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CAZyme Information: EEP79002.1

You are here: Home > Sequence: EEP79002.1

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 Uncinocarpus reesii
Lineage Ascomycota; Eurotiomycetes; ; Onygenaceae; Uncinocarpus; Uncinocarpus reesii
CAZyme ID EEP79002.1
CAZy Family GH43
CAZyme Description GH18 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:C4JLZ0]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1014 112886.13 7.1316
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ureesii1704 7856 336963 96 7760
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.96:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 18 236 1.2e-17 0.6554054054054054

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119363 GH18_CTS3_chitinase 9.07e-149 18 275 1 256
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen Coccidioides posadasii. CTS3 has a chitinase-like glycosyl hydrolase family 18 (GH18) domain; and has homologs in bacteria as well as fungi.
401396 PhoD 3.27e-49 636 923 22 337
PhoD-like phosphatase.
277335 MPP_PhoD 4.07e-40 598 886 1 242
Bacillus subtilis PhoD and related proteins, metallophosphatase domain. PhoD (also known as alkaline phosphatase D/APaseD in Bacillus subtilis) is a secreted phosphodiesterase encoded by phoD of the Pho regulon in Bacillus subtilis. PhoD homologs are found in prokaryotes, eukaryotes, and archaea. PhoD contains a twin arginine (RR) motif and is transported by the Tat (Twin-arginine translocation) translocation pathway machinery (TatAyCy). This family also includes the Fusarium oxysporum Fso1 protein. PhoD belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
226070 PhoD 2.06e-21 553 852 96 420
Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism].
119349 GH18_chitinase-like 1.31e-20 19 205 1 177
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 18 978 12 905
0.0 18 978 12 905
0.0 38 983 2 938
1.41e-312 18 995 47 924
4.50e-174 1 307 1 306

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.14e-120 1 296 3 290
Structure of chitinase, ChiC, from Aspergillus fumigatus. [Aspergillus fumigatus Af293],2Y8V_B Structure of chitinase, ChiC, from Aspergillus fumigatus. [Aspergillus fumigatus Af293],2Y8V_C Structure of chitinase, ChiC, from Aspergillus fumigatus. [Aspergillus fumigatus Af293],2Y8V_D Structure of chitinase, ChiC, from Aspergillus fumigatus. [Aspergillus fumigatus Af293]
2.31e-74 17 294 3 279
Chain X, ENDO-N-ACETYL-BETA-D-GLUCOSAMINIDASE [Trichoderma reesei]
4.14e-11 526 848 44 382
Structure of PhoD [Bacillus subtilis],2YEQ_B Structure of PhoD [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.40e-11 20 280 31 302
Chitinase 2 OS=Rhizopus oligosporus OX=4847 GN=CHI2 PE=1 SV=1
9.54e-11 20 271 31 293
Chitinase 1 OS=Rhizopus oligosporus OX=4847 GN=CHI1 PE=1 SV=1
2.36e-10 526 848 100 438
Alkaline phosphatase D OS=Bacillus subtilis (strain 168) OX=224308 GN=phoD PE=1 SV=3
4.20e-06 81 271 99 290
Chitinase 1 OS=Rhizopus niveus OX=4844 GN=CHI1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999609 0.000445

TMHMM  Annotations      help

There is no transmembrane helices in EEP79002.1.