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Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Human immunodeficiency virus type 2 subtype A (isolate KR) (HIV-2)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.By similarity
Matrix protein p17: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. 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. 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 (By similarity). Host restriction factors such as 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. Host PIN1 apparently facilitates the virion uncoating. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid.By similarity
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.By similarity
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. 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. 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 (By similarity).PROSITE-ProRule annotationBy similarity
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 tRNA3-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 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.By similarity

Miscellaneous

Reverse transcriptase/ribonuclease H: 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

Catalytic activityi

Endopeptidase for which the P1 residue is preferably hydrophobic.PROSITE-ProRule annotation
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.By similarity
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.By similarity
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
  • Mg2+By similarityNote: Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.By similarity
  • Mg2+By similarityNote: Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.By similarity

Enzyme regulationi

Protease: The viral protease is inhibited by many synthetic protease inhibitors (PIs), such as amprenavir, atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. Use of protease inhibitors in tritherapy regimens permit more ambitious therapeutic strategies. Reverse transcriptase/ribonuclease H: 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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei222 – 223Cis/trans isomerization of proline peptide bond; by human PPIA/CYPABy similarity2
Active sitei537For protease activity; shared with dimeric partnerPROSITE-ProRule annotation1
Metal bindingi721Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi796Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi797Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Sitei1011Essential for RT p66/p51 heterodimerizationBy similarity1
Sitei1024Essential for RT p66/p51 heterodimerizationBy similarity1
Metal bindingi1053Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1088Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1108Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1159Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1234Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi1286Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi1322Magnesium; catalytic; for integrase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri389 – 406CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri410 – 427CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1173 – 1214Integrase-typePROSITE-ProRule annotationAdd BLAST42
DNA bindingi1393 – 1440Integrase-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

GO - Biological processi

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 processDNA integration, DNA recombination, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Viral genome integration, Viral penetration into host nucleus, Viral release from host cell, Virion maturation, Virus entry into host cell
LigandLipid-binding, Magnesium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pol polyprotein
Alternative name(s):
Pr160Gag-Pol
Cleaved into the following 11 chains:
Matrix protein p17
Short name:
MA
Capsid protein p24
Short name:
CA
Spacer peptide 1By similarity
Short name:
SP1
Alternative name(s):
p2
Transframe peptide
Short name:
TF
p6-pol
Short name:
p6*
Alternative name(s):
PR
Retropepsin
Alternative name(s):
Exoribonuclease H (EC:3.1.13.2)
p66 RT
Integrase (EC:2.7.7.-By similarity, EC:3.1.-.-By similarity)
Short name:
IN
Gene namesi
Name:gag-pol
OrganismiHuman immunodeficiency virus type 2 subtype A (isolate KR) (HIV-2)
Taxonomic identifieri73484 [NCBI]
Taxonomic lineageiVirusesOrterviralesRetroviridaeOrthoretrovirinaeLentivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007425 Componenti: Genome

Subcellular locationi

Gag-Pol polyprotein :
  • Host cell membrane ; Lipid-anchor
  • 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.By similarity
Integrase :

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host endosome, Host membrane, Host nucleus, Membrane, Virion

Pathology & Biotechi

Keywords - Diseasei

AIDS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00002612962 – 1463Gag-Pol polyproteinAdd BLAST1462
ChainiPRO_00000425042 – 135Matrix protein p17By similarityAdd BLAST134
ChainiPRO_0000042505136 – 365Capsid protein p24By similarityAdd BLAST230
PeptideiPRO_0000042506366 – 382Spacer peptide 1By similarityAdd BLAST17
ChainiPRO_0000042508383 – 431Nucleocapsid protein p7By similarityAdd BLAST49
PeptideiPRO_0000246745432 – 445Transframe peptideSequence analysisAdd BLAST14
ChainiPRO_0000042510446 – 512p6-polSequence analysisAdd BLAST67
ChainiPRO_0000038671513 – 611ProteaseBy similarityAdd BLAST99
ChainiPRO_0000042511612 – 1170Reverse transcriptase/ribonuclease HBy similarityAdd BLAST559
ChainiPRO_0000042512612 – 1050p51 RTBy similarityAdd BLAST439
ChainiPRO_00000425131051 – 1170p15By similarityAdd BLAST120
ChainiPRO_00000425141171 – 1463IntegraseBy similarityAdd BLAST293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei135Phosphotyrosine; by hostBy similarity1

Post-translational modificationi

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. 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.PROSITE-ProRule annotationBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei135 – 136Cleavage; by viral proteaseBy similarity2
Sitei365 – 366Cleavage; by viral proteaseBy similarity2
Sitei382 – 383Cleavage; by viral proteaseBy similarity2
Sitei431 – 432Cleavage; by viral proteaseSequence analysis2
Sitei445 – 446Cleavage; by viral proteaseBy similarity2
Sitei512 – 513Cleavage; by viral proteaseBy similarity2
Sitei611 – 612Cleavage; by viral proteaseBy similarity2
Sitei1050 – 1051Cleavage; by viral protease; partialBy similarity2
Sitei1170 – 1171Cleavage; by viral proteaseBy similarity2

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRIDEiQ74120

Interactioni

Subunit structurei

Matrix protein p17: Homotrimer; further assembles as hexamers of trimers (By similarity). Matrix protein p17: Interacts with gp41 (via C-terminus) (By similarity). Matrix protein p17: interacts with host CALM1; this interaction induces a conformational change in the Matrix protein, triggering exposure of the myristate group (By similarity). Matrix protein p17: interacts with host AP3D1; this interaction allows the polyprotein trafficking to multivesicular bodies during virus assembly (By similarity). Matrix protein p17: Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase (By similarity). Capsid protein p24: Homodimer; the homodimer further multimerizes as homohexamers or homopentamers. Capsid protein p24: Interacts with human PPIA/CYPA (By similarity); This interaction stabilizes the capsid. Capsid protein p24: Interacts with human NUP153 (By similarity). Capsid protein p24: Interacts with host PDZD8; this interaction stabilizes the capsid (By similarity). Capsid protein p24: Interacts with monkey TRIM5; this interaction destabilizes the capsid (By similarity).Protease: Homodimer, whose active site consists of two apposed aspartic acid residues. Reverse transcriptase/ribonuclease H: 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: Homodimer; possibly can form homotetramer. Integrase: Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase. Integrase: Interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1. Integrase: Interacts with human KPNA3; this interaction might play a role in nuclear import of the pre-integration complex (By similarity). Integrase: Interacts with human NUP153; this interaction might play a role in nuclear import of the pre-integration complex (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ74120
SMRiQ74120
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini532 – 601Peptidase A2PROSITE-ProRule annotationAdd BLAST70
Domaini655 – 845Reverse transcriptasePROSITE-ProRule annotationAdd BLAST191
Domaini1044 – 1167RNase HPROSITE-ProRule annotationAdd BLAST124
Domaini1223 – 1374Integrase catalyticPROSITE-ProRule annotationAdd BLAST152

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 31Interaction with Gp41By similarityAdd BLAST25
Regioni191 – 228Interaction with human PPIA/CYPA and NUP153By similarityAdd BLAST38
Regioni279 – 365Dimerization/Multimerization of capsid protein p24By similarityAdd BLAST87
Regioni513 – 517Dimerization of proteaseBy similarity5
Regioni561 – 567Dimerization of proteaseBy similarity7
Regioni600 – 612Dimerization of proteaseBy similarityAdd BLAST13
Regioni838 – 846RT 'primer grip'By similarity9

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi16 – 22Nuclear export signalBy similarity7
Motifi26 – 32Nuclear localization signalBy similarity7
Motifi1008 – 1024Tryptophan repeat motifBy similarityAdd BLAST17

Domaini

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 accommodating the incoming nucleotide. The RNase H domain stabilizes the association of RT with primer-template.By similarity
Reverse transcriptase/ribonuclease H: The tryptophan repeat motif is involved in RT p66/p51 dimerization (By similarity).By similarity
Integrase: The 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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri389 – 406CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri410 – 427CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1173 – 1214Integrase-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

OrthoDBiVOG09000135

Family and domain databases

CDDicd05482 HIV_retropepsin_like, 1 hit
Gene3Di1.10.10.200, 1 hit
1.10.1200.30, 1 hit
1.10.150.90, 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
InterProiView protein in InterPro
IPR001969 Aspartic_peptidase_AS
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
IPR000071 Lentvrl_matrix_N
IPR012344 Matrix_HIV/RSV_N
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR034170 Retropepsin-like_cat_dom
IPR018061 Retropepsins
IPR008916 Retrov_capsid_C
IPR008919 Retrov_capsid_N
IPR010999 Retrovr_matrix
IPR012337 RNaseH-like_sf
IPR002156 RNaseH_domain
IPR036397 RNaseH_sf
IPR000477 RT_dom
IPR010659 RVT_connect
IPR010661 RVT_thumb
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf
PfamiView protein in Pfam
PF00540 Gag_p17, 1 hit
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
PF06815 RVT_connect, 1 hit
PF06817 RVT_thumb, 1 hit
PF00098 zf-CCHC, 2 hits
PRINTSiPR00234 HIV1MATRIX
SMARTiView protein in SMART
SM00343 ZnF_C2HC, 2 hits
SUPFAMiSSF46919 SSF46919, 1 hit
SSF47836 SSF47836, 1 hit
SSF47943 SSF47943, 1 hit
SSF50122 SSF50122, 1 hit
SSF50630 SSF50630, 1 hit
SSF53098 SSF53098, 2 hits
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

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

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: Q74120-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGARSSVLRG KKVDELEKIR LRPGGKKKYR LKHIVWAANE LGKFGLAESL
60 70 80 90 100
LESKEGCQKI ITVLDPLVPT GSENLKSLFN TVCVIWCLHA EEKVKDTEGA
110 120 130 140 150
KQIVQRHLVA ETGTADKMPS TSRPAAPPSG RGGNYPVQQI AGNYSHVPLS
160 170 180 190 200
PRTLNAWVKL VEEKKFGAEV VPGFQALSEG CTPYDINQML NCVGDHQAAM
210 220 230 240 250
QIIREIINEE AADWDVQHPI PGPLPAGQLR EPRGSDIAGT TSTVEEQIQW
260 270 280 290 300
MFRAQNPIPV GNIYRRWIQI GLQKCVRMYN PTNILDVKQG PKEPFQSYVD
310 320 330 340 350
RFYKSLRAEQ TDPAVKNWMT QTLLVQNANP DCKLVLKGLG MNPTLEEMLT
360 370 380 390 400
ACQGIGGPGQ KARLMAEALK EALAPAPIPF AAAQQRRTIK CWNCGKDGHS
410 420 430 440 450
ARQCRAPRRQ GCWKCGKSGH VMANCPERQA GFLRDWPMGK EASQLPRDPS
460 470 480 490 500
PAGADTNSTP SRPSSRPARE VLAAREEAER AENETIQGGD RGLTAPRTRR
510 520 530 540 550
DTTQRGDRGF AAPQFSLWKR PVVTAYVEGQ PVEVLLDTGA DDSIVAGIEL
560 570 580 590 600
GSNYSPKIVG GIGGFINTKE YKNVEIKVLN KKVKATIMTG DTPINIFGRN
610 620 630 640 650
ILTALGMSLN LPVAKVDPIK VILKPGKDGP KVRQWPLTKE KIEALKEICE
660 670 680 690 700
KMEREGQLEE APPTNPYNTP TFAIKKKDKN KWRMLIDFRE LNKVTQEFTE
710 720 730 740 750
IQLGIPHPAG LAKKRRITVL DIGDAYFSIP LHEDFRQYTA FTLPTVNNAE
760 770 780 790 800
PGKRYIYKVL PQGWKGSPAI FQHTMRQVLE PFRKANPDVI LVQYMDDILI
810 820 830 840 850
ASDRTDLEHD RTVLQLKELL NGLGFSTPDE KFQKDPPYKW MGYELWPTKW
860 870 880 890 900
KLQKIQLPQK EVWTVNDIQK LVGVLNWAAQ IYPGIKTKHL CRLIRGKMTL
910 920 930 940 950
TEEVQWTELA EAELEENKII LSQEQEGCYY QEEKELEATV QKDQDNQWTY
960 970 980 990 1000
KIHQGEKILK VGKYAKIKNT HTNGVRLLAH VVQKIGKEAL VIWGRIPKFH
1010 1020 1030 1040 1050
LPVERETWEQ WWDNYWQVTW IPDWDFVSTP PLVRLAFNLV KDPIPGEETF
1060 1070 1080 1090 1100
YTDGSCNRQS KEGKAGYITD RGRDKVRILE QTTNQQAELE AFAMALTDSG
1110 1120 1130 1140 1150
PKANIIVDSQ YVMGIVAGQP TESESKLVNQ IIEEMIKKET LYVAWVPAHK
1160 1170 1180 1190 1200
GIGGNQEVDH LVSQGIRQVL FLEKIEPAQE EHEKYHSNVK ELSHKFGLPK
1210 1220 1230 1240 1250
LVARQIVNTC AQCQQKGEAI HGQVDAELGT WQMDCTHLEG KIIIVAVHVA
1260 1270 1280 1290 1300
SGFIEAEVIP QETGRQTALF LLKLASRWPI THLHTDNGAN FTSQEVKMVA
1310 1320 1330 1340 1350
WWTGIEQSFG VPYNPQSQGV VEAMNHHLKN QISRIREQAN TMETIVLMAV
1360 1370 1380 1390 1400
HCMNFKRRGG IGDMTPAERL INMITTEQEI QFLHAKNSKL KNFRVYFREG
1410 1420 1430 1440 1450
RDQLWKGPGE LLWKGDGAVI VKVGTDIKIV PRRKAKIIRD YGGRREVDSS
1460
SHLEGTREDG EVA
Note: Produced by -1 ribosomal frameshifting.
Length:1,463
Mass (Da):164,851
Last modified:January 23, 2007 - v3
Checksum:i2F11E21FD52E861F
GO
Isoform Gag polyprotein (identifier: Q74119-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry Q74119.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.
Length:521
Mass (Da):57,812
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22047 Genomic DNA Translation: AAA64576.1 Sequence problems.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Similar proteinsi

Entry informationi

Entry nameiPOL_HV2KR
AccessioniPrimary (citable) accession number: Q74120
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 154 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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