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CAZyme Information: OJD15484.1

You are here: Home > Sequence: OJD15484.1

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 Emergomyces pasteurianus
Lineage Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Emergomyces; Emergomyces pasteurianus
CAZyme ID OJD15484.1
CAZy Family GH47
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A1J9QHT6]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1017 113993.88 9.0143
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EpasteurianusEp9510 9078 1447872 128 8950
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 13 261 5.1e-20 0.7027027027027027

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119363 GH18_CTS3_chitinase 3.94e-141 14 271 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 2.61e-47 639 922 24 335
PhoD-like phosphatase.
277335 MPP_PhoD 4.48e-38 599 886 1 241
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 1.39e-25 554 853 96 420
Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism].
119349 GH18_chitinase-like 9.38e-18 15 201 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 1 987 1 912
0.0 1 987 1 912
0.0 33 969 1 924
2.44e-298 1 984 36 910
3.66e-161 1 286 1 286

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.14e-118 1 292 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]
7.27e-79 13 283 3 272
Chain X, ENDO-N-ACETYL-BETA-D-GLUCOSAMINIDASE [Trichoderma reesei]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.01e-09 77 271 101 297
Chitinase 2 OS=Rhizopus oligosporus OX=4847 GN=CHI2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000036 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
361 383
388 410