CAZyme Information: P170DRAFT_460099-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_460099-t37_1-p1
• CAZy Family: GH76
• CAZyme Description: glycoside hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
445		50248.21	7.9968

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000001:378281-379753(+)

Full Sequence      

MLRRYRRALRDVAPLLALAFFVYSVYYFIIWAGRTLEARCMENGHCERVNLRCPEKASRA
ICSSDKNFFLAVGTYEGSATRRRCRDFWPEKIPLDAFNHVNFASAIISPDTYEVLPAHDR
DIDLYARLIRHLGYQNDTKVLITLRDQQKLNSTGLMSSIFSELAASPQTKQRKFLSSLIS
FMTTHGFNGINLDLDLDFDTQDEKQQPDYTNLSRFVANLNIALSKMAGPDELSISFPASE
AYLRRFDLKALHRYVSYINLKPYDGGAARGSRPVANAGVNTAEITSILEHLNCQDVNPNR
IVWGMPFRGHSYTMADGCRSTDCAILSPGLAGHCSQEAGVLLNSEIVGIMQANVVKPQRV
GNGAAKYLSWDNQLVTYYDNETINLQVEFARRQYLAGLMVSTVSDDVHDASFTKQFADAC
RRPAWIQRSAMIADMLKDDRLLRMN

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	82	416	4.8e-34	0.9256756756756757

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	3.81e-34	85	406	14	334	Glyco_18 domain.
395573	Glyco_hydro_18	4.51e-32	92	406	18	307	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	1.54e-31	87	408	18	344	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.
119349	GH18_chitinase-like	1.89e-20	85	264	12	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.
119365	GH18_chitinase	3.20e-19	85	399	14	315	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPL01272.1|CBM18|GH18	5.24e-65	55	422	101	470
EAA67103.1|CBM18|GH18	1.28e-64	36	422	75	467
EAA66648.1|CBM18|GH18	5.04e-64	55	422	142	514
APA10647.1|CBM18|GH18	1.19e-63	62	422	102	464
CAK47333.1|CBM18|GH18	1.23e-63	55	417	147	513

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z05_A	3.89e-16	88	415	21	344	Crystal structure of signalling protein from buffalo (SPB-40) with an acetone induced conformation of Trp78 at 1.49 A resolution [Bubalus bubalis],5Z3S_A Crystal structure of butanol modified signaling protein from buffalo (SPB-40) at 1.65 A resolution [Bubalus bubalis],5Z4W_A Crystal structure of signalling protein from buffalo (SPB-40) with an altered conformation of Trp78 at 1.79 A resolution [Bubalus bubalis]
1XHG_A	3.89e-16	88	415	21	344	Crystal structure of a 40 kDa signalling protein from Porcine (SPP-40) at 2.89A resolution [Sus scrofa],1XRV_A Crystal Structure of the novel secretory signalling protein from Porcine (SPP-40) at 2.1A resolution. [Sus scrofa],1ZB5_A Recognition of peptide ligands by signalling protein from porcine mammary gland (SPP-40): Crystal structure of the complex of SPP-40 with a peptide Trp-Pro-Trp at 2.45A resolution [Sus scrofa],1ZBC_A Crystal Structure of the porcine signalling protein liganded with the peptide Trp-Pro-Trp (WPW) at 2.3 A resolution [Sus scrofa]
1HJV_A	5.26e-16	94	415	25	345	Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_B Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_C Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_D Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJW_A Crystal structure of hcgp-39 in complex with chitin octamer [Homo sapiens],1HJW_B Crystal structure of hcgp-39 in complex with chitin octamer [Homo sapiens],1HJX_A Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_B Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_C Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_D Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1NWR_A Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_B Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_C Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_D Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWS_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWT_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWU_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],7CJ2_A Chain A, Chitinase 3-like 1 (Cartilage glycoprotein-39), isoform CRA_a [Homo sapiens],7CJ2_B Chain B, Chitinase 3-like 1 (Cartilage glycoprotein-39), isoform CRA_a [Homo sapiens]
2ESC_A	7.01e-16	88	415	21	344	Crystal structure of a 40 KDa protective signalling protein from Bovine (SPC-40) at 2.1 A resolution [Bos taurus]
1ZBV_A	1.26e-15	88	415	21	344	Crystal Structure of the goat signalling protein (SPG-40) complexed with a designed peptide Trp-Pro-Trp at 3.2A resolution [Capra hircus],1ZBW_A Crystal structure of the complex formed between signalling protein from goat mammary gland (SPG-40) and a tripeptide Trp-Pro-Trp at 2.8A resolution [Capra hircus],1ZU8_A Crystal structure of the goat signalling protein with a bound trisaccharide reveals that Trp78 reduces the carbohydrate binding site to half [Capra hircus],2AOS_A Protein-protein Interactions of protective signalling factor: Crystal structure of ternary complex involving signalling protein from goat (SPG-40), tetrasaccharide and a tripeptide Trp-pro-Trp at 2.9 A resolution [Capra hircus],2B31_A Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 3.1 A resolution reveals large scale conformational changes in the residues of TIM barrel [Capra hircus],2DSZ_A Three dimensional structure of a goat signalling protein secreted during involution [Capra hircus],2DT0_A Crystal structure of the complex of goat signalling protein with the trimer of N-acetylglucosamine at 2.45A resolution [Capra hircus],2DT1_A Crystal Structure Of The Complex Of Goat Signalling Protein With Tetrasaccharide At 2.09 A Resolution [Capra hircus],2DT2_A Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 2.9A resolution [Capra hircus],2DT3_A Crystal structure of the complex formed between goat signalling protein and the hexasaccharide at 2.28 A resolution [Capra hircus],2O92_A Crystal structure of a signalling protein (SPG-40) complex with tetrasaccharide at 3.0A resolution [Capra hircus],2OLH_A Crystal structure of a signalling protein (SPG-40) complex with cellobiose at 2.78 A resolution [Capra hircus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q5RBP6|CH3L1_PONAB	2.70e-16	88	415	69	393	Chitinase-3-like protein 1 OS=Pongo abelii OX=9601 GN=CHI3L1 PE=2 SV=1
sp|P30922|CH3L1_BOVIN	3.17e-15	88	415	42	366	Chitinase-3-like protein 1 OS=Bos taurus OX=9913 GN=CHI3L1 PE=1 SV=3
sp|P36222|CH3L1_HUMAN	3.17e-15	94	415	46	366	Chitinase-3-like protein 1 OS=Homo sapiens OX=9606 GN=CHI3L1 PE=1 SV=2
sp|Q7YS85|CH3L1_BUBBU	7.64e-15	88	415	42	366	Chitinase-3-like protein 1 OS=Bubalus bubalis OX=89462 GN=CHI3L1 PE=1 SV=3
sp|Q29411|CH3L1_PIG	1.84e-14	88	415	42	366	Chitinase-3-like protein 1 OS=Sus scrofa OX=9823 GN=CHI3L1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000020	0.000001

TMHMM  Annotations     

Start	End
12	31