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CAZyme Information: ASPTUDRAFT_191924-t33_1-p1

You are here: Home > Sequence: ASPTUDRAFT_191924-t33_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 Aspergillus tubingensis
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tubingensis
CAZyme ID ASPTUDRAFT_191924-t33_1-p1
CAZy Family GH172
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1277 137336.12 4.4382
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AtubingensisCBS134.48 12592 767770 274 12318
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:3 3.2.1.14:3 3.2.1.14:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 526 886 1.9e-49 0.918918918918919

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119357 GH18_zymocin_alpha 1.20e-177 526 887 3 344
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
214753 Glyco_18 1.53e-58 524 887 1 333
Glyco_18 domain.
395573 Glyco_hydro_18 7.31e-48 524 886 1 305
Glycosyl hydrolases family 18.
119365 GH18_chitinase 8.10e-44 550 787 6 266
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.
119351 GH18_chitolectin_chitotriosidase 2.31e-42 569 890 30 343
This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 5 1277 1 1263
0.0 5 1277 1 1263
0.0 5 1277 1 1277
7.59e-251 42 1276 31 1280
5.27e-247 41 890 37 838

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.79e-27 550 904 8 351
Crystal Structure of a Novel Regulatory 40 kDa Mammary Gland Protein (MGP-40) secreted during Involution [Capra hircus]
3.48e-26 550 904 8 351
Crystal structure of signalling protein from goat SPG-40 in the presense of N,N',N''-triacetyl-chitotriose at 2.6A resolution [Capra hircus]
1.55e-25 550 904 8 351
Crystal Structure of the goat signalling protein (SPG-40) complexed with a designed peptide Trp-Pro-Trp at 3.2A resolution [Capra hircus],1ZBW_A Crystal structure of the complex formed between signalling protein from goat mammary gland (SPG-40) and a tripeptide Trp-Pro-Trp at 2.8A resolution [Capra hircus],1ZU8_A Crystal structure of the goat signalling protein with a bound trisaccharide reveals that Trp78 reduces the carbohydrate binding site to half [Capra hircus],2AOS_A Protein-protein Interactions of protective signalling factor: Crystal structure of ternary complex involving signalling protein from goat (SPG-40), tetrasaccharide and a tripeptide Trp-pro-Trp at 2.9 A resolution [Capra hircus],2B31_A Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 3.1 A resolution reveals large scale conformational changes in the residues of TIM barrel [Capra hircus],2DSZ_A Three dimensional structure of a goat signalling protein secreted during involution [Capra hircus],2DT0_A Crystal structure of the complex of goat signalling protein with the trimer of N-acetylglucosamine at 2.45A resolution [Capra hircus],2DT1_A Crystal Structure Of The Complex Of Goat Signalling Protein With Tetrasaccharide At 2.09 A Resolution [Capra hircus],2DT2_A Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 2.9A resolution [Capra hircus],2DT3_A Crystal structure of the complex formed between goat signalling protein and the hexasaccharide at 2.28 A resolution [Capra hircus],2O92_A Crystal structure of a signalling protein (SPG-40) complex with tetrasaccharide at 3.0A resolution [Capra hircus],2OLH_A Crystal structure of a signalling protein (SPG-40) complex with cellobiose at 2.78 A resolution [Capra hircus]
1.55e-25 550 904 8 351
Crystal structure of a 40 kDa signalling protein (SPC-40) secreted during involution [Bos taurus]
2.82e-25 550 904 8 351
Crystal structure of signalling protein from buffalo (SPB-40) with an acetone induced conformation of Trp78 at 1.49 A resolution [Bubalus bubalis],5Z3S_A Crystal structure of butanol modified signaling protein from buffalo (SPB-40) at 1.65 A resolution [Bubalus bubalis],5Z4W_A Crystal structure of signalling protein from buffalo (SPB-40) with an altered conformation of Trp78 at 1.79 A resolution [Bubalus bubalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.42e-102 313 886 192 710
Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
1.11e-24 550 904 27 371
Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
1.45e-24 550 904 8 351
Chitinase-3-like protein 1 OS=Ovis aries OX=9940 GN=CHI3L1 PE=1 SV=1
3.75e-24 550 904 29 373
Chitinase-3-like protein 1 OS=Capra hircus OX=9925 GN=CHI3L1 PE=1 SV=1
3.75e-24 550 904 29 373
Chitinase-3-like protein 1 OS=Bubalus bubalis OX=89462 GN=CHI3L1 PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000203 0.999769 CS pos: 23-24. Pr: 0.9481

TMHMM  Annotations      download full data without filtering help

Start End
7 26