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P35049

- TRYP_FUSOX

UniProt

P35049 - TRYP_FUSOX

Protein

Trypsin

Gene
N/A
Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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

    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-SubCell

    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

    MVKFASVVAL VAPLAAAAPQ EIPNIVGGTS ASAGDFPFIV SISRNGGPWC    50
    GGSLLNANTV LTAAHCVSGY AQSGFQIRAG SLSRTSGGIT SSLSSVRVHP 100
    SYSGNNNDLA ILKLSTSIPS GGNIGYARLA ASGSDPVAGS SATVAGWGAT 150
    SEGGSSTPVN LLKVTVPIVS RATCRAQYGT SAITNQMFCA GVSSGGKDSC 200
    QGDSGGPIVD SSNTLIGAVS WGNGCARPNY SGVYASVGAL RSFIDTYA 248
    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 1, 2014
    This is version 90 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