P85084 (CHIT_CARPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 26.
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: Endochitinase EC=3.2.1.14 |
| Organism | Carica papaya (Papaya) |
| Taxonomic identifier | 3649 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Caricaceae › Carica |
Protein attributes
| Sequence length | 243 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Defense against chitin containing fungal pathogens. Shows activity on chitin, tetra-N-acetylglucosamine and chitosan. Ref.1 |
| Catalytic activity | Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Ref.1 |
| Subcellular location | Vacuole By similarity. Note: Vacuolar and protoplast By similarity. UniProtKB P19171 |
| Sequence similarities | Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily. |
| Mass spectrometry | Molecular mass is 26534 Da from positions 1 - 243. Determined by ESI. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Chitin degradation Plant defense Polysaccharide degradation |
| Cellular component | Vacuole |
| Ligand | Chitin-binding |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro chitin catabolic processInferred from electronic annotation. Source: UniProtKB-KW defense responseInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 243 | 243 | Endochitinase | PRO_0000285971 | ||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 23 ↔ 85 | By similarity UniProtKB Q9FRV1 | ||||||||||||||||||||||||||||||||||||
| Disulfide bond | 97 ↔ 105 | By similarity UniProtKB Q9FRV1 | ||||||||||||||||||||||||||||||||||||
| Disulfide bond | 223 ↔ 236 | By similarity UniProtKB Q9FRV1 | ||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Turn | 3 – 5 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 8 – 14 | 7 | ||||||||||||||||||||||||||||||||||||
| Turn | 15 – 19 | 5 | ||||||||||||||||||||||||||||||||||||
| Helix | 31 – 39 | 9 | ||||||||||||||||||||||||||||||||||||
| Helix | 50 – 60 | 11 | ||||||||||||||||||||||||||||||||||||
| Helix | 64 – 67 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 101 – 103 | 3 | ||||||||||||||||||||||||||||||||||||
| Turn | 122 – 124 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 140 – 144 | 5 | ||||||||||||||||||||||||||||||||||||
| Helix | 147 – 159 | 13 | ||||||||||||||||||||||||||||||||||||
| Helix | 168 – 172 | 5 | ||||||||||||||||||||||||||||||||||||
| Helix | 180 – 184 | 5 | ||||||||||||||||||||||||||||||||||||
| Helix | 194 – 198 | 5 | ||||||||||||||||||||||||||||||||||||
| Helix | 210 – 215 | 6 | ||||||||||||||||||||||||||||||||||||
| Helix | 219 – 222 | 4 | ||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Structural characterization of two papaya chitinases, a family GH19 of glycosyl hydrolases." Huet J., Wyckmans J., Wintjens R., Boussard P., Raussens V., Vandenbussche G., Ruysschaert J.M., Azarkan M., Looze Y. Cell. Mol. Life Sci. 63:3042-3054(2006) [PubMed: 17115118] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY. Tissue: Latex. |
| + | Additional computationally mapped references. |
Cross-references
3D structure databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P85084. | ||||||||||||
| SMR | P85084. Positions 1-243. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | GH19. Glycoside Hydrolase Family 19. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR016283. Glyco_hydro_19. IPR000726. Glyco_hydro_19_cat. IPR023346. Lysozyme-like_dom. [Graphical view] | ||||||||||||
| Pfam | PF00182. Glyco_hydro_19. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF001060. Endochitinase. 1 hit. | ||||||||||||
| SUPFAM | SSF53955. SSF53955. 1 hit. | ||||||||||||
| PROSITE | PS00773. CHITINASE_19_1. 1 hit. PS00774. CHITINASE_19_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | CHIT_CARPA | ||||||||
| Accession | Primary (citable) accession number: P85084 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase 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