B1NRR0 · CYVJ_VIOBI
- ProteinCyclotide vibi-J
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids105 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Probably participates in a plant defense mechanism.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Biological Process | defense response |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameCyclotide vibi-J
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Malpighiales > Violaceae > Viola > Viola subgen. Viola > Viola sect. Chamaemelanium
Accessions
- Primary accessionB1NRR0
PTM/Processing
Features
Showing features for signal, propeptide, peptide, cross-link, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-9 | |||||
Sequence: AAFALPALA | ||||||
Propeptide | PRO_0000341434 | 10-71 | ||||
Sequence: TSFEKDFITHETVQEILKKVGSNSNGMLDEQTISALTGKTIISNPLLEEALFKSSNSINALG | ||||||
Peptide | PRO_0000341435 | 72-102 | Cyclotide vibi-J | |||
Sequence: GTFPCGESCVWIPCISKVIGCACKSKVCYKN | ||||||
Cross-link | 72↔102 | Cyclopeptide (Gly-Asn) | ||||
Sequence: GTFPCGESCVWIPCISKVIGCACKSKVCYKN | ||||||
Disulfide bond | 76↔92 | |||||
Sequence: CGESCVWIPCISKVIGC | ||||||
Disulfide bond | 80↔94 | |||||
Sequence: CVWIPCISKVIGCAC | ||||||
Disulfide bond | 85↔99 | |||||
Sequence: CISKVIGCACKSKVC | ||||||
Propeptide | PRO_0000341436 | 103-105 | ||||
Sequence: SLA |
Post-translational modification
This is a cyclic peptide.
Keywords
- PTM
Structure
3D structure databases
Family & Domains
Domain
The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Sequence similarities
Belongs to the cyclotide family. Bracelet subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length105
- Mass (Da)11,116
- Last updated2008-04-29 v1
- Checksum3F629FD0F669CFC1
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: A |