CAZyme Information: PTTG_25636-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_25636-t43_1-p1
• CAZy Family: GT3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
203	ADAS02000007.1|CGC1	21872.36	5.2198

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: location=ADAS02000007.1:99336-100029(+)

Full Sequence      

MAYDLYSPSGDLAGPNAPMFDTCNDPTVKFSVDQAIKTWTSSGFPASQILLGLPAYGYKY
TMPNSELTPTNFSGQSNATSLFFSKFDKSAAPAAPESESAGPTTCGGEEDGHTWLFKDLV
NCGMVTPDGSQGLKGFTRYYDHCSRTPFLFDPSSKTFISYDDARSLARKTRFAKSNGLAG
VNVFDATGDTQDRVLLKAIKSSL

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	1	194	3.3e-28	0.44932432432432434

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.66e-32	1	189	182	334	Glyco_18 domain.
119365	GH18_chitinase	1.05e-24	1	189	207	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	5.43e-23	1	203	249	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].
395573	Glyco_hydro_18	7.89e-22	1	189	173	307	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	5.29e-21	1	203	186	362	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDR43393.1|GH18	2.64e-42	1	203	208	405
CRX79101.1|GH18	4.03e-39	1	183	158	337
CAC35202.1|GH18	4.44e-37	1	203	230	429
AEH16745.1|GH18|3.2.1.14	1.52e-34	1	190	221	387
AFD19009.1|GH18|3.2.1.14	3.84e-33	1	199	256	452

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5XWF_A	1.98e-17	2	200	180	366	Chain A, Fungal chitinase from Rhizomucor miehei (SeMet-substituted proteins) [Rhizomucor miehei]
6BT9_A	1.69e-15	1	189	280	448	Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
5GZU_A	8.98e-12	1	203	231	391	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]
5GZT_B	9.31e-12	1	203	482	642	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]
1ITX_A	1.32e-11	1	203	245	419	Chain A, Glycosyl Hydrolase [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A5FB63|CHIA_FLAJ1	2.09e-13	16	194	264	451	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
sp|P20533|CHIA1_NIACI	8.08e-11	1	203	277	451	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
sp|Q11174|CHIT_CAEEL	2.63e-10	1	184	245	394	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
sp|Q13231|CHIT1_HUMAN	5.98e-10	1	184	210	358	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q9D7Q1|CHIT1_MOUSE	2.71e-09	1	184	210	356	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000042	0.000001

TMHMM  Annotations     

There is no transmembrane helices in PTTG_25636-t43_1-p1.