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P35042 (TRYP_CHOFU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 73. 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

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the activation of delta-endotoxin from Bacillus thuringiensis.

Catalytic activity

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-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 – 1717 Potential
Propeptide18 – 247Activation peptide
PRO_0000028257
Chain25 – 256232Trypsin CFT-1
PRO_0000028258

Regions

Domain25 – 256232Peptidase S1

Sites

Active site701Charge relay system By similarity
Active site1151Charge relay system By similarity
Active site2131Charge relay system By similarity
Site2071Required for specificity By similarity

Amino acid modifications

Disulfide bond55 ↔ 71 By similarity
Disulfide bond180 ↔ 197 By similarity
Disulfide bond209 ↔ 233 By similarity

Sequences

Sequence LengthMass (Da)Tools
P35042 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 4C2A8CBA74CFEF67

FASTA25627,333
        10         20         30         40         50         60 
MRVTLALVAL CLASVAALPE KQQRIVGGSV TTIEQWPSGS ALLYSWNLVT YSQACGGAIL 

        70         80         90        100        110        120 
NTRSILSAAH CFIGDAANRW RIRTGSTWAN SGGVVHNTAL IIIHPSYNTR TLDNDIAILR 

       130        140        150        160        170        180 
SATTIAQNNQ ARPASIAGAN YNLADNQAVW AIGWGATCPG CAGSEQLRHI QIWTVNQNTC 

       190        200        210        220        230        240 
RSRYLEVGGT ITDNMLCSGW LDVGGRDQCQ GDSGGPLFHN NVVVGVCSWG QSCALARYPG 

       250 
VNARVSRFTA WIQANA 

« Hide

References

[1]"Isolation and characterization of a full-length trypsin-encoding cDNA clone from the Lepidopteran insect, Choristoneura fumiferana."
Wang S., Magoulas C., Hickey D.A.
Gene 136:375-376(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Purification and characterization of a trypsin-like digestive enzyme from spruce budworm (Choristoneura fumiferana) responsible for the activation of delta-endotoxin from Bacillus thuringiensis."
Milne R., Kaplan H.
Insect Biochem. Mol. Biol. 23:663-673(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-69, CHARACTERIZATION.
Tissue: Gut juice.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04749 mRNA. Translation: AAA81525.1.

3D structure databases

ProteinModelPortalP35042.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRYP_CHOFU
AccessionPrimary (citable) accession number: P35042
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 16, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries