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Q4X1N0 (CUTI1_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable cutinase 1

EC=3.1.1.74
Alternative name(s):
Cutin hydrolase 1
Gene names
ORF Names:AFUA_2G09380
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Seems, in this nonpathogenic fungi, to play an important role in flavor formation By similarity.

Catalytic activity

Cutin + H2O = cutin monomers.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the cutinase family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncutinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 211193Probable cutinase 1
PRO_0000233109

Sites

Active site1251 By similarity
Active site1801 By similarity
Active site1931 By similarity

Amino acid modifications

Disulfide bond36 ↔ 183 By similarity
Disulfide bond114 ↔ 176 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4X1N0 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 43B8A1C7C8956014

FASTA21121,856
        10         20         30         40         50         60 
MKFALLSLAA MAVASPVAID VRQTAITGDE LRTGPCEPIT FIFARGSTEP GLLGITTGPG 

        70         80         90        100        110        120 
VCNALKLSRP GQVACQGVGP AYIADLASNF LPQGTSQVAI DEAAGLFKLA ASKCPDTKIV 

       130        140        150        160        170        180 
AGGYSQGAAV MHGAIRNLPS NVQNMIKGVV LFGDTRNKQD GGRIPNFPTD RTKIYCAFGD 

       190        200        210 
LVCDGTLIIT PAHLSYGDDV PSATSFLLSK V 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000001 Genomic DNA. Translation: EAL93235.1.
RefSeqXP_755273.1. XM_750180.1.

3D structure databases

ProteinModelPortalQ4X1N0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00004868; CADAFUAP00004868; CADAFUAG00004868.
GeneID3513265.
KEGGafm:AFUA_2G09380.

Phylogenomic databases

eggNOGNOG239470.
HOGENOMHOG000171425.
KOK08095.
OMACEPITFI.
OrthoDBEOG779P8P.

Family and domain databases

InterProIPR000675. Cutinase.
IPR011150. Cutinase_monf.
[Graphical view]
PfamPF01083. Cutinase. 1 hit.
[Graphical view]
PRINTSPR00129. CUTINASE.
PROSITEPS00155. CUTINASE_1. 1 hit.
PS00931. CUTINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCUTI1_ASPFU
AccessionPrimary (citable) accession number: Q4X1N0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 5, 2005
Last modified: January 22, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families