Q000H7 (Q000H7_9HIV1) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Pol protein EMBL ABJ52797.1

Gene names

Name:

pol EMBL ABJ52797.1

Organism

Human immunodeficiency virus 1 EMBL ABJ52797.1

Taxonomic identifier

11676 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	404 AA.
Sequence status	Fragment.
Protein existence	Evidence 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. RuleBase RU004064 Contains 1 peptidase A2 domain. SAAS SAAS000477 Contains 1 reverse transcriptase domain. RuleBase RU000322

Ontologies

Keywords
Biological process	Virus entry into host cell SAAS SAAS001969
Molecular function	Aspartyl protease RuleBase RU000453 Hydrolase Nucleotidyltransferase Protease RNA-directed DNA polymerase SAAS SAAS001995 Transferase
Technical term	3D-structure PDB 3R0W PDB 3R0Y PDB 4FAE PDB 4FAF PDB 4EYR PDB 3SO9 PDB 3SPK Multifunctional enzyme SAAS SAAS021109
Gene Ontology (GO)
Biological_process	RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Experimental info
	Non-terminal residue	1	1	EMBL ABJ52797.1
	Non-terminal residue	404	1	EMBL ABJ52797.1

Sequences

	Sequence		Length	Mass (Da)
	Q000H7 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 7F9B09F6308A139D	FASTA	404	46,066
	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

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

DQ988164 Genomic DNA. Translation: ABJ52797.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3R0W	X-ray	1.70	A/B	1-99	[»]
3R0Y	X-ray	1.65	A/B	1-99	[»]
3SO9	X-ray	2.87	A/B	1-99	[»]
3SPK	X-ray	1.24	A/B	1-99	[»]
4EYR	X-ray	1.80	A/B	1-99	[»]
4FAE	X-ray	2.30	A/B	1-99	[»]
4FAF	X-ray	2.10	A/B	1-99	[»]

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.40.70.10. 1 hit.

InterPro

IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR000477. RVT.
IPR010661. RVT_thumb.
[Graphical view]

Pfam

PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06817. RVT_thumb. 1 hit.
[Graphical view]

SUPFAM

SSF50630. Pept_Aspartic. 1 hit.

PROSITE

PS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50878. RT_POL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q000H7.

Entry information

Entry name

Q000H7_9HIV1

Accession

Primary (citable) accession number: Q000H7

Entry history

Integrated into UniProtKB/TrEMBL:	November 14, 2006
Last sequence update:	November 14, 2006
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)