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Entry version 152 (02 Jun 2021)
Sequence version 2 (23 Jan 2007)
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Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Bovine immunodeficiency virus (strain R29) (BIV) (Bovine immunodeficiency-like 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>
-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

Matrix protein p16 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane.

By similarity

Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Interaction between incoming particle-associated Gag proteins and host dynein allows intracellular microtubule-dependent virus transport toward the perinuclear region, prior to nucleus translocation and integration into host genome.

1 Publication

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 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 primer. 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 (By similarity).

By similarity

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 (By similarity).

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 switching 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 (By similarity).By similarity
The sequence shown is that of isolate R29-127.

<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

  • Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus. EC:3.1.26.13
  • 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. EC:3.1.13.2

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 sitei497PROSITE-ProRule annotation1

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 fingeri403 – 420CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri421 – 438CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1199 – 1240Integrase-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 bindingi1419 – 1465Integrase-typePROSITE-ProRule annotationAdd BLAST47

<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 processCytoplasmic inwards viral transport, DNA integration, DNA recombination, Host-virus interaction, Microtubular inwards viral transport, Viral genome integration, Viral release from host cell, Virion maturation, Virus entry into host cell
LigandMagnesium, Metal-binding, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
A02.005

<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
Alternative name(s):
Pr170Gag-Pol
Cleaved into the following 8 chains:
Matrix protein p16
Short name:
MA
Capsid protein p26
Short name:
CA
Alternative name(s):
p11
Protease (EC:3.4.23.-)
Alternative name(s):
P119
Retropepsin
Reverse transcriptase/ribonuclease H (EC:2.7.7.49, EC:2.7.7.7, EC:3.1.26.13)
Short name:
RT
Alternative name(s):
Exoribonuclease H (EC:3.1.13.2)
P72
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:gag-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>OrganismiBovine immunodeficiency virus (strain R29) (BIV) (Bovine immunodeficiency-like virus)
<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 identifieri417296 [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 lineageiVirusesRiboviriaPararnaviraeArtverviricotaRevtraviricetesOrterviralesRetroviridaeOrthoretrovirinaeLentivirus
<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 hostiBos taurus (Bovine) [TaxID: 9913]

<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, 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 '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_00002723241 – 1475Gag-Pol polyproteinAdd BLAST1475
ChainiPRO_00002723251 – 126Matrix protein p16Sequence analysisAdd BLAST126
<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_0000272326127 – 148p2LBy similarityAdd BLAST22
ChainiPRO_0000272327149 – 367Capsid protein p26Sequence analysisAdd BLAST219
PeptideiPRO_0000272328368 – 392p3By similarityAdd BLAST25
ChainiPRO_0000272329393 – 472Transframe peptideSequence analysisAdd BLAST80
ChainiPRO_0000038823473 – 562ProteaseSequence analysisAdd BLAST90
ChainiPRO_0000038824563 – 1193Reverse transcriptase/ribonuclease HSequence analysisAdd BLAST631
ChainiPRO_00000388251194 – 1475IntegraseSequence analysisAdd BLAST282

<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. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity).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>Sitei126 – 127Cleavage; by viral proteaseSequence analysis2
Sitei148 – 149Cleavage; by viral proteaseSequence analysis2
Sitei367 – 368Cleavage; by viral proteaseBy similarity2
Sitei392 – 393Cleavage; by viral proteaseBy similarity2
Sitei472 – 473Cleavage; by viral proteaseSequence analysis2
Sitei562 – 563Cleavage; by viral proteaseSequence analysis2
Sitei1193 – 1194Cleavage; by viral proteaseSequence analysis2

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

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

Interacts with host light chain cytoplasmic dynein DYNLL1; this interaction is critical for intracellular microtubule-dependent viral genome transport.

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

11475
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
P19560

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
P19560

<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>Domaini492 – 565Peptidase A2PROSITE-ProRule annotationAdd BLAST74
Domaini619 – 806Reverse transcriptasePROSITE-ProRule annotationAdd BLAST188
Domaini999 – 1119RNase HPROSITE-ProRule annotationAdd BLAST121
Domaini1248 – 1400Integrase catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni130 – 159DisorderedSequence analysisAdd BLAST30

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi130 – 154Polar residuesSequence analysisAdd BLAST25

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri403 – 420CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri421 – 438CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1199 – 1240Integrase-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Family and domain databases

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
3.30.420.10, 2 hits
3.30.70.270, 2 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
IPR000721, Gag_p24
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
IPR010661, RVT_thumb
IPR001878, Znf_CCHC
IPR036875, Znf_CCHC_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00607, Gag_p24, 1 hit
PF00552, IN_DBD_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
PF06817, RVT_thumb, 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
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 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
Note: This strategy of translation probably allows the virus to modulate the quantity of each viral protein.
Isoform Gag-Pol polyprotein (identifier: P19560-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><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
MKRRELEKKL RKVRVTPQQD KYYTIGNLQW AIRMINLMGI KCVCDEECSA
60 70 80 90 100
AEVALIITQF SALDLENSPI RGKEEVAIKN TLKVFWSLLA GYKPESTETA
110 120 130 140 150
LGYWEAFTYR EREARADKEG EIKSIYPSLT QNTQNKKQTS NQTNTQSLPA
160 170 180 190 200
ITTQDGTPRF DPDLMKQLKI WSDATERNGV DLHAVNILGV ITANLVQEEI
210 220 230 240 250
KLLLNSTPKW RLDVQLIESK VREKENAHRT WKQHHPEAPK TDEIIGKGLS
260 270 280 290 300
SAEQATLISV ECRETFRQWV LQAAMEVAQA KHATPGPINI HQGPKEPYTD
310 320 330 340 350
FINRLVAALE GMAAPETTKE YLLQHLSIDH ANEDCQSILR PLGPNTPMEK
360 370 380 390 400
KLEACRVVGS QKSKMQFLVA AMKEMGIQSP IPAVLPHTPE AYASQTSGPE
410 420 430 440 450
DGRRCYGCGK TGHLKRNCKQ QKCYHCGKPG HQARNCRSKN REVLLCPLWA
460 470 480 490 500
EEPTTEQFSP EQHEFCDPIC TPSYIRLDKQ PFIKVFIGGR WVKGLVDTGA
510 520 530 540 550
DEVVLKNIHW DRIKGYPGTP IKQIGVNGVN VAKRKTHVEW RFKDKTGIID
560 570 580 590 600
VLFSDTPVNL FGRSLLRSIV TCFTLLVHTE KIEPLPVKVR GPGPKVPQWP
610 620 630 640 650
LTKEKYQALK EIVKDLLAEG KISEAAWDNP YNTPVFVIKK KGTGRWRMLM
660 670 680 690 700
DFRELNKITV KGQEFSTGLP YPPGIKECEH LTAIDIKDAY FTIPLHEDFR
710 720 730 740 750
PFTAFSVVPV NREGPIERFQ WNVLPQGWVC SPAIYQTTTQ KIIENIKKSH
760 770 780 790 800
PDVMLYQYMD DLLIGSNRDD HKQIVQEIRD KLGSYGFKTP DEKVQEERVK
810 820 830 840 850
WIGFELTPKK WRFQPRQLKI KNPLTVNELQ QLVGNCVWVQ PEVKIPLYPL
860 870 880 890 900
TDLLRDKTNL QEKIQLTPEA IKCVEEFNLK LKDPEWKDRI REGAELVIKI
910 920 930 940 950
QMVPRGIVFD LLQDGNPIWG GVKGLNYDHS NKIKKILRTM NELNRTVVIM
960 970 980 990 1000
TGREASFLLP GSSEDWEAAL QKEESLTQIF PVKFYRHSCR WTSICGPVRE
1010 1020 1030 1040 1050
NLTTYYTDGG KKGKTAAAVY WCEGRTKSKV FPGTNQQAEL KAICMALLDG
1060 1070 1080 1090 1100
PPKMNIITDS RYAYEGMREE PETWAREGIW LEIAKILPFK QYVGVGWVPA
1110 1120 1130 1140 1150
HKGIGGNTEA DEGVKKALEQ MAPCSPPEAI LLKPGEKQNL ETGIYMQGLR
1160 1170 1180 1190 1200
PQSFLPRADL PVAITGTMVD SELQLQLLNI GTEHIRIQKD EVFMTCFLEN
1210 1220 1230 1240 1250
IPSATEDHER WHTSPDILVR QFHLPKRIAK EIVARCQECK RTTTSPVRGT
1260 1270 1280 1290 1300
NPRGRFLWQM DNTHWNKTII WVAVETNSGL VEAQVIPEET ALQVALCILQ
1310 1320 1330 1340 1350
LIQRYTVLHL HSDNGPCFTA HRIENLCKYL GITKTTGIPY NPQSQGVVER
1360 1370 1380 1390 1400
AHRDLKDRLA AYQGDCETVE AALSLALVSL NKKRGGIGGH TPYEIYLESE
1410 1420 1430 1440 1450
HTKYQDQLEQ QFSKQKIEKW CYVRNRRKEW KGPYKVLWDG DGAAVIEEEG
1460 1470
KTALYPHRHM RFIPPPDSDI QDGSS
Note: Produced by -1 ribosomal frameshifting at the gag-pol genes boundary.
Length:1,475
Mass (Da):168,063
Last modified:January 23, 2007 - 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:i4D249DCBB6158A78
GO
Isoform Gag polyprotein (identifier: P19558-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P19558.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:476
Mass (Da):53,440
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti17P → L in strain: Isolate R29-106 and Isolate R29-Nadin. 1
Natural varianti117D → E in strain: Isolate R29-106. 1
Natural varianti454T → I in strain: Isolate R29-Nadin. 1
Natural varianti577V → I in strain: Isolate R29-Nadin. 1
Natural varianti645R → K in strain: Isolate R29-Nadin. 1
Natural varianti729V → I in strain: Isolate R29-Nadin. 1
Natural varianti1095V → I in strain: Isolate R29-Nadin. 1
Natural varianti1226K → R in strain: Isolate R29-106 and Isolate R29-Nadin. 1
Natural varianti1244T → A in strain: Isolate R29-106 and Isolate R29-Nadin. 1

