UniProtKB - P03355 (POL_MLVMS)
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Protein
Gag-Pol polyprotein
Gene
gag-pol
Organism
Moloney murine leukemia virus (isolate Shinnick) (MoMLV)
Status
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.2 Publications
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 (PubMed:25209668).By similarity1 Publication
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 (Potential). Cleaves the translation initiation factor eIF4G leading to the inhibition of host cap-dependent translation (PubMed:14610163).PROSITE-ProRule annotation1 Publication
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.2 Publications
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 538-Asp and 540-Gly.2 Publications
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).Curated
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
Catalytic activityi
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation
Endonucleolytic cleavage to 5'-phosphomonoester.PROSITE-ProRule annotation
Cofactori
Protein has several cofactor binding sites:- Mg2+PROSITE-ProRule annotationNote: The RT polymerase active site binds 2 magnesium ions.PROSITE-ProRule annotation
- Mg2+CuratedNote: Binds 1 magnesium ions for ribonuclease H (RNase H) activity.1 Publication
- Mg2+CuratedNote: Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.Curated
Enzyme regulationi
Protease: Most efficiently inhibited by Amprenavir, which is able to block Gag-Pol processing in infected cells.1 Publication
pH dependencei
Optimum pH is 5.0 for protease activity.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 566 | Protease; shared with dimeric partnerPROSITE-ProRule annotation | 1 | |
Metal bindingi | 809 | Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 883 | Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 884 | Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 1183 | Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 1221 | Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 1242 | Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 1312 | MagnesiumPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 1455 | Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 1514 | Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 502 – 519 | CCHC-typePROSITE-ProRule annotation1 PublicationAdd BLAST | 18 | |
Zinc fingeri | 1387 – 1427 | HHCC-type1 PublicationAdd BLAST | 41 |
GO - Molecular functioni
- aspartic-type endopeptidase activity Source: UniProtKB
- DNA binding Source: CAFA
- DNA-directed DNA polymerase activity Source: UniProtKB-KW
- retroviral 3' processing activity Source: CAFA
- RNA binding Source: UniProtKB-KW
- RNA-directed DNA polymerase activity Source: UniProtKB-KW
- RNA-DNA hybrid ribonuclease activity Source: UniProtKB-EC
- structural constituent of virion Source: UniProtKB-KW
- zinc ion binding Source: InterPro
GO - Biological processi
- DNA catabolic process Source: CAFA
- DNA recombination Source: UniProtKB-KW
- establishment of integrated proviral latency Source: UniProtKB-KW
- suppression by virus of host gene expression Source: UniProtKB-KW
- viral entry into host cell Source: UniProtKB-KW
- viral genome integration into host DNA Source: CAFA
- viral translational readthrough Source: UniProtKB
- virion assembly Source: InterPro
Keywordsi
Enzyme and pathway databases
BRENDAi | 2.7.7.49 3393 3.1.13.2 3393 3.4.23.B5 3393 |
Protein family/group databases
MEROPSi | A02.008 |
Names & Taxonomyi
Protein namesi | Recommended name: Gag-Pol polyproteinShort name: Pr180gag-pol Cleaved into the following 7 chains: Alternative name(s): pp12 Alternative name(s): p14 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 Alternative name(s): p46 |
Gene namesi | Name:gag-pol |
Organismi | Moloney murine leukemia virus (isolate Shinnick) (MoMLV) |
Taxonomic identifieri | 928306 [NCBI] |
Taxonomic lineagei | Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Gammaretrovirus › Murine leukemia virus › |
Virus hosti | Mus musculus (Mouse) [TaxID: 10090] |
Proteomesi |
|
Subcellular locationi
Gag-Pol polyprotein :
- Virion By similarity
- Host cell membrane By similarity; Lipid-anchor By similarity
- Host late endosome membrane By similarity; Lipid-anchor By similarity
- host multivesicular body By similarity Note: These locations are probably linked to virus assembly sites.Curated
Matrix protein p15 :
- Virion Curated
Capsid protein p30 :
- Virion Curated
Nucleocapsid protein p10-Pol :
- Virion Curated
RNA-binding phosphoprotein p12 :
- Host cytoplasm 2 Publications Note: Localizes to the host cytoplasm early in infection and binds to the mitotic chromosomes later on.2 Publications
GO - Cellular componenti
- host cell late endosome membrane Source: UniProtKB-SubCell
- host cell plasma membrane Source: UniProtKB-SubCell
- host multivesicular body Source: UniProtKB-SubCell
- membrane Source: UniProtKB-KW
- protein-DNA complex Source: CAFA
- viral nucleocapsid Source: UniProtKB-KW
Keywords - Cellular componenti
Capsid protein, Host cell membrane, Host cytoplasm, Host endosome, Host membrane, Membrane, Viral matrix protein, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 114 | P → A: Slight reduction in the number of virus-like particles produced. | 1 | |
Mutagenesisi | 137 | S → A: No effect on reverse transcription activity. 1 Publication | 1 | |
Mutagenesisi | 148 | S → A: No effect on reverse transcription activity; when associated with A-150. 1 Publication | 1 | |
Mutagenesisi | 150 | S → A: No effect on reverse transcription activity; when associated with A-148. 1 Publication | 1 | |
Mutagenesisi | 165 | Y → A: Drastic reduction in the number of virus-like particles produced. 1 Publication | 1 | |
Mutagenesisi | 192 | S → A: Complete loss of reverse transcription activity. 1 Publication | 1 | |
Mutagenesisi | 192 | S → A: Complete loss of stable anchoring of viral PIC to mitotic chromosomes; when associated with A-196. 1 Publication | 1 | |
Mutagenesisi | 192 | S → D: Complete loss of reverse transcription activity. 1 Publication | 1 | |
Mutagenesisi | 196 | S → A: Complete loss of stable anchoring of viral PIC to mitotic chromosomes; when associated with A-192. 1 Publication | 1 | |
Mutagenesisi | 196 | S → A: No effect on reverse transcription activity. 1 Publication | 1 | |
Mutagenesisi | 209 | S → A: Strongly reduced reverse transcription activity. 1 Publication | 1 | |
Mutagenesisi | 209 | S → D: Strongly reduced reverse transcription activity. 1 Publication | 1 | |
Mutagenesisi | 212 | S → A: No effect on reverse transcription activity. 1 Publication | 1 | |
Mutagenesisi | 1244 | R → A: No effect on readthrough between Gag and Pol. 1 Publication | 1 | |
Mutagenesisi | 1247 | F → A: No effect on readthrough between Gag and Pol. 1 Publication | 1 | |
Mutagenesisi | 1248 | A → K: Almost complete loss of readthrough between Gag and Pol. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3562 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostSequence analysis1 Publication | |||
ChainiPRO_0000390795 | 2 – 1738 | Gag-Pol polyproteinAdd BLAST | 1737 | |
ChainiPRO_5000053618 | 2 – 131 | Matrix protein p15Add BLAST | 130 | |
ChainiPRO_5000053619 | 132 – 215 | RNA-binding phosphoprotein p12Add BLAST | 84 | |
ChainiPRO_5000053620 | 216 – 478 | Capsid protein p30Add BLAST | 263 | |
ChainiPRO_5000053621 | 479 – 534 | Nucleocapsid protein p10-PolAdd BLAST | 56 | |
ChainiPRO_5000053622 | 535 – 659 | ProteaseAdd BLAST | 125 | |
ChainiPRO_5000053623 | 660 – 1330 | Reverse transcriptase/ribonuclease HAdd BLAST | 671 | |
ChainiPRO_5000053624 | 1331 – 1738 | IntegraseAdd BLAST | 408 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine; by hostSequence analysis1 Publication | 1 | |
Modified residuei | 192 | Phosphoserine; by host1 Publication | 1 |
Post-translational modificationi
Gag-Pol polyprotein: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination.By similarity
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.1 Publication
Capsid protein p30: Sumoylated; which is required for virus replication.1 Publication
RNA-binding phosphoprotein p12: Phosphorylated on serine residues.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 131 – 132 | Cleavage; by viral protease1 Publication | 2 | |
Sitei | 215 – 216 | Cleavage; by viral protease1 Publication | 2 | |
Sitei | 478 – 479 | Cleavage; by viral protease1 Publication | 2 | |
Sitei | 534 – 535 | Cleavage; by viral protease1 Publication | 2 | |
Sitei | 659 – 660 | Cleavage; by viral protease1 Publication | 2 | |
Sitei | 1330 – 1331 | Cleavage; by viral protease1 Publication | 2 |
Keywords - PTMi
Lipoprotein, Myristate, Phosphoprotein, Ubl conjugationPTM databases
iPTMneti | P03355 |
PhosphoSitePlusi | P03355 |
Miscellaneous databases
PMAP-CutDBi | O92808 |
Interactioni
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 (PubMed:12093170). Capsid protein p30: Interacts with mouse UBE2I and mouse PIAS4 (PubMed:16352559). Gag-Pol polyprotein: Interacts (via PPXY motif) with host NEDD4 (PubMed:15908698). Gag-Pol polyprotein: Interacts (via PSAP motif) with host TSG101 (PubMed:15908698). Gag-Pol polyprotein: Interacts (via LYPX(n)L motif) with host PDCD6IP (PubMed:15908698). 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 (PubMed:14636559, PubMed:27329342). Integrase: Homodimer (PubMed:14599799).PROSITE-ProRule annotationBy similarity6 Publications
Protein-protein interaction databases
ELMi | P03355 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Turni | 488 – 491 | Combined sources | 4 | |
Helixi | 496 – 498 | Combined sources | 3 | |
Turni | 505 – 507 | Combined sources | 3 | |
Beta strandi | 510 – 512 | Combined sources | 3 | |
Helixi | 514 – 516 | Combined sources | 3 | |
Beta strandi | 520 – 522 | Combined sources | 3 | |
Beta strandi | 524 – 526 | Combined sources | 3 | |
Helixi | 529 – 532 | Combined sources | 4 | |
Helixi | 684 – 687 | Combined sources | 4 | |
Turni | 689 – 691 | Combined sources | 3 | |
Helixi | 693 – 696 | Combined sources | 4 | |
Beta strandi | 702 – 704 | Combined sources | 3 | |
Helixi | 727 – 742 | Combined sources | 16 | |
Beta strandi | 745 – 749 | Combined sources | 5 | |
Beta strandi | 757 – 759 | Combined sources | 3 | |
Beta strandi | 763 – 766 | Combined sources | 4 | |
Beta strandi | 770 – 772 | Combined sources | 3 | |
Helixi | 775 – 778 | Combined sources | 4 | |
Helixi | 791 – 795 | Combined sources | 5 | |
Beta strandi | 804 – 810 | Combined sources | 7 | |
Turni | 811 – 813 | Combined sources | 3 | |
Helixi | 814 – 816 | Combined sources | 3 | |
Beta strandi | 817 – 819 | Combined sources | 3 | |
Turni | 821 – 823 | Combined sources | 3 | |
Helixi | 824 – 827 | Combined sources | 4 | |
Beta strandi | 829 – 831 | Combined sources | 3 | |
Helixi | 834 – 836 | Combined sources | 3 | |
Beta strandi | 840 – 846 | Combined sources | 7 | |
Helixi | 854 – 872 | Combined sources | 19 | |
Beta strandi | 876 – 881 | Combined sources | 6 | |
Beta strandi | 884 – 891 | Combined sources | 8 | |
Helixi | 892 – 909 | Combined sources | 18 | |
Turni | 915 – 917 | Combined sources | 3 | |
Beta strandi | 919 – 927 | Combined sources | 9 | |
Beta strandi | 930 – 933 | Combined sources | 4 | |
Helixi | 941 – 948 | Combined sources | 8 | |
Helixi | 956 – 966 | Combined sources | 11 | |
Helixi | 967 – 969 | Combined sources | 3 | |
Helixi | 976 – 979 | Combined sources | 4 | |
Turni | 980 – 985 | Combined sources | 6 | |
Helixi | 997 – 1011 | Combined sources | 15 | |
Beta strandi | 1025 – 1044 | Combined sources | 20 | |
Beta strandi | 1047 – 1057 | Combined sources | 11 | |
Helixi | 1060 – 1063 | Combined sources | 4 | |
Helixi | 1067 – 1086 | Combined sources | 20 | |
Beta strandi | 1091 – 1094 | Combined sources | 4 | |
Turni | 1100 – 1104 | Combined sources | 5 | |
Helixi | 1116 – 1123 | Combined sources | 8 | |
Turni | 1126 – 1128 | Combined sources | 3 | |
Beta strandi | 1129 – 1131 | Combined sources | 3 | |
Turni | 1139 – 1141 | Combined sources | 3 | |
Beta strandi | 1169 – 1171 | Combined sources | 3 | |
Beta strandi | 1177 – 1189 | Combined sources | 13 | |
Beta strandi | 1192 – 1200 | Combined sources | 9 | |
Beta strandi | 1205 – 1211 | Combined sources | 7 | |
Helixi | 1217 – 1231 | Combined sources | 15 | |
Turni | 1232 – 1234 | Combined sources | 3 | |
Beta strandi | 1235 – 1241 | Combined sources | 7 | |
Helixi | 1244 – 1249 | Combined sources | 6 | |
Helixi | 1273 – 1282 | Combined sources | 10 | |
Beta strandi | 1285 – 1293 | Combined sources | 9 | |
Helixi | 1303 – 1321 | Combined sources | 19 | |
Helixi | 1346 – 1355 | Combined sources | 10 | |
Beta strandi | 1358 – 1360 | Combined sources | 3 | |
Turni | 1361 – 1364 | Combined sources | 4 | |
Beta strandi | 1365 – 1368 | Combined sources | 4 | |
Beta strandi | 1371 – 1374 | Combined sources | 4 | |
Helixi | 1376 – 1390 | Combined sources | 15 | |
Helixi | 1394 – 1402 | Combined sources | 9 | |
Turni | 1403 – 1405 | Combined sources | 3 | |
Beta strandi | 1407 – 1410 | Combined sources | 4 | |
Helixi | 1413 – 1422 | Combined sources | 10 | |
Helixi | 1425 – 1431 | Combined sources | 7 | |
Beta strandi | 1661 – 1667 | Combined sources | 7 | |
Beta strandi | 1670 – 1673 | Combined sources | 4 | |
Beta strandi | 1676 – 1687 | Combined sources | 12 | |
Beta strandi | 1690 – 1693 | Combined sources | 4 | |
Beta strandi | 1696 – 1698 | Combined sources | 3 | |
Helixi | 1702 – 1704 | Combined sources | 3 | |
Beta strandi | 1705 – 1707 | Combined sources | 3 | |
Turni | 1714 – 1716 | Combined sources | 3 | |
Beta strandi | 1717 – 1719 | Combined sources | 3 | |
Turni | 1726 – 1728 | Combined sources | 3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1D0E | X-ray | 3.00 | A/B | 683-937 | [»] | |
1D1U | X-ray | 2.30 | A | 683-937 | [»] | |
1I6J | X-ray | 2.00 | A | 683-937 | [»] | |
1MML | X-ray | 1.80 | A | 669-933 | [»] | |
1N4L | X-ray | 2.00 | A | 683-937 | [»] | |
1NND | X-ray | 2.30 | A | 683-937 | [»] | |
1QAI | X-ray | 2.30 | A/B | 669-933 | [»] | |
1QAJ | X-ray | 2.30 | A/B | 683-937 | [»] | |
1ZTT | X-ray | 1.85 | A | 683-937 | [»] | |
1ZTW | X-ray | 1.80 | A | 683-937 | [»] | |
2FJV | X-ray | 2.05 | A | 683-937 | [»] | |
2FJW | X-ray | 1.95 | A | 683-937 | [»] | |
2FJX | X-ray | 1.80 | A | 683-937 | [»] | |
2FVP | X-ray | 2.25 | A | 683-937 | [»] | |
2FVQ | X-ray | 2.30 | A | 683-937 | [»] | |
2FVR | X-ray | 2.20 | A | 683-937 | [»] | |
2FVS | X-ray | 2.35 | A | 683-937 | [»] | |
2HB5 | X-ray | 1.59 | A | 1157-1330 | [»] | |
2M9U | NMR | - | A | 1659-1738 | [»] | |
2MQV | NMR | - | A | 479-534 | [»] | |
2MS0 | NMR | - | A/C | 479-534 | [»] | |
2MS1 | NMR | - | A | 479-534 | [»] | |
2R2R | X-ray | 2.10 | A | 683-937 | [»] | |
2R2S | X-ray | 2.80 | A | 683-937 | [»] | |
2R2T | X-ray | 2.00 | A | 683-937 | [»] | |
2R2U | X-ray | 2.30 | A | 683-937 | [»] | |
3FSI | X-ray | 1.75 | A | 683-937 | [»] | |
3NNQ | X-ray | 2.69 | A/B | 1331-1435 | [»] | |
4M94 | X-ray | 2.14 | A | 683-937 | [»] | |
4M95 | X-ray | 1.72 | A | 683-937 | [»] | |
4MH8 | X-ray | 3.00 | A | 683-1330 | [»] | |
4NZG | X-ray | 2.15 | A/B/C/D | 1338-1435 | [»] | |
4XO0 | X-ray | 1.70 | A | 683-937 | [»] | |
4XPC | X-ray | 1.68 | A | 683-937 | [»] | |
4XPE | X-ray | 1.78 | A | 683-937 | [»] | |
5DMQ | X-ray | 4.00 | A | 683-1330 | [»] | |
5DMR | X-ray | 2.80 | A | 1159-1330 | [»] | |
5VBS | X-ray | 1.75 | A | 683-937 | [»] | |
DisProti | DP00651 | |||||
ProteinModelPortali | P03355 | |||||
SMRi | P03355 | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03355 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 560 – 631 | Peptidase A2PROSITE-ProRule annotationAdd BLAST | 72 | |
Domaini | 741 – 932 | Reverse transcriptasePROSITE-ProRule annotationAdd BLAST | 192 | |
Domaini | 1174 – 1320 | RNase HPROSITE-ProRule annotationAdd BLAST | 147 | |
Domaini | 1444 – 1602 | Integrase catalyticPROSITE-ProRule annotationAdd BLAST | 159 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 345 – 393 | Interaction with host PIAS4By similarityAdd BLAST | 49 | |
Regioni | 430 – 435 | Interaction with host UBE2IBy similarity | 6 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 438 – 478 | Sequence analysisAdd BLAST | 41 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 111 – 114 | PTAP/PSAP motifBy similarity | 4 | |
Motifi | 130 – 134 | LYPX(n)L motifBy similarity | 5 | |
Motifi | 162 – 165 | PPXY motifBy similarity | 4 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 71 – 193 | Pro-richPROSITE-ProRule annotationAdd BLAST | 123 | |
Compositional biasi | 440 – 501 | Arg-richPROSITE-ProRule annotationAdd BLAST | 62 |
Domaini
Gag-Pol 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. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus egress. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which potentially interacts with the UEV domain of TSG101. The junction between the matrix protein p15 and RNA-binding phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which potentially interacts with PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in budding and possibly drive residual virus release. contains.By similarity
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 502 – 519 | CCHC-typePROSITE-ProRule annotation1 PublicationAdd BLAST | 18 | |
Zinc fingeri | 1387 – 1427 | HHCC-type1 PublicationAdd BLAST | 41 |
Keywords - Domaini
Coiled coil, Zinc-fingerPhylogenomic databases
OrthoDBi | VOG090000AJ |
Family and domain databases
CDDi | cd06095 RP_RTVL_H_like, 1 hit |
Gene3Di | 1.10.150.1801 hit 1.10.375.101 hit 2.40.70.101 hit 3.30.420.102 hits |
InterProi | View protein in InterPro IPR001969 Aspartic_peptidase_AS IPR000840 G_retro_matrix IPR036946 G_retro_matrix_sf IPR002079 Gag_p12 IPR003036 Gag_P30 IPR001584 Integrase_cat-core 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 IPR001878 Znf_CCHC IPR036875 Znf_CCHC_sf |
Pfami | View protein in Pfam PF01140 Gag_MA, 1 hit PF01141 Gag_p12, 1 hit PF02093 Gag_p30, 1 hit PF00075 RNase_H, 1 hit PF00665 rve, 1 hit PF00077 RVP, 1 hit PF00078 RVT_1, 1 hit PF00098 zf-CCHC, 1 hit |
SMARTi | View protein in SMART SM00343 ZnF_C2HC, 1 hit |
SUPFAMi | SSF47836 SSF47836, 1 hit SSF47943 SSF47943, 1 hit SSF50630 SSF50630, 1 hit SSF53098 SSF53098, 2 hits SSF57756 SSF57756, 1 hit |
