CAZyme Information: CPAR2_502120-T-p1

Basic Information

• Species: Candida parapsilosis
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida parapsilosis
• CAZyme ID: CPAR2_502120-T-p1
• CAZy Family: GT22
• CAZyme Description: Has domain(s) with predicted catalytic activity, hydrolase activity, hydrolyzing O-glycosyl compounds activity and role in carbohydrate metabolic process

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
808	Contig006139_C_parapsilosis_CDC317|CGC4	85397.88	3.8417

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CparapsilosisCDC317	5984	578454	147	5837

• Gene Location: location=Contig006139_C_parapsilosis_CDC317:477617-480043(+)

Full Sequence      

MLLQSLFAVLATSAASALVAADNIALYWGQNVEGQQKRLSEYCENPDFEIVILSSITNFY
TGFGDFDFNCYKNRTTLEMICHNFEEDIKHCQQKGKKVLLSLGAPTSVDPVGFDNTEDAV
KLAENLWGRFGNGDGKEKPFGNALIDGFDLHITTGSDTGYVEFAEALRSKFDGSKNFLLT
ASPSCVFPNPQLGQVLSKVPLDYTFVQFYDSPCQTNKAFNFDTWSKFADSAPNPNMKSYL
GLTTRGYTQSFIPPKDLPEFIKKVNCDSNFDGISLWDASGAWLKDIVGDWLINKNARYID
EIKYVLENETCPSPSSSTTASSSTEPSSSEEPTSSAEPTSSEEPTSSAEPTSSEESTSSA
EPTSSEESTSSAEPTSSAEPTSSAEPSSSEEPTSSAEPSSSEEPTSSAEPSSSEEPTSSA
EPTSSAEPSSSEEPTSSAEPTSSEESTSSTEPTSSAESSSSEEPTSSAEPSSSEEPTSST
EPTSSEEPTSSEEPTSSAESTSSTEPTSSTEPSSSQEQQNTDEASSEEPTTTPEADVSSS
TLDSTTVITITSCHDDGCTQVPVTTGVTVITEEYTTYTTYCPLTTATTDETKHSSKDSIE
TKTDVGTTIVTITSCEENRCTPVAVTTGVITITENDTVYTTYCPLPTTKGDTSENVAPTT
TTGAPGAPKSTIEKEEASRSKGEQGVHEVTAEKTTVTMGAEKTTGTTSAASGEETTVAGG
AHEVPEETKTSTVVVASESKGTNTEESATTVATIAPVEVQSEESTEKASSTAAATEEVPV
STYEGKGVRSFAMENIMTIPLLCLALLF

Enzyme Prediction     

EC	3.2.1.14:12

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	22	249	1.1e-18	0.6722972972972973

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119356	GH18_hevamine_XipI_class_III	2.05e-81	23	304	2	280	This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin.
395573	Glyco_hydro_18	4.01e-12	23	210	1	176	Glycosyl hydrolases family 18.
404761	Flocculin_t3	1.13e-09	607	646	1	44	Flocculin type 3 repeat. This repeat is found in the Flocculation protein FLO9 close to its C-terminus.
119349	GH18_chitinase-like	8.89e-07	24	210	1	177	The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
404761	Flocculin_t3	4.13e-05	545	584	1	44	Flocculin type 3 repeat. This repeat is found in the Flocculation protein FLO9 close to its C-terminus.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCE43987.1|GH18	3.47e-316	1	808	1	808
CCG21946.1|GH18	3.48e-216	1	320	1	320
CCE43988.1|GH18	1.58e-119	2	317	1	307
CCE43989.1|GH18	8.50e-87	1	315	1	308
CCG21947.1|GH18	1.70e-85	1	315	1	307

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2UY2_A	6.41e-53	20	289	4	277	ScCTS1_apo crystal structure [Saccharomyces cerevisiae],2UY3_A ScCTS1_8-chlorotheophylline crystal structure [Saccharomyces cerevisiae],2UY4_A ScCTS1_acetazolamide crystal structure [Saccharomyces cerevisiae],2UY5_A ScCTS1_kinetin crystal structure [Saccharomyces cerevisiae],4TXE_A ScCTS1 in complex with compound 5 [Saccharomyces cerevisiae]
2XVN_A	5.12e-32	22	306	1	307	A. fumigatus chitinase A1 phenyl-methylguanylurea complex [Aspergillus fumigatus],2XVN_B A. fumigatus chitinase A1 phenyl-methylguanylurea complex [Aspergillus fumigatus],2XVN_C A. fumigatus chitinase A1 phenyl-methylguanylurea complex [Aspergillus fumigatus]
4TX6_A	5.24e-32	22	306	2	308	AfChiA1 in complex with compound 1 [Aspergillus fumigatus A1163],4TX6_B AfChiA1 in complex with compound 1 [Aspergillus fumigatus A1163]
2XTK_A	5.24e-32	22	306	2	308	ChiA1 from Aspergillus fumigatus in complex with acetazolamide [Aspergillus fumigatus A1163],2XTK_B ChiA1 from Aspergillus fumigatus in complex with acetazolamide [Aspergillus fumigatus A1163],2XUC_A Natural product-guided discovery of a fungal chitinase inhibitor [Aspergillus fumigatus],2XUC_B Natural product-guided discovery of a fungal chitinase inhibitor [Aspergillus fumigatus],2XUC_C Natural product-guided discovery of a fungal chitinase inhibitor [Aspergillus fumigatus],2XVP_A ChiA1 from Aspergillus fumigatus, apostructure [Aspergillus fumigatus A1163],2XVP_B ChiA1 from Aspergillus fumigatus, apostructure [Aspergillus fumigatus A1163]
3D5H_A	2.52e-31	23	278	4	255	Crystal structure of haementhin from Haemanthus multiflorus at 2.0A resolution: Formation of a novel loop on a TIM barrel fold and its functional significance [Scadoxus multiflorus],3HU7_A Structural characterization and binding studies of a plant pathogenesis related protein heamanthin from haemanthus multiflorus reveal its dual inhibitory effects against xylanase and alpha-amylase [Scadoxus multiflorus],3M7S_A Crystal structure of the complex of xylanase GH-11 and alpha amylase inhibitor protein with cellobiose at 2.4 A resolution [Scadoxus multiflorus],3OIH_A Crystal Structure of the complex of xylanase-alpha-amylase inhibitor Protein (XAIP-I) with trehalose at 1.87 A resolution [Scadoxus multiflorus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P40953|CHI2_CANAL	4.53e-80	11	324	11	320	Chitinase 2 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CHT2 PE=1 SV=2
sp|Q5AAH2|CHI1_CANAL	1.67e-54	14	318	10	300	Chitinase 1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CHT1 PE=1 SV=1
sp|P46876|CHI1_CANAX	2.29e-54	14	318	10	300	Chitinase 1 OS=Candida albicans OX=5476 GN=CHT1 PE=3 SV=2
sp|P29029|CHIT_YEAST	6.06e-50	20	319	25	318	Endochitinase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=CTS1 PE=1 SV=2
sp|P40954|CHI3_CANAL	1.99e-48	3	319	4	320	Chitinase 3 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CHT3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000390	0.999564	CS pos: 21-22. Pr: 0.5241

TMHMM  Annotations     

There is no transmembrane helices in CPAR2_502120-T-p1.