Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi5 – 51Calcium 1
Active sitei38 – 381
Metal bindingi47 – 471Calcium 1
Metal bindingi57 – 571Calcium 2
Metal bindingi60 – 601Calcium 2
Metal bindingi62 – 621Calcium 2
Metal bindingi64 – 641Calcium 2
Metal bindingi66 – 661Calcium 2
Active sitei71 – 711
Metal bindingi82 – 821Calcium 1; via carbonyl oxygen
Metal bindingi85 – 851Calcium 1
Metal bindingi87 – 871Calcium 1; via carbonyl oxygen
Metal bindingi89 – 891Calcium 1; via carbonyl oxygen
Active sitei225 – 2251

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 279279ThermitasePRO_0000076421Add
BLAST

Interactioni

Protein-protein interaction databases

MINTiMINT-1504839.

Structurei

Secondary structure

1
279
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 114Combined sources
Helixi14 – 174Combined sources
Helixi20 – 245Combined sources
Beta strandi33 – 397Combined sources
Turni46 – 516Combined sources
Beta strandi52 – 576Combined sources
Turni58 – 614Combined sources
Beta strandi68 – 703Combined sources
Helixi71 – 8010Combined sources
Beta strandi84 – 885Combined sources
Beta strandi97 – 1026Combined sources
Beta strandi108 – 1103Combined sources
Helixi112 – 12413Combined sources
Beta strandi128 – 1325Combined sources
Beta strandi136 – 1383Combined sources
Helixi141 – 15212Combined sources
Beta strandi156 – 1605Combined sources
Beta strandi163 – 1664Combined sources
Turni172 – 1743Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi207 – 2137Combined sources
Turni214 – 2163Combined sources
Beta strandi217 – 2215Combined sources
Helixi224 – 23916Combined sources
Turni240 – 2423Combined sources
Helixi245 – 25410Combined sources
Beta strandi255 – 2573Combined sources
Turni260 – 2645Combined sources
Beta strandi267 – 2704Combined sources
Helixi273 – 2786Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP04072.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 277245Peptidase S8Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1TECX-ray2.20E1-279[»]
1THMX-ray1.37A1-279[»]
2TECX-ray1.98E1-279[»]
3TECX-ray2.00E1-279[»]
ProteinModelPortaliP04072.
SMRiP04072. Positions 1-279.
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: May 11, 2016
This is version 100 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.