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Protein

Protease

Gene

L3

Organism
Equine adenovirus B serotype 2 (EAdV-2) (Equine adenovirus 2)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cells cytoskeletal keratins K7 and K18 (By similarity).By similarity

Catalytic activityi

Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid).

Enzyme regulationi

Requires DNA and protease cofactor for maximal activation. Inside nascent virions, becomes partially activated by binding to the viral DNA, allowing it to cleave the cofactor that binds to the protease and fully activates it. Actin, like the viral protease cofactor, seems to act as a cofactor in the cleavage of cytokeratin 18 and of actin itself (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei53 – 531By similarity
Active sitei70 – 701By similarity
Active sitei121 – 1211By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

DNA-binding

Protein family/group databases

MEROPSiC05.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Protease (EC:3.4.22.39)
Alternative name(s):
Adenain
Adenovirus protease
Short name:
AVP
Adenovirus proteinase
Endoprotease
Gene namesi
ORF Names:L3
OrganismiEquine adenovirus B serotype 2 (EAdV-2) (Equine adenovirus 2)
Taxonomic identifieri67603 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirusEquine mastadenovirus B
Virus hostiEquus caballus (Horse) [TaxID: 9796]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201ProteasePRO_0000218041Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi103 – 103InterchainBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei45 – 462Cleavage; by autolysisSequence analysis

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts with protease cofactor pVI-C; this interaction is necessary for protease activation.By similarity

Structurei

3D structure databases

ProteinModelPortaliO40958.
SMRiO40958. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C5 family.Curated

Family and domain databases

Gene3Di3.40.395.10. 1 hit.
InterProiIPR000855. Peptidase_C5.
[Graphical view]
PfamiPF00770. Peptidase_C5. 1 hit.
[Graphical view]
PIRSFiPIRSF001218. Protease_ADV. 1 hit.
PRINTSiPR00703. ADVENDOPTASE.
ProDomiPD003705. Peptidase_C5. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

O40958-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSTETELKR ILSDLNVTPL LLGTYDKRFP GFVSKAKPCP IVNTAFGETG
60 70 80 90 100
GEHWIAMAWY PPNNSFYMFD PFGFSDQKLK QIYDFEYQGL LRRSALTSSK
110 120 130 140 150
DRCVQLIRST DTVQGPNSAG CGLFGGLFLK SFACNPARPR NGNPIIDIVR
160 170 180 190 200
GVPNERFTDP SSLPILYRNQ ENMYAFLENN SPYFVSHERE IKRKTAFDYI

Q
Length:201
Mass (Da):22,816
Last modified:January 1, 1998 - v1
Checksum:i9216143479E7D7D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L80007 Genomic DNA. Translation: AAB88061.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L80007 Genomic DNA. Translation: AAB88061.1.

3D structure databases

ProteinModelPortaliO40958.
SMRiO40958. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC05.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.395.10. 1 hit.
InterProiIPR000855. Peptidase_C5.
[Graphical view]
PfamiPF00770. Peptidase_C5. 1 hit.
[Graphical view]
PIRSFiPIRSF001218. Protease_ADV. 1 hit.
PRINTSiPR00703. ADVENDOPTASE.
ProDomiPD003705. Peptidase_C5. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

  1. "Sequence analysis of equine adenovirus 2 hexon and 23K proteinase genes indicates a phylogenetic origin distinct from equine adenovirus 1."
    Reubel G.H., Studdert M.J.
    Virus Res. 50:41-56(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 385/75.

Entry informationi

Entry nameiPRO_ADEE2
AccessioniPrimary (citable) accession number: O40958
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: October 14, 2015
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell (By similarity).By similarity

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.