Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 97 (08 May 2019)
Sequence version 2 (28 Feb 2018)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Gag-Pro polyprotein

Gene

pro

Organism
Simian retrovirus SRV-2
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

Matrix protein p10: Matrix protein.Curated
Nucleocapsid protein p14: Nucleocapsid protein.Curated
Capsid protein p27: capsid protein.Curated
Protease 17 kDa: 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 annotationBy similarity
Protease 13 kDa: 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 annotationBy similarity
G-patch peptide: Enhances the activity of the reverse transcriptase. May be part of the mature RT.By similarity

<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

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 sitei782Protease; shared with dimeric partnerPROSITE-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 fingeri544 – 561CCHC-typePROSITE-ProRule annotationAdd BLAST18

<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, Hydrolase, Protease, Viral nucleoprotein
Biological processNucleotide metabolism
LigandMagnesium, Metal-binding, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
A02.009

<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-Pro polyprotein
Cleaved into the following 9 chains:
Nucleocapsid protein-dUTPase (EC:3.6.1.23By similarity)
Short name:
NC-dUTPase
Protease 17 kDaBy similarity (EC:3.4.23.-PROSITE-ProRule annotation)
Protease 13 kDaBy similarity (EC:3.4.23.-PROSITE-ProRule annotation)
G-patch peptideBy similarity
<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:pro
Synonyms:prt
<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>OrganismiSimian retrovirus SRV-2
<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 identifieri39068 [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 lineageiVirusesOrterviralesRetroviridaeOrthoretrovirinaeBetaretrovirus
<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 hostiMacaca mulatta (Rhesus macaque) [TaxID: 9544]
<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
  • UP000007229 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

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

Protease 13 kDa :
Protease 17 kDa :

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Viral matrix 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 <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 methionineiRemoved; by hostBy similarity
<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_00001995522 – 908Gag-Pro polyproteinAdd BLAST907
ChainiPRO_00004432162 – 100Matrix protein p10By similarityAdd BLAST99
ChainiPRO_0000443217101 – 213Phosphorylated protein pp24By similarityAdd BLAST113
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000443218101 – 159By similarityAdd BLAST59
ChainiPRO_0000443219160 – 213Phosphorylated protein pp18By similarityAdd BLAST54
ChainiPRO_0000443220214 – 297p12By similarityAdd BLAST84
ChainiPRO_0000443221298 – 523Capsid protein p27By similarityAdd BLAST226
ChainiPRO_0000443222524 – 756Nucleocapsid protein-dUTPaseBy similarityAdd BLAST233
ChainiPRO_0000443223757 – 908Protease 17 kDaBy similarityAdd BLAST152
ChainiPRO_0000443224757 – 874Protease 13 kDaBy similarityAdd BLAST118
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_0000443225875 – 908G-patch peptideAdd BLAST34

<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

Protease 17 kDa: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa without the GDP domain.By similarity
Gag-Pro polyprotein: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles.By similarity
Gag-Pro polyprotein: Specific enzymatic cleavages in vivo yield mature proteins.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>Sitei100 – 101Cleavage; by viral proteaseBy similarity2
Sitei159 – 160Cleavage; by viral proteaseBy similarity2
Sitei213 – 214Cleavage; by viral proteaseBy similarity2
Sitei297 – 298Cleavage; by viral proteaseBy similarity2
Sitei523 – 524Cleavage; by viral proteaseBy similarity2
Sitei756 – 757Cleavage; by viral proteaseBy similarity2
Sitei874 – 875Cleavage; by viral proteaseBy similarity2

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P51518

<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

Protease 17 kDa: Homodimer. G-patch peptide: Interacts with the reverse transcriptase/ribonuclease H. Nucleocapsid protein-dUTPase: Homotrimer.By 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>Domaini777 – 853Peptidase A2PROSITE-ProRule annotationAdd BLAST77
Domaini864 – 908G-patchPROSITE-ProRule annotationAdd BLAST45

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 coili215 – 251Sequence analysisAdd BLAST37

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>Motifi200 – 203PPXY motifBy similarity4
Motifi208 – 211PTAP/PSAP 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 biasi627 – 630Poly-GlnSequence analysis4

<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 release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Phosphorylated protein pp24 and phosphorylated protein pp18 contains one L domain: a PPXY motif which binds to the WW domains of the ubiquitin ligase NEDD4.By similarity
Protease 17 kDa: The glycine-rich G-patch domain (GPD) is present at the C-terminus of the protease from which it is then detached by the protease itself.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri544 – 561CCHC-typePROSITE-ProRule annotationAdd BLAST18

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05482 HIV_retropepsin_like, 1 hit
cd07557 trimeric_dUTPase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.30, 1 hit
1.10.150.490, 1 hit
1.10.375.10, 1 hit
2.40.70.10, 1 hit
2.70.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR003322 B_retro_matrix
IPR038124 B_retro_matrix_sf
IPR029054 dUTPase-like
IPR036157 dUTPase-like_sf
IPR033704 dUTPase_trimeric
IPR000467 G_patch_dom
IPR000721 Gag_p24
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR034170 Retropepsin-like_cat_dom
IPR018061 Retropepsins
IPR008916 Retrov_capsid_C
IPR008919 Retrov_capsid_N
IPR010999 Retrovr_matrix
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00692 dUTPase, 1 hit
PF01585 G-patch, 1 hit
PF02337 Gag_p10, 1 hit
PF00607 Gag_p24, 1 hit
PF00077 RVP, 1 hit
PF00098 zf-CCHC, 1 hit

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD004265 B_retro_matrix_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00443 G_patch, 1 hit
SM00343 ZnF_C2HC, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47836 SSF47836, 1 hit
SSF47943 SSF47943, 1 hit
SSF50630 SSF50630, 1 hit
SSF51283 SSF51283, 1 hit
SSF57756 SSF57756, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50175 ASP_PROT_RETROV, 1 hit
PS00141 ASP_PROTEASE, 1 hit
PS50174 G_PATCH, 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>Sequences (3)i

<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.

This entry describes 3 <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-Pro polyprotein (identifier: P51518-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MGQELSQHEL YVEQLKKALK TRGVKVKGND LLKFFDFVKD TCPWFPQEGT
60 70 80 90 100
IDIKRWRRVG DCFQDYYNTF GPEKIPVTAF SYWNLIKDLI DKKEADPQVM
110 120 130 140 150
AAVTQTEKIL KVSSQTDLRD NSHNKDMDLI SLESDDEEAK APSEKMTMSN
160 170 180 190 200
KSPKKYPAML ASQNNNTDKD PDLSEVDWDG LEDEAAKYHN PDWPPFLSRP
210 220 230 240 250
PPYNRTAATA PAVMAVVNPK EELKEKISQL EEQIKLEELH QSLIIRLQKL
260 270 280 290 300
KTGNERVTSS GNIESHSRTP KWPGQCLPKG KYLINKNTEE YPPKDIFPVT
310 320 330 340 350
ETMDGQGQAW RHHNGFDFTV IKELKTAVSQ YGATAPYTLA IVESIADNWL
360 370 380 390 400
TPTDWNTLVR AVLSGGDHLI WKSEFFENCR DTAKRNQQAG NGWDFDMLTG
410 420 430 440 450
SGNYANTDAQ MQYDPGLFAQ IQAAATNAWR KLPVKGDPGA SLTGVKQGPD
460 470 480 490 500
EPFADFVHRL ITTAGRIFGN AEAGVDYVKQ LAYENANPAC QAAIRPYRKK
510 520 530 540 550
TDLTGYIRLC SDIGPSYQQG LAMAAAFSGQ TVKDLLNNKN KDRGGCFKCG
560 570 580 590 600
KKGHFAKDCR DHSNKNPESK VPGLCPRCKR GKHWANECKS KTDSQGNPLP
610 620 630 640 650
PHQGNRDEGP APGPEASLWG SQLCSSQQQQ SISKLNRASP GSAGLDLCST
660 670 680 690 700
THTVLTPEMG PQTLATGVYG PLPPNTFGLI LGRGSTTVKG LQIYPGVIDN
710 720 730 740 750
DYTGEFKIMA RAISSIITIP QGERIAQLVL LPLLRTAHKI QHPYRGDKNF
760 770 780 790 800
GSSDIFWVQP ITHQKPSLVL WLDGKAFTGL IDTGADVTII KQEDWPSHWP
810 820 830 840 850
TTETLTNLRG IGQSNNPRQS SKYLTWKDKE NNSGLIKPFV IPNLPVNLWG
860 870 880 890 900
RDLLSQMKIM MCSPNDIVTA QMLAQGYSPG KGLGKREDGI LQPIPNSGQL

DRKGFGNF
Note: Produced by -1 ribosomal frameshifting between gag-pro.1 Publication
Length:908
Mass (Da):100,877
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:iDF8D823B89B0845F
GO
Isoform Gag polyprotein (identifier: P51516-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P51516.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.1 Publication
Length:654
Mass (Da):73,220
GO
Isoform Gag-Pro-Pol polyprotein (identifier: P51517-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P51517.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshiftings between gag-pro and pro-pol.1 Publication
Length:1,768
Mass (Da):197,910
GO

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
M16605 Genomic RNA No translation available.

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
M16605 Genomic RNA No translation available.

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein family/group databases

MEROPSiA02.009

Proteomic databases

PRIDEiP51518

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd05482 HIV_retropepsin_like, 1 hit
cd07557 trimeric_dUTPase, 1 hit
Gene3Di1.10.1200.30, 1 hit
1.10.150.490, 1 hit
1.10.375.10, 1 hit
2.40.70.10, 1 hit
2.70.40.10, 1 hit
InterProiView protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR003322 B_retro_matrix
IPR038124 B_retro_matrix_sf
IPR029054 dUTPase-like
IPR036157 dUTPase-like_sf
IPR033704 dUTPase_trimeric
IPR000467 G_patch_dom
IPR000721 Gag_p24
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR034170 Retropepsin-like_cat_dom
IPR018061 Retropepsins
IPR008916 Retrov_capsid_C
IPR008919 Retrov_capsid_N
IPR010999 Retrovr_matrix
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf
PfamiView protein in Pfam
PF00692 dUTPase, 1 hit
PF01585 G-patch, 1 hit
PF02337 Gag_p10, 1 hit
PF00607 Gag_p24, 1 hit
PF00077 RVP, 1 hit
PF00098 zf-CCHC, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD004265 B_retro_matrix_N, 1 hit
SMARTiView protein in SMART
SM00443 G_patch, 1 hit
SM00343 ZnF_C2HC, 2 hits
SUPFAMiSSF47836 SSF47836, 1 hit
SSF47943 SSF47943, 1 hit
SSF50630 SSF50630, 1 hit
SSF51283 SSF51283, 1 hit
SSF57756 SSF57756, 2 hits
PROSITEiView protein in PROSITE
PS50175 ASP_PROT_RETROV, 1 hit
PS00141 ASP_PROTEASE, 1 hit
PS50174 G_PATCH, 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 nameiPRO_SRV2
<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: P51518
<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: October 1, 1996
Last sequence update: February 28, 2018
Last modified: May 8, 2019
This is version 97 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
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