dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: GBF61191.1

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Basic Information help

Species

Trichophyton mentagrophytes

Lineage

Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton mentagrophytes

CAZyme ID

GBF61191.1

CAZy Family

CBM18|GH18

CAZyme Description

killer toxin subunits alpha/beta

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
436		48261.14	6.7587

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmentagrophytesTIMM2789	7958	N/A	98	7860

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in GBF61191.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	79	343	9.2e-50	0.7297297297297297

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119365	GH18_chitinase	7.11e-58	81	320	1	267	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.
214753	Glyco_18	6.95e-57	80	324	1	245	Glyco_18 domain.
119357	GH18_zymocin_alpha	2.70e-53	80	324	1	250	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.
395573	Glyco_hydro_18	2.91e-51	80	378	1	281	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	1.26e-47	108	329	29	257	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
2.40e-140	52	324	6	285
3.92e-126	37	323	44	325
5.64e-122	38	324	70	407
5.64e-122	38	324	70	407
2.83e-116	52	324	44	296

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.70e-29	73	321	1	260	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with reaction products (GlcNAc)2,3 [Ostrinia furnacalis],3WQV_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)5 [Ostrinia furnacalis],3WQW_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)6 [Ostrinia furnacalis]
6.76e-29	81	324	6	259	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
9.54e-29	73	321	1	260	Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]
1.35e-28	72	321	18	278	Crystal structure of an insect chitinase from the Asian corn borer, Ostrinia furnacalis [Ostrinia furnacalis]
2.46e-28	73	321	1	260	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2 [Ostrinia furnacalis]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.21e-35	37	321	334	618	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
9.40e-28	79	321	23	276	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
1.90e-24	80	319	45	342	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
2.84e-23	69	321	17	273	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
1.82e-22	101	324	45	276	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000204	0.999774	CS pos: 26-27. Pr: 0.9668

TMHMM Annotations help

There is no transmembrane helices in GBF61191.1.