 – 507CCHC-typePROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1339 – 1377HHCC-typeBy similarityAdd BLAST39

<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 functionAspartyl protease, DNA-binding, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed DNA polymerase, Transferase, Viral nucleoprotein
Biological processDNA integration, DNA recombination, Host-virus interaction, Viral genome integration, Virus entry into host cell
LigandMagnesium, Metal-binding, Zinc

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_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:
Gag-Pol polyprotein
Cleaved into the following 7 chains:
Matrix protein p15
Short name:
MA
Alternative name(s):
pp12
Capsid protein p30
Short name:
CA
Protease (EC:3.4.23.-PROSITE-ProRule annotation)
Short name:
PR
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):
p80
Integrase (EC:2.7.7.-, EC:3.1.-.-)
Short name:
IN
Alternative name(s):
p46
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_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>OrganismiWoolly monkey sarcoma virus (WMSV) (Smian sarcoma-associated virus)
<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 identifieri11970 [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 lineageiVirusesOrterviralesRetroviridaeOrthoretrovirinaeGammaretrovirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 hostiLagothrix (woolly monkeys) [TaxID: 9518]
<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
  • UP000167400 <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
  • UP000203831 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

Gag-Pol polyprotein :
Matrix protein p15 :
Capsid protein p30 :
Nucleocapsid protein p10-Pol :
Protease :
RNA-binding phosphoprotein p12 :

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host endosome, Host membrane, Membrane, Viral matrix protein, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2983

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedSequence analysis
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001254972 – 1687Gag-Pol polyproteinAdd BLAST1686
ChainiPRO_00004428672 – 128Matrix protein p15Add BLAST127
ChainiPRO_0000442868129 – 196RNA-binding phosphoprotein p12Add BLAST68
ChainiPRO_0000442869197 – 455Capsid protein p30Add BLAST259
ChainiPRO_0000442870456 – 517Nucleocapsid protein p10-PolAdd BLAST62
ChainiPRO_0000442871518 – 641ProteaseAdd BLAST124
ChainiPRO_0000442872642 – 1310Reverse transcriptase/ribonuclease HAdd BLAST669
ChainiPRO_00004428731311 – 1683IntegraseAdd BLAST373

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Lipidationi2N-myristoyl glycine; by hostSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation.By similarity
RNA-binding phosphoprotein p12: Phosphorylated on serine residues.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>Sitei128 – 129Cleavage; by viral proteaseBy similarity2
Sitei196 – 197Cleavage; by viral proteaseBy similarity2
Sitei455 – 456Cleavage; by viral proteaseBy similarity2
Sitei517 – 518Cleavage; by viral proteaseBy similarity2
Sitei641 – 642Cleavage; by viral proteaseBy similarity2
Sitei1310 – 1311Cleavage; by viral proteaseBy similarity2

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P03359

<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 p30: Homohexamer; further associates as homomultimer (By similarity). Capsid protein p30: The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers (By similarity). Gag-Pol polyprotein: Interacts (via PPXY motif) with host NEDD4 (By similarity). Gag-Pol polyprotein: Interacts (via PSAP motif) with host TSG101 (By similarity). Reverse transcriptase/ribonuclease H: The reverse transcriptase is a monomer (Potential). Reverse transcriptase/ribonuclease H: Interacts (via RNase domains) with host release factor ETF1; this interaction is essential for translational readthrough of amber codon between viral gag and pol genes, as well as for viral replication (By similarity). Integrase: Homodimer (By similarity).PROSITE-ProRule annotationBy similarity

<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>Domaini544 – 614Peptidase A2PROSITE-ProRule annotationAdd BLAST71
Domaini721 – 912Reverse transcriptasePROSITE-ProRule annotationAdd BLAST192
Domaini1171 – 1299RNase HPROSITE-ProRule annotationAdd BLAST129
Domaini1394 – 1552Integrase catalyticPROSITE-ProRule annotationAdd BLAST159

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili408 – 455Sequence analysisAdd BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi108 – 111PTAP/PSAP motifBy similarity4
Motifi140 – 143PPXY motifBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi92 – 217Pro-richPROSITE-ProRule annotationAdd BLAST126
Compositional biasi134 – 137Poly-LeuSequence analysis4
Compositional biasi1677 – 1682Poly-ArgSequence analysis6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Gag polyprotein: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which potentially interacts with the UEV domain of TSG101.By similarity

<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 fingeri490 – 507CCHC-typePROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1339 – 1377HHCC-typeBy similarityAdd BLAST39

