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Protein

Cutinase

Gene

CUT1

Organism
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
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. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection.

Catalytic activityi

Cutin + H2O = cutin monomers.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 1381By similarity
Active sitei193 – 1931By similarity
Active sitei206 – 2061By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

ESTHERimaggr-cutas. Cutinase.

Names & Taxonomyi

Protein namesi
Recommended name:
Cutinase (EC:3.1.1.74)
Alternative name(s):
Cutin hydrolase
Gene namesi
Name:CUT1
ORF Names:MGG_01943
OrganismiMagnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Taxonomic identifieri242507 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe
Proteomesi
  • UP000009058 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiFungiDB:MGG_01943.

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 – 228212CutinasePRO_0000006443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 196By similarity
Disulfide bondi127 ↔ 189By similarity
Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP30272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cutinase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP30272.
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.
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.

P30272-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQFITVALTL IALASASPIA TNVEKPSELE ARQLNSVRND LISGNAAACP
60 70 80 90 100
SVILIFARAS GEVGNMGLSA GTNVASALER EFRNDIWVQG VGDPYDAALS
110 120 130 140 150
PNFLPAGTTQ GAIDEAKRMF TLANTKCPNA AVVAGGYSQG TAVMFNAVSE
160 170 180 190 200
MPAAVQDQIK GVVLFGYTKN LQNRGRIPDF PTEKTEVYCN ASDAVCFGTL
210 220
FLLPAHFLYT TESSIAAPNW LIRQIRAA
Length:228
Mass (Da):24,192
Last modified:June 12, 2007 - v3
Checksum:i36BF2F253B8F7709
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771A → R in strain: 4091-5-8.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61500 Genomic DNA. Translation: CAA43717.1.
CM001236 Genomic DNA. Translation: EHA46959.1.
PIRiS20448.
RefSeqiXP_003719326.1. XM_003719278.1.

Genome annotation databases

EnsemblFungiiMGG_01943T0; MGG_01943T0; MGG_01943.
GeneIDi2681158.
KEGGimgr:MGG_01943.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61500 Genomic DNA. Translation: CAA43717.1.
CM001236 Genomic DNA. Translation: EHA46959.1.
PIRiS20448.
RefSeqiXP_003719326.1. XM_003719278.1.

3D structure databases

ProteinModelPortaliP30272.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERimaggr-cutas. Cutinase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiMGG_01943T0; MGG_01943T0; MGG_01943.
GeneIDi2681158.
KEGGimgr:MGG_01943.

Organism-specific databases

EuPathDBiFungiDB:MGG_01943.

Phylogenomic databases

InParanoidiP30272.
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.
PROSITEiPS00155. CUTINASE_1. 1 hit.
PS00931. CUTINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and analysis of CUT1, a cutinase gene from Magnaporthe grisea."
    Sweigard J.A., Chumley F.G., Valent B.
    Mol. Gen. Genet. 232:174-182(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 4091-5-8.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 70-15 / ATCC MYA-4617 / FGSC 8958.

Entry informationi

Entry nameiCUTI_MAGO7
AccessioniPrimary (citable) accession number: P30272
Secondary accession number(s): A4QQQ3, G4NG02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 12, 2007
Last modified: July 6, 2016
This is version 100 of the entry and version 3 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.