Reviewed, UniProtKB/Swiss-Prot Q73368 (POL_HV1B9)

Names and origin

Protein names

Recommended name:
    Gag-Pol polyprotein
Alternative name(s):
    Pr160Gag-Pol
Cleaved into the following 11 chains:
    1- Recommended name:
            Matrix protein p17
                Short name=MA
    2- Recommended name:
            Capsid protein p24
                Short name=CA
    3- Recommended name:
            Spacer peptide p2
    4- Recommended name:
            Nucleocapsid protein p7
                Short name=NC
    5- Recommended name:
            Transframe peptide
                Short name=TF
    6- Recommended name:
            p6-pol
                Short name=p6*
    7- Recommended name:
            Protease
              EC=3.4.23.16
        Alternative name(s):
            Retropepsin
            PR
    8- Recommended name:
            Reverse transcriptase/ribonuclease H
              EC=2.7.7.49
              EC=2.7.7.7
              EC=3.1.26.4
        Alternative name(s):
            p66 RT
    9- Recommended name:
            p51 RT
    10- Recommended name:
            p15
    11- Recommended name:
            Integrase
                Short name=IN

Gene names

Name:

gag-pol

Organism

Human immunodeficiency virus type 1 (strain 89.6 group M subtype B) (HIV-1)

Taxonomic identifier

401671 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	1435 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation By similarity. Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to plays a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. It binds in the cytoplasm the human BAF protein which prevent autointegration of the viral genome, and might be included in virions at the ration of zero to 3 BAF dimer per virion. The myristoylation signal and the NLS thus exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu By similarity. Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is dissassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species By similarity. Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity By similarity. 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. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles By similarity. 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(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 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. 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 allow 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 By similarity.
Catalytic activity	Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro. Endonucleolytic cleavage to 5'-phosphomonoester. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Cofactor	Binds 2 magnesium ions for reverse transcriptase polymerase activity By similarity. Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding By similarity. Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions By similarity.
Enzyme regulation	The viral protease is inhibited by many synthetic protease inhibitors (PIs), such as amprenavir, atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. RT can be inhibited either by nucleoside RT inhibitors (NRTIs) or by non nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators, whereas NNRTIs inhibit DNA polymerization by binding a small hydrophobic pocket near the RT active site and inducing an allosteric change in this region. Classical NRTIs are abacavir, adefovir (PMEA), didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA), zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic effective treatment of AIDS associate two NRTIs and one NNRTI. Use of protease inhibitors in tritherapy regimens permit more ambitious therapeutic strategies By similarity.
Subunit structure	Pre-integration complex interacts with human HMGA1. Matrix protein p17 is a trimer. Interacts with gp120 and human BAF. Capsid is a homodimer. Interacts with human PPIA/CYPA. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. Integrase is a homodimer and possibly can form homotetramer. Integrase interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1 By similarity.
Subcellular location	Matrix protein p17: Virion Potential. Host nucleus By similarity. Host cytoplasm By similarity. Host cell membrane; Lipid-anchor Potential. Note: Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane By similarity. Capsid protein p24: Virion Potential. Nucleocapsid protein p7: Virion Potential. Reverse transcriptase/ribonuclease H: Virion Potential. Integrase: Virion Potential. Host nucleus Potential. Host cytoplasm Potential. Note: Nuclear at initial phase, cytoplasmic at assembly Potential.
Domain	The reverse transcriptase/ribonuclease H (RT) is structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accomodating the incoming nucleotide. The RNase H domain stabilizes the association of RT with primer-template By similarity. The tryptophan repeat motif is involved in RT p66/p51 dimerization By similarity. Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein By similarity.
Post-translational modification	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. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid protein p7 might be further cleaved after virus entry By similarity. Capsid protein p24 is phosphorylated By similarity. Matrix protein p17 is tyrosine phosphorylated presumably in the virion by a host kinase. This modification targets the matrix protein to the nucleus By similarity.
Miscellaneous	Capsid protein p24 is able to bind macaque TRIM5-alpha or owl monkey TRIMCyp, preventing reverse transcription of the viral genome and succesfull infection of macaque or owl monkey by HIV-1 By similarity. 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. HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K). Resistance to inhibitors associated with mutations are observed both in viral protease and in reverse transcriptase. Most of the time, single mutations confer only a modest reduction in drug susceptibility. Combination of several mutations is usually required to develop a high-level drug resistance. These mutations are predominantly found in clade B viruses and not in other genotypes. They are listed in the clade B representative isolate HXB2 (AC P04585).
Sequence similarities	Contains 2 CCHC-type zinc fingers. Contains 1 integrase catalytic domain. Contains 1 integrase-type DNA-binding domain. Contains 1 integrase-type zinc finger. Contains 1 peptidase A2 domain. Contains 1 reverse transcriptase domain. Contains 1 RNase H domain.

