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UniProtKB/Swiss-Prot entry Q91CL9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CATV_NPVAP
Primary accession number Q91CL9
Secondary accession numbers None
Integrated into Swiss-Prot on September 26, 2003
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 36)
Name and origin of the protein
Protein name Viral cathepsin [Precursor]
Synonyms V-cath
EC 3.4.22.50
Cysteine proteinase
CP
Gene name
Name: VCATH
From
Antheraea pernyi nuclear polyhedrosis virus (ApNPV) [TaxID: 161494] 
Taxonomy Viruses; dsDNA viruses, no RNA stage; Baculoviridae; Alphabaculovirus.
Virus host Antheraea pernyi (Chinese oak silk moth) [TaxID: 7119]
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=A;
DOI=10.1263/jbb.93.183; PubMed=16233185 [NCBI, ExPASy, EBI, Israel, Japan]
Huang Y.J., Kobayashi J., Yoshimura T.;
"Genome mapping and gene analysis of Antheraea pernyi nucleopolyhedrovirus for improvement of baculovirus expression vector system.";
J. Biosci. Bioeng. 93:183-191(2002).
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.
  • PTM: Synthesized as an inactive proenzyme and activated by proteolytic removal of the inhibitory propeptide (By similarity).
  • SIMILARITY: Belongs to the peptidase C1 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB072731; BAB69773.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_611001.1; -.
3D structure databases
HSSP P80067; 1JQP. [HSSP ENTRY / PDB]
ModBase Q91CL9.
Protein family/group databases
MEROPS C01.083; -.
Ontologies
GO
GO:0004197; Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.
PANTHER PTHR12411; Peptidase_C1A; 1.
Pfam PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.
PRINTS PR00705; PAPAIN.
ProDom PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00645; Pept_C1; 1.
SMART graphical view of domain structure.
PROSITE PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.
ProtoNet Q91CL9.
Genome annotation databases
GeneID 5141489; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycoprotein; Hydrolase; Protease; Signal; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    16  16     Potential. 
PROPEP   17   113  97     Activation peptide (Potential). PRO_0000322203
CHAIN   114   324  211     Viral cathepsin. PRO_0000050574
ACT_SITE   137   137        By similarity. 
ACT_SITE   270   270        By similarity. 
ACT_SITE   290   290        By similarity. 
CARBOHYD   159   159        N-linked (GlcNAc...) (Potential). 
DISULFID   134   175        By similarity. 
DISULFID   168   208        By similarity. 
DISULFID   263   311        By similarity. 
Sequence information
Length: 324 AA [This is the length of the unprocessed precursor] Molecular weight: 36770 Da [This is the MW of the unprocessed precursor] CRC64: AA1D457183DEC547 [This is a checksum on the sequence]
        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 

Q91CL9 in FASTA format

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View entry in raw text format (no links)
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