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M32690 Genomic RNA Translation: AAA91271.1 Sequence problems.
L04972 Genomic DNA Translation: AAA42767.1 Sequence problems.

Protein sequence database of the Protein Information Resource

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PIRi
B34742, GNLJBT

Keywords - Coding sequence diversityi

Ribosomal frameshifting

<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
M32690 Genomic RNA Translation: AAA91271.1 Sequence problems.
L04972 Genomic DNA Translation: AAA42767.1 Sequence problems.
PIRiB34742, GNLJBT

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KKRX-ray2.45A1257-1405[»]
3KKSX-ray2.20A/B1257-1405[»]
SMRiP19560
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiA02.005

Miscellaneous databases

EvolutionaryTraceiP19560

Protein Ontology

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PROi
PR:P19560

Family and domain databases

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
3.30.420.10, 2 hits
3.30.70.270, 2 hits
InterProiView protein in InterPro
IPR001969, Aspartic_peptidase_AS
IPR043502, DNA/RNA_pol_sf
IPR000721, Gag_p24
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
IPR010661, RVT_thumb
IPR001878, Znf_CCHC
IPR036875, Znf_CCHC_sf
PfamiView protein in Pfam
PF00607, Gag_p24, 1 hit
PF00552, IN_DBD_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
PF06817, RVT_thumb, 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
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 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

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MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOL_BIV29
<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: P19560
Secondary accession number(s): P19561, Q65593
<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: February 1, 1991
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 152 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
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