Species | Trichophyton mentagrophytes | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton mentagrophytes | |||||||||||
CAZyme ID | GBF66566.1 | |||||||||||
CAZy Family | GT41 | |||||||||||
CAZyme Description | endochitinase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.14:3 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH18 | 30 | 306 | 1.5e-26 | 0.9256756756756757 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
119356 | GH18_hevamine_XipI_class_III | 7.07e-105 | 30 | 325 | 1 | 280 | This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. |
395573 | Glyco_hydro_18 | 1.50e-21 | 31 | 306 | 1 | 304 | Glycosyl hydrolases family 18. |
119349 | GH18_chitinase-like | 8.64e-11 | 54 | 216 | 24 | 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. |
411773 | SP4_N | 0.009 | 479 | 551 | 279 | 351 | N-terminal domain of transcription factor Specificity Protein (SP) 4. Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
3.04e-106 | 4 | 345 | 3 | 352 | |
3.04e-106 | 4 | 345 | 3 | 352 | |
1.41e-98 | 1 | 341 | 1 | 353 | |
8.56e-98 | 1 | 341 | 1 | 353 | |
1.49e-94 | 14 | 345 | 13 | 353 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.32e-96 | 30 | 328 | 1 | 308 | A. fumigatus chitinase A1 phenyl-methylguanylurea complex [Aspergillus fumigatus],2XVN_B A. fumigatus chitinase A1 phenyl-methylguanylurea complex [Aspergillus fumigatus],2XVN_C A. fumigatus chitinase A1 phenyl-methylguanylurea complex [Aspergillus fumigatus] |
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2.40e-96 | 30 | 328 | 2 | 309 | AfChiA1 in complex with compound 1 [Aspergillus fumigatus A1163],4TX6_B AfChiA1 in complex with compound 1 [Aspergillus fumigatus A1163] |
|
2.40e-96 | 30 | 328 | 2 | 309 | ChiA1 from Aspergillus fumigatus in complex with acetazolamide [Aspergillus fumigatus A1163],2XTK_B ChiA1 from Aspergillus fumigatus in complex with acetazolamide [Aspergillus fumigatus A1163],2XUC_A Natural product-guided discovery of a fungal chitinase inhibitor [Aspergillus fumigatus],2XUC_B Natural product-guided discovery of a fungal chitinase inhibitor [Aspergillus fumigatus],2XUC_C Natural product-guided discovery of a fungal chitinase inhibitor [Aspergillus fumigatus],2XVP_A ChiA1 from Aspergillus fumigatus, apostructure [Aspergillus fumigatus A1163],2XVP_B ChiA1 from Aspergillus fumigatus, apostructure [Aspergillus fumigatus A1163] |
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1.71e-46 | 28 | 327 | 4 | 287 | ScCTS1_apo crystal structure [Saccharomyces cerevisiae],2UY3_A ScCTS1_8-chlorotheophylline crystal structure [Saccharomyces cerevisiae],2UY4_A ScCTS1_acetazolamide crystal structure [Saccharomyces cerevisiae],2UY5_A ScCTS1_kinetin crystal structure [Saccharomyces cerevisiae],4TXE_A ScCTS1 in complex with compound 5 [Saccharomyces cerevisiae] |
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7.51e-38 | 32 | 324 | 3 | 268 | cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity [Parkia platycephala] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 1 | 720 | 1 | 740 | Probable endochitinase ARB_07371 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07371 PE=3 SV=1 |
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2.16e-107 | 1 | 344 | 1 | 355 | Endochitinase 2 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS2 PE=3 SV=2 |
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4.84e-107 | 4 | 345 | 3 | 352 | Endochitinase 2 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS2 PE=3 SV=2 |
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2.64e-95 | 14 | 345 | 13 | 353 | Endochitinase A1 OS=Neosartorya fumigata OX=746128 GN=chiA1 PE=1 SV=1 |
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4.79e-94 | 14 | 345 | 13 | 353 | Endochitinase A1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiA1 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000254 | 0.999763 | CS pos: 23-24. Pr: 0.9780 |
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