CAZyme Information: ASPCADRAFT_33395-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_33395-t33_1-p1
• CAZy Family: GH63
• CAZyme Description: glycoside hydrolase family 18 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
553	KV907504|CGC9	59468.85	3.8357

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcarbonariusITEM5010	11735	602072	260	11475

• Gene Location: location=KV907504:132837-134495(-)

Full Sequence      

TCSYVKVVSGDSCASLVEECGISADEFYDYNPSSDLCSTLVAGQYVCCSSGTLPNFAPSA
YANGTCYTYNVVSGDTCSALAATYSLTADKIDNFNSDTWGWYGCDDLQAGQAICLSDGNP
PFPVALANAVCGPQVPDTSFANVTVGDWPTMNPCPLNACCDTWGQCGATPDYCNDTLAAT
GAPGTAPPGSNGCISNCGTTIVNTAITPSSYSAIGYFDASNVERPCLQMNAFSISPQKFT
HVHFAFGNITSNFSISIAGAEEQFTYFRKLKDMKRIISFGGWEFSTSPETYMIFREGVSA
AHRDTLVQNIVSFLDEYDLDSVDIDWEYPGEPDIPGIPAGSDDEGSNYLKFLVALREALP
SKSISITASASYWYLKAFPIAEMVEVVDYIVFMTYDLHGTWDLGDKYADSGCPAGDCLFS
HVNLTETVWALSMISKAPAATSSIMVGVASYGRSFEMASAGCYSSSCTWTAEEAPGPCTQ
TTGFISNAEINQILAENSDAERIFDEGSDSDILVYNETQWVGYMTNTTKSTRAAFYERFN
FAGTSEWAIGLEE

Enzyme Prediction     

EC	3.2.1.14:3	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	211	550	3.2e-49	0.9290540540540541

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	2.66e-178	214	552	3	345	Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
214753	Glyco_18	2.04e-57	214	551	3	333	Glyco_18 domain.
395573	Glyco_hydro_18	5.67e-49	214	550	3	305	Glycosyl hydrolases family 18.
119365	GH18_chitinase	1.49e-38	233	456	20	267	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.
119349	GH18_chitinase-like	4.44e-35	214	397	2	178	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS25711.1|CBM18|CBM50|GH18	1.18e-207	1	552	282	836
AEO70565.1|CBM18|CBM50|GH18	3.69e-206	2	552	303	857
QGA14670.1|CBM18|CBM50|GH18	6.21e-206	2	553	311	868
UKZ79393.1|CBM18|CBM50|GH18	1.96e-205	2	551	329	886
UKZ53593.1|CBM18|CBM50|GH18	5.22e-205	2	551	329	886

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1LG1_A	6.64e-24	234	553	25	343	Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
1GUV_A	6.74e-24	234	553	25	343	Structure of human chitotriosidase [Homo sapiens]
4WJX_A	7.81e-24	234	553	25	343	Crystal structure of human chitotriosidase-1 catalytic domain at 1.0 A resolution [Homo sapiens],4WK9_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (0.3mM) at 1.10 A resolution [Homo sapiens],4WKA_A Crystal structure of human chitotriosidase-1 catalytic domain at 0.95 A resolution [Homo sapiens],4WKF_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (2.5mM) at 1.10 A resolution [Homo sapiens],4WKH_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (1mM) at 1.05 A resolution [Homo sapiens],5NR8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7a [Homo sapiens],5NRA_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7g [Homo sapiens],5NRF_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7i [Homo sapiens]
6JJR_A	8.23e-24	234	553	25	343	Crystal structure of human chitotriosidase-1 (hChit1) catalytic domain in complex with compound 2-8-14 [Homo sapiens],6JK6_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 2-8-s2 [Homo sapiens]
1HKK_A	1.20e-23	234	553	25	343	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	8.99e-109	1	548	192	708	Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	1.20e-25	209	553	20	366	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q6RY07|CHIA_RAT	3.94e-25	209	553	20	366	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q95M17|CHIA_BOVIN	5.63e-24	209	553	20	366	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q13231|CHIT1_HUMAN	1.02e-22	234	553	46	364	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000006	0.000047

TMHMM  Annotations     

There is no transmembrane helices in ASPCADRAFT_33395-t33_1-p1.