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P06873 (PRTK_TRIAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteinase K
EC=3.4.21.64
Alternative name(s):
Endopeptidase K
Tritirachium alkaline proteinase
Gene names
Name:PROK
OrganismTritirachium album (Engyodontium album)
Taxonomic identifier37998 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Engyodontium

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes keratin at aromatic and hydrophobic residues.

Catalytic activity

Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.

Cofactor

Binds 2 calcium ions per subunit.

Sequence similarities

Belongs to the peptidase S8 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515
Propeptide16 – 10590
PRO_0000027138
Chain106 – 384279Proteinase K
PRO_0000027139

Sites

Active site1441Charge relay system
Active site1741Charge relay system
Active site3291Charge relay system
Metal binding1211Calcium 2; via carbonyl oxygen
Metal binding2801Calcium 1; via carbonyl oxygen
Metal binding2821Calcium 1; via carbonyl oxygen
Metal binding3051Calcium 1
Metal binding3651Calcium 2

Amino acid modifications

Disulfide bond139 ↔ 228
Disulfide bond283 ↔ 354

Experimental info

Sequence conflict1841S → SG AA sequence Ref.2
Sequence conflict1841S → SG AA sequence Ref.3
Sequence conflict312 – 3165SILST → DLS AA sequence Ref.2
Sequence conflict312 – 3165SILST → DLS AA sequence Ref.3
Sequence conflict312 – 3165SILST → DLS AA sequence Ref.4
Sequence conflict3741V → F AA sequence Ref.2
Sequence conflict3771Missing AA sequence Ref.2
Sequence conflict3771Missing AA sequence Ref.3

Secondary structure

1 ......................................................... 384
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06873 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: 00E1B111F0EFF5C4

FASTA38440,300
        10         20         30         40         50         60 
MRLSVLLSLL PLALGAPAVE QRSEAAPLIE ARGEMVANKY IVKFKEGSAL SALDAAMEKI 

        70         80         90        100        110        120 
SGKPDHVYKN VFSGFAATLD ENMVRVLRAH PDVEYIEQDA VVTINAAQTN APWGLARISS 

       130        140        150        160        170        180 
TSPGTSTYYY DESAGQGSCV YVIDTGIEAS HPEFEGRAQM VKTYYYSSRD GNGHGTHCAG 

       190        200        210        220        230        240 
TVGSRTYGVA KKTQLFGVKV LDDNGSGQYS TIIAGMDFVA SDKNNRNCPK GVVASLSLGG 

       250        260        270        280        290        300 
GYSSSVNSAA ARLQSSGVMV AVAAGNNNAD ARNYSPASEP SVCTVGASDR YDRRSSFSNY 

       310        320        330        340        350        360 
GSVLDIFGPG TSILSTWIGG STRSISGTSM ATPHVAGLAA YLMTLGKTTA ASACRYIADT 

       370        380 
ANKGDLSNIP FGTVNLLAYN NYQA

« Hide

References

[1]"Proteinase K from Tritirachium album Limber. Characterization of the chromosomal gene and expression of the cDNA in Escherichia coli."
Gunkel F.A., Gassen H.G.
Eur. J. Biochem. 179:185-194(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: ATCC 22563 / Limber.
[2]"Proteinase K - a new subclass of the subtilisins. The amino acid sequence of the enzyme."
Jany K.-D., Lederer G., Mayer B.
Biol. Chem. Hoppe-Seyler 367:87-87(1986)
Cited for: PROTEIN SEQUENCE OF 106-384.
[3]"Amino acid sequence of proteinase K from the mold Tritirachium album limber. Proteinase K - a subtilisin-related enzyme with disulfide bonds."
Jany K.-D., Lederer G., Mayer B.
FEBS Lett. 199:139-144(1986)
Cited for: PROTEIN SEQUENCE OF 106-384.
[4]"Proteinase K from Tritirachium album limber. I. Molecular mass and sequence around the active site serine residue."
Jany K.-D., Mayer B.
Biol. Chem. Hoppe-Seyler 366:485-492(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 259-343.
[5]"Three-dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin."
Paehler A., Banerjee A., Dattagupta J.K., Fujiwara T., Lindner K., Pal G.P., Suck D., Weber G., Saenger W.
EMBO J. 3:1311-1314(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
[6]"Crystal structure of calcium-free proteinase K at 1.5-A resolution."
Mueller A., Hinrichs W., Wolf W.M., Saenger W.
J. Biol. Chem. 269:23108-23111(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[7]"Crystal structure of a complex formed between proteolytically-generated lactoferrin fragment and proteinase K."
Singh T.P., Sharma S., Karthikeyan S., Betzel C., Bhatia K.L.
Proteins 33:30-38(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X14689 Genomic DNA. Translation: CAA32820.1.
X14688 mRNA. Translation: CAA32819.1.
PIRSUTIKA. S02142.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJRX-ray2.44E106-384[»]
1CNMX-ray2.20A106-384[»]
1EGQX-ray1.55A106-384[»]
1HT3X-ray1.80A106-384[»]
1IC6X-ray0.98A106-384[»]
1OYOX-ray2.02A106-384[»]
1P7VX-ray1.08A106-384[»]
1P7WX-ray1.02A106-384[»]
1PEKX-ray2.20E106-384[»]
1PFGX-ray2.50A106-384[»]
1PJ8X-ray2.20A106-384[»]
1PTKX-ray2.40A106-384[»]
2DP4X-ray2.90E106-384[»]
2DQKX-ray1.93A106-384[»]
2DUJX-ray1.67A106-384[»]
2G4VX-ray2.14A106-384[»]
2HD4X-ray2.15A106-384[»]
2HPZX-ray1.69A106-384[»]
2ID8X-ray1.27A106-384[»]
2PKCX-ray1.50A106-384[»]
2PQ2X-ray1.82A106-384[»]
2PRKX-ray1.50A106-384[»]
2PWAX-ray0.83A106-384[»]
2PWBX-ray1.90A106-384[»]
2PYZX-ray1.79A106-384[»]
2V8BX-ray0.94A106-384[»]
3AJ8X-ray1.10A106-384[»]
3AJ9X-ray1.10A106-384[»]
3D9QX-ray1.43X106-384[»]
3DDZX-ray1.70X106-384[»]
3DE0X-ray1.90X106-384[»]
3DE1X-ray2.00X106-384[»]
3DE2X-ray2.10X106-384[»]
3DE3X-ray1.43X106-384[»]
3DE4X-ray1.80X106-384[»]
3DE5X-ray2.10X106-384[»]
3DE6X-ray2.20X106-384[»]
3DE7X-ray2.30X106-384[»]
3DVQX-ray1.02X106-384[»]
3DVRX-ray1.02X106-384[»]
3DVSX-ray1.02X106-384[»]
3DW1X-ray1.03X106-384[»]
3DW3X-ray0.99X106-384[»]
3DWEX-ray0.99X106-384[»]
3DYBX-ray1.32A106-384[»]
3GT3X-ray1.50A106-384[»]
3GT4X-ray1.76A106-384[»]
3I2YX-ray1.00X106-384[»]
3I30X-ray0.99X106-384[»]
3I34X-ray1.00X106-384[»]
3I37X-ray1.00X106-384[»]
3L1KX-ray1.55A106-384[»]
3OSZX-ray2.26A106-384[»]
3PRKX-ray2.20E106-384[»]
3PTLX-ray1.30A106-384[»]
3Q40X-ray1.80A106-384[»]
3Q5GX-ray1.77A106-384[»]
3QMPX-ray1.10A106-384[»]
4B5LX-ray1.60A106-384[»]
4DJ5X-ray1.80X106-384[»]
4FONX-ray1.05A106-384[»]
ProteinModelPortalP06873.
SMRP06873. Positions 106-384.
ModBaseSearch...

Protein family/group databases

Allergome8265. Tri al Proteinase K.
MEROPSS08.054.

Proteomic databases

PRIDEP06873.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.200. 1 hit.
InterProIPR010259. Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
[Graphical view]
PANTHERPTHR10795. PTHR10795. 1 hit.
PfamPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
SUPFAMSSF52743. Pept_S8_S53. 1 hit.
SSF54897. Prot_inh_propept. 1 hit.
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL1075070.
EvolutionaryTraceP06873.

Entry information

Entry namePRTK_TRIAL
AccessionPrimary (citable) accession number: P06873
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1990
Last modified: April 3, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents