P60994 (ERVB_TABDI) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 43.
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: Ervatamin-B Short name=ERV-B EC=3.4.22.- |
| Organism | Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria) |
| Taxonomic identifier | 52861 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Rauvolfioideae › Tabermontantaneae › Tabernaemontana |
Protein attributes
| Sequence length | 215 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Cysteine protease. |
| Subcellular location | |
| Tissue specificity | Laticifer. |
| Post-translational modification | Not glycosylated. |
| Miscellaneous | Stable in 8 M urea and 2.5 M GuHCl at neutral pH, in 40% acetonitrile, 70% ethanol and 50% methanol. Unstable in SDS. |
| Sequence similarities | Belongs to the peptidase C1 family. |
| Biophysicochemical properties | pH dependence: Active from pH 3.0 to 10.5. Temperature dependence: Active up to 62 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 215 | 215 | Ervatamin-B | PRO_0000050558 | |||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||
| Active site | 25 | 1 | |||||||||||||||||||||||||||||||||||||||
| Active site | 158 | 1 | |||||||||||||||||||||||||||||||||||||||
| Active site | 178 | 1 | By similarity | ||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 22 ↔ 63 | ||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 56 ↔ 96 | ||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 152 ↔ 203 | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Helix | 7 – 10 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 21 – 23 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 25 – 42 | 18 | |||||||||||||||||||||||||||||||||||||||
| Helix | 50 – 56 | 7 | |||||||||||||||||||||||||||||||||||||||
| Helix | 68 – 78 | 11 | |||||||||||||||||||||||||||||||||||||||
| Turn | 84 – 86 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 108 – 111 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 117 – 126 | 10 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 129 – 133 | 5 | |||||||||||||||||||||||||||||||||||||||
| Helix | 138 – 141 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 145 – 148 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 158 – 168 | 11 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 171 – 177 | 7 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 189 – 193 | 5 | |||||||||||||||||||||||||||||||||||||||
| Helix | 202 – 204 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 210 – 213 | 4 | |||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Proposed amino acid sequence and the 1.63 A X-ray crystal structure of a plant cysteine protease, ervatamin B: some insights into the structural basis of its stability and substrate specificity." Biswas S., Chakrabarti C., Kundu S., Jagannadham M.V., Dattagupta J.K. Proteins 51:489-497(2003) [PubMed: 12784208] [Abstract] Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). |
| [2] | "Purification and characterization of a stable cysteine protease ervatamin B, with two disulfide bridges, from the latex of Ervatamia coronaria." Kundu S., Sundd M., Jagannadham M.V. J. Agric. Food Chem. 48:171-179(2000) [PubMed: 10691612] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21, CHARACTERIZATION. Tissue: Latex. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | A59428. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P60994. | ||||||||||||
| SMR | P60994. Positions 1-215. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| MEROPS | C01.099. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR000169. Pept_cys_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. [Graphical view] | ||||||||||||
| PANTHER | PTHR12411. Peptidase_C1A. 1 hit. | ||||||||||||
| Pfam | PF00112. Peptidase_C1. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00705. PAPAIN. | ||||||||||||
| SMART | 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 | ERVB_TABDI | ||||||||
| Accession | Primary (citable) accession number: P60994 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
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