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CAZyme Information: FPRO_15501-t41_1-p1

You are here: Home > Sequence: FPRO_15501-t41_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Fusarium proliferatum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
CAZyme ID FPRO_15501-t41_1-p1
CAZy Family GT34
CAZyme Description uncharacterized protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
181 19172.18 9.7655
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FproliferatumET1 16509 1227346 366 16143
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in FPRO_15501-t41_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE5 68 180 3.9e-21 0.6243386243386243

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395860 Cutinase 1.43e-24 68 180 1 110
Cutinase.
238382 Lipase 0.006 138 162 17 41
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
9.35e-118 1 181 1 181
9.35e-118 1 181 1 181
9.35e-118 1 181 1 181
5.79e-69 1 180 1 183
2.46e-44 1 180 1 187

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.20e-15 64 180 74 187
Structure of cutinase from Trichoderma reesei in its native form. [Trichoderma reesei QM6a],4PSD_A Structure of Trichoderma reesei cutinase native form. [Trichoderma reesei QM6a],4PSE_A Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor [Trichoderma reesei QM6a],4PSE_B Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor [Trichoderma reesei QM6a]
1.41e-11 61 178 14 131
Crystal structure of Aspergillus oryzae cutinase [Aspergillus oryzae]
6.23e-11 61 178 5 122
Structure of Aspergillus oryzae cutinase expressed in Pichia pastoris, crystallized in the presence of Paraoxon [Aspergillus oryzae]
8.55e-10 59 179 19 142
Chain A, CUTINASE [Fusarium vanettenii]
2.46e-08 61 164 16 119
Chain A, cutinase [Malbranchea cinnamomea]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.29e-21 59 181 31 152
Cutinase CUT2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=CUT2 PE=1 SV=1
2.01e-21 7 180 11 177
Cutinase OS=Blumeria hordei OX=2867405 GN=CUT1 PE=3 SV=1
3.37e-18 69 178 31 138
Cutinase OS=Botryotinia fuckeliana OX=40559 GN=cutA PE=1 SV=1
3.85e-16 59 171 50 158
Cutinase 4 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=cut4 PE=2 SV=1
9.95e-16 69 180 31 139
Cutinase OS=Monilinia fructicola OX=38448 GN=CUT1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000287 0.999715 CS pos: 16-17. Pr: 0.9235

TMHMM  Annotations      help

There is no transmembrane helices in FPRO_15501-t41_1-p1.