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Protein

Protease

Gene

L3

Organism
Ovine adenovirus D serotype 7 (isolate OAV287) (OAdV-7) (Ovine adenovirus 7)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 cell cytoskeletal keratins K7 and K18.UniRule annotation

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.UniRule annotation

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).
Cleaves adenovirus and host cell proteins 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).UniRule annotation

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.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei55UniRule annotation1
Active sitei72UniRule annotation1
Active sitei122UniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionDNA-binding, Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiC05.001.

Names & Taxonomyi

Protein namesi
Recommended name:
ProteaseUniRule annotation (EC:3.4.22.39UniRule annotation)
Alternative name(s):
AdenainUniRule annotation
Adenovirus proteaseUniRule annotation
Short name:
AVPUniRule annotation
Adenovirus proteinaseUniRule annotation
EndoproteaseUniRule annotation
Gene namesi
Name:L3UniRule annotation
OrganismiOvine adenovirus D serotype 7 (isolate OAV287) (OAdV-7) (Ovine adenovirus 7)
Taxonomic identifieri114430 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeAtadenovirus
Virus hostiOvis aries (Sheep) [TaxID: 9940]
Proteomesi
  • UP000008089 Componenti: Genome

Subcellular locationi

  • Virion UniRule annotation
  • Host nucleus UniRule annotation

  • Note: Present in about 10 copies per virion.UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002180461 – 201ProteaseAdd BLAST201

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi104Interchain (with C-10 in cleaved protease cofactor pVI-C)UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei52 – 53Cleavage; by autolysisUniRule annotation2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.UniRule annotation

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts with protease cofactor pVI-C; this interaction is necessary for protease activation.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ83906.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C5 family.UniRule annotation

Phylogenomic databases

OrthoDBiVOG090000OU.

Family and domain databases

HAMAPiMF_04059. ADV_PRO. 1 hit.
InterProiView protein in InterPro
IPR000855. Peptidase_C5.
PfamiView protein in Pfam
PF00770. Peptidase_C5. 1 hit.
PIRSFiPIRSF001218. Protease_ADV. 1 hit.
PRINTSiPR00703. ADVENDOPTASE.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD003705. Peptidase_C5. 1 hit.

Sequencei

Sequence statusi: Complete.

Q83906-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGTSESELK NLISSLHLNN GFLGIFDCRF PGFLQKSKIQ TAIINTGPRE
60 70 80 90 100
QGGIHWITLA LEPISYKLFI FDPLGWKDTQ LIKFYNFSLN SLIKRSALNN
110 120 130 140 150
SDRCITVERN TQSVQCTCAG SCGLFCIFFL YCFHFYKQNV FKSWLFQKLN
160 170 180 190 200
GSTPSLIPCE PHLLHENQTF LYDFLNAKSV YFRKNYRTFI ENTKTGLIKT

H
Length:201
Mass (Da):23,194
Last modified:November 1, 1996 - v1
Checksum:i496509DCA5BB22C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40839 Genomic DNA. Translation: AAA84980.1.
RefSeqiNP_659524.1. NC_004037.2.

Genome annotation databases

GeneIDi949183.
KEGGivg:949183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40839 Genomic DNA. Translation: AAA84980.1.
RefSeqiNP_659524.1. NC_004037.2.

3D structure databases

ProteinModelPortaliQ83906.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC05.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi949183.
KEGGivg:949183.

Phylogenomic databases

OrthoDBiVOG090000OU.

Family and domain databases

HAMAPiMF_04059. ADV_PRO. 1 hit.
InterProiView protein in InterPro
IPR000855. Peptidase_C5.
PfamiView protein in Pfam
PF00770. Peptidase_C5. 1 hit.
PIRSFiPIRSF001218. Protease_ADV. 1 hit.
PRINTSiPR00703. ADVENDOPTASE.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD003705. Peptidase_C5. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPRO_ADEO7
AccessioniPrimary (citable) accession number: Q83906
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: May 10, 2017
This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.