dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: KNZ61836.1

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Basic Information help

Species

Puccinia sorghi

Lineage

Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia sorghi

CAZyme ID

KNZ61836.1

CAZy Family

GT22

CAZyme Description

Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A0L6VM62]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
474	LAVV01003899\|CGC1	51411.54	6.9442

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsorghiRO10H11247	21769	N/A	691	21078

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in KNZ61836.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	96	456	3e-37	0.7702702702702703

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.69e-40	149	456	66	330	Glyco_18 domain.
395573	Glyco_hydro_18	3.87e-39	137	456	51	303	Glycosyl hydrolases family 18.
225862	ChiA	8.28e-35	143	468	120	431	Chitinase, GH18 family [Carbohydrate transport and metabolism].
119365	GH18_chitinase	6.08e-34	149	456	84	318	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	7.00e-32	151	452	68	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
2.94e-166	30	471	36	417
2.41e-66	276	471	1	197
8.74e-46	103	461	45	394
2.29e-45	142	453	31	336
2.32e-45	142	468	94	394

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
9.00e-22	146	466	115	412	Chain A, Glycosyl Hydrolase [Niallia circulans]
4.49e-20	140	459	148	447	Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
7.33e-20	143	456	103	373	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]
8.27e-20	143	456	354	624	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]
1.25e-18	147	451	62	333	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.35e-20	146	466	147	444	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
1.34e-17	147	451	83	354	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
2.61e-16	140	338	112	300	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
2.01e-14	134	455	73	403	Chitinase B OS=Serratia marcescens OX=615 GN=chiB PE=1 SV=1
2.50e-14	143	451	83	356	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000352	0.999639	CS pos: 20-21. Pr: 0.8890

TMHMM Annotations help

There is no transmembrane helices in KNZ61836.1.