O17473 (CATL_BRUPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 3, 2012.
Version 69.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cathepsin L-like EC=3.4.22.15 |
| Organism | Brugia pahangi (Filarial nematode worm) |
| Taxonomic identifier | 6280 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Spirurida › Filarioidea › Onchocercidae › Brugia![]() |
Protein attributes
| Sequence length | 395 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity. |
| Sequence similarities | Belongs to the peptidase C1 family. |
Ontologies
| Keywords | |
|---|---|
| Domain | Signal |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Disulfide bond Zymogen |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 16 | 16 | Potential | |||||||||||||||||||||||||||||||||||||
| Propeptide | 17 – 181 | 165 | Activation peptide Potential | PRO_0000026293 | ||||||||||||||||||||||||||||||||||||
| Chain | 182 – 395 | 214 | Cathepsin L-like | PRO_0000026294 | ||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||
| Active site | 206 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||
| Active site | 342 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||
| Active site | 363 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 203 ↔ 246 | Ref.2 | ||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 237 ↔ 278 | Ref.2 | ||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 337 ↔ 385 | Ref.2 | ||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Turn | 188 – 192 | 5 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 202 – 204 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 206 – 223 | 18 | ||||||||||||||||||||||||||||||||||||||
| Helix | 231 – 237 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 251 – 258 | 8 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 259 – 261 | 3 | ||||||||||||||||||||||||||||||||||||||
| Turn | 266 – 268 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 279 – 283 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 300 – 310 | 11 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 313 – 316 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 322 – 326 | 5 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 343 – 349 | 7 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 358 – 362 | 5 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 367 – 369 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 374 – 378 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 384 – 386 | 3 | ||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Cathepsin L-like cysteine protease from Brugia pahangi third stage larvae." Selzer P.M., Huong X., Britton C., McKerrow J.H. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Molecular model of Brugia pahangi third-stage larvae cysteine protease." Selzer P.M., Chen X., Cohen F.E., McKerrow J.H. Submitted (JUL-1998) to the PDB data bank Cited for: 3D-STRUCTURE MODELING OF 182-395, DISULFIDE BONDS. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF031819 mRNA. Translation: AAB86867.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | O17473. | ||||||||||||
| SMR | O17473. Positions 182-395. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR025661. Pept_asp_AS. IPR000169. Pept_cys_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view] | ||||||||||||
| PANTHER | PTHR12411. PTHR12411. 1 hit. | ||||||||||||
| Pfam | PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00705. PAPAIN. | ||||||||||||
| SMART | SM00848. Inhibitor_I29. 1 hit. SM00645. Pept_C1. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00640. THIOL_PROTEASE_ASN. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. False negative. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | CATL_BRUPA | ||||||||
| Accession | Primary (citable) accession number: O17473 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
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 |

Clusters with
