dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: PTTG_02749-t43_1-p1

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Basic Information help

Species

Puccinia triticina

Lineage

Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina

CAZyme ID

PTTG_02749-t43_1-p1

CAZy Family

GH16

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
534	ADAS02000015.1\|CGC1	58634.90	9.7898

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1	15692	630390	814	14878

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.14:2

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	241	512	6.5e-42	0.6317567567567568

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	2.83e-45	238	506	111	334	Glyco_18 domain.
119365	GH18_chitinase	5.33e-37	238	506	129	322	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.
225862	ChiA	4.61e-33	238	519	171	435	Chitinase, GH18 family [Carbohydrate transport and metabolism].
395573	Glyco_hydro_18	6.36e-33	238	506	108	307	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	2.22e-25	239	498	117	333	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
1.69e-57	238	523	133	408
3.92e-52	242	518	157	427
1.21e-51	242	500	86	337
5.45e-50	242	509	135	392
1.28e-48	242	506	141	398

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.53e-33	242	519	105	368	Chain A, Fungal chitinase from Rhizomucor miehei (SeMet-substituted proteins) [Rhizomucor miehei]
6.51e-18	238	506	167	406	Chain A, Glycosyl Hydrolase [Niallia circulans]
8.04e-18	242	516	181	403	Crystal structure of chitinase 40 from thermophilic bacteria Streptomyces thermoviolaceus. [Streptomyces thermoviolaceus],4W5U_B Crystal structure of chitinase 40 from thermophilic bacteria Streptomyces thermoviolaceus. [Streptomyces thermoviolaceus]
4.05e-16	242	523	642	885	Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZU_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_A Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
4.55e-16	242	523	893	1136	Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
7.26e-18	242	516	381	605	Chitinase 63 OS=Streptomyces plicatus OX=1922 GN=chtA PE=1 SV=2
1.73e-17	242	514	380	602	Chitinase C OS=Streptomyces lividans OX=1916 GN=chiC PE=2 SV=1
8.04e-17	238	506	199	438	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
3.11e-13	242	501	138	358	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
1.45e-12	242	515	169	392	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000222	0.999747	CS pos: 28-29. Pr: 0.6276

TMHMM Annotations help

There is no transmembrane helices in PTTG_02749-t43_1-p1.