dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: FUNGIDB

help

CAZyme Information: POW10238.1

You are here: Home > Sequence: POW10238.1

Basic Information help

Species

Puccinia striiformis

Lineage

Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis

CAZyme ID

POW10238.1

CAZy Family

GH5

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
596		64498.04	5.7130

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pstriiformis93-210	15090	N/A	0	15090

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	213	579	6.3e-50	0.9256756756756757

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	3.22e-57	214	578	1	330	Glyco_18 domain.
395573	Glyco_hydro_18	1.49e-56	214	578	1	303	Glycosyl hydrolases family 18.
119365	GH18_chitinase	1.29e-55	285	576	91	316	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	9.22e-52	198	594	26	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351	GH18_chitolectin_chitotriosidase	8.49e-51	285	574	77	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
1.73e-119	202	596	23	420
3.50e-90	399	595	1	199
7.00e-76	215	594	26	405
1.34e-63	242	575	7	336
3.00e-58	205	591	18	399

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.42e-36	278	587	122	411	Chain A, Glycosyl Hydrolase [Niallia circulans]
2.23e-35	284	581	163	447	Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
1.02e-32	257	573	44	333	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1.04e-32	257	573	44	333	Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]
1.42e-32	257	573	44	333	Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.32e-34	278	587	154	443	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
3.60e-31	257	573	65	354	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
1.11e-28	241	573	54	352	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
1.55e-25	253	573	61	356	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
2.26e-25	259	582	98	388	Endochitinase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chit1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.998967	0.001052

TMHMM Annotations help

There is no transmembrane helices in POW10238.1.