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Q91CL9 (CATV_NPVAP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismAntheraea pernyi nuclear polyhedrosis virus (ApNPV)
Taxonomic identifier161494 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageBaculoviridaeAlphabaculovirus
Virus hostAntheraea pernyi (Chinese oak silk moth) [TaxID: 7119]

Protein attributes

Sequence length324 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
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 11397Activation peptide Potential
PRO_0000322203
Chain114 – 324211Viral cathepsin
PRO_0000050574

Sites

Active site1371 By similarity
Active site2701 By similarity
Active site2901 By similarity

Amino acid modifications

Glycosylation1591N-linked (GlcNAc...); by host Potential
Disulfide bond134 ↔ 175 By similarity
Disulfide bond168 ↔ 208 By similarity
Disulfide bond263 ↔ 311 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91CL9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: AA1D457183DEC547

FASTA32436,770
        10         20         30         40         50         60 
MNKIVLYLLV YGATLGAAYD LLKAPSYFEE FLHKFNKNYS SESEKLRRFK IFQHNLEEII 

        70         80         90        100        110        120 
NKNQNDTSAQ YEINKFSDLS KDETISKYTG LSLPLQKQNF CEVVVLDRPP DKGPLEFDWR 

       130        140        150        160        170        180 
RLNKVTSVKN QGMCGACWAF ATLGSLESQF AIKHDQLINL SEQQLIDCDF VDVGCDGGLL 

       190        200        210        220        230        240 
HTAYEAVMNM GGIQAENDYP YEANNGPCRV NAAKFVVRVK KCYRYVTLFE EKLKDLLRIV 

       250        260        270        280        290        300 
GPIPVAIDAS DIVGYKRGII RYCENHGLNH AVLLVGYGVE NGIPFWILKN TWGADWGEQG 

       310        320 
YFRVQQNINA CGIKNELPSS AEIY 

« Hide

References

[1]"Genome mapping and gene analysis of Antheraea pernyi nucleopolyhedrovirus for improvement of baculovirus expression vector system."
Huang Y.J., Kobayashi J., Yoshimura T.
J. Biosci. Bioeng. 93:183-191(2002) [PubMed: 16233185] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB072731 Genomic DNA. Translation: BAB69773.1.
RefSeqYP_611001.1. NC_008035.3.

3D structure databases

ProteinModelPortalQ91CL9.
ModBaseSearch...

Protein family/group databases

MEROPSC01.083.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5141489.

Phylogenomic databases

ProtClustDBCLSP2509984.

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.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. 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_NPVAP
AccessionPrimary (citable) accession number: Q91CL9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: December 1, 2001
Last modified: November 16, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families