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 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P03355-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW
60 70 80 90 100
PRDGTFNRDL ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF
110 120 130 140 150
VHPKPPPPLP PSAPSLPLEP PRSTPPRSSL YPALTPSLGA KPKPQVLSDS
160 170 180 190 200
GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG EATPAGEAPD PSPMASRLRG
210 220 230 240 250
RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN NNPSFSEDPG
260 270 280 290 300
KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR
310 320 330 340 350
PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN
360 370 380 390 400
LAKVKGITQG PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ
410 420 430 440 450
SAPDIGRKLE RLEDLKNKTL GDLVREAEKI FNKRETPEER EERIRRETEE
460 470 480 490 500
KEERRRTEDE QKEKERDRRR HREMSKLLAT VVSGQKQDRQ GGERRRSQLD
510 520 530 540 550
RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDDQG GQGQEPPPEP
560 570 580 590 600
RITLKVGGQP VTFLVDTGAQ HSVLTQNPGP LSDKSAWVQG ATGGKRYRWT
610 620 630 640 650
TDRKVHLATG KVTHSFLHVP DCPYPLLGRD LLTKLKAQIH FEGSGAQVMG
660 670 680 690 700
PMGQPLQVLT LNIEDEHRLH ETSKEPDVSL GSTWLSDFPQ AWAETGGMGL
710 720 730 740 750
AVRQAPLIIP LKATSTPVSI KQYPMSQEAR LGIKPHIQRL LDQGILVPCQ
760 770 780 790 800
SPWNTPLLPV KKPGTNDYRP VQDLREVNKR VEDIHPTVPN PYNLLSGLPP
810 820 830 840 850
SHQWYTVLDL KDAFFCLRLH PTSQPLFAFE WRDPEMGISG QLTWTRLPQG
860 870 880 890 900
FKNSPTLFDE ALHRDLADFR IQHPDLILLQ YVDDLLLAAT SELDCQQGTR
910 920 930 940 950
ALLQTLGNLG YRASAKKAQI CQKQVKYLGY LLKEGQRWLT EARKETVMGQ
960 970 980 990 1000
PTPKTPRQLR EFLGTAGFCR LWIPGFAEMA APLYPLTKTG TLFNWGPDQQ
1010 1020 1030 1040 1050
KAYQEIKQAL LTAPALGLPD LTKPFELFVD EKQGYAKGVL TQKLGPWRRP
1060 1070 1080 1090 1100
VAYLSKKLDP VAAGWPPCLR MVAAIAVLTK DAGKLTMGQP LVILAPHAVE
1110 1120 1130 1140 1150
ALVKQPPDRW LSNARMTHYQ ALLLDTDRVQ FGPVVALNPA TLLPLPEEGL
1160 1170 1180 1190 1200
QHNCLDILAE AHGTRPDLTD QPLPDADHTW YTDGSSLLQE GQRKAGAAVT
1210 1220 1230 1240 1250
TETEVIWAKA LPAGTSAQRA ELIALTQALK MAEGKKLNVY TDSRYAFATA
1260 1270 1280 1290 1300
HIHGEIYRRR GLLTSEGKEI KNKDEILALL KALFLPKRLS IIHCPGHQKG
1310 1320 1330 1340 1350
HSAEARGNRM ADQAARKAAI TETPDTSTLL IENSSPYTSE HFHYTVTDIK
1360 1370 1380 1390 1400
DLTKLGAIYD KTKKYWVYQG KPVMPDQFTF ELLDFLHQLT HLSFSKMKAL
1410 1420 1430 1440 1450
LERSHSPYYM LNRDRTLKNI TETCKACAQV NASKSAVKQG TRVRGHRPGT
1460 1470 1480 1490 1500
HWEIDFTEIK PGLYGYKYLL VFIDTFSGWI EAFPTKKETA KVVTKKLLEE
1510 1520 1530 1540 1550
IFPRFGMPQV LGTDNGPAFV SKVSQTVADL LGIDWKLHCA YRPQSSGQVE
1560 1570 1580 1590 1600
RMNRTIKETL TKLTLATGSR DWVLLLPLAL YRARNTPGPH GLTPYEILYG
1610 1620 1630 1640 1650
APPPLVNFPD PDMTRVTNSP SLQAHLQALY LVQHEVWRPL AAAYQEQLDR
1660 1670 1680 1690 1700
PVVPHPYRVG DTVWVRRHQT KNLEPRWKGP YTVLLTTPTA LKVDGIAAWI
1710 1720 1730
HAAHVKAADP GGGPSSRLTW RVQRSQNPLK IRLTREAP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF033811 Genomic RNA Translation: AAC82568.1 Sequence problems. J02255 Genomic RNA No translation available. |
PIRi | A03956 GNMV1M |
RefSeqi | NP_057933.2, NC_001501.1 |
Genome annotation databases
GeneIDi | 2193424 |
KEGGi | vg:2193424 |
Keywords - Coding sequence diversityi
RNA suppression of terminationSimilar proteinsi
Entry informationi
Entry namei | POL_MLVMS | |
Accessioni | P03355Primary (citable) accession number: P03355 Secondary accession number(s): O92808 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 31, 2018 | |
Last modified: | April 25, 2018 | |
This is version 165 of the entry and version 5 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |