Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00775 (TRYP_STRGR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 90. 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

Names and origin

Protein namesRecommended name:
Trypsin

EC=3.4.21.4
Alternative name(s):
SGT
Gene names
Name:sprT
OrganismStreptomyces griseus
Taxonomic identifier1911 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length259 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.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 3232
Propeptide33 – 364Activation peptide
PRO_0000028307
Chain37 – 259223Trypsin
PRO_0000028308

Regions

Domain37 – 257221Peptidase S1

Sites

Active site731Charge relay system
Active site1181Charge relay system
Active site2081Charge relay system
Site2021Required for specificity

Amino acid modifications

Disulfide bond58 ↔ 74
Disulfide bond177 ↔ 192
Disulfide bond204 ↔ 233

Experimental info

Sequence conflict95 – 962Missing AA sequence Ref.2

Secondary structure

............................................. 259
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00775 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 050233AFF1F64823

FASTA25926,776
        10         20         30         40         50         60 
MKHFLRALKR CSVAVATVAI AVVGLQPVTA SAAPNPVVGG TRAAQGEFPF MVRLSMGCGG 

        70         80         90        100        110        120 
ALYAQDIVLT AAHCVSGSGN NTSITATGGV VDLQSSSAVK VRSTKVLQAP GYNGTGKDWA 

       130        140        150        160        170        180 
LIKLAQPINQ PTLKIATTTA YNQGTFTVAG WGANREGGSQ QRYLLKANVP FVSDAACRSA 

       190        200        210        220        230        240 
YGNELVANEE ICAGYPDTGG VDTCQGDSGG PMFRKDNADE WIQVGIVSWG YGCARPGYPG 

       250 
VYTEVSTFAS AIASAARTL 

« Hide

References

[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64471 Genomic DNA. Translation: AAA26820.1. Sequence problems.
PIRTRSMG. JQ1302.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OS8X-ray1.55A37-259[»]
1OSSX-ray1.93A37-259[»]
1SGTX-ray1.70A37-259[»]
2FMJX-ray1.65A37-251[»]
3BEUX-ray1.05A/B37-259[»]
3I77X-ray2.10A37-259[»]
3I78X-ray3.00A37-259[»]
ProteinModelPortalP00775.
SMRP00775. Positions 37-259.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.4.21.4. 6035.

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

EvolutionaryTraceP00775.

Entry information

Entry nameTRYP_STRGR
AccessionPrimary (citable) accession number: P00775
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1994
Last modified: November 13, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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