Ontologies

Keywords
Biological process	Capsid maturation DNA integration DNA recombination
Cellular component	Capsid protein Host cell membrane Host cytoplasm Host membrane Host nucleus Membrane Virion
Coding sequence diversity	Ribosomal frameshifting
Disease	AIDS
Domain	Repeat Zinc-finger
Ligand	Magnesium Metal-binding RNA-binding Viral nucleoprotein Zinc
Molecular function	Aspartyl protease DNA-directed DNA polymerase Endonuclease Hydrolase Nuclease Nucleotidyltransferase Protease RNA-directed DNA polymerase Transferase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	DNA integration Inferred from electronic annotation. Source: UniProtKB-KW DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro viral procapsid maturation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW integrase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease H activity Inferred from electronic annotation. Source: EC structural molecule activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

Note: Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.

Isoform Gag-Pol polyprotein (identifier: Q73368-1)

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.

Note: Produced by -1 ribosomal frameshifting.

Isoform Gag polyprotein (identifier: Q73367-1)

The sequence of this isoform can be found in the external entry Q73367-1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by conventional translation.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed; by host By similarity
	Chain	2 – 1435	1434	Gag-Pol polyprotein		PRO_0000261263
	Chain	2 – 132	131	Matrix protein p17 By similarity		PRO_0000250973
	Chain	133 – 363	231	Capsid protein p24 By similarity		PRO_0000250974
	Peptide	364 – 377	14	Spacer peptide p2 By similarity		PRO_0000250975
	Chain	378 – 432	55	Nucleocapsid protein p7 By similarity		PRO_0000250976
	Peptide	433 – 440	8	Transframe peptide Potential		PRO_0000250977
	Chain	441 – 488	48	p6-pol Potential		PRO_0000250978
	Chain	489 – 587	99	Protease By similarity		PRO_0000250979
	Chain	588 – 1147	560	Reverse transcriptase/ribonuclease H By similarity		PRO_0000250980
	Chain	588 – 1027	440	p51 RT By similarity		PRO_0000250981
	Chain	1028 – 1147	120	p15 By similarity		PRO_0000250982
	Chain	1148 – 1435	288	Integrase By similarity		PRO_0000250983
Regions
	Domain	508 – 577	70	Peptidase A2
	Domain	631 – 821	191	Reverse transcriptase
	Domain	1021 – 1144	124	RNase H
	Domain	1201 – 1351	151	Integrase catalytic
	Zinc finger	390 – 407	18	CCHC-type 1
	Zinc finger	411 – 428	18	CCHC-type 2
	Zinc finger	1150 – 1191	42	Integrase-type
	DNA binding	1370 – 1417	48	Integrase-type
	Region	814 – 822	9	RT 'primer grip' By similarity
	Motif	16 – 22	7	Nuclear export signal By similarity
	Motif	26 – 32	7	Nuclear localization signal By similarity
	Motif	985 – 1001	17	Tryptophan repeat motif By similarity
Sites
	Active site	513	1	For protease activity; shared with dimeric partner By similarity
	Metal binding	697	1	Magnesium; catalytic; for reverse transcriptase activity By similarity
	Metal binding	772	1	Magnesium; catalytic; for reverse transcriptase activity By similarity
	Metal binding	773	1	Magnesium; catalytic; for reverse transcriptase activity By similarity
	Metal binding	1030	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	1065	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	1085	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	1136	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	1211	1	Magnesium; catalytic; for integrase activity By similarity
