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Reviewed, UniProtKB/Swiss-Prot Q8QLK1 (CATV_NPVMC)

Last modified March 3, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Viral cathepsin
      Short name=V-cath
    EC=3.4.22.50
Alternative name(s):
    Cysteine proteinase
      Short name=CP
Gene names
Name: VCATH
OrganismMamestra configurata nucleopolyhedrovirus (MacoNPV)
Taxonomic identifier191492 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageBaculoviridaeAlphabaculovirus
Virus hostMamestra configurata (bertha armyworm) [TaxID: 174822]

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. May participate in the degradation of foreign protein expressed by the baculovirus system By similarity.

Catalytic activity

Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B.

Post-translational modification

Synthesized as an inactive proenzyme and activated by proteolytic removal of the inhibitory propeptide By similarity.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 126110Activation peptide Potential
PRO_0000322213
Chain127 – 337211Viral cathepsin
PRO_0000050583

Sites

Active site1501 By similarity
Active site2831 By similarity
Active site3031 By similarity

Amino acid modifications

Disulfide bond147 ↔ 188 By similarity
Disulfide bond181 ↔ 221 By similarity
Disulfide bond276 ↔ 324 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8QLK1-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 2437696EAA2A1AAC

FASTA33737,890
        10         20         30         40         50         60 
MNKILILLLL VSAVLTSHDQ VVAVTIKPNL YNINSAPLYF EKFISQYNKQ YSSEDEKKYR 

        70         80         90        100        110        120 
YNIFRHNIES INAKNSRNDS AVYKINRFAD MTKNEVVNRH TGLASGDIGA NFCETIVVDG 

       130        140        150        160        170        180 
PGQRQRPANF DWRNYNKVTS VKDQGMCGAC WAFAGLGALE SQYAIKYDRL IDLAEQQLVD 

       190        200        210        220        230        240 
CDFVDMGCDG GLIHTAYEQI MHIGGVEQEY DYPYKAVRLP CAVKPHKFAV GVRNCYRYVL 

       250        260        270        280        290        300 
LSEERLEDLL RHVGPIAIAV DAVDLTDYYG GVISFCENNG LNHAVLLVGY GIENNVPYWT 

       310        320        330 
IKNSWGSDYG ENGYVRIRRG VNSCGMINEL ASSAQIA 

« Hide

References

[1]"Sequence and organization of the Mamestra configurata nucleopolyhedrovirus genome."
Li Q., Donly C., Li L., Willis L.G., Theilmann D.A., Erlandson M.
Virology 294:106-121(2002) [PubMed: 11886270] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 90/2.

Cross-references

Sequence databases

U59461 Genomic DNA. Translation: AAM09141.1.

3D structure databases

HSSPHSSP built from PDB template 1JQP based on UniProtKB P80067.
ModBaseSearch...

Protein family/group databases

MEROPSC01.083.

Enzyme and pathway databases

BRENDA3.4.22.50. 298760.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
ProDomPD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATV_NPVMC
AccessionPrimary (citable) accession number: Q8QLK1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2002
Last modified: March 3, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents