CAZyme Information: Z517_06267-t43_1-p1

Basic Information

• Species: Fonsecaea pedrosoi
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Fonsecaea; Fonsecaea pedrosoi
• CAZyme ID: Z517_06267-t43_1-p1
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
817	KN846972|CGC20	83750.94	4.4521

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FpedrosoiCBS271-37	12573	1442368	46	12527

• Gene Location: location=KN846972:1326903-1329475(-)

Full Sequence      

MFAASLLATAAFISSTIATPMFGARSAVAKRAPSQPSLAVYWGQGPNQKRLAEFCADTTM
DIIPIGFVNVFPDQTGGPGTNYGNACGGVTWKSPEGVQTNVFTSCGQIATDVAICQGMGK
KILASIGGAESGNFIATSDSAKDFADFLWGAFGPVQDPTLVDYPRPFGLNTVVDGFDLDI
ESGSNFGYADLVNQLRVRFQEDTSKSYIISSAPQCVVPDAHLDDAIKNSIIDYVFVQYYN
TDSCSAASLFSSGSLNTAADITFGWAQWLKQNSKNQNIKMFLGLPASNIAANPNHYLSLD
QAQALIEQYACSSTYQSLFGGVMLWEATYSDNNQQNGKSYAANIKDIFGKLSCAPPTTTS
TSTTTTTTTTSTTTTTTTTTTTTTTTTTTTTTSPIPTTTTTTTTTTTSEVVAPTSTSTSS
STTTTTTEIPAVTTSSTTSSSPVPTTTSESTTTTTYSHSLGPIGGSTTTSSESSTSTSTT
TTYSNTLGPIGGSTTTSSSTTTTVSSTLGPIGETTTTSSSTTTTYSHTLGPIGETTSSST
VPPAVTTSSYSHSLGHGSSTSSVYVSPATTSSASATSTTGWQWGDWTSAGSSPVDPTSTK
TTTTSAPVSWADWSATTSATGQYTVTVWTTVYTDIGPNGYTTHPYHYTTTVPVAAATTTA
PFVWPTNADGCPRGFHTTVTVCSVCAPTVVTVTLTVPEATATAVMTQTVVPVRPTDVAAA
PVHPSGTETPVAAASSTWTYSQPAGNGASTPVAAATTSAGSNSGWLAPSPSSASSTPVAP
ISITPFTGGATAAQSQLPGTMLSVVICAAVAISGLFL

Enzyme Prediction     

EC	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	38	342	2.1e-21	0.7162162162162162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119356	GH18_hevamine_XipI_class_III	5.57e-103	38	346	3	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	1.23e-16	38	287	2	223	Glycosyl hydrolases family 18.
119363	GH18_CTS3_chitinase	1.50e-10	106	326	59	252	GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen Coccidioides posadasii. CTS3 has a chitinase-like glycosyl hydrolase family 18 (GH18) domain; and has homologs in bacteria as well as fungi.
119349	GH18_chitinase-like	6.36e-08	65	240	2	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.
119350	GH18_chitinase_D-like	1.57e-06	61	342	29	311	GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAO61685.1|GH18	4.35e-88	32	358	25	345
EAL85930.1|GH18	5.18e-87	32	358	25	345
QSS69866.1|GH18	1.46e-83	7	358	1	348
BCR90928.1|GH18	8.16e-82	32	355	24	344
QSS51884.1|GH18	4.06e-81	7	358	1	347

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2XVN_A	1.05e-92	37	347	2	306	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	1.08e-92	37	347	3	307	AfChiA1 in complex with compound 1 [Aspergillus fumigatus A1163],4TX6_B AfChiA1 in complex with compound 1 [Aspergillus fumigatus A1163]
2XTK_A	1.08e-92	37	347	3	307	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]
2UY2_A	1.48e-54	37	352	7	291	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]
1HVQ_A	2.27e-34	38	346	3	271	CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR [Hevea brasiliensis],1LLO_A Chain A, HEVAMINE [Hevea brasiliensis],2HVM_A Hevamine A At 1.8 Angstrom Resolution [Hevea brasiliensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q873Y0|CHIA1_ASPFM	7.73e-89	32	358	25	345	Endochitinase A1 OS=Neosartorya fumigata OX=746128 GN=chiA1 PE=1 SV=1
sp|Q4WEP7|CHIA1_ASPFU	9.21e-88	32	358	25	345	Endochitinase A1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiA1 PE=3 SV=1
sp|Q92223|CHIA1_EMEND	1.55e-80	27	358	19	348	Endochitinase A OS=Emericella nidulans OX=162425 GN=chiA PE=2 SV=3
sp|G5EB30|CHIA1_EMENI	1.55e-80	27	358	19	348	Endochitinase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chiA PE=1 SV=1
sp|P54197|CHI2_COCP7	6.90e-78	34	358	27	347	Endochitinase 2 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS2 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.509737	0.490246

TMHMM  Annotations     

There is no transmembrane helices in Z517_06267-t43_1-p1.