A3FH86 (A3FH86_9HIV1) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Protease EMBL ABN55216.1

Gene names

Name:

pol EMBL ABN55216.1

Organism

Human immunodeficiency virus 1 EMBL ABN55216.1

Taxonomic identifier

11676 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	99 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Contains 1 peptidase A2 domain. SAAS SAAS009007

Ontologies

Keywords
Molecular function	Aspartyl protease RuleBase RU000453 Hydrolase Protease
Technical term	3D-structure PDB 2PC0
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 ABN55216.1
	Non-terminal residue	99	1	EMBL ABN55216.1

Sequences

	Sequence		Length	Mass (Da)
	A3FH86 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: 189F5EE42D82533D	FASTA	99	10,820
	10 20 30 40 50 60 PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMNLPG RWKPKMIGGI GGFIKVRQYD 70 80 90 QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNF

References

[1]	"Use of peripheral blood DNA for genotype antiretroviral resistance testing in drug-naive HIV-infected subjects." Vicenti I., Razzolini F., Saladini F., Romano L., Zazzi M. Clin. Infect. Dis. 44:1657-1661(2007) [PubMed: 17516412] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Conformational flexibility in the flap domains of ligand-free HIV protease." Heaslet H., Rosenfeld R., Giffin M., Lin Y.C., Tam K., Torbett B.E., Elder J.H., McRee D.E., Stout C.D. Acta Crystallogr. D Biol. Crystallogr. 63:866-875(2007) [PubMed: 17642513] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

EF376542 Genomic DNA. Translation: ABN55216.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PC0	X-ray	1.40	A	1-99	[»]

ProteinModelPortal

A3FH86.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Family and domain databases

InterPro

IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[Graphical view]

Gene3D

G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.

Pfam

PF00077. RVP. 1 hit.
[Graphical view]

SUPFAM

SSF50630. Pept_Aspartic. 1 hit.

PROSITE

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

ProtoNet

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Entry information

Entry name

A3FH86_9HIV1

Accession

Primary (citable) accession number: A3FH86

Entry history

Integrated into UniProtKB/TrEMBL:	March 20, 2007
Last sequence update:	March 20, 2007
Last modified:	November 16, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)