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Protein

Probable cutinase 1

Gene

AFLA_039350

Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle.By similarity

Catalytic activityi

Cutin + H2O = cutin monomers.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei135 – 1351By similarity
Active sitei190 – 1901By similarity
Active sitei203 – 2031By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

ESTHERiaspor-q2u199. Cutinase.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable cutinase 1 (EC:3.1.1.74)
Alternative name(s):
Cutin hydrolase 1
Gene namesi
ORF Names:AFLA_039350
OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic identifieri332952 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000001875 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AFLA_039350.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 224206Probable cutinase 1PRO_0000395249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 193By similarity
Disulfide bondi124 ↔ 186By similarity

Keywords - PTMi

Disulfide bond

Family & Domainsi

Sequence similaritiesi

Belongs to the cutinase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171425.
KOiK08095.
OMAiFGFTRNV.
OrthoDBiEOG779P8P.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000675. Cutinase/axe.
IPR011150. Cutinase_monf.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
PRINTSiPR00129. CUTINASE.
SMARTiSM01110. Cutinase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00155. CUTINASE_1. 1 hit.
PS00931. CUTINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

B8NCM8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVMLRSLLVS ALAALAAASP IAEPADQSLE ARQLGSSNDL TNGACKDVTL
60 70 80 90 100
IFARGSTEMG NMGTVIGPPL CSALKSKLGA DKVACQGVGG LYTGGLMQNA
110 120 130 140 150
LPQNTDPGAI STAKSLFEQA STKCPNTQIV AGGYSQGSAV IDNAVQQLSA
160 170 180 190 200
EVKDKVKGVV FFGFTRNLQD KGQIPNYPKD NVKVFCAMGD LVCDGTLIVT
210 220
AAHLTYTINA PEAASFLASK VQSA
Length:224
Mass (Da):23,073
Last modified:March 3, 2009 - v1
Checksum:i662B8FC13B10CF76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963476 Genomic DNA. Translation: EED52233.1.
RefSeqiXP_002377397.1. XM_002377356.1.

Genome annotation databases

EnsemblFungiiCADAFLAT00005262; CADAFLAP00005262; CADAFLAG00005262.
GeneIDi7911427.
KEGGiafv:AFLA_039350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963476 Genomic DNA. Translation: EED52233.1.
RefSeqiXP_002377397.1. XM_002377356.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiaspor-q2u199. Cutinase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFLAT00005262; CADAFLAP00005262; CADAFLAG00005262.
GeneIDi7911427.
KEGGiafv:AFLA_039350.

Organism-specific databases

EuPathDBiFungiDB:AFLA_039350.

Phylogenomic databases

HOGENOMiHOG000171425.
KOiK08095.
OMAiFGFTRNV.
OrthoDBiEOG779P8P.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000675. Cutinase/axe.
IPR011150. Cutinase_monf.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
PRINTSiPR00129. CUTINASE.
SMARTiSM01110. Cutinase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00155. CUTINASE_1. 1 hit.
PS00931. CUTINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes aflatoxin contamination of food and feed."
    Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E., Bhatnagar D., Bennett J.W., Dean R., Payne G.A.
    Genome Announc. 3:E0016815-E0016815(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167.

Entry informationi

Entry nameiCUTI3_ASPFN
AccessioniPrimary (citable) accession number: B8NCM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: March 3, 2009
Last modified: May 11, 2016
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.