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P05895

- POL_SIVVT

UniProt

P05895 - POL_SIVVT

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Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Simian immunodeficiency virus agm.vervet (isolate AGM TYO-1) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi

Functioni

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).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 myristointegration complex. The myristoylation signal and the NLS 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).By similarity
Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with host PPIA/CYPA protects the virus from restriction by host TRIM5-alpha and from an unknown antiviral activity in host cells. This capsid restriction by TRIM5 is one of the factors which restricts SIV to the simian species (By similarity).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).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. 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 annotation
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 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 can probably 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).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 SIV genome, a 5 bp duplication of host DNA is produced at the ends of SIV integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity).By similarity

Catalytic activityi

Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.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.
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation

Cofactori

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).By similarity
Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions (By similarity).By similarity

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei145 – 1462Cleavage; by viral proteaseBy similarity
Sitei233 – 2342Cis/trans isomerization of proline peptide bond; by human PPIA/CYPABy similarity
Sitei376 – 3772Cleavage; by viral proteaseBy similarity
Sitei443 – 4442Cleavage; by viral proteaseBy similarity
Sitei515 – 5162Cleavage; by viral proteaseBy similarity
Active sitei540 – 5401For protease activity; shared with dimeric partnerPROSITE-ProRule annotation
Sitei616 – 6172Cleavage; by viral proteaseSequence Analysis
Metal bindingi728 – 7281Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi803 – 8031Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi804 – 8041Magnesium; catalytic; for reverse transcriptase activityBy similarity
Sitei1018 – 10181Essential for RT p66/p51 heterodimerizationBy similarity
Sitei1031 – 10311Essential for RT p66/p51 heterodimerizationBy similarity
Sitei1057 – 10582Cleavage; by viral proteaseBy similarity
Metal bindingi1114 – 11141Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1165 – 11651Magnesium; catalytic; for RNase H activityBy similarity
Sitei1176 – 11772Cleavage; by viral proteaseBy similarity
Metal bindingi1240 – 12401Magnesium; catalytic; for integrase activityBy similarity
Metal bindingi1292 – 12921Magnesium; catalytic; for integrase activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri402 – 41918CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri423 – 44018CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1179 – 122042Integrase-typePROSITE-ProRule annotationAdd
BLAST
DNA bindingi1399 – 144648Integrase-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. DNA-directed DNA polymerase activity Source: UniProtKB-KW
  4. exoribonuclease H activity Source: UniProtKB-EC
  5. RNA binding Source: UniProtKB-KW
  6. RNA-directed DNA polymerase activity Source: UniProtKB-KW
  7. RNA-DNA hybrid ribonuclease activity Source: InterPro
  8. structural molecule activity Source: InterPro
  9. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA integration Source: UniProtKB-KW
  2. DNA recombination Source: UniProtKB-KW
  3. establishment of integrated proviral latency Source: UniProtKB-KW
  4. suppression by virus of host gene expression Source: UniProtKB-KW
  5. viral entry into host cell Source: UniProtKB-KW
  6. viral penetration into host nucleus Source: UniProtKB-KW
  7. viral release from host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

Keywords - Biological processi

DNA 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, Virion maturation, Virus entry into host cell, Virus exit from host cell

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, RNA-binding, Viral nucleoprotein, Zinc

Protein family/group databases

MEROPSiA02.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pol polyprotein
Alternative name(s):
Pr160Gag-Pol
Cleaved into the following 9 chains:
Matrix protein p17
Short name:
MA
Capsid protein p24
Short name:
CA
p6-pol
Short name:
p6*
Alternative name(s):
PR
Retropepsin
Alternative name(s):
Exoribonuclease H (EC:3.1.13.2)
p66 RT
Integrase
Short name:
IN
Gene namesi
Name:gag-pol
OrganismiSimian immunodeficiency virus agm.vervet (isolate AGM TYO-1) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet)
Taxonomic identifieri11731 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiCercopithecidae (Old World monkeys) [TaxID: 9527]

Subcellular locationi

Chain Matrix protein p17 : Virion Curated. Host nucleus By similarity. Host cytoplasm By similarity. Host cell membrane Curated; Lipid-anchor Curated
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).By similarity
Chain Integrase : Virion Curated. Host nucleus Curated. Host cytoplasm Curated
Note: Nuclear at initial phase, cytoplasmic at assembly.Curated

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. host cell nucleus Source: UniProtKB-KW
  3. host cell plasma membrane Source: UniProtKB-KW
  4. intracellular Source: GOC
  5. membrane Source: UniProtKB-KW
  6. viral nucleocapsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 14671466Gag-Pol polyproteinPRO_0000306015Add
BLAST
Chaini2 – 145144Matrix protein p17By similarityPRO_0000306016Add
BLAST
Chaini146 – 376231Capsid protein p24By similarityPRO_0000306017Add
BLAST
Chaini377 – 44367Nucleocapsid protein p7By similarityPRO_0000306018Add
BLAST
Chaini444 – 51572p6-polSequence AnalysisPRO_0000306019Add
BLAST
Chaini516 – 616101ProteaseBy similarityPRO_0000306020Add
BLAST
Chaini617 – 1176560Reverse transcriptase/ribonuclease HBy similarityPRO_0000306021Add
BLAST
Chaini617 – 1057441p51 RTBy similarityPRO_0000306022Add
BLAST
Chaini1058 – 1176119p15By similarityPRO_0000306023Add
BLAST
Chaini1177 – 1467291IntegraseBy similarityPRO_0000306024Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity

Post-translational modificationi

Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit.PROSITE-ProRule annotation
Capsid protein p24 is phosphorylated.

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRIDEiP05895.

Interactioni

Subunit structurei

Matrix protein p17 is a trimer. Interacts with gp120. 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. The integrase is a homodimer and possibly a homotetramer (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP05895.
SMRiP05895. Positions 6-106, 155-440, 517-610, 623-1173, 1177-1222, 1232-1446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini535 – 60672Peptidase A2PROSITE-ProRule annotationAdd
BLAST
Domaini662 – 852191Reverse transcriptasePROSITE-ProRule annotationAdd
BLAST
Domaini1051 – 1173123RNase HPROSITE-ProRule annotationAdd
BLAST
Domaini1230 – 1380151Integrase catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni845 – 8539RT 'primer grip'By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi16 – 227Nuclear export signalBy similarity
Motifi26 – 327Nuclear localization signalBy similarity
Motifi1015 – 103117Tryptophan repeat motifBy similarityAdd
BLAST

Domaini

The p66 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).By similarity
The tryptophan repeat motif is involved in RT p66/p51 dimerization.By similarity

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
Contains 1 integrase-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 integrase-type zinc finger.PROSITE-ProRule annotation
Contains 1 peptidase A2 domain.PROSITE-ProRule annotation
Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation
Contains 1 RNase H domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri402 – 41918CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri423 – 44018CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1179 – 122042Integrase-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

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.
4.10.60.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
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.
IPR012344. Matrix_N_HIV/RSV.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00540. 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.
[Graphical view]
PRINTSiPR00234. HIV1MATRIX.
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF46919. SSF46919. 1 hit.
SSF47353. SSF47353. 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.
PROSITEiPS50175. 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]

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. Align

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: P05895) [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
MGAATSALNR RQLDKFEHIR LRPTGKKKYQ IKHLIWAGKE MERFGLHERL
60 70 80 90 100
LESEEGCKKI IEVLYPLEPT GSEGLKSLFN LVCVLFCVHK DKEVKDTEEA
110 120 130 140 150
VAIVRQCCHL VEKERNAERN TTETSSGQKK NDKGVTVPPG GSQNFPAQQQ
160 170 180 190 200
GNAWIHVPLS PRTLNAWVKA VEEKKFGAEI VPMFQALSEG CTPYDINQML
210 220 230 240 250
NVLGDHQGAL QIVKEIINEE AAQWDIAHPP PAGPLPAGQL RDPRGSDIAG
260 270 280 290 300
TTSTVQEQLE WIYTANPRVD VGAIYRRWII LGLQKCVKMY NPVSVLDIRQ
310 320 330 340 350
GPKEAFKDYV DRFYKAIRAE QASGEVKQWM TESLLIQNAN PDCKVILKGL
360 370 380 390 400
GMHPTLEEML TACQGVGGPS YKAKVMAEMM QNMQSQNMMQ QGGQRGRPRP
410 420 430 440 450
PVKCYNCGKF GHMQRQCPEP RKMRCLKCGK PGHLAKDCRG QVNFFRVWTV
460 470 480 490 500
DGGKTEKFSR RYSWSGTECA SSTERHHPIR PSKEAPAAIC RERETTEGAK
510 520 530 540 550
EESTGNESGL DRGIFFELPL WRRPIKTVYI EGVPIKALLD TGADDTIIKE
560 570 580 590 600
NDLQLSGPWR PKIIGGIGGG LNVKEYNDRE VKIEDKILRG TILLGATPIN
610 620 630 640 650
IIGRNLLAPA VPRLVMGQLS EKIPVTPVKL KEGARGPCVR QWPLSKEKIE
660 670 680 690 700
ALQEICSQLE QEGKISRVGG ENAYNTPIFC IKKKDKSQWR MLVDFRELNK
710 720 730 740 750
ATQDFFEVQL GIPHPAGLRK MRQITVLDVG DAYYSIPLDP NFRKYTAFTI
760 770 780 790 800
PTVNNQGPGI RYQFNCLPQG WKGSPTIFQN TAASILEEIK RNLPALTIVQ
810 820 830 840 850
YMDDLWVGSQ ENEHTHDKLV EQLRTKLQAW GLETPEKKMQ KEPPYEWMGY
860 870 880 890 900
KLWPHKWELS RIQLEEKDEW TVNDIQKLVG KLNWAAQLYP GLKTRICKLI
910 920 930 940 950
TGGKKNLLEL VAWTPEAEAE YAENAEILKT EQEGTYYKPG IPIRAAVQKL
960 970 980 990 1000
EGGQWSYQFK QEGQVLKVGK YTKQKNTHTN ELRTLAGLVQ KICKEALVIW
1010 1020 1030 1040 1050
GILPVLELPI EREVWEQWWA DYWQVSWIPE WDFVSTPPLL KLWYTLTKEP
1060 1070 1080 1090 1100
IPKEDVYYVG ACNRNSKEGK AGYISQYGKQ RVETLENTTN QQAKLTAIKM
1110 1120 1130 1140 1150
ALEDSGPNVN IVTDSQYAMG ILTAQPTQSD SPLVEQIIAL MIQKQQIYLQ
1160 1170 1180 1190 1200
WVPAHKGIGG NEEIDKLVSK GIRRVLFLEK IEEAQEKHER YHNNWKNLAD
1210 1220 1230 1240 1250
TYGLPQIVAK EIVAMCPKCQ IKGEPVHGQV DASPGTWQMD CTHLEKKVVI
1260 1270 1280 1290 1300
VAVHVASGFI EAEVIPRETG KETAKFLLKI LSRWPITQLH TDNGPNFTSQ
1310 1320 1330 1340 1350
EVAAICWWGK IEHTTGIPYN PQSQGSIESM NKQLKEIIGK IRDDCQYTEA
1360 1370 1380 1390 1400
AVLMACILHN FKRKGGIGGQ TSAERLINII TTQLEIQHLQ TKIQKILNFR
1410 1420 1430 1440 1450
VYYREGRDPV WKGPAQLIWK GEGAVVLKDG SDLKVVPRRK AKIIKDYEPK
1460
QRVGNEGDVE GTRGSDN

Note: Produced by -1 ribosomal frameshifting.

Length:1,467
Mass (Da):166,058
Last modified:October 2, 2007 - v2
Checksum:i648A153B331B9992
GO
Isoform Gag polyprotein (identifier: P05892-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry P05892.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by conventional translation.

Length:519
Mass (Da):58,143
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07805 Genomic DNA. Translation: CAA30658.1. Sequence problems.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07805 Genomic DNA. Translation: CAA30658.1 . Sequence problems.

3D structure databases

ProteinModelPortali P05895.
SMRi P05895. Positions 6-106, 155-440, 517-610, 623-1173, 1177-1222, 1232-1446.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi A02.003.

Proteomic databases

PRIDEi P05895.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.10.200. 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.
4.10.60.10. 1 hit.
InterProi IPR001969. Aspartic_peptidase_AS.
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.
IPR012344. Matrix_N_HIV/RSV.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
IPR001878. Znf_CCHC.
[Graphical view ]
Pfami 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.
[Graphical view ]
PRINTSi PR00234. HIV1MATRIX.
SMARTi SM00343. ZnF_C2HC. 2 hits.
[Graphical view ]
SUPFAMi SSF46919. SSF46919. 1 hit.
SSF47353. SSF47353. 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.
PROSITEi 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 ]
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Publicationsi

  1. "Sequence of simian immunodeficiency virus from African green monkey, a new member of the HIV/SIV group."
    Fukasawa M., Miura T., Hasegawa A., Morikawa S., Tsujimoto H., Miki K., Kitamura T., Hayami M.
    Nature 333:457-461(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPOL_SIVVT
AccessioniPrimary (citable) accession number: P05895
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 2, 2007
Last modified: October 29, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

This is an African green monkey isolate.
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.

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

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