Reviewed
Homo Sapiens (Human) [TaxID: 9606]
Gag-pol[Gene ID: 155348 ]
♦Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA)
♦ Capsid protein p24 (CA)
♦ Spacer peptide 1 (SP1) (p2)
♦ Nucleocapsid protein p7 (NC)
♦ Transframe peptide (TF)
♦ p6-pol (p6*)
♦ Protease (EC 3.4.23.16) (PR) (Retropepsin)
♦ Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT)
♦ p51 RT
♦ p15
♦ Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
♦ Capsid protein p24 (CA)
♦ Spacer peptide 1 (SP1) (p2)
♦ Nucleocapsid protein p7 (NC)
♦ Transframe peptide (TF)
♦ p6-pol (p6*)
♦ Protease (EC 3.4.23.16) (PR) (Retropepsin)
♦ Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT)
♦ p51 RT
♦ p15
♦ Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
Human Immunodeficiency Virus Type 1 Group M Subtype B (isolate HXB2) (HIV-1)
Viruses> Retro-transcribing Viruses> Retroviridae> Orthoretrovirinae> Lentivirus> Primate Lentivirus Group> Human Immunodeficiency Virus 1> HIV-1 Group M> HIV-1 M:B> Human Immunodeficiency Virus Type 1 Group M Subtype B (isolate HXB2) (HIV-1)
3040055 ; 2349226 ; 2162350 ; 8420982 ; 8035478 ; 8513493 ; 7801128 ; 7835426 ; 8648689 ;
9223641 ; 9573231 ; 10604476 ; 10494040 ; 9931246 ; 11044125 ; 11160682 ; 12206668 ; 11929983 ;
11932404 ; 12477841 ; 12660176 ; 12505164 ; 15065874 ; 16221683 ; 16904152 ; 17070549 ; 17108052 ;
17656588 ; 18343475 ; 19914170 ; 19956697 ; 19327811 ; 20573829 ; 20554775 ; 20828778 ; 23785198 ;
24132393 ; 24554657 ; 24500712 ; 8791726 ; 9878383 ; 11700285 ; 11983066 ; 12873766 ; 15353349 ;
16815734 ; 21762797 ; 24907482 ; 24933691 ; 2682266 ; 1956054 ; 1959614 ; 1304383 ; 8289249 ;
8278812 ; 7523679 ; 8654825 ; 8535785 ; 7540935 ; 8648598 ; 8807858 ; 8868486 ; 9108091 ;
9003516 ; 9827997 ; 9554878 ; 9790666 ; 9575185 ; 9485357 ; 9689112 ; 9772165 ; 10429209 ;
10890912 ; 11170214 ; 11575933 ; 12051725 ; 12534276 ; 15095972 ; 15537347
9223641 ; 9573231 ; 10604476 ; 10494040 ; 9931246 ; 11044125 ; 11160682 ; 12206668 ; 11929983 ;
11932404 ; 12477841 ; 12660176 ; 12505164 ; 15065874 ; 16221683 ; 16904152 ; 17070549 ; 17108052 ;
17656588 ; 18343475 ; 19914170 ; 19956697 ; 19327811 ; 20573829 ; 20554775 ; 20828778 ; 23785198 ;
24132393 ; 24554657 ; 24500712 ; 8791726 ; 9878383 ; 11700285 ; 11983066 ; 12873766 ; 15353349 ;
16815734 ; 21762797 ; 24907482 ; 24933691 ; 2682266 ; 1956054 ; 1959614 ; 1304383 ; 8289249 ;
8278812 ; 7523679 ; 8654825 ; 8535785 ; 7540935 ; 8648598 ; 8807858 ; 8868486 ; 9108091 ;
9003516 ; 9827997 ; 9554878 ; 9790666 ; 9575185 ; 9485357 ; 9689112 ; 9772165 ; 10429209 ;
10890912 ; 11170214 ; 11575933 ; 12051725 ; 12534276 ; 15095972 ; 15537347
Various pathway(s) in which protein is involved
Not Available
MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEA
LDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQM
LKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRF
YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGH
TARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTRRELQVWGRDNNSPSEAGADRQGTVSFNFPQVTLWQRPLVT
IKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKLK
PGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGD
AYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWG
LTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEP
VHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPE
WEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNRGRQKVVTLTDTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDQS
ESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKVLFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQ
VDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTGATVRAACWWAGIKQEFGIPYNPQSQGVVES
MNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQD
NSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED
LDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQM
LKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRF
YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGH
TARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTRRELQVWGRDNNSPSEAGADRQGTVSFNFPQVTLWQRPLVT
IKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKLK
PGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGD
AYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWG
LTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEP
VHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPE
WEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNRGRQKVVTLTDTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDQS
ESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKVLFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQ
VDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTGATVRAACWWAGIKQEFGIPYNPQSQGVVES
MNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQD
NSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED
1435
Not Available
Not Available
23-01-2007
Evidence at protein level
Amino Acid | Count | % Frequency | Amino Acid | Count | % Frequency |
---|---|---|---|---|---|
Alanine (A) | Leucine (L) | ||||
Arginine (R) | Lysine (K) | ||||
Asparagine (N) | Methionine (M) | ||||
Aspartic Acid (D) | Phenylalanine (F) | ||||
Cysteine (C) | Proline (P) | ||||
Glutamine (Q) | Serine (S) | ||||
Glutamic Acid (E) | Threonine (T) | ||||
Glycine (G) | Tryptophan (W) | ||||
Histidine (H) | Tyrosine (Y) | ||||
Isoleucine (I) | Valine (V) |
% Number of Residues in Helices | % Number of Residues in Strands | % Number of Residues in Coils |
---|---|---|
♦Gag-Pol polyprotein: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation.
♦ Matrix protein p17: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).
♦ Capsid protein p24: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion (PubMed:8648689). Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (PubMed:12660176). Host restriction factors such as monkey TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (PubMed:23785198). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (PubMed:24554657).
♦ Nucleocapsid protein p7: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.
♦ Protease: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane (PubMed:9573231, PubMed:11932404). Cleavages take place as an ordered, step-wise cascade to yield mature proteins (PubMed:9573231, PubMed:11932404). This process is called maturation (PubMed:9573231, PubMed:11932404). Displays maximal activity during the budding process just prior to particle release from the cell (PubMed:9573231, PubMed:11932404). Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (PubMed:7835426). Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (PubMed:12660176, PubMed:19914170).
♦ Reverse transcriptase/ribonuclease H: 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(3)-Lys 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 two polypurine tracts (PPTs) situated at the 5'-end and near the center 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 PPTs that have not been removed by RNase H as primers. PPTs 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.
♦ 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, Vpr 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, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. 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 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration.
♦ Matrix protein p17: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).
♦ Capsid protein p24: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion (PubMed:8648689). Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (PubMed:12660176). Host restriction factors such as monkey TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (PubMed:23785198). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (PubMed:24554657).
♦ Nucleocapsid protein p7: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.
♦ Protease: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane (PubMed:9573231, PubMed:11932404). Cleavages take place as an ordered, step-wise cascade to yield mature proteins (PubMed:9573231, PubMed:11932404). This process is called maturation (PubMed:9573231, PubMed:11932404). Displays maximal activity during the budding process just prior to particle release from the cell (PubMed:9573231, PubMed:11932404). Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (PubMed:7835426). Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (PubMed:12660176, PubMed:19914170).
♦ Reverse transcriptase/ribonuclease H: 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(3)-Lys 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 two polypurine tracts (PPTs) situated at the 5'-end and near the center 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 PPTs that have not been removed by RNase H as primers. PPTs 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.
♦ 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, Vpr 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, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. 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 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration.
