CAZyme Information: AFUB_052270-T-p1

Basic Information

• Species: Aspergillus fumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus
• CAZyme ID: AFUB_052270-T-p1
• CAZy Family: GH3
• CAZyme Description: Ortholog(s) have chitinase activity and role in autolysis

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
866	scf_000004_A_fumigatus_A1163|CGC21	86770.56	4.1063

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfumigatusA1163	10106	451804	199	9907

• Gene Location: location=scf_000004_A_fumigatus_A1163:940130-942871(-)

Full Sequence      

MVSSKLSFVATAVAALAPLASAFDASSRSNLAIYWGQGPNQLRLSHFCQETSLDIINIGF
INYFPDMSPGHWPGSNFGNQCDGSVYVTNDGVVTKLLSGCHQIMEDIPICQAAGKKVLLS
IGGAYPPDQSILSEDSAVAFATFLWGAFGPVAEGWEGPRPFGDVVVDGFDFDIEHNGGFG
YATMVNTFRQYFNQVPERKFYLSAAPQCIIPDAQLSDAIFNAAFDFIWIQYYNTAACSAK
SFIDTSLGTFNFDAWVTVLKASASKDAKLYVGLPASETAANQGYYLTPDEVESLVSTYMD
RYPDTFGGIMLWEATASENNQIDGAPYADHMKDILLHCDPSPPVTSSSAIPSSTPVTTPS
PSSSAVPSSTPAVSETPSPSSSAVPSSTPVASSTPVVPGTSASSSPVSSSSAIAPSTPVV
PGTSVPSSTPVASSTPVVPGTSASSSPVSSSSAVASSTPVVPGTSTSSSTPVASSTPVVP
GTSASSSPVSSSSAVAPSTPVVPGTSVPSSTPAIPGGSSSSSEAVASSTPLVTLTLTVSP
TPAPSSSESSSTDLSSSTQTDVGTAPSQPAGPSTTATATTSSSSSSTDESSTTVGSGNGN
GSGSTTTTAATDSITAAPTATSSATATGATSEPVTITTVIVTSYIDICPTGFTTVTTTYT
TTYCPGTNTATATATVTNPPSGPGGAGSQTTAPTVPEGWTTTVTVCTQCAAKPTTVTLTL
PVTETGSTSTDAVPAPPAATGEGSNPTQPSGASPTGGNGSFSEEPVPPPAVTQVSTSTEI
VTLVRPTSSRPLILGTGTVHPSSTLAVKPSAKPSGQNSGSSSHVPIPPSYTQEAVSPLST
GAASRVTGLGHGLVLTVLTLSAFFVL

Enzyme Prediction     

EC	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	30	282	3.6e-23	0.6756756756756757

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119356	GH18_hevamine_XipI_class_III	6.46e-117	29	333	1	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	2.20e-17	30	276	1	223	Glycosyl hydrolases family 18.
119350	GH18_chitinase_D-like	5.38e-09	102	312	61	293	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.
119349	GH18_chitinase-like	1.36e-06	110	233	60	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.
223021	PHA03247	0.005	679	848	2708	2859	large tegument protein UL36; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAO61685.1|GH18	0.0	1	866	1	825
EAL85930.1|GH18	0.0	1	866	1	888
BAE61604.1|GH18	4.35e-159	1	852	1	827
BCS11270.1|GH18	1.34e-152	9	355	8	359
CAK40432.1|GH18	5.84e-150	9	353	8	357

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4TX6_A	1.78e-231	28	337	1	310	AfChiA1 in complex with compound 1 [Aspergillus fumigatus A1163],4TX6_B AfChiA1 in complex with compound 1 [Aspergillus fumigatus A1163]
2XVN_A	9.81e-231	29	337	1	309	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]
2XTK_A	1.02e-230	29	337	2	310	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	6.49e-62	24	335	1	287	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]
2GSJ_A	7.56e-42	31	313	3	254	cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity [Parkia platycephala]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4WEP7|CHIA1_ASPFU	0.0	1	866	1	888	Endochitinase A1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiA1 PE=3 SV=1
sp|Q873Y0|CHIA1_ASPFM	0.0	1	866	1	825	Endochitinase A1 OS=Neosartorya fumigata OX=746128 GN=chiA1 PE=1 SV=1
sp|A2QUQ2|CHIA1_ASPNC	1.04e-150	9	353	8	357	Endochitinase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=ctcA PE=2 SV=1
sp|P54197|CHI2_COCP7	1.41e-123	12	346	12	348	Endochitinase 2 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS2 PE=3 SV=2
sp|Q1EAR5|CHI2_COCIM	3.69e-123	12	346	12	348	Endochitinase 2 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS2 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000210	0.999739	CS pos: 22-23. Pr: 0.9782

TMHMM  Annotations     

There is no transmembrane helices in AFUB_052270-T-p1.