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Protein

Antimicrobial peptide 1b

Gene
N/A
Organism
Triticum kiharae (Wheat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds chitin. WAMP-1a has antifungal activity against the fungi F.solani (IC50=5 µg/ml), F.verticillioides (IC50=30 µg/ml), F.oxysporum (IC50=5 µg/ml), B.sorokiniana (IC50=5 µg/ml), B.cinerea (IC50=20 µg/ml) and N.crassa (IC50=10 µg/ml). Inhibits hyphal elongation and causes browning of hyphae in F.oxysporum. Causes destruction and discoloration of spores in B.sorokiniana. Inhibits the development of disease caused by the fungus P.infestans on potato tubers. Has antibacterial activity against the Gram-negative bacteria P.syringae and E.carotovora, and the Gram-positive bacterium C.michiganensis.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Fungicide

Keywords - Biological processi

Plant defense

Keywords - Ligandi

Chitin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Antimicrobial peptide 1b1 Publication
Short name:
WAMP-1b1 Publication
Alternative name(s):
Antimicrobial peptide H11 Publication
Short name:
Tk-AMP-H11 Publication
Cleaved into the following chain:
Antimicrobial peptide 1a1 Publication
Short name:
WAMP-1a1 Publication
OrganismiTriticum kiharae (Wheat)
Taxonomic identifieri376535 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeTriticinaeTriticum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 4545Antimicrobial peptide 1b1 PublicationPRO_0000388709Add
BLAST
Peptidei1 – 4444Antimicrobial peptide 1a1 PublicationPRO_0000388710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 19PROSITE-ProRule annotationBy similarity
Disulfide bondi13 ↔ 25PROSITE-ProRule annotationBy similarity
Disulfide bondi16 ↔ 44PROSITE-ProRule annotationBy similarity
Disulfide bondi18 ↔ 32PROSITE-ProRule annotationBy similarity
Disulfide bondi37 ↔ 41PROSITE-ProRule annotationBy similarity

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
45
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources
Beta strandi18 – 203Combined sources
Turni21 – 233Combined sources
Beta strandi24 – 263Combined sources
Helixi29 – 324Combined sources
Beta strandi36 – 394Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LB7NMR-A1-44[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4343Chitin-binding type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 1 hit.
PROSITEiPS50941. CHIT_BIND_I_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P85966-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
AQRCGDQARG AKCPNCLCCG KYGFCGSGDA YCGAGSCQSQ CRGCR
Length:45
Mass (Da):4,601
Last modified:November 3, 2009 - v1
Checksum:iA3D66D4DC97429E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161C → N AA sequence (PubMed:16269343).Curated

Mass spectrometryi

Molecular mass is 4588.1 Da from positions 1 - 45. Determined by MALDI. 2 Publications
Molecular mass is 4431.9 Da from positions 1 - 44. Determined by MALDI. 2 Publications
Molecular mass is 4590 Da from positions 1 - 45. Determined by MALDI. 2 Publications
Molecular mass is 4434 Da from positions 1 - 44. Determined by MALDI. 2 Publications

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LB7NMR-A1-44[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 1 hit.
PROSITEiPS50941. CHIT_BIND_I_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY.
    Tissue: Seed1 Publication.
  2. Cited for: PROTEIN SEQUENCE OF 1-33, MASS SPECTROMETRY.
    Tissue: Seed1 Publication.

Entry informationi

Entry nameiAMP_TRIKH
AccessioniPrimary (citable) accession number: P85966
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: November 3, 2009
Last modified: February 17, 2016
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.