dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: RO3G_14659-t26_1-p1

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Basic Information help

Species

Rhizopus delemar

Lineage

Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus delemar

CAZyme ID

RO3G_14659-t26_1-p1

CAZy Family

GT2|GT2

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
371		41668.60	9.7932

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RdelemarRA99-880	17703	246409	244	17459

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in RO3G_14659-t26_1-p1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	25	359	1.1e-62	0.956081081081081

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	2.80e-74	26	353	1	334	Glyco_18 domain.
119365	GH18_chitinase	7.55e-68	27	353	1	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.
395573	Glyco_hydro_18	2.09e-66	26	353	1	307	Glycosyl hydrolases family 18.
225862	ChiA	2.50e-59	26	362	39	431	Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351	GH18_chitolectin_chitotriosidase	8.16e-55	43	355	29	341	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
5.63e-140	19	369	23	411
1.05e-135	23	369	33	420
9.61e-135	25	368	2	386
8.92e-98	20	368	22	413
1.80e-91	19	353	34	398

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.91e-44	37	367	17	369	Chain A, Fungal chitinase from Rhizomucor miehei (SeMet-substituted proteins) [Rhizomucor miehei]
6.31e-35	37	364	45	388	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]
7.03e-35	37	364	296	639	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]
2.02e-34	23	359	2	355	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
7.16e-34	35	356	26	360	Crystal structure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXN_B Crystal structure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.49e-28	23	353	39	389	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
1.27e-27	19	356	38	441	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
8.03e-27	1	354	1	447	Chitinase ChiA OS=Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101) OX=376686 GN=chiA PE=1 SV=1
3.28e-26	38	362	223	551	Chitinase A OS=Serratia marcescens OX=615 GN=chiA PE=1 SV=3
2.86e-25	43	353	52	363	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000246	0.999728	CS pos: 19-20. Pr: 0.9820

TMHMM Annotations help

There is no transmembrane helices in RO3G_14659-t26_1-p1.