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Protein
Submitted name:

Protease

Gene

pol

Organism
Human immunodeficiency virus 1
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl proteaseUniRule annotation, Hydrolase, Protease

Names & Taxonomyi

Protein namesi
Submitted name:
ProteaseImported
Gene namesi
Name:polImported
OrganismiHuman immunodeficiency virus 1Imported
Taxonomic identifieri11676 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DCKX-ray1.80A/B1-99[»]
3DCRX-ray1.40A/B1-99[»]
3HZCX-ray1.45A1-99[»]
3I2LX-ray1.50A/B1-99[»]
3IA9X-ray1.30A/B1-99[»]
3SA3X-ray1.65A/B1-99[»]
3SA4X-ray1.80A/B1-99[»]
3SA5X-ray1.65A/B1-99[»]
3SA6X-ray1.75A/B1-99[»]
3SA7X-ray1.50A/B1-99[»]
3SA8X-ray1.50A/B1-99[»]
3SA9X-ray1.70A/B1-99[»]
3SAAX-ray1.95A/B1-99[»]
3SABX-ray1.50A/B1-99[»]
3SACX-ray1.50A/B1-99[»]
ProteinModelPortaliO38732.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO38732.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 8970Peptidase A2InterPro annotationAdd
BLAST

Sequence similaritiesi

Contains peptidase A2 domain.SAAS annotation

Family and domain databases

Gene3Di2.40.70.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
[Graphical view]
PfamiPF00077. RVP. 1 hit.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

O38732-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PQITLWQRPL VTIRIGGQLK EALLDTGADD TVLEEMNLPG KWKPKMIGGI
60 70 80 90
GGFIKVRQYD QIPIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNF
Length:99
Mass (Da):10,804
Last modified:January 1, 1998 - v1
Checksum:i99165F743CCCFB3A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported
Non-terminal residuei99 – 991Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF024907 Genomic RNA. Translation: AAB83409.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF024907 Genomic RNA. Translation: AAB83409.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DCKX-ray1.80A/B1-99[»]
3DCRX-ray1.40A/B1-99[»]
3HZCX-ray1.45A1-99[»]
3I2LX-ray1.50A/B1-99[»]
3IA9X-ray1.30A/B1-99[»]
3SA3X-ray1.65A/B1-99[»]
3SA4X-ray1.80A/B1-99[»]
3SA5X-ray1.65A/B1-99[»]
3SA6X-ray1.75A/B1-99[»]
3SA7X-ray1.50A/B1-99[»]
3SA8X-ray1.50A/B1-99[»]
3SA9X-ray1.70A/B1-99[»]
3SAAX-ray1.95A/B1-99[»]
3SABX-ray1.50A/B1-99[»]
3SACX-ray1.50A/B1-99[»]
ProteinModelPortaliO38732.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO38732.

Family and domain databases

Gene3Di2.40.70.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
[Graphical view]
PfamiPF00077. RVP. 1 hit.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its Gag substrate cleavage sites."
    Zhang Y.M., Imamichi H., Imamichi T., Lane H.C., Falloon J., Vasudevachari M.B., Salzman N.P.
    J. Virol. 71:6662-6670(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site."
    Torbeev V.Y., Mandal K., Terechko V.A., Kent S.B.
    Bioorg. Med. Chem. Lett. 18:4554-4557(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS).
  3. "Hydrogen bonds at the protein-inhibitor interface in the HIV-1 protease / inhibitors complexes probed by total chemical synthesis and X-ray crystallography."
    Torbeev V.Y., Kent S.B.H.
    Submitted (JUN-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
  4. "Protease Inhibitors that protrude out from substrate envelope are more susceptible to developing drug resistance."
    Altman M.D., Nalam M.N.L., Ali A., Cao H., Rana T.M., Schiffer C.A., Tidor B.
    Submitted (JUN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).

Entry informationi

Entry nameiO38732_9HIV1
AccessioniPrimary (citable) accession number: O38732
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: April 13, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.