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Protein

Thermitase

Gene
N/A
Organism
Thermoactinomyces vulgaris
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of proteins, including collagen.

Cofactori

Note: Binds 3 calcium ions or 2 calcium ions and 1 sodium ion per subunit. The sodium ion is bound at calcium concentrations up to 5 mM. At 100 mM calcium 3 calcium ions are bound.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi5Calcium 11
Active sitei381
Metal bindingi47Calcium 11
Metal bindingi57Calcium 21
Metal bindingi60Calcium 21
Metal bindingi62Calcium 21
Metal bindingi64Calcium 21
Metal bindingi66Calcium 21
Active sitei711
Metal bindingi82Calcium 1; via carbonyl oxygen1
Metal bindingi85Calcium 11
Metal bindingi87Calcium 1; via carbonyl oxygen1
Metal bindingi89Calcium 1; via carbonyl oxygen1
Active sitei2251

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.66. 6282.

Protein family/group databases

MEROPSiS08.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Thermitase (EC:3.4.21.66)
OrganismiThermoactinomyces vulgaris
Taxonomic identifieri2026 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesThermoactinomycetaceaeThermoactinomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000764211 – 279ThermitaseAdd BLAST279

Interactioni

Protein-protein interaction databases

MINTiMINT-1504839.

Structurei

Secondary structure

1279
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 11Combined sources4
Helixi14 – 17Combined sources4
Helixi20 – 24Combined sources5
Beta strandi33 – 39Combined sources7
Turni46 – 51Combined sources6
Beta strandi52 – 57Combined sources6
Turni58 – 61Combined sources4
Beta strandi68 – 70Combined sources3
Helixi71 – 80Combined sources10
Beta strandi84 – 88Combined sources5
Beta strandi97 – 102Combined sources6
Beta strandi108 – 110Combined sources3
Helixi112 – 124Combined sources13
Beta strandi128 – 132Combined sources5
Beta strandi136 – 138Combined sources3
Helixi141 – 152Combined sources12
Beta strandi156 – 160Combined sources5
Beta strandi163 – 166Combined sources4
Turni172 – 174Combined sources3
Beta strandi178 – 184Combined sources7
Beta strandi202 – 205Combined sources4
Beta strandi207 – 213Combined sources7
Turni214 – 216Combined sources3
Beta strandi217 – 221Combined sources5
Helixi224 – 239Combined sources16
Turni240 – 242Combined sources3
Helixi245 – 254Combined sources10
Beta strandi255 – 257Combined sources3
Turni260 – 264Combined sources5
Beta strandi267 – 270Combined sources4
Helixi273 – 278Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TECX-ray2.20E1-279[»]
1THMX-ray1.37A1-279[»]
2TECX-ray1.98E1-279[»]
3TECX-ray2.00E1-279[»]
ProteinModelPortaliP04072.
SMRiP04072.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04072.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 277Peptidase S8Add BLAST245

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.40.50.200. 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.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04072-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
YTPNDPYFSS RQYGPQKIQA PQAWDIAEGS GAKIAIVDTG VQSNHPDLAG
60 70 80 90 100
KVVGGWDFVD NDSTPQNGNG HGTHCAGIAA AVTNNSTGIA GTAPKASILA
110 120 130 140 150
VRVLDNSGSG TWTAVANGIT YAADQGAKVI SLSLGGTVGN SGLQQAVNYA
160 170 180 190 200
WNKGSVVVAA AGNAGNTAPN YPAYYSNAIA VASTDQNDNK SSFSTYGSVV
210 220 230 240 250
DVAAPGSWIY STYPTSTYAS LSGTSMATPH VAGVAGLLAS QGRSASNIRA
260 270
AIENTADKIS GTGTYWAKGR VNAYKAVQY
Length:279
Mass (Da):28,366
Last modified:November 1, 1986 - v1
Checksum:i8065049BC8927AC0
GO

Sequence databases

PIRiA00973. SUMYTV.

Cross-referencesi

Sequence databases

PIRiA00973. SUMYTV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TECX-ray2.20E1-279[»]
1THMX-ray1.37A1-279[»]
2TECX-ray1.98E1-279[»]
3TECX-ray2.00E1-279[»]
ProteinModelPortaliP04072.
SMRiP04072.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1504839.

Protein family/group databases

MEROPSiS08.007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.21.66. 6282.

Miscellaneous databases

EvolutionaryTraceiP04072.

Family and domain databases

Gene3Di3.40.50.200. 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.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHET_THEVU
AccessioniPrimary (citable) accession number: P04072
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: November 2, 2016
This is version 102 of the entry and version 1 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

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.