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Protein

Cutinase

Gene

tglA

Organism
Aspergillus oryzae (Yellow koji mold)
Status
Unreviewed-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.UniRule annotation

Catalytic activityi

Cutin + H2O = cutin monomers.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esteraseUniRule annotation

Protein family/group databases

ESTHERiaspor-TGLA. Cutinase.

Names & Taxonomyi

Protein namesi
Recommended name:
CutinaseUniRule annotation (EC:3.1.1.74UniRule annotation)
Gene namesi
Name:tglAImported
OrganismiAspergillus oryzae (Yellow koji mold)Imported
Taxonomic identifieri5062 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

  • Secreted UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

SecretedUniRule annotation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919UniRule annotationAdd
BLAST
Chaini20 – 254235CutinaseUniRule annotationPRO_5005144949Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00001982.

Structurei

3D structure databases

ProteinModelPortaliQ9P960.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 253173CutinaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cutinase family.UniRule annotation

Keywords - Domaini

SignalUniRule annotation

Phylogenomic databases

eggNOGiENOG410IZ4T. Eukaryota.
ENOG41122XJ. LUCA.
HOGENOMiHOG000088892.

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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLAIKSLFV SLLGASVLAS PLPSNALVER NAPLNEFLSA LLSHLPAIDG
60 70 80 90 100
TIDAVSGVIT DFDQLLADLT GARTTQNGYI GVCTDYTVLF ARGTSEPGNV
110 120 130 140 150
GVLVGPPLSE AFEQAVGAKA LSFQGVNGYN ADVAGYLAGG DAAGSKSMAS
160 170 180 190 200
LASEVLSKCP DTKLVMSGYS QGCQIVHNAV EQLPAADASK ISSVLLFGDP
210 220 230 240 250
YAGKAFPNVD ASRVHTVCHA GDTICNNSVV ILPPHLTYAV DVTNAVQFAV

AAAN
Length:254
Mass (Da):26,020
Last modified:October 1, 2000 - v1
Checksum:i44273AFF3EC6C387
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB039325 Genomic DNA. Translation: BAA92327.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB039325 Genomic DNA. Translation: BAA92327.1.

3D structure databases

ProteinModelPortaliQ9P960.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5062.CADAORAP00001982.

Protein family/group databases

ESTHERiaspor-TGLA. Cutinase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IZ4T. Eukaryota.
ENOG41122XJ. LUCA.
HOGENOMiHOG000088892.

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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of the triacylglycerol lipase gene of Aspergillus oryzae and its expression in Escherichia coli."
    Toida J., Fukuzawa M., Kobayashi G., Ito K., Sekiguchi J.
    FEMS Microbiol. Lett. 189:159-164(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: RIB128Imported.

Entry informationi

Entry nameiQ9P960_ASPOZ
AccessioniPrimary (citable) accession number: Q9P960
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.