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Reviewed, UniProtKB/Swiss-Prot P35049 (TRYP_FUSOX)

Last modified June 16, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Trypsin
    EC=3.4.21.4
OrganismFusarium oxysporum
Taxonomic identifier5507 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesmitosporic HypocrealesFusariumFusarium oxysporum species complex

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Subcellular location

Secreted.

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 term3D-structure
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

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 – 258Activation peptide
PRO_0000028301
Chain26 – 248223Trypsin
PRO_0000028302

Regions

Domain25 – 248224Peptidase S1

Sites

Active site651Charge relay system
Active site1081Charge relay system
Active site2041Charge relay system
Site1981Required for specificity

Amino acid modifications

Disulfide bond50 ↔ 66
Disulfide bond174 ↔ 189
Disulfide bond200 ↔ 225

Secondary structure

...................................... 248
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35049-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 1A0EBA88C3E70294

FASTA24824,576
        10         20         30         40         50         60 
MVKFASVVAL VAPLAAAAPQ EIPNIVGGTS ASAGDFPFIV SISRNGGPWC GGSLLNANTV 

        70         80         90        100        110        120 
LTAAHCVSGY AQSGFQIRAG SLSRTSGGIT SSLSSVRVHP SYSGNNNDLA ILKLSTSIPS 

       130        140        150        160        170        180 
GGNIGYARLA ASGSDPVAGS SATVAGWGAT SEGGSSTPVN LLKVTVPIVS RATCRAQYGT 

       190        200        210        220        230        240 
SAITNQMFCA GVSSGGKDSC QGDSGGPIVD SSNTLIGAVS WGNGCARPNY SGVYASVGAL 


RSFIDTYA 

« Hide

References

[1]"The sequence and X-ray structure of the trypsin from Fusarium oxysporum."
Rypniewski W.R., Hastrup S., Betzel C., Dauter M., Dauter Z., Papendorf G., Branner S., Wilson K.S.
Protein Eng. 6:341-348(1993) [PubMed: 8332590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[2]"Structure of inhibited trypsin from Fusarium oxysporum at 1.55 A."
Rypniewski W.R., Dambmann C., von der Osten C., Dauter M., Wilson K.S.
Acta Crystallogr. D 51:73-84(1995) [PubMed: 15299338] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

S63827 mRNA. Translation: AAB27568.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FN8X-ray0.81A25-248[»]
1FY4X-ray0.81A25-248[»]
1FY5X-ray0.81A25-248[»]
1GDNX-ray0.81A25-248[»]
1GDQX-ray0.93A25-248[»]
1GDUX-ray1.07A25-248[»]
1PPZX-ray1.23A25-248[»]
1PQ5X-ray0.85A25-248[»]
1PQ7X-ray0.80A25-248[»]
1PQ8X-ray1.00A25-248[»]
1PQAX-ray1.23A25-248[»]
1TRYX-ray1.55A25-248[»]
1XVMX-ray1.10A25-248[»]
1XVOX-ray0.84A25-248[»]
2G51X-ray1.84A25-248[»]
2G52X-ray1.84A25-248[»]
2VU8X-ray1.80E25-248[»]
ModBaseSearch...

Protein family/group databases

MEROPSS01.103.

Enzyme and pathway databases

BRENDA3.4.21.4. 15244.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRYP_FUSOX
AccessionPrimary (citable) accession number: P35049
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents