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Protein

Proteinase K

Gene

PROK

Organism
Engyodontium album (Tritirachium album)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes keratin at aromatic and hydrophobic residues.

Catalytic activityi

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

Cofactori

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi121Calcium 2; via carbonyl oxygen1
Active sitei144Charge relay system1
Active sitei174Charge relay system1
Metal bindingi280Calcium 1; via carbonyl oxygen1
Metal bindingi282Calcium 1; via carbonyl oxygen1
Metal bindingi305Calcium 11
Active sitei329Charge relay system1
Metal bindingi365Calcium 21

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.64. 6510.

Protein family/group databases

MEROPSiS08.054.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteinase K (EC:3.4.21.64)
Alternative name(s):
Endopeptidase K
Tritirachium alkaline proteinase
Gene namesi
Name:PROK
OrganismiEngyodontium album (Tritirachium album)
Taxonomic identifieri37998 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesCordycipitaceaeParengyodontium

Pathology & Biotechi

Protein family/group databases

Allergomei8265. Tri al Proteinase K.

Chemistry databases

ChEMBLiCHEMBL1075070.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 15Add BLAST15
PropeptideiPRO_000002713816 – 1052 PublicationsAdd BLAST90
ChainiPRO_0000027139106 – 384Proteinase KAdd BLAST279

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi139 ↔ 228
Disulfide bondi283 ↔ 354

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PRIDEiP06873.

Interactioni

Chemistry databases

BindingDBiP06873.

Structurei

Secondary structure

1384
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi107 – 109Combined sources3
Helixi113 – 118Combined sources6
Beta strandi121 – 124Combined sources4
Beta strandi127 – 129Combined sources3
Turni132 – 137Combined sources6
Beta strandi138 – 145Combined sources8
Helixi152 – 154Combined sources3
Beta strandi158 – 166Combined sources9
Beta strandi171 – 173Combined sources3
Helixi174 – 183Combined sources10
Turni185 – 187Combined sources3
Beta strandi194 – 199Combined sources6
Helixi209 – 222Combined sources14
Helixi223 – 225Combined sources3
Beta strandi231 – 236Combined sources6
Beta strandi238 – 241Combined sources4
Helixi244 – 255Combined sources12
Beta strandi258 – 263Combined sources6
Beta strandi266 – 270Combined sources5
Helixi271 – 273Combined sources3
Turni276 – 278Combined sources3
Beta strandi282 – 288Combined sources7
Beta strandi292 – 294Combined sources3
Beta strandi300 – 303Combined sources4
Beta strandi306 – 309Combined sources4
Beta strandi311 – 317Combined sources7
Turni318 – 320Combined sources3
Beta strandi321 – 325Combined sources5
Helixi328 – 344Combined sources17
Turni350 – 352Combined sources3
Helixi353 – 360Combined sources8
Beta strandi361 – 364Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4WOBX-ray1.90A106-384[»]
4WOCX-ray1.60A106-384[»]
4ZARX-ray1.15A106-384[»]
5AMXX-ray1.01A106-384[»]
5AVJX-ray1.45A106-384[»]
5AVKX-ray1.45A106-384[»]
5CW1X-ray1.45A106-384[»]
5I9Selectron microscopy1.75A106-384[»]
ProteinModelPortaliP06873.
SMRiP06873.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06873.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini140 – 365Peptidase S8Add BLAST226

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated
Contains 1 peptidase S8 domain.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR000209. 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. Propept_inh.
IPR010259. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06873-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLSVLLSLL PLALGAPAVE QRSEAAPLIE ARGEMVANKY IVKFKEGSAL
60 70 80 90 100
SALDAAMEKI SGKPDHVYKN VFSGFAATLD ENMVRVLRAH PDVEYIEQDA
110 120 130 140 150
VVTINAAQTN APWGLARISS TSPGTSTYYY DESAGQGSCV YVIDTGIEAS
160 170 180 190 200
HPEFEGRAQM VKTYYYSSRD GNGHGTHCAG TVGSRTYGVA KKTQLFGVKV
210 220 230 240 250
LDDNGSGQYS TIIAGMDFVA SDKNNRNCPK GVVASLSLGG GYSSSVNSAA
260 270 280 290 300
ARLQSSGVMV AVAAGNNNAD ARNYSPASEP SVCTVGASDR YDRRSSFSNY
310 320 330 340 350
GSVLDIFGPG TSILSTWIGG STRSISGTSM ATPHVAGLAA YLMTLGKTTA
360 370 380
ASACRYIADT ANKGDLSNIP FGTVNLLAYN NYQA
Length:384
Mass (Da):40,300
Last modified:January 1, 1990 - v2
Checksum:i00E1B111F0EFF5C4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti184S → SG AA sequence (Ref. 2) Curated1
Sequence conflicti184S → SG AA sequence (Ref. 3) Curated1
Sequence conflicti312 – 316SILST → DLS AA sequence (Ref. 2) Curated5
Sequence conflicti312 – 316SILST → DLS AA sequence (Ref. 3) Curated5
Sequence conflicti312 – 316SILST → DLS AA sequence (PubMed:3924077).Curated5
Sequence conflicti374V → F AA sequence (Ref. 2) Curated1
Sequence conflicti377Missing AA sequence (Ref. 2) Curated1
Sequence conflicti377Missing AA sequence (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14689 Genomic DNA. Translation: CAA32820.1.
X14688 mRNA. Translation: CAA32819.1.
PIRiS02142. SUTIKA.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14689 Genomic DNA. Translation: CAA32820.1.
X14688 mRNA. Translation: CAA32819.1.
PIRiS02142. SUTIKA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4WOBX-ray1.90A106-384[»]
4WOCX-ray1.60A106-384[»]
4ZARX-ray1.15A106-384[»]
5AMXX-ray1.01A106-384[»]
5AVJX-ray1.45A106-384[»]
5AVKX-ray1.45A106-384[»]
5CW1X-ray1.45A106-384[»]
5I9Selectron microscopy1.75A106-384[»]
ProteinModelPortaliP06873.
SMRiP06873.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP06873.
ChEMBLiCHEMBL1075070.

Protein family/group databases

Allergomei8265. Tri al Proteinase K.
MEROPSiS08.054.

Proteomic databases

PRIDEiP06873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.21.64. 6510.

Miscellaneous databases

EvolutionaryTraceiP06873.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR000209. 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. Propept_inh.
IPR010259. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRTK_ENGAL
AccessioniPrimary (citable) accession number: P06873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.