Species | Cenococcum geophilum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Dothideomycetes; ; Gloniaceae; Cenococcum; Cenococcum geophilum | |||||||||||
CAZyme ID | K441DRAFT_672063-t45_1-p1 | |||||||||||
CAZy Family | PL42 | |||||||||||
CAZyme Description | glycoside hydrolase family 18 protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
EC | 3.2.1.96:2 |
---|
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
119363 | GH18_CTS3_chitinase | 5.83e-79 | 1 | 206 | 78 | 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. |
270494 | UBA_scDdi1_like | 3.56e-10 | 282 | 315 | 3 | 36 | UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar proteins. Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also called transporter regulator RS1 (RS1) which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. |
270569 | UBA2_UBP5 | 1.06e-07 | 282 | 317 | 5 | 40 | UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5). UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain. |
119349 | GH18_chitinase-like | 1.46e-06 | 1 | 205 | 70 | 209 | 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. |
270495 | UBA_cnDdi1_like | 3.14e-05 | 283 | 312 | 1 | 30 | UBA domain found in Cryptococcus neoformans DNA-damage response protein Ddi1 and similar proteins. The family includes some uncharacterized Ddi and similar proteins which show a high level of sequence similarity with yeast Ddi1. Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in yeast. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.67e-121 | 1 | 316 | 93 | 408 | |
4.72e-115 | 1 | 316 | 93 | 411 | |
1.66e-112 | 1 | 317 | 450 | 769 | |
6.02e-78 | 1 | 316 | 91 | 357 | |
6.39e-78 | 1 | 316 | 92 | 359 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.71e-47 | 1 | 210 | 91 | 273 | 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] |
|
2.30e-36 | 1 | 206 | 81 | 260 | Chain X, ENDO-N-ACETYL-BETA-D-GLUCOSAMINIDASE [Trichoderma reesei] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000030 | 0.000003 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.