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P35049

- TRYP_FUSOX

UniProt

P35049 - TRYP_FUSOX

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Protein

Trypsin

Gene
N/A
Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed - 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

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-KW
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 – 446
Beta strandi47 – 5610
Beta strandi59 – 624
Helixi64 – 674
Helixi72 – 743
Beta strandi75 – 806
Beta strandi82 – 9110
Beta strandi93 – 986
Beta strandi110 – 1167
Beta strandi141 – 1477
Beta strandi162 – 1698
Helixi171 – 1788
Turni180 – 1823
Beta strandi187 – 1904
Beta strandi207 – 2093
Beta strandi215 – 2217
Beta strandi223 – 2264
Beta strandi232 – 2365
Turni237 – 2393
Helixi241 – 2477

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
Links Updated
S63827 mRNA. Translation: AAB27568.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S63827 mRNA. Translation: AAB27568.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FN8 X-ray 0.81 A 25-248 [» ]
1FY4 X-ray 0.81 A 25-248 [» ]
1FY5 X-ray 0.81 A 25-248 [» ]
1GDN X-ray 0.81 A 25-248 [» ]
1GDQ X-ray 0.93 A 25-248 [» ]
1GDU X-ray 1.07 A 25-248 [» ]
1PPZ X-ray 1.23 A 25-248 [» ]
1PQ5 X-ray 0.85 A 25-248 [» ]
1PQ7 X-ray 0.80 A 25-248 [» ]
1PQ8 X-ray 1.00 A 25-248 [» ]
1PQA X-ray 1.23 A 25-248 [» ]
1TRY X-ray 1.55 A 25-248 [» ]
1XVM X-ray 1.10 A 25-248 [» ]
1XVO X-ray 0.84 A 25-248 [» ]
2G51 X-ray 1.84 A 25-248 [» ]
2G52 X-ray 1.84 A 25-248 [» ]
2VU8 X-ray 1.80 E 25-248 [» ]
ProteinModelPortali P35049.
SMRi P35049. Positions 25-248.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S01.103.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P35049.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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).

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: October 29, 2014
This is version 91 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