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Protein

Proteinase p15

Gene

gag

Organism
Avian myeloblastosis associated virus (MAV)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Specifically liberates the five major structural proteins from the common gag precursor, as well as reverse transcriptase and integrase from the gag-pol precursor.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.B13. 592.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteinase p15 (EC:3.4.23.-)
Gene namesi
Name:gag
OrganismiAvian myeloblastosis associated virus (MAV)
Taxonomic identifieri11960 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeAlpharetrovirusunclassified Alpharetrovirus
Virus hostiGalliformes [TaxID: 8976]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 124124Proteinase p15PRO_0000199554Add
BLAST

Interactioni

Subunit structurei

The protease is active as a homodimer.

Structurei

Secondary structure

1
124
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Beta strandi7 – 93Combined sources
Beta strandi12 – 198Combined sources
Beta strandi21 – 233Combined sources
Beta strandi28 – 369Combined sources
Beta strandi44 – 463Combined sources
Turni47 – 493Combined sources
Beta strandi56 – 583Combined sources
Beta strandi74 – 785Combined sources
Beta strandi80 – 856Combined sources
Beta strandi95 – 973Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi105 – 1095Combined sources
Helixi111 – 1166Combined sources
Beta strandi120 – 1223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MVPX-ray2.20A/B1-124[»]
2MVPmodel-A/B1-124[»]
ProteinModelPortaliP26315.
SMRiP26315. Positions 1-124.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26315.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 11382Peptidase A2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 peptidase A2 domain.PROSITE-ProRule 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: Complete.

P26315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LAMTMEHKDR PLVRVILTNT GSHPVKQRSV YITALLDSGA DITIISEEDW
60 70 80 90 100
PTDWPVMEAA NPQIHGIGGG IPMRKSRDMI EVGVINRDGS LERPLLLFPA
110 120
VAMVRGSILG RDCLQGLGLR LTNL
Length:124
Mass (Da):13,596
Last modified:May 1, 1992 - v1
Checksum:i3B8FF451AF43BBB1
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MVPX-ray2.20A/B1-124[»]
2MVPmodel-A/B1-124[»]
ProteinModelPortaliP26315.
SMRiP26315. Positions 1-124.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.23.B13. 592.

Miscellaneous databases

EvolutionaryTraceiP26315.

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. "Isolation, biochemical characterization and crystallization of the p15gag proteinase of myeloblastosis associated virus expressed in E. coli."
    Pichova I., Strop P., Sedlacek J., Kapralek F., Benes V., Travnicek M., Pavlickova L., Soucek M., Kostka V., Foundling S.
    Int. J. Biochem. 24:235-242(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 1-8.
  2. "Amino acid sequence of p15 from avian myeloblastosis virus complex."
    Sauer R.T., Allen D.W., Niall H.D.
    Biochemistry 20:3784-3791(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE.
  3. "Subsite specificity of the proteinase from myeloblastosis associated virus."
    Konvalinka J., Blaha I., Skrabana R., Sedlacek J., Pichova I., Kapralek F., Kostka V., Strop P.
    FEBS Lett. 282:73-76(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SPECIFICITY STUDIES.
  4. "Specificity studies on retroviral proteinase from myeloblastosis-associated virus."
    Strop P., Konvalinka J., Stys D., Pavlickova L., Blaha I., Velek J., Travnicek M., Kostka V., Sedlacek J.
    Biochemistry 30:3437-3443(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SPECIFICITY STUDIES.
  5. "Structural studies of the retroviral proteinase from avian myeloblastosis associated virus."
    Ohlendorf D.H., Foundling S.I., Wendoloski J.J., Sedlacek J., Strop P., Salemme F.R.
    Proteins 14:382-391(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiGAG_AVIMA
AccessioniPrimary (citable) accession number: P26315
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: January 20, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is synthesized as a Gag-Pol polyprotein.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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.