CAZyme Information: PTTG_00503-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_00503-t43_1-p1
• CAZy Family: AA3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
420		45508.54	9.2039

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=ADAS02000703.1:5852-7880(+)

Full Sequence      

MRSLSQSFLGSFLLASLLLATITDARRVRGDGSAKVNGYYPTYNSDAQSPAQIDWAAYTD
VLFFPIIPEKDGSLSFDPALSKQQASDLVKGFVEEAQKHKVNPVFSVGGWTASQQFSNLA
ATAASRHHFAQSLVNFAKQHRFTGLDLDWEYPNGDGIGCNTKRPTDVVNFGLLVKEIRAL
WPEGELSAAVSLNGFNGATGLVATAEETALLAKNLDYINLMAYDVYGLWSKTSGPIAPLD
ATCADEDSAQSVKTGFQIALKQGFKASQVLLGIPGYAKRFQLTSSKLVPKIVGGNKASFY
YQQKTATMPPGGAFDDKAGKNICGVFEGAGGSYLVNELISNGYLAQDQSRGLGGYRRHFD
NCSGQPFLVSKKYLISYDDKASTVLKAKFAKKNKMGGIYFFDTMGPAKETVREARKVFSN

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	34	404	7e-51	0.9290540540540541

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	3.28e-58	35	402	1	330	Glyco_18 domain.
119365	GH18_chitinase	7.82e-55	38	400	3	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.
395573	Glyco_hydro_18	3.56e-54	35	402	1	303	Glycosyl hydrolases family 18.
225862	ChiA	1.71e-48	35	414	39	431	Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351	GH18_chitolectin_chitotriosidase	1.44e-47	106	398	76	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAP42832.1|GH18	1.14e-183	1	420	1	420
CDR43393.1|GH18	6.93e-76	39	415	29	402
CRX79101.1|GH18	2.72e-64	84	399	22	336
AYA60264.1|GH18	2.47e-60	13	405	11	388
AEH16745.1|GH18|3.2.1.14	8.00e-57	35	405	43	385

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ITX_A	9.72e-41	44	416	56	416	Chain A, Glycosyl Hydrolase [Niallia circulans]
5XWF_A	1.42e-32	43	398	7	347	Chain A, Fungal chitinase from Rhizomucor miehei (SeMet-substituted proteins) [Rhizomucor miehei]
5GZT_B	3.06e-29	21	402	268	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]
5GZU_A	8.90e-29	95	402	104	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]
6BT9_A	3.32e-27	95	405	152	447	Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P20533|CHIA1_NIACI	1.01e-38	2	416	11	448	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
sp|Q9D7Q1|CHIT1_MOUSE	1.28e-25	100	397	89	352	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|Q13231|CHIT1_HUMAN	1.11e-24	100	285	89	276	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q9WTV1|CH3L1_RAT	7.43e-24	100	397	87	346	Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
sp|Q11174|CHIT_CAEEL	7.70e-24	72	399	90	392	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000257	0.999724	CS pos: 25-26. Pr: 0.9785

TMHMM  Annotations     

There is no transmembrane helices in PTTG_00503-t43_1-p1.