3.4.23.16 , 2.7.7.49 , 2.7.7.7 , 3.1.26.13 , 3.1.13.2 , 2.7.7.- , 3.1.-.-
GO:0003677 ; GO:0003723 ; GO:0003887 ; GO:0003964 ; GO:0004190 ;
GO:0004523 ; GO:0004533 ; GO:0005198 ; GO:0006278 ; GO:0006310 ;
GO:0008233 ; GO:0008270 ; GO:0008289 ; GO:0008907 ; GO:0019013 ;
GO:0019058 ; GO:0019061 ; GO:0019064 ; GO:0019068 ; GO:0019072 ;
GO:0020002 ; GO:0030260 ; GO:0039651 ; GO:0039657 ; GO:0042025 ;
GO:0042802 ; GO:0044826 ; GO:0051169 ; GO:0055036 ; GO:0072494 ;
GO:0075713 ; GO:0075732
GO:0004523 ; GO:0004533 ; GO:0005198 ; GO:0006278 ; GO:0006310 ;
GO:0008233 ; GO:0008270 ; GO:0008289 ; GO:0008907 ; GO:0019013 ;
GO:0019058 ; GO:0019061 ; GO:0019064 ; GO:0019068 ; GO:0019072 ;
GO:0020002 ; GO:0030260 ; GO:0039651 ; GO:0039657 ; GO:0042025 ;
GO:0042802 ; GO:0044826 ; GO:0051169 ; GO:0055036 ; GO:0072494 ;
GO:0075713 ; GO:0075732
♦ Gag-Pol polyprotein: Host cell membrane
♦ Lipid-anchor . Host endosome, host multivesicular body . Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. .
♦ Matrix protein p17: Virion membrane
♦ Lipid-anchor . Host nucleus . Host cytoplasm .
♦ Capsid protein p24: Virion .
♦ Nucleocapsid protein p7: Virion .
♦ Reverse transcriptase/ribonuclease H: Virion .
♦ Integrase: Virion . Host nucleus . Host cytoplasm . Note=Nuclear at initial phase, cytoplasmic at assembly. .
♦ Lipid-anchor . Host endosome, host multivesicular body . Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. .
♦ Matrix protein p17: Virion membrane
♦ Lipid-anchor . Host nucleus . Host cytoplasm .
♦ Capsid protein p24: Virion .
♦ Nucleocapsid protein p7: Virion .
♦ Reverse transcriptase/ribonuclease H: Virion .
♦ Integrase: Virion . Host nucleus . Host cytoplasm . Note=Nuclear at initial phase, cytoplasmic at assembly. .
♦DOMAIN 508 577 Peptidase A2.
♦ DOMAIN 631 821 Reverse transcriptase.
♦ DOMAIN 1021 1144 RNase H.
♦ DOMAIN 1201 1351 Integrase catalytic.
♦ DOMAIN 631 821 Reverse transcriptase.
♦ DOMAIN 1021 1144 RNase H.
♦ DOMAIN 1201 1351 Integrase catalytic.
MOTIF 16 22 Nuclear export signal. ; MOTIF 26 32 Nuclear localization signal. ; MOTIF 985 1001 Tryptophan repeat motif.
