CAZyme Information: KIW19305.1

Basic Information

• Species: Exophiala spinifera
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala spinifera
• CAZyme ID: KIW19305.1
• CAZy Family: GT20
• CAZyme Description: GH18 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0D2BL30]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
548		57892.73	5.1852

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EspiniferaCBS89968	12110	N/A	61	12049

• Gene Location: location=KN847493:3574768-3576571(-)

Full Sequence      

MPCSRFFLIPILCLVNVYANLVLASGSEWNDDIAKRAHDPLNTIESKQEHHFAGLGPRDS
AARSSYWKPLRLSQREPPSDFEAQLADVANQLTSSLNTLWALIQREYNIGPPVIASGSSH
PTVYPITFANSHGSYPTPGPSSTPTAAASSSSSSSQQTPSGTYAFNPQASDLNIVYYSQT
DLTKTVTLTQVCSDPSVDVVILAFITSLFGKGGYPSMNMASNCWAPSAAQQNAGATGLLD
CVGDGFAVQISSCQSLGKKVLISMGGIYSNLQISSTDQATQAAQLLWNLFLGGTDAATAP
LRPYGSVVLDGIDLDNENPSNAQYMPSLMAALRTLMATDSAKSYYLSAAPQCPQPDQSIL
VPGLLDVVDFFNVQFYNNPSCQLGSGQGFLDSLTSWSSSLLLPAVHGGPGPSSRPRSPPR
RKRSRASLSTRRTQIPPASFGDAAPGASSNGGGGGDDDNDDNTGFMNINNGVTYPRLLVG
TPAFGAAGTGYVTVAQYKDILEQVKALRLPNVAGAMFWDGAYEIRSGAPVDGAGTNKTYV
QVVRDVLG

Enzyme Prediction     

EC	3.2.1.14:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	174	503	1.1e-22	0.7331081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119356	GH18_hevamine_XipI_class_III	2.70e-57	175	545	5	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	1.57e-15	248	377	54	176	Glycosyl hydrolases family 18.
119349	GH18_chitinase-like	1.20e-13	174	377	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.
119350	GH18_chitinase_D-like	1.48e-11	195	378	26	195	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.
226000	Chi1	4.61e-06	246	378	87	212	Chitinase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAS55554.1|GH18|3.2.1.14	1.51e-52	175	527	16	290
CAC07217.1|GH18	2.70e-52	175	527	33	307
AET14352.1|GH18	3.71e-51	175	527	82	356
ADF57308.1|GH18	4.84e-51	174	527	33	307
QLI65876.1|GH18	1.02e-49	175	527	82	356

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2GSJ_A	4.41e-29	174	399	4	207	cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity [Parkia platycephala]
2UY2_A	5.29e-29	168	378	2	195	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	2.22e-28	187	400	15	209	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]
1KR0_A	9.44e-27	187	400	15	209	Chain A, Hevamine A [Hevea brasiliensis]
1KR1_A	1.76e-26	187	400	15	209	Chain A, Hevamine A [Hevea brasiliensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6QDR4|CHI3_METAN	2.67e-53	175	527	16	290	Endochitinase 3 (Fragment) OS=Metarhizium anisopliae OX=5530 GN=chi3 PE=1 SV=1
sp|E9ENC6|CHI3_METRA	1.88e-51	175	527	33	307	Endochitinase 3 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chi3 PE=3 SV=1
sp|P51614|CHIT3_VITVI	9.95e-30	187	400	40	237	Acidic endochitinase OS=Vitis vinifera OX=29760 GN=CHIT3 PE=2 SV=1
sp|P36910|CHIE_BETVU	2.96e-29	188	396	41	228	Acidic endochitinase SE2 OS=Beta vulgaris OX=161934 GN=SE2 PE=1 SV=1
sp|P36908|CHIA_CICAR	4.05e-29	188	399	39	228	Acidic endochitinase OS=Cicer arietinum OX=3827 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000221	0.999777	CS pos: 24-25. Pr: 0.9809

TMHMM  Annotations     

There is no transmembrane helices in KIW19305.1.