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P05896 (POL_SIVM1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gag-Pol polyprotein
Alternative name(s):
Pr160Gag-Pol

Cleaved into the following 9 chains:

  1. Matrix protein p17
    Short name=MA
  2. Capsid protein p24
    Short name=CA
  3. Nucleocapsid protein p7
    Short name=NC
  4. p6-pol
    Short name=p6*
  5. Protease
    EC=3.4.23.16
    Alternative name(s):
    PR
    Retropepsin
  6. Reverse transcriptase/ribonuclease H
    EC=2.7.7.49
    EC=2.7.7.7
    EC=3.1.26.13
    Alternative name(s):
    Exoribonuclease H
    EC=3.1.13.2
    p66 RT
  7. p51 RT
  8. p15
  9. Integrase
    Short name=IN
Gene names
Name:gag-pol
OrganismSimian immunodeficiency virus (isolate Mm142-83) (SIV-mac) (Simian immunodeficiency virus rhesus monkey) [Complete proteome]
Taxonomic identifier11733 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostCercopithecidae (Old World monkeys) [TaxID: 9527]

Protein attributes

Sequence length1448 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 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.

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.

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. 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.

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 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.

Catalytic activity

Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.

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).

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.

Subunit structure

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.

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 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.

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 By similarity.

Capsid protein p24 is phosphorylated.

Miscellaneous

This is a macaque 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.

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 processDNA integration
DNA recombination
Host gene expression shutoff by virus
Host translation 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
   Cellular componentCapsid protein
Host cell membrane
Host cytoplasm
Host membrane
Host nucleus
Membrane
Virion
   Coding sequence diversityRibosomal frameshifting
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Magnesium
Metal-binding
RNA-binding
Viral nucleoprotein
Zinc
   Molecular functionAspartyl protease
DNA-directed DNA polymerase
Endonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Protease
RNA-directed DNA polymerase
Transferase
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processDNA integration

Inferred from electronic annotation. Source: UniProtKB-KW

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

establishment of integrated proviral latency

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host translation

Inferred from electronic annotation. Source: UniProtKB-KW

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

viral penetration into host nucleus

Inferred from electronic annotation. Source: UniProtKB-KW

viral release from host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from electronic annotation. Source: GOC

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral nucleocapsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-DNA hybrid ribonuclease activity

Inferred from electronic annotation. Source: InterPro

RNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

aspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

exoribonuclease H activity

Inferred from electronic annotation. Source: UniProtKB-EC

structural molecule activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

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: P05896-1)

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: P05894-1)

The sequence of this isoform can be found in the external entry P05894.
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 14481447Gag-Pol polyprotein
PRO_0000306035
Chain2 – 135134Matrix protein p17 By similarity
PRO_0000306036
Chain136 – 364229Capsid protein p24 By similarity
PRO_0000306037
Chain365 – 43369Nucleocapsid protein p7 By similarity
PRO_0000306038
Chain434 – 50067p6-pol Potential
PRO_0000306039
Chain501 – 59696Protease By similarity
PRO_0000306040
Chain597 – 1155559Reverse transcriptase/ribonuclease H By similarity
PRO_0000306041
Chain597 – 1035439p51 RT By similarity
PRO_0000306042
Chain1036 – 1155120p15 By similarity
PRO_0000306043
Chain1156 – 1448293Integrase By similarity
PRO_0000306044

Regions

Domain517 – 58670Peptidase A2
Domain640 – 830191Reverse transcriptase
Domain1029 – 1152124RNase H
Domain1209 – 1359151Integrase catalytic
Zinc finger391 – 40818CCHC-type 1
Zinc finger412 – 42918CCHC-type 2
Zinc finger1158 – 119942Integrase-type
DNA binding1378 – 142548Integrase-type
Region823 – 8319RT 'primer grip' By similarity
Motif16 – 227Nuclear export signal By similarity
Motif26 – 327Nuclear localization signal By similarity
Motif993 – 100917Tryptophan repeat motif By similarity

Sites

Active site5221For protease activity; shared with dimeric partner By similarity
Metal binding7061Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding7811Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding7821Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding10381Magnesium; catalytic; for RNase H activity By similarity
Metal binding10731Magnesium; catalytic; for RNase H activity By similarity
Metal binding10931Magnesium; catalytic; for RNase H activity By similarity
Metal binding11441Magnesium; catalytic; for RNase H activity By similarity
Metal binding12191Magnesium; catalytic; for integrase activity By similarity
Metal binding12711Magnesium; catalytic; for integrase activity By similarity
Site135 – 1362Cleavage; by viral protease By similarity
Site364 – 3652Cleavage; by viral protease By similarity
Site433 – 4342Cleavage; by viral protease By similarity
Site500 – 5012Cleavage; by viral protease By similarity
Site596 – 5972Cleavage; by viral protease By similarity
Site9961Essential for RT p66/p51 heterodimerization By similarity
Site10091Essential for RT p66/p51 heterodimerization By similarity
Site1035 – 10362Cleavage; by viral protease By similarity
Site1155 – 11562Cleavage; by viral protease By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine; by host By similarity

Secondary structure

............................................ 1448
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Gag-Pol polyprotein [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 460D13331B3E68E5

FASTA1,448163,372
        10         20         30         40         50         60 
MGARNSVLSG KKADELEKIR LRPGGKKKYM LKHVVWAANE LDRFGLAESL LENKEGCQKI 

        70         80         90        100        110        120 
LSVLAPLVPT GSENLKSLYN TVCVIWCIHA EEKVKHTEEA KQIVQRHLVM ETGTAETMPK 

