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Q000H7 (Q000H7_9HIV1) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
Gene names
Name:pol EMBL ABJ52797.1
OrganismHuman immunodeficiency virus 1 EMBL ABJ52797.1
Taxonomic identifier11676 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length404 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). SAAS SAAS001995

Sequence similarities

Belongs to the retroviral Pol polyprotein family.

Contains 1 reverse transcriptase domain. RuleBase RU000322

Contains peptidase A2 domain. SAAS SAAS021109

Contains peptidase Adomain. SAAS SAAS021109

Contains reverse transcriptase domain. SAAS SAAS021109

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Experimental info

Non-terminal residue11 EMBL ABJ52797.1
Non-terminal residue4041 EMBL ABJ52797.1

Sequences

Sequence LengthMass (Da)Tools
Q000H7 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 7F9B09F6308A139D

FASTA40446,066
        10         20         30         40         50         60 
PQITLWQRPI VTIKIGGQLK EALLDTGADD TVLEDINLPG RWKPKMIGGI GGFVKVRQYD 

        70         80         90        100        110        120 
QVPIEICGHK VIGTVLVGPT PTNVIGRNLM TQIGCTLNFP ISPIETVPVK LKPGMDGPKV 

       130        140        150        160        170        180 
KQWPLTEEKI KALIEICAEL EKEGKISKIG PENPYNTPVF AIKKKNSTKW RKLVDFRELN 

       190        200        210        220        230        240 
KRTQDFWEVQ LGIPHPAGLK KNKSVTVLDV GDAYFSVPLD EDFRKYTAFT IPSINNETPG 

       250        260        270        280        290        300 
IRYQYNVLPQ GWKGSPSIFQ SSMTKILEPF RKQNPDIVIY QYVDDLYVGS DLEIGQHRAK 

       310        320        330        340        350        360 
IDELRQHLWK WGFYTPEQKH QKEPPFLWMG YELHPDKWTV QPIVLPEKDS WTVNDIQKLV 

       370        380        390        400 
GKLNWASQIY PGIKVRQLCK LLRGTKTLTE VVPLTREAEL ELAE 

« Hide

References

[1]Whitcomb J., Kiss L., Parkin N., Limoli K., Petropoulos C.J.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: WAC2 EMBL ABJ52797.1.
[2]"The higher barrier of darunavir and tipranavir resistance for HIV-1 protease."
Wang Y., Liu Z., Brunzelle J.S., Kovari I.A., Dewdney T.G., Reiter S.J., Kovari L.C.
Biochem. Biophys. Res. Commun. 412:737-742(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 1-99.
[3]"Crystal structures of multidrug-resistant HIV-1 protease in complex with two potent anti-malarial compounds."
Yedidi R.S., Liu Z., Wang Y., Brunzelle J.S., Kovari I.A., Woster P.M., Kovari L.C., Gupta D.
Biochem. Biophys. Res. Commun. 421:413-417(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-99.
[4]"Higher desolvation energy reduces molecular recognition in multi-drug resistant HIV-1 protease."
Wang Y., Dewdney T.G., Liu Z., Reiter S.J., Brunzelle J.S., Kovari I.A., Kovari L.C.
Submitted (MAY-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-99.
[5]"Insights into the mechanism of drug resistance: X-ray structure analysis of multi-drug resistant HIV-1 protease ritonavir complex."
Liu Z., Yedidi R.S., Wang Y., Dewdney T.G., Reiter S.J., Brunzelle J.S., Kovari I.A., Kovari L.C.
Biochem. Biophys. Res. Commun. 431:232-238(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-99.
[6]"Crystallographic study of multi-drug resistant HIV-1 protease lopinavir complex: mechanism of drug recognition and resistance."
Liu Z., Yedidi R.S., Wang Y., Dewdney T.G., Reiter S.J., Brunzelle J.S., Kovari I.A., Kovari L.C.
Biochem. Biophys. Res. Commun. 437:199-204(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ988164 Genomic DNA. Translation: ABJ52797.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3R0WX-ray1.70A/B1-99[»]
3R0YX-ray1.65A/B1-99[»]
3SO9X-ray2.87A/B1-99[»]
3SPKX-ray1.24A/B1-99[»]
4EYRX-ray1.80A/B1-99[»]
4FAEX-ray2.30A/B1-99[»]
4FAFX-ray2.10A/B1-99[»]
4L1AX-ray1.90A/B1-99[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.70.10. 1 hit.
InterProIPR001969. Aspartic_peptidase_AS.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR000477. RT_dom.
IPR010661. RVT_thumb.
[Graphical view]
PfamPF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06817. RVT_thumb. 1 hit.
[Graphical view]
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50878. RT_POL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ000H7.

Entry information

Entry nameQ000H7_9HIV1
AccessionPrimary (citable) accession number: Q000H7
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: July 9, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)