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Protein

Probable cutinase 2

Gene

An11g00110

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei126 – 1261PROSITE-ProRule annotation
Active sitei181 – 1811PROSITE-ProRule annotation
Active sitei194 – 1941PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

ESTHERiaspnc-cuti2. Cutinase.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable cutinase 2 (EC:3.1.1.74)
Alternative name(s):
Cutin hydrolase 2
Gene namesi
ORF Names:An11g00110
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006706 Componenti: Chromosome 7R

Organism-specific databases

EuPathDBiFungiDB:An11g00110.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 271255Probable cutinase 2PRO_5000242393Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi37 ↔ 184By similarity
Disulfide bondi115 ↔ 177By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliA5ABE6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi210 – 26960Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the cutinase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171425.
KOiK08095.
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.
PROSITEiPS00931. CUTINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A5ABE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLPYFLLGL AGLAAASPMG LAERQLSDGN ELRDGSCKPI IFIFARASTE
60 70 80 90 100
PGLLGISTGP AVCNDLKMAK AGQVLCQGVG PAYTADLMSN ALPDNTSPAA
110 120 130 140 150
ISESESLFKL AASKCPNSQI LAGGYSQGTA VMDDSIKQLP DDVKDKIKGV
160 170 180 190 200
VLFGYTRNAQ EGGQIGNFPK DKVKIYCAMG DLVCDGTLIV TAAHFTYVMN
210 220 230 240 250
TGEASQWLES KLSDTTTSSL TGSSSSDTSS STSTGDSSSE SSSAAGLGGL
260 270
SGLTGLGSST SGGFPSLASL F
Length:271
Mass (Da):27,628
Last modified:June 12, 2007 - v1
Checksum:i90A73A60C15B1E5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270218 Genomic DNA. Translation: CAK48244.1.
RefSeqiXP_001394015.1. XM_001393978.1.

Genome annotation databases

EnsemblFungiiCADANGAT00008344; CADANGAP00008197; CADANGAG00008344.
GeneIDi4984242.
KEGGiang:ANI_1_1504094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270218 Genomic DNA. Translation: CAK48244.1.
RefSeqiXP_001394015.1. XM_001393978.1.

3D structure databases

ProteinModelPortaliA5ABE6.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiaspnc-cuti2. Cutinase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANGAT00008344; CADANGAP00008197; CADANGAG00008344.
GeneIDi4984242.
KEGGiang:ANI_1_1504094.

Organism-specific databases

EuPathDBiFungiDB:An11g00110.

Phylogenomic databases

HOGENOMiHOG000171425.
KOiK08095.
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.
PROSITEiPS00931. CUTINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiCUTI2_ASPNC
AccessioniPrimary (citable) accession number: A5ABE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: June 12, 2007
Last modified: July 6, 2016
This is version 43 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.