       130        140        150        160        170        180 
TSRPTAPFSG RGGNYPVQQI GGNYTHLPLS PRTLNAWVKL IEEKKFGAEV VSGFQALSEG 

       190        200        210        220        230        240 
CLPYDINQML NCVGDHQAAM QIIRDIINEE AADWDLQHPQ QAPQQGQLRE PSGSDIAGTT 

       250        260        270        280        290        300 
STVEEQIQWM YRQQNPIPVG NIYRRWIQLG LQKCVRMYNP TNILDVKQGP KEPFQSYVDR 

       310        320        330        340        350        360 
FYKSLRAEQT DPAVKNWMTQ TLLIQNANPD CKLVLKGLGT NPTLEEMLTA CQGVGGPGQK 

       370        380        390        400        410        420 
ARLMAEALKE ALAPAPIPFA AAQQKGPRKP IKCWNCGKEG HSARQCRAPR RQGCWKCGKM 

       430        440        450        460        470        480 
DHVMAKCPNR QAGFFRPWPL GKEAPQFPHG SSASGADANC SPRRTSCGSA KELHALGQAA 

       490        500        510        520        530        540 
ERKQREALQG GDRGFAAPQF SLWRRPVVTA HIEGQPVEVL LDTGADDSIV TGIELGPHYT 

       550        560        570        580        590        600 
PKIVGGIGGF INTKEYKNVE IEVLGKRIKG TIMTGDTPIN IFGRNLLTAL GMSLNLPIAK 

       610        620        630        640        650        660 
VEPVKSPLKP GKDGPKLKQW PLSKEKIVAL REICEKMEKD GQLEEAPPTN PYNTPTFAIK 

       670        680        690        700        710        720 
KKDKNKWRML IDFRELNRVT QDFTEVQLGI PHPAGLAKRK RITVLDIGDA YFSIPLDEEF 

       730        740        750        760        770        780 
RQYTAFTLPS VNNAEPGKRY IYKVLPQGWK GSPAIFQYTM RHVLEPFRKA NPDVTLVQYM 

       790        800        810        820        830        840 
DDILIASDRT DLEHDRVVLQ LKELLNSIGF SSPEEKFQKD PPFQWMGYEL WPTKWKLQKI 

       850        860        870        880        890        900 
ELPQRETWTV NDIQKLVGVL NWAAQIYPGI KTKHLCRLIR GKMTLTEEVQ WTEMAEAEYE 

       910        920        930        940        950        960 
ENKIILSQEQ EGCYYQESKP LEATVIKSQD NQWSYKIHQE DKILKVGKFA KIKNTHTNGV 

       970        980        990       1000       1010       1020 
RLLAHVIQKI GKEAIVIWGQ VPKFHLPVEK DVWEQWWTDY WQVTWIPEWD FISTPPLVRL 

      1030       1040       1050       1060       1070       1080 
VFNLVKDPIE GEETYYVDGS CSKQSKEGKA GYITDRGKDK VKVLEQTTNQ QAELEAFLMA 

      1090       1100       1110       1120       1130       1140 
LTDSGPKANI IVDSQYVMGI ITGCPTESES RLVNQIIEEM IKKTEIYVAW VPAHKGIGGN 

      1150       1160       1170       1180       1190       1200 
QEIDHLVSQG IRQVLFLEKI EPAQEEHSKY HSNIKELVFK FGLPRLVAKQ IVDTCDKCHQ 

      1210       1220       1230       1240       1250       1260 
KGEAIHGQVN SDLGTWQMDC THLEGKIVIV AVHVASGFIE AEVIPQETGR QTALFLLKLA 

      1270       1280       1290       1300       1310       1320 
SRWPITHLHT DNGANFASQE VKMVAWWAGI EHTFGVPYNP QSQGVVEAMN HHLKNQIDRI 

      1330       1340       1350       1360       1370       1380 
REQANSVETI VLMAVHCMNF KRRGGIGDMT PAERLINMIT TEQEIQFQQS KNSKFKNFRV 

      1390       1400       1410       1420       1430       1440 
YYREGRDQLW KGPGELLWKG EGAVILKVGT DIKVVPRRKA KIIKDYGGGK EMDSSSHMED 


TGEAREVA 

« Hide

Isoform Gag polyprotein [UniParc].

See P05894.

References

[1]"Sequence of simian immunodeficiency virus from macaque and its relationship to other human and simian retroviruses."
Chakrabarti L., Guyader M., Alizon M., Daniel M.D., Desrosiers R.C., Tiollais P., Sonigo P.
Nature 328:543-547(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Domain flexibility in retroviral proteases: structural implications for drug resistant mutations."
Rose R.B., Craik C.S., Stroud R.M.
Biochemistry 37:2607-2621(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 498-595.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00277 Genomic DNA. Translation: CAA68380.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZ5X-ray2.00A498-595[»]
1C6VX-ray3.00A/B/C/D1205-1368[»]
1SIVX-ray2.50A/B498-596[»]
1TCWX-ray2.40A/B498-596[»]
1YTIX-ray2.20A498-595[»]
1YTJX-ray2.50A498-595[»]
ProteinModelPortalP05896.
SMRP05896. Positions 2-135, 146-352, 383-432, 498-596, 599-1151, 1156-1201, 1210-1368, 1371-1425.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.10.200. 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.
InterProIPR001969. 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]
PfamPF00540. 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]
PRINTSPR00234. HIV1MATRIX.
SMARTSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMSSF46919. 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.
PROSITEPS50175. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP05896.

Entry information

Entry namePOL_SIVM1
AccessionPrimary (citable) accession number: P05896
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 2, 2007
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references