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Protein

Cycloviolacin-O14

Gene
N/A
Organism
Viola odorata (Sweet violet)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably participates in a plant defense mechanism. Has hemolytic activity.PROSITE-ProRule annotationCurated1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cytolysis, Hemolysis, Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Cycloviolacin-O14
OrganismiViola odorata (Sweet violet)
Taxonomic identifieri97441 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesViolaceaeViola

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 3131Cycloviolacin-O14PROSITE-ProRule annotation1 PublicationPRO_0000294943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 ↔ 31Cyclopeptide (Gly-Asn)1 Publication
Disulfide bondi6 ↔ 20PROSITE-ProRule annotation1 Publication
Disulfide bondi10 ↔ 22PROSITE-ProRule annotation1 Publication
Disulfide bondi15 ↔ 28PROSITE-ProRule annotation1 Publication

Post-translational modificationi

This is a cyclic peptide.PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
31
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Beta strandi11 – 133Combined sources
Beta strandi20 – 245Combined sources
Beta strandi27 – 304Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GJ0NMR-A1-31[»]
ProteinModelPortaliP85177.
SMRiP85177. Positions 1-31.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP85177.

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.1 Publication

Sequence similaritiesi

Belongs to the cyclotide family. Moebius subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Knottin

Family and domain databases

InterProiIPR005535. Cyclotide.
[Graphical view]
PfamiPF03784. Cyclotide. 1 hit.
[Graphical view]
SUPFAMiSSF57038. SSF57038. 1 hit.
PROSITEiPS51052. CYCLOTIDE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P85177-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
GSIPACGESC FKGKCYTPGC SCSKYPLCAK N
Length:31
Mass (Da):3,204
Last modified:July 10, 2007 - v1
Checksum:i97C33BD73E187CE8
GO

Mass spectrometryi

Molecular mass is 3177.4 Da from positions 1 - 31. Determined by MALDI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GJ0NMR-A1-31[»]
ProteinModelPortaliP85177.
SMRiP85177. Positions 1-31.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP85177.

Family and domain databases

InterProiIPR005535. Cyclotide.
[Graphical view]
PfamiPF03784. Cyclotide. 1 hit.
[Graphical view]
SUPFAMiSSF57038. SSF57038. 1 hit.
PROSITEiPS51052. CYCLOTIDE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability."
    Ireland D.C., Colgrave M.L., Craik D.J.
    Biochem. J. 400:1-12(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, STRUCTURE BY NMR, DISULFIDE BONDS.

Entry informationi

Entry nameiCYO14_VIOOD
AccessioniPrimary (citable) accession number: P85177
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: December 9, 2015
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

This peptide is cyclic. The start position was chosen by similarity to OAK1 (kalata-B1) for which the DNA sequence is known.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.