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Protein

Antimicrobial peptide Ar-AMP

Gene
N/A
Organism
Amaranthus retroflexus (Redroot amaranth) (Redroot pigweed)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Chitin-binding protein that inhibits the growth of the fungal pathogens B.cinerea, F.culmorum, H.sativum and A.consortiale, but not that of R.solani. Induces morphological changes in the fungal pathogens F.culmorum, H.sativum and R.solani, but not in A.consortiale and B.cinerea. Has antibacterial activity against the Gram-positive bacterium B.subtilis, but lacks antibacterial activity against the Gram-negative bacterium E.coli.1 Publication

GO - Molecular functioni

  • chitin binding Source: UniProtKB

GO - Biological processi

  • defense response to fungus Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • killing of cells of other organism Source: UniProtKB-KW
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 Ar-AMP
OrganismiAmaranthus retroflexus (Redroot amaranth) (Redroot pigweed)
Taxonomic identifieri124763 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeAmaranthus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
PeptideiPRO_000025798126 – 55Antimicrobial peptide Ar-AMPAdd BLAST30
PropeptideiPRO_000025798256 – 89Removed in mature form1 PublicationAdd BLAST34

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi29 ↔ 40PROSITE-ProRule annotationBy similarity
Disulfide bondi34 ↔ 46PROSITE-ProRule annotationBy similarity
Disulfide bondi39 ↔ 53PROSITE-ProRule annotationBy similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliQ5I2B2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 68Chitin-binding type-1PROSITE-ProRule annotationAdd BLAST43

Sequence similaritiesi

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

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR013006. Antimicrobial_C6_CS.
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[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.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS60011. PLANT_C6_AMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5I2B2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNMKSVALI VIVMMAFMMV DPSMGAGECV QGRCPSGMCC SQFGYCGRGP
60 70 80
KYCGRASTTV DHQADAAAAA ATKTANNPTD AKLAGAGSP
Length:89
Mass (Da):9,039
Last modified:February 15, 2005 - v1
Checksum:iB74BF22FE38E0488
GO

Mass spectrometryi

Molecular mass is 3153.6 Da from positions 26 - 55. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY861660 mRNA. Translation: AAW56634.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY861660 mRNA. Translation: AAW56634.1.

3D structure databases

ProteinModelPortaliQ5I2B2.
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.
InterProiIPR013006. Antimicrobial_C6_CS.
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[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.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS60011. PLANT_C6_AMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMP_AMARE
AccessioniPrimary (citable) accession number: Q5I2B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 15, 2005
Last modified: October 5, 2016
This is version 41 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

Direct protein sequencing

Documents

  1. 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.