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Protein

Cutinase 2

Gene

AN7541

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle.1 Publication

Catalytic activityi

Cutin + H2O = cutin monomers.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei130By similarity1
Active sitei185By similarity1
Active sitei198By similarity1

GO - Molecular functioni

  • cutinase activity Source: UniProtKB

GO - Biological processi

  • cellular carbohydrate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17223.

Protein family/group databases

ESTHERiemeni-q5avy9. Cutinase.
mycoCLAPiCUT5B_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Cutinase 2 (EC:3.1.1.74)
Alternative name(s):
Cutin hydrolase 2
Gene namesi
ORF Names:AN7541
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome IV
  • UP000005890 Componenti: Partially assembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000039526118 – 255Cutinase 2Add BLAST238

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi40 ↔ 188By similarity
Disulfide bondi119 ↔ 181By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliQ5AVY9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi218 – 251Ser-richAdd BLAST34

Sequence similaritiesi

Belongs to the cutinase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171425.
InParanoidiQ5AVY9.
KOiK08095.
OrthoDBiEOG092C4OIR.

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.

Q5AVY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHFKLLSLAA LAGLSVASPL NLDERQLGSS SGNDLRDGDC KPVTFIFARA
60 70 80 90 100
STEPGLLGMS TGPAVCNDLK ADASLGGVAC QGVGPKYTAG LAENALPQGT
110 120 130 140 150
SSAAINEAKE LFELAASKCP DTRIVAGGYS QGTAVMHGAI PDLSDEIKDK
160 170 180 190 200
IAGVVLFGDT RNKQDGGQIK NFPKDKIKIY CATGDLVCDG TLVVTAAHFT
210 220 230 240 250
YVANTGEASK WLEQQLASMP ASTSTSSSSS SSSSAPASQT SQSSGLSSWF

SGLGN
Length:255
Mass (Da):26,074
Last modified:July 13, 2010 - v2
Checksum:i581932254FF32B8A
GO

Sequence cautioni

The sequence CBF79598 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAA62121 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490511 mRNA. Translation: ABF50887.1.
AACD01000129 Genomic DNA. Translation: EAA62121.1. Sequence problems.
BN001304 Genomic DNA. Translation: CBF79598.1. Sequence problems.
RefSeqiXP_680810.1. XM_675718.1.

Genome annotation databases

EnsemblFungiiCADANIAT00000647; CADANIAP00000647; CADANIAG00000647.
EAA62121; EAA62121; AN7541.2.
GeneIDi2869670.
KEGGiani:AN7541.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490511 mRNA. Translation: ABF50887.1.
AACD01000129 Genomic DNA. Translation: EAA62121.1. Sequence problems.
BN001304 Genomic DNA. Translation: CBF79598.1. Sequence problems.
RefSeqiXP_680810.1. XM_675718.1.

3D structure databases

ProteinModelPortaliQ5AVY9.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiemeni-q5avy9. Cutinase.
mycoCLAPiCUT5B_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00000647; CADANIAP00000647; CADANIAG00000647.
EAA62121; EAA62121; AN7541.2.
GeneIDi2869670.
KEGGiani:AN7541.2.

Phylogenomic databases

HOGENOMiHOG000171425.
InParanoidiQ5AVY9.
KOiK08095.
OrthoDBiEOG092C4OIR.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17223.

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...

Entry informationi

Entry nameiCUTI2_EMENI
AccessioniPrimary (citable) accession number: Q5AVY9
Secondary accession number(s): C8VBM7, Q1HFR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 13, 2010
Last modified: November 30, 2016
This is version 57 of the entry and version 2 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.