	Metal binding	1263	1	Magnesium; catalytic; for integrase activity By similarity
	Site	132 – 133	2	Cleavage; by viral protease By similarity
	Site	221 – 222	2	Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA By similarity
	Site	363 – 364	2	Cleavage; by viral protease By similarity
	Site	377 – 378	2	Cleavage; by viral protease By similarity
	Site	432 – 433	2	Cleavage; by viral protease Potential
	Site	440 – 441	2	Cleavage; by viral protease By similarity
	Site	488 – 489	2	Cleavage; by viral protease By similarity
	Site	587 – 588	2	Cleavage; by viral protease By similarity
	Site	988	1	Essential for RT p66/p51 heterodimerization By similarity
	Site	1001	1	Essential for RT p66/p51 heterodimerization By similarity
	Site	1027 – 1028	2	Cleavage; by viral protease; partial By similarity
	Site	1147 – 1148	2	Cleavage; by viral protease By similarity
Amino acid modifications
	Modified residue	132	1	Phosphotyrosine; by host By similarity
	Lipidation	2	1	N-myristoyl glycine; by host By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform Gag-Pol polyprotein [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 33D6D5E320BE48FE	FASTA	1,435	161,526
	10 20 30 40 50 60 MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPSL LETSEGCRQI 70 80 90 100 110 120 LGQLQSSLQT GSEELKSLYN TVATLYCVHQ RIEVKDTKEA LDKIEEEQNK SKKKAQQAAA 130 140 150 160 170 180 DTGNSSQVSQ NYPIVQNIQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT 190 200 210 220 230 240 PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRLHPVQA GPVAPGQMRE PRGSDIAGTT 250 260 270 280 290 300 STLQEQIGWM TNNPPIPVGE IYKRWIILGL NKIVRMYSPS SILDIKQGPK EPFRDYVDRF 310 320 330 340 350 360 YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPG ATLEEMMTAC QGVGGPGHKA 370 380 390 400 410 420 RVLAEAMSQV TNSATIMMQR GNFRNQRKTV KCFNCGKEGH IAKNCRAPRK KGCWKCGKEG 430 440 450 460 470 480 HQMKDCTERQ ANFFRENLAF PQGKAREFSS EQTRANSPTR RELQVWGGDN NSLSEAGADR 490 500 510 520 530 540 QGTVSLSFPQ ITLWQRPLVT IKVGGQLKEA LLDTGADDTV LEDMSLPGRW KPKMIGGIGG 550 560 570 580 590 600 FIKVRQYEQI DIEICGHKAK GTVLVGPTPV NIIGRNLLTQ IGCTLNFPIS PIETVPVKLK 610 620 630 640 650 660 PGMDGPKVKQ WPLTEEKIKA LVEICTEMEK EGKISKIGPE NPYNTPVFAI KKKDSTKWRK 670 680 690 700 710 720 LVDFRELNKR TQDFWEVQLG IPHPAGLKKK KSVTVLDVGD AYFSVPLDED FRKYTAFTIP 730 740 750 760 770 780 SINNETPGIR YQYNVLPQGW KGSPAIFQSS MTKILEPFRK QNPDIVIYQY MDDLYVGSDL 790 800 810 820 830 840 EIGQHRAKIE DLRQHLLKWG FTTPDKKHQK EPPFLWMGYE LHPDKWTVQP IVLPEKDSWT 850 860 870 880 890 900 VNDIQKLVGK LNWASQIYAG IKVKQLCKLL RGTKALTEVV PLTEEAELEL AENREILKEP 910 920 930 940 950 960 VHGVYYDPTK DLIAELQKQG QGQWTYQIYQ EPYKNLKTGK YARMRGAHTN DVKQLTEAVQ 970 980 990 1000 1010 1020 KIATESIVIW GKTPKFKLPI QKETWEAWWT DYWQATWIPE WEFVNTPPLV KLWYQLEKEP 1030 1040 1050 1060 1070 1080 IVGAETFYVD GAANRDTKSG KAGYVTDRGR QKVVSLADTT NQKTELQAIH LALQDSGLEV 1090 1100 1110 1120 1130 1140 NIVTDSQYAL GIIQAQPDKS ESELVSQIIE QLIKKEKVYL AWVPAHKGIG GNEQVDKLVS 1150 1160 1170 1180 1190 1200 AGIRKVLFLD GIDKAQEEHE KYHTNWRAMA SDFNLPPVVA KEIVASCNKC QLKGEAMHGQ 1210 1220 1230 1240 1250 1260 VDCSPGIWQL DCTHLEGKVI LVAVHVASGY IEAEVIPAET GQETAYFLLK LAGRWPVKTI 1270 1280 1290 1300 1310 1320 HTDNGSNFTS TTVKAACWWA GIKQEFGIPY NPQSQGVVES MNKELKKIIG QVRDQAEHLK 1330 1340 1350 1360 1370 1380 TAVQMAVFIH NFKRKGGIGG YSAGERIVDI IASDIQTKEL QKQITKIQNF RVYYRDSRDP 1390 1400 1410 1420 1430 LWKGPAKLLW KGEGAVVIQD NSDIKVVPRR KAKIIRDYGK QMAGDDCVAS RQDED
	Isoform Gag polyprotein. See Q73367.	FASTA	–	–

References

[1]

"An infectious molecular clone of an unusual macrophage-tropic and highly cytopathic strain of human immunodeficiency virus type 1." Collman R., Balliet J.W., Gregory S.A., Friedman H., Kolson D.L., Nathanson N., Srinivasan A. J. Virol. 66:7517-7521(1992) [PubMed: 1433527] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Web resources

HIV drug resistance mutations

hivdb

HIV drug resistance database

BioAfrica: HIV bioinformatics in Africa

Cross-references

Sequence databases
EMBL GenBank DDBJ	U39362 Genomic DNA. Translation: AAA81037.1.
PIR	A47330. B47330. C47330. D47330. F47330. S32132.
3D structure databases
HSSP	HSSP built from PDB template 1DTT based on UniProtKB P04585.
ModBase	Search...
Family and domain databases
InterPro	IPR000721. Gag_p24. IPR001037. Integrase_C_retrovir. IPR001584. Integrase_cat-core. IPR017856. Integrase_Zn-bd_dom-like_N. IPR003308. Integrase_Zn-bd_dom_N. IPR000071. Lentvrl_matrix_N. IPR001995. Peptidase_A2_cat. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. IPR012337. PolynucTfrase_RNaseH_fold. IPR008916. Retrov_capsid_C. IPR008919. Retrov_capsid_N. IPR010999. Retrovr_matrix_N. IPR000477. Reverse_transcriptase. IPR002156. RNase_H. IPR010659. RVT_connect. IPR010661. RVT_thumb. IPR013084. Znf_CCH_retrovir. IPR001878. Znf_CCHC. [Graphical view]
Gene3D	G3DSA:2.30.30.10. Integrase_C. 1 hit. G3DSA:1.10.10.200. Intgrase_N_Zn_bd. 1 hit. G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit. G3DSA:1.10.1200.30. Retrov_capsid_C. 1 hit. G3DSA:1.10.375.10. Retrov_capsid_N. 1 hit. G3DSA:4.10.60.10. Znf_CCH_retrovir. 1 hit.
Pfam	PF00540. Gag_p17. 1 hit. PF00607. Gag_p24. 1 hit. PF00552. Integrase. 1 hit. PF02022. Integrase_Zn. 1 hit. PF00075. RnaseH. 1 hit. PF00665. rve. 1 hit. PF00078. RVT_1. 1 hit. PF06815. RVT_connect. 1 hit. PF06817. RVT_thumb. 1 hit. PF00098. zf-CCHC. 2 hits. [Graphical view]
PRINTS	PR00234. HIV1MATRIX.
SMART	SM00343. ZnF_C2HC. 2 hits. [Graphical view]
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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POL_HV1B9

Accession

Primary (citable) accession number: Q73368

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)