X-ray crystallography (174); NMR spectroscopy (8)
1A30 1BV7 1BV9 1BVE 1BVG 1BWA 1BWB 1C0T 1C0U 1C1B 1C1C 1DMP 1DTQ 1DTT 1E6J
1EP4 1ESK 1EX4 1EXQ 1FB7 1FK9 1FKO 1FKP 1G6L 1HIV 1HVH 1HVR 1HWR 1HXB 1JKH
1JLA 1JLB 1JLC 1JLE 1JLF 1JLG 1JLQ 1KLM 1LV1 1LW0 1LW2 1LWC 1LWE 1LWF 1NCP
1O1W 1ODW 1ODY 1QBR 1QBS 1QBT 1QBU 1REV 1RT1 1RT2 1RT3 1RT4 1RT5 1RT6 1RT7
1RTD 1RTH 1RTI 1RTJ 1S1T 1S1U 1S1V 1S1W 1S1X 1T05 1TAM 1TKT 1TKX 1TKZ 1TL1
1TL3 1VRT 1VRU 2HND 2HNY 2HNZ 2KOD 2NPH 2OPP 2OPQ 2OPR 2OPS 2RF2 2RKI 2WHH
2WOM 2WON 2YNF 2YNG 2YNH 2YNI 3AO2 3C6T 3C6U 3DI6 3DLE 3DLG 3DM2 3DMJ 3DOK
3DOL 3DOX 3DRP 3DRR 3DRS 3DYA 3E01 3FFI 3I0R 3I0S 3KJV 3KK1 3KK2 3KK3 3KT2
3KT5 3LAK 3LAL 3LAM 3LAN 3LP0 3LP1 3LP2 3M8P 3M8Q 3MEC 3MED 3MEE 3MEG 3N3I
3NBP 3PHV 3QIN 3QIO 3QIP 3T19 3T1A 3TAM 4B3O 4B3P 4B3Q 4I7F 4KSE 4KV8 4NCG
4Q1W 4Q1X 4Q1Y 4Q5M 4QLH 4U1H 4U1I 4U1J 4U7Q 4U7V 5DGU 5DGW 5EU7 5HRN 5HRP
5HRR 5HRS 5IM7 5J2M 5J2N 5J2P 5J2Q 5K14 5KAO 5T82 5XOS 5XOT 5YRS 6BSG 6BSH
6BSI 6BSJ
1EP4 1ESK 1EX4 1EXQ 1FB7 1FK9 1FKO 1FKP 1G6L 1HIV 1HVH 1HVR 1HWR 1HXB 1JKH
1JLA 1JLB 1JLC 1JLE 1JLF 1JLG 1JLQ 1KLM 1LV1 1LW0 1LW2 1LWC 1LWE 1LWF 1NCP
1O1W 1ODW 1ODY 1QBR 1QBS 1QBT 1QBU 1REV 1RT1 1RT2 1RT3 1RT4 1RT5 1RT6 1RT7
1RTD 1RTH 1RTI 1RTJ 1S1T 1S1U 1S1V 1S1W 1S1X 1T05 1TAM 1TKT 1TKX 1TKZ 1TL1
1TL3 1VRT 1VRU 2HND 2HNY 2HNZ 2KOD 2NPH 2OPP 2OPQ 2OPR 2OPS 2RF2 2RKI 2WHH
2WOM 2WON 2YNF 2YNG 2YNH 2YNI 3AO2 3C6T 3C6U 3DI6 3DLE 3DLG 3DM2 3DMJ 3DOK
3DOL 3DOX 3DRP 3DRR 3DRS 3DYA 3E01 3FFI 3I0R 3I0S 3KJV 3KK1 3KK2 3KK3 3KT2
3KT5 3LAK 3LAL 3LAM 3LAN 3LP0 3LP1 3LP2 3M8P 3M8Q 3MEC 3MED 3MEE 3MEG 3N3I
3NBP 3PHV 3QIN 3QIO 3QIP 3T19 3T1A 3TAM 4B3O 4B3P 4B3Q 4I7F 4KSE 4KV8 4NCG
4Q1W 4Q1X 4Q1Y 4Q5M 4QLH 4U1H 4U1I 4U1J 4U7Q 4U7V 5DGU 5DGW 5EU7 5HRN 5HRP
5HRR 5HRS 5IM7 5J2M 5J2N 5J2P 5J2Q 5K14 5KAO 5T82 5XOS 5XOT 5YRS 6BSG 6BSH
6BSI 6BSJ
♦ACT_SITE 513 513 For protease activity
♦ shared with dimeric partner.
♦ shared with dimeric partner.
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.