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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]

Interactioni

Chemistry

BindingDBiO92139.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HVIX-ray1.80A/B1-99[»]
1ZP8X-ray2.02A1-99[»]
2BQVX-ray2.10A/B1-99[»]
2I4WX-ray1.55A/B1-99[»]
ProteinModelPortaliO92139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO92139.

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.

O92139-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG RWKPKMIGGI
60 70 80 90
GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNF
Length:99
Mass (Da):10,793
Last modified:November 1, 1998 - v1
Checksum:i188EBF142D824E20
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
AF078594 Genomic DNA. Translation: AAC61562.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF078594 Genomic DNA. Translation: AAC61562.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HVIX-ray1.80A/B1-99[»]
1ZP8X-ray2.02A1-99[»]
2BQVX-ray2.10A/B1-99[»]
2I4WX-ray1.55A/B1-99[»]
ProteinModelPortaliO92139.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiO92139.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO92139.

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. "Influence of Stereochemistry on Activity and Binding Modes for C2 Symmetry-Based Diol Inhibitors of HIV-1 Protease."
    Hosur M.V., Bhat T.N., Kempf D., Baldwin E.T., Liu B., Gulnik S., Wideburg N.E., Norbeck D.W., Appelt K., Erickson J.W.
    J. Am. Chem. Soc. 116:847-855(1994)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
  2. "HIV-1 protease from patients in the United States who have not received protease inhibitors."
    Shafer R.W., Hsu P., Winters M.A., Kozal M.J., Merigan T.C., Gingeras T.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: JIDP28W0Imported.
  3. "1,2,3-triazole as a peptide surrogate in the rapid synthesis of HIV-1 protease inhibitors."
    Brik A., Alexandratos J., Lin Y.C., Elder J.H., Olson A.J., Wlodawer A., Goodsell D.S., Wong C.H.
    ChemBioChem 6:1167-1169(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS).
  4. "A new class of HIV-1 protease inhibitors containing a tertiary alcohol in the transition-state mimicking scaffold."
    Ekegren J.K., Unge T., Safa M.Z., Wallberg H., Samuelsson B., Hallberg A.
    J. Med. Chem. 48:8098-8102(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
  5. "Suppression of HIV-1 protease inhibitor resistance by phosphonate-mediated solvent anchoring."
    Cihlar T., He G.X., Liu X., Chen J.M., Hatada M., Swaminathan S., McDermott M.J., Yang Z.Y., Mulato A.S., Chen X., Leavitt S.A., Stray K.M., Lee W.A.
    J. Mol. Biol. 363:635-647(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).

Entry informationi

Entry nameiO92139_9HIV1
AccessioniPrimary (citable) accession number: O92139
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1998
Last sequence update: November 1, 1998
Last modified: February 17, 2016
This is version 89 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.