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UniProtKB/Swiss-Prot entry P06873


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRTK_TRIAL
Primary accession number P06873
Secondary accession numbers None
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 1, 1990 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 82)
Name and origin of the protein
Protein name Proteinase K [Precursor]
Synonyms EC 3.4.21.64
Tritirachium alkaline proteinase
Endopeptidase K
Gene name
Name: PROK
From
Tritirachium album (Engyodontium album) [TaxID: 37998] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; mitosporic Ascomycota; Engyodontium.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=ATCC 22563 / Limber;
PubMed=2645134 [NCBI, ExPASy, EBI, Israel, Japan]
Gunkel F.A., Gassen H.G.;
"Proteinase K from Tritirachium album Limber. Characterization of the chromosomal gene and expression of the cDNA in Escherichia coli.";
Eur. J. Biochem. 179:185-194(1989).
[2]
PROTEIN SEQUENCE OF 106-384.
Jany K.-D., Lederer G., Mayer B.;
"Proteinase K - a new subclass of the subtilisins. The amino acid sequence of the enzyme.";
Biol. Chem. Hoppe-Seyler 367:87-87(1986).
[3]
PROTEIN SEQUENCE OF 106-384.
Jany K.-D., Lederer G., Mayer B.;
"Amino acid sequence of proteinase K from the mold Tritirachium album limber. Proteinase K - a subtilisin-related enzyme with disulfide bonds.";
FEBS Lett. 199:139-144(1986).
[4]
PROTEIN SEQUENCE OF 259-343.
PubMed=3924077 [NCBI, ExPASy, EBI, Israel, Japan]
Jany K.-D., Mayer B.;
"Proteinase K from Tritirachium album limber. I. Molecular mass and sequence around the active site serine residue.";
Biol. Chem. Hoppe-Seyler 366:485-492(1985).
[5]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
PubMed=6378621 [NCBI, ExPASy, EBI, Israel, Japan]
Paehler A., Banerjee A., Dattagupta J.K., Fujiwara T., Lindner K., Pal G.P., Suck D., Weber G., Saenger W.;
"Three-dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin.";
EMBO J. 3:1311-1314(1984).
[6]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
PubMed=8083213 [NCBI, ExPASy, EBI, Israel, Japan]
Mueller A., Hinrichs W., Wolf W.M., Saenger W.;
"Crystal structure of calcium-free proteinase K at 1.5-A resolution.";
J. Biol. Chem. 269:23108-23111(1994).
[7]
X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS).
DOI=10.1002/(SICI)1097-0134(19981001)33:1<30::AID-PROT3>3.3.CO;2-W; PubMed=9741842 [NCBI, ExPASy, EBI, Israel, Japan]
Singh T.P., Sharma S., Karthikeyan S., Betzel C., Bhatia K.L.;
"Crystal structure of a complex formed between proteolytically-generated lactoferrin fragment and proteinase K.";
Proteins 33:30-38(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X14689; CAA32820.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14688; CAA32819.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S02142; SUTIKA.
3D structure databases
PDB
1BJR; X-ray; 2.44 A; E=106-384.[ExPASy / RCSB / EBI]
1CNM; X-ray; 2.20 A; A=106-384.[ExPASy / RCSB / EBI]
1EGQ; X-ray; 1.55 A; A=106-384.[ExPASy / RCSB / EBI]
1HT3; X-ray; 1.80 A; A=106-384.[ExPASy / RCSB / EBI]
1IC6; X-ray; 0.98 A; A=106-384.[ExPASy / RCSB / EBI]
1OYO; X-ray; 2.02 A; A=106-384.[ExPASy / RCSB / EBI]
1P7V; X-ray; 1.08 A; A=106-384.[ExPASy / RCSB / EBI]
1P7W; X-ray; 1.02 A; A=106-384.[ExPASy / RCSB / EBI]
1PEK; X-ray; 2.20 A; E=106-384.[ExPASy / RCSB / EBI]
1PFG; X-ray; 2.50 A; A=106-384.[ExPASy / RCSB / EBI]
1PJ8; X-ray; 2.20 A; A=106-384.[ExPASy / RCSB / EBI]
1PTK; X-ray; 2.40 A; A=106-384.[ExPASy / RCSB / EBI]
2DP4; X-ray; 2.90 A; E=106-384.[ExPASy / RCSB / EBI]
2DQK; X-ray; 1.93 A; A=106-384.[ExPASy / RCSB / EBI]
2DUJ; X-ray; 1.67 A; A=106-384.[ExPASy / RCSB / EBI]
2G4V; X-ray; 2.14 A; A=106-384.[ExPASy / RCSB / EBI]
2HD4; X-ray; 2.15 A; A=106-384.[ExPASy / RCSB / EBI]
2HPZ; X-ray; 1.69 A; A=106-384.[ExPASy / RCSB / EBI]
2ID8; X-ray; 1.27 A; A=106-384.[ExPASy / RCSB / EBI]
2PKC; X-ray; 1.50 A; A=106-384.[ExPASy / RCSB / EBI]
2PQ2; X-ray; 1.82 A; A=106-384.[ExPASy / RCSB / EBI]
2PRK; X-ray; 1.50 A; A=106-384.[ExPASy / RCSB / EBI]
2PWA; X-ray; 0.83 A; A=106-384.[ExPASy / RCSB / EBI]
2PWB; X-ray; 1.90 A; A=106-384.[ExPASy / RCSB / EBI]
2PYZ; X-ray; 1.79 A; A=106-384.[ExPASy / RCSB / EBI]
3PRK; X-ray; 2.20 A; E=106-384.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BJR; -.
