CAZyme Information: PABG_11372-t30_1-p1

Basic Information

• Species: Paracoccidioides brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; NA; Paracoccidioides; Paracoccidioides brasiliensis
• CAZyme ID: PABG_11372-t30_1-p1
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
277	KN305532|CGC9	30495.58	6.2410

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PbrasiliensisPb03	8548	482561	121	8427

• Gene Location: location=KN305532:1932792-1934048(+)

Full Sequence      

MPPAQNPSHEKQAAVVNTAIVGLVLISVVQRNCLFSCDAKSKCGKYAPKRLENYPLNASI
METGTDIRVKVLWYYGRILWEALSNGCEQIKDCKYTSKRSGSFLVYIPSLIQAEVHALGA
LQANVTLATSRVDIDWEYPVADRGGAEDGFRTYVQFSKELRAAVGNIYGITMALSDSYCE
GFDDKGMAQYVDWFNFMTYDIHGTWDGSSKWTNGVFTPIQGLDLLWRNSVPPEKVSLGLA
FYGRSFALADPSYTTPGCTFTRDGDGTSGGAKPVNVL

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	131	253	2.6e-25	0.3783783783783784

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	1.01e-28	132	271	111	270	Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
214753	Glyco_18	5.35e-28	132	273	111	267	Glyco_18 domain.
119365	GH18_chitinase	2.08e-25	132	246	129	266	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	9.40e-24	132	256	108	237	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	5.09e-23	133	273	117	267	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
QSS62098.1|CBM18|GH18	6.09e-57	33	273	68	396
QSS71211.1|GH18	1.34e-56	132	273	67	218
CAP74296.1|CBM18|GH18	4.37e-44	132	270	236	384
BAE65677.1|GH18	1.68e-42	132	271	108	282
QGA21067.1|GH18	2.81e-36	126	265	90	242

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	3.03e-17	132	256	121	264	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	3.53e-16	132	256	121	264	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
4W5U_A	9.63e-13	132	267	178	328	Crystal structure of chitinase 40 from thermophilic bacteria Streptomyces thermoviolaceus. [Streptomyces thermoviolaceus],4W5U_B Crystal structure of chitinase 40 from thermophilic bacteria Streptomyces thermoviolaceus. [Streptomyces thermoviolaceus]
5WUP_A	4.86e-12	132	252	212	350	Crystal structure of a insect group III chitinase (CAD1) from Ostrinia furnacalis [Ostrinia furnacalis],5WV9_A Crystal structure of a insect group III chitinase complex with (GlcNAc)6 (CAD1-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
3ARS_A	1.75e-11	132	276	289	475	Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - apo structure of mutant W275G [Vibrio harveyi],3ART_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with DEQUALINIUM [Vibrio harveyi],3ARU_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with PENTOXIFYLLINE [Vibrio harveyi],3AS0_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with Sanguinarine [Vibrio harveyi],3AS1_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with chelerythrine [Vibrio harveyi],3AS2_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with Propentofylline [Vibrio harveyi],3AS3_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with 2-(imidazolin-2-yl)-5-isothiocyanatobenzofuran [Vibrio harveyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9W092|CHIT2_DROME	1.73e-12	132	246	163	287	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
sp|P11220|CHIT_STRPL	5.08e-11	132	277	378	541	Chitinase 63 OS=Streptomyces plicatus OX=1922 GN=chtA PE=1 SV=2
sp|P32823|CHIA_PSEO7	1.01e-10	132	276	308	494	Chitinase A OS=Pseudoalteromonas piscicida OX=43662 GN=chiA PE=1 SV=1
sp|P36362|CHIT_MANSE	1.18e-10	132	249	141	277	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|P36909|CHIT_STRLI	1.67e-10	132	277	377	540	Chitinase C OS=Streptomyces lividans OX=1916 GN=chiC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.938471	0.061563

TMHMM  Annotations     

There is no transmembrane helices in PABG_11372-t30_1-p1.