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P35049 (TRYP_FUSOX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 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: UniProtKB-KW

   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 – 247Activation peptide
PRO_0000028301
Chain25 – 248224Trypsin
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 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
[3]"Fusarium oxysporum trypsin at atomic resolution at 100 and 283 K: a study of ligand binding."
Rypniewski W.R., Ostergaard P.R., Norregaard-Madsen M., Dauter M., Wilson K.S.
Acta Crystallogr. 57:8-19(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.81 ANGSTROMS).
[4]"Trypsin revisited: crystallography AT (SUB) atomic resolution and quantum chemistry revealing details of catalysis."
Schmidt A., Jelsch C., Ostergaard P., Rypniewski W., Lamzin V.S.
J. Biol. Chem. 278:43357-43362(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.80 ANGSTROMS).
[5]"Structure of Locusta migratoria protease inhibitor 3 (LMPI-3) in complex with Fusarium oxysporum trypsin."
Leone P., Roussel A., Kellenberger C.
Acta Crystallogr. 64:1165-1171(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S63827 mRNA. Translation: AAB27568.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP35049.
SMRP35049. Positions 25-248.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.103.

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...

Other

EvolutionaryTraceP35049.

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: October 16, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references