1CNM; -.
1EGQ; -.
1HT3; -.
1IC6; -.
1OYO; -.
1P7V; -.
1P7W; -.
1PEK; -.
1PFG; -.
1PJ8; -.
1PTK; -.
2DP4; -.
2DQK; -.
2DUJ; -.
2G4V; -.
2HD4; -.
2HPZ; -.
2ID8; -.
2PKC; -.
2PQ2; -.
2PRK; -.
2PWA; -.
2PWB; -.
2PYZ; -.
3PRK; -.
ModBase P06873.
Protein family/group databases
MEROPS S08.054; -.
Ontologies
GO
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000209; Pept_S8_S53.
IPR015500; Peptidase_S8_subtilisin-rel.
IPR010259; Prot_inh_S8A.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.200; Pept_S8_S53; 1.
PANTHER PTHR10795; SubtilSerProt; 1.
Pfam PF00082; Peptidase_S8; 1.
PF05922; Subtilisin_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00723; SUBTILISIN.
PROSITE PS00136; SUBTILASE_ASP; 1.
PS00137; SUBTILASE_HIS; 1.
PS00138; SUBTILASE_SER; 1.
BLOCKS P06873.
ProtoNet P06873.
Other
SWISS-3DIMAGE P06873.
LinkHub P06873; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Protease; Serine protease; Signal; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    15  15      
PROPEP   16   105  90      PRO_0000027138
CHAIN   106   384  279     Proteinase K. PRO_0000027139
ACT_SITE   144   144        Charge relay system. 
ACT_SITE   174   174        Charge relay system. 
ACT_SITE   329   329        Charge relay system. 
METAL   121   121        Calcium 2; via carbonyl oxygen. 
METAL   280   280        Calcium 1; via carbonyl oxygen. 
METAL   282   282        Calcium 1; via carbonyl oxygen. 
METAL   305   305        Calcium 1. 
METAL   365   365        Calcium 2. 
DISULFID   139   228         
DISULFID   283   354         
CONFLICT   184   184        S -> SG (in Ref. 2 and 3). 
CONFLICT   312   316        SILST -> DLS (in Ref. 2, 3 and 4). 
CONFLICT   374   374        V -> F (in Ref. 2; AA sequence). 
CONFLICT   377   377        Missing (in Ref. 2 and 3). 
HELIX   113   118  6      
TURN   132   137  6      
STRAND   138   145  8      
HELIX   152   154  3      
STRAND   158   166  9      
STRAND   171   173  3      
HELIX   174   183  10      
TURN   185   187  3      
STRAND   194   199  6      
HELIX   209   222  14      
HELIX   223   225  3      
STRAND   231   236  6      
HELIX   244   255  12      
STRAND   259   263  5      
STRAND   266   270  5      
HELIX   271   273  3      
TURN   276   278  3      
STRAND   282   288  7      
STRAND   292   294  3      
STRAND   306   309  4      
STRAND   311   317  7      
TURN   318   320  3      
STRAND   321   325  5      
HELIX   328   344  17      
TURN   350   352  3      
HELIX   353   360  8      
STRAND   361   364  4      
Sequence information
Length: 384 AA [This is the length of the unprocessed precursor] Molecular weight: 40300 Da [This is the MW of the unprocessed precursor] CRC64: 00E1B111F0EFF5C4 [This is a checksum on the sequence]
        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 

P06873 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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