Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Antifungal peptide 1

Gene
N/A
Organism
Eucommia ulmoides (Hardy rubber tree)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Has antifungal activity against P.infestans, A.lycopersici, V.dahliae, G.zeae, A.nicotianae, F.moniliforme, F.oxysporum and C.gossypii.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntimicrobial, Fungicide
Biological processPlant defense
LigandChitin-binding

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Antifungal peptide 1
Alternative name(s):
EAFP1
OrganismiEucommia ulmoides (Hardy rubber tree)
Taxonomic identifieri4392 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGarryalesEucommiaceaeEucommia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001248161 – 41Antifungal peptide 1Add BLAST41

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi3 ↔ 17PROSITE-ProRule annotation
Disulfide bondi7 ↔ 37PROSITE-ProRule annotation
Disulfide bondi11 ↔ 23PROSITE-ProRule annotation
Disulfide bondi16 ↔ 30PROSITE-ProRule annotation
Disulfide bondi35 ↔ 39PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP83596.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 41Chitin-binding type-1PROSITE-ProRule annotationAdd BLAST38

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiView protein in InterPro
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
PRINTSiPR00451. CHITINBINDNG.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000609. Chitin_bd_1. 1 hit.
SMARTiView protein in SMART
SM00270. ChtBD1. 1 hit.
SUPFAMiSSF57016. SSF57016. 1 hit.
PROSITEiView protein in PROSITE
PS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P83596-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
QTCASRCPRP CNAGLCCSIY GYCGSGNAYC GAGNCRCQCR G
Length:41
Mass (Da):4,229
Last modified:June 27, 2003 - v1
Checksum:i8F775334FAABAAB4
GO

Mass spectrometryi

Molecular mass is 4201.43 Da from positions 1 - 41. Determined by MALDI. 1 Publication

Cross-referencesi

3D structure databases

ProteinModelPortaliP83596.
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.
InterProiView protein in InterPro
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
PRINTSiPR00451. CHITINBINDNG.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000609. Chitin_bd_1. 1 hit.
SMARTiView protein in SMART
SM00270. ChtBD1. 1 hit.
SUPFAMiSSF57016. SSF57016. 1 hit.
PROSITEiView protein in PROSITE
PS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEAP1_EUCUL
AccessioniPrimary (citable) accession number: P83596
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 27, 2003
Last modified: February 15, 2017
This is version 56 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.