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
416at10239

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06095 RP_RTVL_H_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.150.180, 1 hit
1.10.375.10, 1 hit
2.40.70.10, 1 hit
3.30.420.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR000840 G_retro_matrix
IPR036946 G_retro_matrix_sf
IPR003036 Gag_P30
IPR001584 Integrase_cat-core
IPR040643 MLVIN_C
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR018061 Retropepsins
IPR008919 Retrov_capsid_N
IPR010999 Retrovr_matrix
IPR012337 RNaseH-like_sf
IPR002156 RNaseH_domain
IPR036397 RNaseH_sf
IPR034145 RP_RTVL-H-like
IPR000477 RT_dom
IPR041577 RT_RNaseH_2
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf
IPR015416 Znf_H2C2_histone_UAS-bd

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01140 Gag_MA, 1 hit
PF02093 Gag_p30, 1 hit
PF18697 MLVIN_C, 1 hit
PF00075 RNase_H, 1 hit
PF17919 RT_RNaseH_2, 1 hit
PF00665 rve, 1 hit
PF00077 RVP, 1 hit
PF00078 RVT_1, 1 hit
PF00098 zf-CCHC, 1 hit
PF09337 zf-H2C2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00343 ZnF_C2HC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47836 SSF47836, 1 hit
SSF47943 SSF47943, 1 hit
SSF50630 SSF50630, 1 hit
SSF53098 SSF53098, 2 hits
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
PS50879 RNASE_H, 1 hit
PS50878 RT_POL, 1 hit
PS50158 ZF_CCHC, 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>. 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_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.

P03359-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGQNNSTPLS LTLDHWKDVR TRAHNLSVKI RKGKWQTFCS SEWPTFGVGW
60 70 80 90 100
PPEGTFNLSV IFAVKRIVFQ ETGGHPDQVP YIVVWQDLAQ SPPPWVPPSA
110 120 130 140 150
KIAVVSSPEN TRGPSAGRPS APPRPPIYPA TDDLLLLSEP PPYPAALPPP
160 170 180 190 200
LAPPAVGPAP GQAPDSSDPE GPAAGTRSRR ARSPADDSGP DSTVILPLRA
210 220 230 240 250
IGPPAEPNGL VPLQYWPFSS ADLYNWKSNH PSFSENPAGL TGLLESLMFS
260 270 280 290 300
HQPTWDDCQQ LLQILFTTEE RERILLEARK NVLGDNGAPT QLENLINEAF
310 320 330 340 350
PLNRPQWDYN TAAGRERLLV YRRTLVAGLK GAARRPTNLA KVREVLQGPA
360 370 380 390 400
EPPSVFLERL MEAYRRYTPF DPSEEGQQAA VAMAFIGQSA PDIKKKLQRL
410 420 430 440 450
EGLQDYSLQD LVREAEKVYH KRETEEERQE REKKEAEERE RRRDRRQEKN
460 470 480 490 500
LTRILAAVVS ERGSRDRQTG NLSNRARKTP RDGRPPLDKD QCAYCKEKGH
510 520 530 540 550
WARECPQKKN VREAKVLALD DQGSRGSDPL PEPRVTLTVE GTPIEFLVDT
560 570 580 590 600
GAEHSVLTQP MGKVGSRRTV VEGATGSKVY PWTTKRLLKI GHKQVTHSFL
610 620 630 640 650
VIPECPAPLL GRDLLTKLKA QIQFSAEGPQ VTWEDRPTMC LVLNLEEEYR
660 670 680 690 700
LHEKPVPSSI DPSWLQLFPT VWAERAGMGL ANQVPPVVVE LRSGASPVAV
710 720 730 740 750
RQYPMSKEAR EGIRPHIQRF LDLGVLVPCQ SPWNTPLLPV KKPGTNDYRP
760 770 780 790 800
VQDLREINKR VQDIHPTVPN PYNLLSSLPP SHTWYSVLDL KDAFFCLKLH
810 820 830 840 850
PNSQPLFAFE WRDPEKGNTG QLTWTRLPQG FKNSPTLFDE ALHRDLAPFR
860 870 880 890 900
ALNPQVVLLQ YVDDLLVAAP TYRDCKEGTQ KLLQELSKLG YRVSAKKAQL
910 920 930 940 950
CQKEVTYLGY LLKEGKRWLT PARKATVMKI PPPTTPRQVR EFLGTAGFCR
960 970 980 990 1000
LWIPGFASLA APLYPLTKES IPFIWTEEHQ KAFDRIKEAL LSAPALALPD
1010 1020 1030 1040 1050
LTKPFTLYVD ERAGVARGVL TQTLGPWRRP VAYLSKKLDP VASGWPTCLK
1060 1070 1080 1090 1100
AVAAVALLLK DADKLTLGQN VTVIASHSLE SIVRQPPDRW MTNARMTHYQ
1110 1120 1130 1140 1150
SLLLNERVSF APPAVLNPAT LLPVESEATP VHRCSEILAE ETGTRRDLKD
1160 1170 1180 1190 1200
QPLPGVPAWY TDGSSFIAEG KRRAGAAIVD GKRTVWASSL PEGTSAQKAE
1210 1220 1230 1240 1250
LVALTQALRL AEGKDINIYT DSRYAFATAH IHGAIYKQRG LLTSAGKDIK
1260 1270 1280 1290 1300
NKEEILALLE AIHLPKRVAI IHCPGHQKGN DPVATGNRRA DEAAKQAALS
1310 1320 1330 1340 1350
TRVLAETTKP QELIXPAQVK TRPGELTPDR GKEFIQRLHQ LTHLGPEKLL
1360 1370 1380 1390 1400
QLVNRTSLLI PNLQSAVREV TSQCQACAMT NAVTTYRETG KRQRGDRPGV
1410 1420 1430 1440 1450
YWEVDFTEVK PGRYGNRYLL VFIDTFSGWV EAFPTKTETA LTVCKKILEE
1460 1470 1480 1490 1500
ILPRFGIPKV LGSDNGPAFV AQVSQGLATQ LGINWKLHCA YRPQSSGQVE
1510 1520 1530 1540 1550
RMNRTIKETL TKLALETGXK DWVALLPLAL LRARNTPGRF GLTPYEILYG
1560 1570 1580 1590 1600
GPPPILESGG TLGPDDNFLP VLFTHLKALE VVRTQIWDQI KEVYKPGTVA
1610 1620 1630 1640 1650
IPHPFQVGDQ VLVRRHRPGS LEPRWKGPYL VLLTTPTAVK VDGIAAWVHA
1660 1670 1680
SHLKPAPPSA PDESWELEKA DHPLKLRIRR RRNESAK
Length:1,687
Mass (Da):188,011
Last modified:January 31, 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:i4E5B6C98176DE554
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 ALV83312 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA24515 differs from that shown.Curated

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

More...
DDBJi
Links Updated
KT724051 Genomic DNA Translation: ALV83312.1 Different initiation.
V01201 Genomic DNA Translation: CAA24515.1 Sequence problems.

Protein sequence database of the Protein Information Resource

More...
PIRi
A05071

NCBI Reference Sequences

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RefSeqi
YP_001165470.1, NC_009424.4

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5176146

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:5176146

<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
KT724051 Genomic DNA Translation: ALV83312.1 Different initiation.
V01201 Genomic DNA Translation: CAA24515.1 Sequence problems.
PIRiA05071
RefSeqiYP_001165470.1, NC_009424.4

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Chemistry databases

ChEMBLiCHEMBL2983

Proteomic databases

PRIDEiP03359

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5176146
KEGGivg:5176146

Phylogenomic databases

OrthoDBi416at10239

Family and domain databases

CDDicd06095 RP_RTVL_H_like, 1 hit
Gene3Di1.10.150.180, 1 hit
1.10.375.10, 1 hit
2.40.70.10, 1 hit
3.30.420.10, 2 hits
InterProiView protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR000840 G_retro_matrix
IPR036946 G_retro_matrix_sf
IPR003036 Gag_P30
IPR001584 Integrase_cat-core
IPR040643 MLVIN_C
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR018061 Retropepsins
IPR008919 Retrov_capsid_N
IPR010999 Retrovr_matrix
IPR012337 RNaseH-like_sf
IPR002156 RNaseH_domain
IPR036397 RNaseH_sf
IPR034145 RP_RTVL-H-like
IPR000477 RT_dom
IPR041577 RT_RNaseH_2
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf
IPR015416 Znf_H2C2_histone_UAS-bd
PfamiView protein in Pfam
PF01140 Gag_MA, 1 hit
PF02093 Gag_p30, 1 hit
PF18697 MLVIN_C, 1 hit
PF00075 RNase_H, 1 hit
PF17919 RT_RNaseH_2, 1 hit
PF00665 rve, 1 hit
PF00077 RVP, 1 hit
PF00078 RVT_1, 1 hit
PF00098 zf-CCHC, 1 hit
PF09337 zf-H2C2, 1 hit
SMARTiView protein in SMART
SM00343 ZnF_C2HC, 1 hit
SUPFAMiSSF47836 SSF47836, 1 hit
SSF47943 SSF47943, 1 hit
SSF50630 SSF50630, 1 hit
SSF53098 SSF53098, 2 hits
SSF57756 SSF57756, 1 hit
PROSITEiView protein in PROSITE
PS50175 ASP_PROT_RETROV, 1 hit
PS00141 ASP_PROTEASE, 1 hit
PS50994 INTEGRASE, 1 hit
PS50879 RNASE_H, 1 hit
PS50878 RT_POL, 1 hit
PS50158 ZF_CCHC, 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 nameiPOL_WMSV
<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: P03359
Secondary accession number(s): A0A0U3TYK5
<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/Swiss-Prot: July 21, 1986
Last sequence update: January 31, 2018
Last modified: May 8, 2019
This is version 90 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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