ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9YWK4

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CATV_NPVBS
Primary accession number Q9YWK4
Secondary accession numbers None
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
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
Buzura suppressaria nuclear polyhedrosis virus (BsNPV) [TaxID: 74320] 
Taxonomy Viruses; dsDNA viruses, no RNA stage; Baculoviridae; Alphabaculovirus.
Virus host Lepidoptera (butterflies and moths) [TaxID: 7088]
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9820162 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Z.H., Arif B.M., Jin F., Martens J.W.M., Chen X.W., Sun J.S., Zuidema D., Goldbach R.W., Vlak J.M.;
"Distinct gene arrangement in the Buzura suppressaria single-nucleocapsid nucleopolyhedrovirus genome.";
J. Gen. Virol. 79:2841-2851(1998).
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
AF058929; AAC77812.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P80067; 1JQP. [HSSP ENTRY / PDB]
ModBase Q9YWK4.
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 Q9YWK4.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Hydrolase; Protease; Signal; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    21  21     Potential. 
PROPEP   22   116  95     Activation peptide (Potential). PRO_0000322205
CHAIN   117   331  215     Viral cathepsin. PRO_0000050576
ACT_SITE   140   140        By similarity. 
ACT_SITE   274   274        By similarity. 
ACT_SITE   294   294        By similarity. 
DISULFID   137   178        By similarity. 
DISULFID   171   211        By similarity. 
DISULFID   267   315        By similarity. 
Sequence information
Length: 331 AA [This is the length of the unprocessed precursor] Molecular weight: 37744 Da [This is the MW of the unprocessed precursor] CRC64: 6DB980A418FA2BBC [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKKLVICIIL NLIVAKNYAF AYDLLKAGDY FETFLANYNK MYNDTSEKER RFSIFQQTLE 

        70         80         90        100        110        120 
EINYKNRLND SAVYQINKFA DLSKNEIISK YTGLNMPVQT TNFCKTIVID QPPGKGPLNF 

       130        140        150        160        170        180 
DWRQQNKVTS IKNQKACGAC WAFATLASIE SQYAIKNNVH IDLSEQQMID CDYVDMGCDG 

       190        200        210        220        230        240 
GLLHTAFEQM IQMGELVQEH EYPYAGVNKP CELRGDETGV VKVKGCYRYV VFREEKLKDL 

       250        260        270        280        290        300 
LRAVGPIPMA IDASGIVNYH HGIIHYCENY GLNHAVLLVG YGVENNVPFW TFKNTWGKDW 

       310        320        330 
GEEGYFRVRQ NVDACGMTNE LASSAVIDWD A
Q9YWK4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!