dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Trichoderma virens

Lineage

Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma virens

CAZyme ID

TRIVIDRAFT_66617-t45_1-p1

CAZy Family

GH75

CAZyme Description

glycoside hydrolase family 18 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1273		139387.14	4.7679

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TvirensGv29-8	12405	413071	0	12405

Gene Location

Enzyme Prediction help

EC	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	490	849	5.1e-54	0.9695945945945946

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	3.27e-171	489	836	2	345	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	2.16e-62	490	835	3	333	Glyco_18 domain.
395573	Glyco_hydro_18	2.73e-55	490	834	3	305	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	2.27e-45	490	841	2	342	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.
119365	GH18_chitinase	2.06e-43	489	731	1	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.

CAZyme Hits help

E-Value	Query Start	Query End	Hit Start
1	1273	1	1283
435	1273	3	841
22	1267	18	1306
14	842	21	857
14	842	21	857

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.53e-35	490	838	10	353	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 [Ostrinia furnacalis],5Y2B_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with HEPTA-N-ACETYLCHITOOCTAOSE (NAG)7 [Ostrinia furnacalis]
3.23e-35	490	838	10	353	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a piperidine-thienopyridine derivative [Ostrinia furnacalis],6JAW_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a napthalimide derivative [Ostrinia furnacalis],6JAX_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with chitooctaose [(GlcN)8] [Ostrinia furnacalis],6JAY_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a dipyrido-pyrimidine derivative [Ostrinia furnacalis]
2.87e-28	490	838	4	337	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]
2.87e-28	490	838	4	337	Crystal structure of signalling protein from goat SPG-40 in the presense of N,N',N''-triacetyl-chitotriose at 2.6A resolution [Capra hircus]
3.87e-28	490	838	4	337	Crystal Structure of a Novel Regulatory 40 kDa Mammary Gland Protein (MGP-40) secreted during Involution [Capra hircus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.92e-90	311	940	223	820	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
4.73e-32	474	839	9	368	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
8.93e-31	474	839	9	368	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
1.22e-30	474	839	9	368	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
1.15e-27	474	839	9	368	Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000185	0.999767	CS pos: 22-23. Pr: 0.9691

TMHMM Annotations help

There is no transmembrane helices in TRIVIDRAFT_66617-t45_1-p1.

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