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UniProtKB/Swiss-Prot entry Q9PYY5


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

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Entry information
Entry name CATV_GVXN
Primary accession number Q9PYY5
Secondary accession numbers None
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 45)
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
Synonyms: 58
From
Xestia c-nigrum granulosis virus (XnGV) (Xestia c-nigrum granulovirus) [TaxID: 51677] 
Taxonomy Viruses; dsDNA viruses, no RNA stage; Baculoviridae; Betabaculovirus.
Virus host Xestia [TaxID: 320016]
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1006/viro.1999.9894; PubMed=10502508 [NCBI, ExPASy, EBI, Israel, Japan]
Hayakawa T., Ko R., Okano K., Seong S.I., Goto C., Maeda S.;
"Sequence analysis of the Xestia c-nigrum granulovirus genome.";
Virology 262:277-297(1999).
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
AF162221; AAF05172.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_059206.1; -.
3D structure databases
HSSP P80067; 1JQP. [HSSP ENTRY / PDB]
ModBase Q9PYY5.
Protein family/group databases
MEROPS C01.047; -.
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 Q9PYY5.
Genome annotation databases
GeneID 1442292; -.
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    28  28     Potential. 
PROPEP   29   133  105     Activation peptide (Potential). PRO_0000322219
CHAIN   134   346  213     Viral cathepsin. PRO_0000050589
ACT_SITE   157   157        By similarity. 
ACT_SITE   289   289        By similarity. 
ACT_SITE   309   309        By similarity. 
CARBOHYD   175   175        N-linked (GlcNAc...) (Potential). 
CARBOHYD   230   230        N-linked (GlcNAc...) (Potential). 
DISULFID   154   195        By similarity. 
DISULFID   188   228        By similarity. 
DISULFID   281   330        By similarity. 
Sequence information
Length: 346 AA [This is the length of the unprocessed precursor] Molecular weight: 38819 Da [This is the MW of the unprocessed precursor] CRC64: 4B82DB0376C7C951 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLFFNFYKHI MFLPWVFCVA LLTLNVCAVS YIAYDMSNAQ ELFNEFVVKY NKVYKDDQEK 

        70         80         90        100        110        120 
EARFEIFKQN LADINARNAL EDSAMFEINS RADISSNELL QKLTGLKLSL MRGEKKNSFC 

       130        140        150        160        170        180 
TPTVISGDSS GKVPDSFDWR DRNSVTSVKM QKECGSCWAF SAVANIESLY HIKHNVSLDL 

       190        200        210        220        230        240 
SEQQLVDCDK VNNGCNGGLM SWAFEGIIRA GGISYEAPYP YTGVDGVCKN TTRYVQLSGC 

       250        260        270        280        290        300 
YAYDLRSEKK LRQVLHEKGP VSVAIDVVDL TNYKSGVAKH CSVDHGLNHG VLLVGYGQEN 

       310        320        330        340 
DVKYWTLKNS WGSDWGEQGF FRIKRDVNSC GILNQFAASA ILSSSS 

Q9PYY5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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