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Protein

Cutinase 3

Gene

AN7180

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei133 – 1331By similarity
Active sitei188 – 1881By similarity
Active sitei201 – 2011By similarity

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

Protein family/group databases

ESTHERiemeni-CUTI3. Cutinase.
mycoCLAPiCUT5C_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Cutinase 3 (EC:3.1.1.74)
Alternative name(s):
Cutin hydrolase 3
Gene namesi
ORF Names:AN7180
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

Organism-specific databases

EuPathDBiFungiDB:AN7180.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 221204Cutinase 3PRO_0000395262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 191By similarity
Disulfide bondi122 ↔ 184By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliQ5AX00.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cutinase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171425.
InParanoidiQ5AX00.
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.

Q5AX00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFHTILLAA LASLVIATPL PSDTDVSLER RQSMNSNDLE KGDCKSVAFI
60 70 80 90 100
FARGSTEIGN MGFVVGPGVC SNLKSTLGSD KVACQGVGGA YTAGLIQNAL
110 120 130 140 150
PANTDSGSIK EAVKMFDLAA KCPDTQIVAG GYSQGSAVID NAIQKLDDST
160 170 180 190 200
RDRVKGVVLF GFTRNLQDKG QIPGYPKDQT KVYCAVGDLV CSGTLIITAS
210 220
HMTYGLNAGD AAKFLASQVS V
Length:221
Mass (Da):23,074
Last modified:April 26, 2005 - v1
Checksum:i851820532CD96475
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490506 mRNA. Translation: ABF50882.1.
AACD01000122 Genomic DNA. Translation: EAA61432.1.
BN001304 Genomic DNA. Translation: CBF78915.1.
RefSeqiXP_664784.1. XM_659692.1.

Genome annotation databases

EnsemblFungiiCADANIAT00000274; CADANIAP00000274; CADANIAG00000274.
EAA61432; EAA61432; AN7180.2.
GeneIDi2869828.
KEGGiani:AN7180.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490506 mRNA. Translation: ABF50882.1.
AACD01000122 Genomic DNA. Translation: EAA61432.1.
BN001304 Genomic DNA. Translation: CBF78915.1.
RefSeqiXP_664784.1. XM_659692.1.

3D structure databases

ProteinModelPortaliQ5AX00.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiemeni-CUTI3. Cutinase.
mycoCLAPiCUT5C_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00000274; CADANIAP00000274; CADANIAG00000274.
EAA61432; EAA61432; AN7180.2.
GeneIDi2869828.
KEGGiani:AN7180.2.

Organism-specific databases

EuPathDBiFungiDB:AN7180.

Phylogenomic databases

HOGENOMiHOG000171425.
InParanoidiQ5AX00.
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

« Hide 'large scale' publications
  1. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiCUTI3_EMENI
AccessioniPrimary (citable) accession number: Q5AX00
Secondary accession number(s): C8VD42, Q1HFR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: April 26, 2005
Last modified: May 11, 2016
This is version 60 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.