Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Trypsin

Gene
N/A
Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Charge relay system
Active sitei108 – 1081Charge relay system
Sitei198 – 1981Required for specificity
Active sitei204 – 2041Charge relay system

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.4. 2351.

Protein family/group databases

MEROPSiS01.103.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin (EC:3.4.21.4)
OrganismiFusarium oxysporum (Fusarium vascular wilt)
Taxonomic identifieri5507 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium oxysporum species complex

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 247Activation peptidePRO_0000028301
Chaini25 – 248224TrypsinPRO_0000028302Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 66
Disulfide bondi174 ↔ 189
Disulfide bondi200 ↔ 225

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 446Combined sources
Beta strandi47 – 5610Combined sources
Beta strandi59 – 624Combined sources
Helixi64 – 674Combined sources
Helixi72 – 743Combined sources
Beta strandi75 – 806Combined sources
Beta strandi82 – 9110Combined sources
Beta strandi93 – 986Combined sources
Beta strandi110 – 1167Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi162 – 1698Combined sources
Helixi171 – 1788Combined sources
Turni180 – 1823Combined sources
Beta strandi187 – 1904Combined sources
Beta strandi207 – 2093Combined sources
Beta strandi215 – 2217Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi232 – 2365Combined sources
Turni237 – 2393Combined sources
Helixi241 – 2477Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP35049.
SMRiP35049. Positions 25-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35049.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 248224Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35049-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKFASVVAL VAPLAAAAPQ EIPNIVGGTS ASAGDFPFIV SISRNGGPWC
60 70 80 90 100
GGSLLNANTV LTAAHCVSGY AQSGFQIRAG SLSRTSGGIT SSLSSVRVHP
110 120 130 140 150
SYSGNNNDLA ILKLSTSIPS GGNIGYARLA ASGSDPVAGS SATVAGWGAT
160 170 180 190 200
SEGGSSTPVN LLKVTVPIVS RATCRAQYGT SAITNQMFCA GVSSGGKDSC
210 220 230 240
QGDSGGPIVD SSNTLIGAVS WGNGCARPNY SGVYASVGAL RSFIDTYA
Length:248
Mass (Da):24,576
Last modified:February 1, 1994 - v1
Checksum:i1A0EBA88C3E70294
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S63827 mRNA. Translation: AAB27568.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S63827 mRNA. Translation: AAB27568.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP35049.
SMRiP35049. Positions 25-248.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.21.4. 2351.

Miscellaneous databases

EvolutionaryTraceiP35049.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1992) [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(1994) [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(2000) [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(2002) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).

Entry informationi

Entry nameiTRYP_FUSOX
AccessioniPrimary (citable) accession number: P35049
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 1, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.