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P12451

- POL_HV2SB

UniProt

P12451 - POL_HV2SB

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Protein
Gag-Pol polyprotein
Gene
gag-pol
Organism
Human immunodeficiency virus type 2 subtype A (isolate SBLISY) (HIV-2)
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.
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 play 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. 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.
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 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 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 By similarity.
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.
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 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration By similarity.

Catalytic activityi

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).
Endopeptidase for which the P1 residue is preferably hydrophobic.

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei135 – 1362Cleavage; by viral protease By similarity
Sitei222 – 2232Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA By similarity
Sitei364 – 3652Cleavage; by viral protease By similarity
Sitei381 – 3822Cleavage; by viral protease By similarity
Sitei430 – 4312Cleavage; by viral protease Reviewed prediction
Sitei444 – 4452Cleavage; by viral protease By similarity
Sitei511 – 5122Cleavage; by viral protease By similarity
Active sitei536 – 5361For protease activity; shared with dimeric partner By similarity
Sitei610 – 6112Cleavage; by viral protease By similarity
Metal bindingi720 – 7201Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal bindingi795 – 7951Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal bindingi796 – 7961Magnesium; catalytic; for reverse transcriptase activity By similarity
Sitei1010 – 10101Essential for RT p66/p51 heterodimerization By similarity
Sitei1023 – 10231Essential for RT p66/p51 heterodimerization By similarity
Sitei1049 – 10502Cleavage; by viral protease; partial By similarity
Metal bindingi1052 – 10521Magnesium; catalytic; for RNase H activity By similarity
Metal bindingi1087 – 10871Magnesium; catalytic; for RNase H activity By similarity
Metal bindingi1107 – 11071Magnesium; catalytic; for RNase H activity By similarity
Metal bindingi1158 – 11581Magnesium; catalytic; for RNase H activity By similarity
Sitei1169 – 11702Cleavage; by viral protease By similarity
Metal bindingi1233 – 12331Magnesium; catalytic; for integrase activity By similarity
Metal bindingi1285 – 12851Magnesium; catalytic; for integrase activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri388 – 40518CCHC-type 1
Add
BLAST
Zinc fingeri409 – 42618CCHC-type 2
Add
BLAST
Zinc fingeri1172 – 121342Integrase-type
Add
BLAST
DNA bindingi1392 – 143948Integrase-type
Add
BLAST

GO - Molecular functioni

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

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
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
Short name:
IN
Gene namesi
Name:gag-pol
OrganismiHuman immunodeficiency virus type 2 subtype A (isolate SBLISY) (HIV-2)
Taxonomic identifieri11718 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007427: Genome

Subcellular locationi

Chain Matrix protein p17 : Virion Reviewed prediction. Host nucleus By similarity. Host cytoplasm By similarity. Host cell membrane; Lipid-anchor Reviewed prediction
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.
Chain Capsid protein p24 : Virion Reviewed prediction
Chain Integrase : Virion Reviewed prediction. Host nucleus Reviewed prediction. Host cytoplasm Reviewed prediction
Note: Nuclear at initial phase, cytoplasmic at assembly Reviewed prediction.

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-SubCell
  2. host cell nucleus Source: UniProtKB-SubCell
  3. host cell plasma membrane Source: UniProtKB-SubCell
  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

Pathology & Biotechi

Keywords - Diseasei

AIDS

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host By similarity
Chaini2 – 14621461Gag-Pol polyprotein
PRO_0000261299Add
BLAST
Chaini2 – 135134Matrix protein p17 By similarity
PRO_0000042515Add
BLAST
Chaini136 – 364229Capsid protein p24 By similarity
PRO_0000042516Add
BLAST
Peptidei365 – 38117Spacer peptide p2 By similarity
PRO_0000042517Add
BLAST
Chaini382 – 43049Nucleocapsid protein p7 By similarity
PRO_0000042519Add
BLAST
Peptidei431 – 44414Transframe peptide Reviewed prediction
PRO_0000246748Add
BLAST
Chaini445 – 51167p6-pol Reviewed prediction
PRO_0000042521Add
BLAST
Chaini512 – 61099Protease By similarity
PRO_0000038672Add
BLAST
Chaini611 – 1169559Reverse transcriptase/ribonuclease H By similarity
PRO_0000042522Add
BLAST
Chaini611 – 1049439p51 RT By similarity
PRO_0000042523Add
BLAST
Chaini1050 – 1169120p15 By similarity
PRO_0000042524Add
BLAST
Chaini1170 – 1462293Integrase By similarity
PRO_0000042525Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Lipoprotein, Myristate

Interactioni

Subunit structurei

Matrix protein p17 is a trimer. 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.

Structurei

3D structure databases

ProteinModelPortaliP12451.
SMRiP12451. Positions 2-135, 145-380, 384-429, 512-610, 613-1165, 1170-1215, 1224-1381, 1385-1439.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini531 – 60070Peptidase A2
Add
BLAST
Domaini654 – 844191Reverse transcriptase
Add
BLAST
Domaini1043 – 1166124RNase H
Add
BLAST
Domaini1222 – 1373152Integrase catalytic
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni837 – 8459RT 'primer grip' By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi16 – 227Nuclear export signal By similarity
Motifi26 – 327Nuclear localization signal By similarity
Motifi1007 – 102317Tryptophan repeat motif By similarity
Add
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.
The tryptophan repeat motif is involved in RT p66/p51 dimerization By similarity.

Sequence similaritiesi

Contains 1 RNase H domain.

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: P12451-1) [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.

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MGAKNSVLRG KKADELEKIR LRPGGKKKYR LKHIVWAANE LDRFGLTESL     50
LESKEGCQKI ISVLEPLVPT GSENLKSLYN TTCVIWCLHA EEKVKDTEEA 100
KRIVGRHLVA ETETAEKMPN ISRPTAPPSG KGGNFPVQQI GGNYVHLPLS 150
PRTLNAWVKL VEEKKFGAEV VPGFQALSEG CTPYDINQML NCVGDHQAAM 200
QIIREIINEE AADWDVQHPI PGPLPAGQLR DPRGSDIAGT TSTVEEQIEW 250
MYRQENPVPV GNIYRRWIQI GLQKCVRMYN PTNILDIKQG PKESFQSYVD 300
RFYKSLRAEQ TDAAVKNWMT QTLLVQSNPD CKLVLKGLGM NPTLEEMLTA 350
CQGIGGPGQK ARLMAEALKE AMRPAPIPFA AAQQKRAIKC WNCGKEGHSA 400
RQCRAPRRQG CWKCGKSGHI MANCPDRQAG FLRAWTMGKE APQLPRGPKF 450
AGANTNSTPN GSSSGPTGEV HAAREKTERA ETKTIQRSDR GLAASRARRD 500
TTQRDDRGLA APQFSLWKRP VVTAYIEDQP VEVLLDTGAD DSIVAGIELG 550
SNYSPKIVGG IGGFINTKEY KDVEIRVLNK KVRATIMTGD TPINIFGRNI 600
LTALGMSLNL PVAKIEPVKV TLKPGKDGPK QRQWPLTREK IEALREICEK 650
MEREGQLEEA PPTNPYNTPT FAIKKKDKNK WRMLIDFREL NKVTQDFTEV 700
QLGIPHPAGL AKKRRITVLD VGDAYFSIPL YEDFRQYTAF TLPSVNNAEP 750
GKRYIYKVLP QGWKGSPAIF QYTMRQVLEP FRKANPDVII VQYMDDILIA 800
SDRTDLEHDK VVLQLKELLN GLGFSTPDEK FQKDPPYQWM GYELWPTKWK 850
LQKIQLPQKE VWTVNDIQKL VGVLNWAAQI YPGIKTKHLC KLIRGKMTPT 900
EEVQWTELAE AELEENKIIL SQEQEGHYYQ EEKELEATVQ KDQDNQWTYK 950
VHQGEKILKV GKYAKIKNTH TNGVRLLAQV VQKIGKEALV IWGRIPKFHL 1000
PVERETWEQW WDNYWQVTWI PDWDFVSTPP LVRLAFNLVK DPIPGAETFY 1050
TDGSCNRQSK EGKAGYITDR GKDKVRILEQ TTNQQAELEA FAMAVTDSGP 1100
KVNIVVDSQY VMGIVTGQPA ESESRIVNKI IEEMIKKEAI YVAWVPAHKG 1150
IGGNQEIDHL VSQGIRQVLF LERIEPAQEE HGKYHSNVKE LAHKFGLPNL 1200
VARQIVNTCA QCQQKGEAIH GQVNAELGTW QMDCTHLEGK IIIVAVHVAS 1250
GFIEAEVIPQ ESGRQTALFL LKLASRWPIT HLHTDNGANF TSQEVKMVAW 1300
WVGIEQSFGV PYNPQSQGVV EAMNHHLKNQ IERIREQANT METIVLMAVH 1350
CMNFKRRGGI GDMTPVERLV NMITTEQEIQ FLQAKNSKLK NFRVYFREGR 1400
NQLWQGPGEL LWKGDGAVIV KVGTDIKVIP RRKAKIIRDY GPRQEMDSGS 1450
HLEGAREDGE MA 1462

Note: Produced by -1 ribosomal frameshifting.

Length:1,462
Mass (Da):165,014
Last modified:January 23, 2007 - v3
Checksum:iDBA366324EA0167E
GO
Isoform Gag polyprotein (identifier: P12450-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry P12450.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by conventional translation.

Length:520
Mass (Da):58,175
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04498 Genomic DNA. Translation: AAB00746.1. Sequence problems.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04498 Genomic DNA. Translation: AAB00746.1 . Sequence problems.

3D structure databases

ProteinModelPortali P12451.
SMRi P12451. Positions 2-135, 145-380, 384-429, 512-610, 613-1165, 1170-1215, 1224-1381, 1385-1439.
ModBasei Search...
MobiDBi Search...

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 ]
ProtoNeti Search...

Publicationsi

  1. "Molecular and biological characterization of a replication competent human immunodeficiency type 2 (HIV-2) proviral clone."
    Franchini G., Fargnoli K.A., Giombini F., Jagodzinski L.L., de Rossi A., Bosch M., Biberfeld G., Fenyo A.M., Albert J., Gallo R.C., Wong-Staal F.
    Proc. Natl. Acad. Sci. U.S.A. 86:2433-2437(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Proteolytic processing and particle maturation."
    Vogt V.M.
    Curr. Top. Microbiol. Immunol. 214:95-131(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  3. Cited for: REVIEW.
  4. "Mechanisms of retroviral recombination."
    Negroni M., Buc H.
    Annu. Rev. Genet. 35:275-302(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. Cited for: REVIEW.

Entry informationi

Entry nameiPOL_HV2SB
AccessioniPrimary (citable) accession number: P12451
Secondary accession number(s): Q85570
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Complete proteome, 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

Dasty 3

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