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P00775

- TRYP_STRGR

UniProt

P00775 - TRYP_STRGR

Protein

Trypsin

Gene

sprT

Organism
Streptomyces griseus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (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 sitei73 – 731Charge relay system
    Active sitei118 – 1181Charge relay system
    Sitei202 – 2021Required for specificity
    Active sitei208 – 2081Charge relay system

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    BRENDAi3.4.21.4. 6035.

    Protein family/group databases

    MEROPSiS01.101.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trypsin (EC:3.4.21.4)
    Alternative name(s):
    SGT
    Gene namesi
    Name:sprT
    OrganismiStreptomyces griseus
    Taxonomic identifieri1911 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Add
    BLAST
    Propeptidei33 – 364Activation peptide1 PublicationPRO_0000028307
    Chaini37 – 259223TrypsinPRO_0000028308Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi58 ↔ 74
    Disulfide bondi177 ↔ 192
    Disulfide bondi204 ↔ 233

    Keywords - PTMi

    Disulfide bond, Zymogen

    Structurei

    Secondary structure

    1
    259
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni45 – 473
    Beta strandi51 – 544
    Turni55 – 573
    Beta strandi58 – 647
    Beta strandi67 – 704
    Helixi72 – 743
    Beta strandi77 – 815
    Beta strandi85 – 895
    Beta strandi91 – 955
    Beta strandi99 – 10810
    Beta strandi113 – 1164
    Beta strandi120 – 1267
    Beta strandi137 – 1393
    Beta strandi142 – 15211
    Beta strandi165 – 1728
    Helixi174 – 1807
    Helixi182 – 1843
    Helixi187 – 1893
    Beta strandi190 – 1934
    Beta strandi196 – 1994
    Beta strandi211 – 2155
    Beta strandi221 – 23414
    Beta strandi240 – 2445
    Helixi245 – 25612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OS8X-ray1.55A37-252[»]
    1OSSX-ray1.93A37-252[»]
    1SGTX-ray1.70A37-259[»]
    2FMJX-ray1.65A37-251[»]
    3BEUX-ray1.05A/B37-259[»]
    3I77X-ray2.10A37-259[»]
    3I78X-ray3.00A37-259[»]
    ProteinModelPortaliP00775.
    SMRiP00775. Positions 37-259.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00775.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 257221Peptidase 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.

    P00775-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKHFLRALKR CSVAVATVAI AVVGLQPVTA SAAPNPVVGG TRAAQGEFPF    50
    MVRLSMGCGG ALYAQDIVLT AAHCVSGSGN NTSITATGGV VDLQSSSAVK 100
    VRSTKVLQAP GYNGTGKDWA LIKLAQPINQ PTLKIATTTA YNQGTFTVAG 150
    WGANREGGSQ QRYLLKANVP FVSDAACRSA YGNELVANEE ICAGYPDTGG 200
    VDTCQGDSGG PMFRKDNADE WIQVGIVSWG YGCARPGYPG VYTEVSTFAS 250
    AIASAARTL 259
    Length:259
    Mass (Da):26,776
    Last modified:February 1, 1994 - v2
    Checksum:i050233AFF1F64823
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 962Missing AA sequence (PubMed:804314)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64471 Genomic DNA. Translation: AAA26820.1. Sequence problems.
    PIRiJQ1302. TRSMG.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64471 Genomic DNA. Translation: AAA26820.1 . Sequence problems.
    PIRi JQ1302. TRSMG.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OS8 X-ray 1.55 A 37-252 [» ]
    1OSS X-ray 1.93 A 37-252 [» ]
    1SGT X-ray 1.70 A 37-259 [» ]
    2FMJ X-ray 1.65 A 37-251 [» ]
    3BEU X-ray 1.05 A/B 37-259 [» ]
    3I77 X-ray 2.10 A 37-259 [» ]
    3I78 X-ray 3.00 A 37-259 [» ]
    ProteinModelPortali P00775.
    SMRi P00775. Positions 37-259.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.101.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.4.21.4. 6035.

    Miscellaneous databases

    EvolutionaryTracei P00775.

    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. "Molecular cloning and nucleotide sequence of Streptomyces griseus trypsin gene."
      Kim J.C., Cha S.H., Jeong S.T., Oh S.K., Byun S.M.
      Biochem. Biophys. Res. Commun. 181:707-713(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 10137 / DSM 40855 / NBRC 3430 / NCIMB 8232 / NCTC 6961.
    2. "Amino acid sequence of Streptomyces griseus trypsin. Cyanogen bromide fragments and complete sequence."
      Olafson R.W., Jurasek L., Carpenter M.R., Smillie L.B.
      Biochemistry 14:1168-1177(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 37-259.
    3. "Refined crystal structure of Streptomyces griseus trypsin at 1.7-A resolution."
      Read R.J., James M.N.G.
      J. Mol. Biol. 200:523-551(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiTRYP_STRGR
    AccessioniPrimary (citable) accession number: P00775
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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