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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

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

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)DescriptionActionsGraphical viewLength
PeptideiPRO_00003887091 – 45Antimicrobial peptide 1b1 PublicationAdd BLAST45
PeptideiPRO_00003887101 – 44Antimicrobial peptide 1a1 PublicationAdd BLAST44

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

145
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 8Combined sources4
Beta strandi18 – 20Combined sources3
Turni21 – 23Combined sources3
Beta strandi24 – 26Combined sources3
Helixi29 – 32Combined sources4
Beta strandi36 – 39Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LB7NMR-A1-44[»]
SMRiP85966.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 43Chitin-binding type-1PROSITE-ProRule annotationAdd BLAST43

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)DescriptionActionsGraphical viewLength
Sequence conflicti16C → N AA sequence (PubMed:16269343).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LB7NMR-A1-44[»]
SMRiP85966.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

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...

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: November 2, 2016
This is version 23 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.