CAZyme Information: ASPCADRAFT_2151-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_2151-t33_1-p1
• CAZy Family: GH55
• CAZyme Description: glycoside hydrolase family 18 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
873	KV907495|CGC10	95493.89	4.1483

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=KV907495:778037-781268(-)

Full Sequence      

MGWAGCLRLQKGQRICLSEGTPPFPAPMENALCGPQVPGTTQPSGMAASNWTNLNPCPLN
ACCDIWGQCGISDEFCTNDPADTGAPGTAKNGTNGCISNCGTNITNNEDQPSSIKRIGYF
ESWNLDRPCLNMDISKFQGNDYYTHVHWAFANITTDWEVDVSGDQDQFNGLLNLTGMNRI
LSFGGWGFSTTSYTYSILRDGVMDGNRQTLAKNIANFIVDHDLDGVDFDWEYPGAQDIPG
IPADSPKSPERYLEFLKLLRSELPSSKSLSIAAPASYWYLKNFPIKDMAAVVDYIVYMTY
DLHGQWDYQRTYADSGCPDGGCLRSQVNKTETAYALSMITKAGVPAKQVVAGLALYGRSF
KMENPSCSGPECHFTGPESGAEPGSCTQTAGYLSNYEIYQIIGQADNPEVYGNISITQYQ
DEGDVLIYDEDNWVSWLSPSSYASRRSWTGGLNFAGTSDWAVDLNQTYASNGTGEAVSND
VEDNYQICDYSKAYSSLDALSTASGGLRSDCIALYALQVLIDMLDVAYANYTAVNNGYNE
LFSYYVTYMEDMVPKVLIDDFMFNKSTTTEWMTFPSLGYGMDYFTCKLGNGDEIPCTEIN
GTNVREEIEEKATTLILSDHKAYDTALTNAGIDEDWVEYSTYTYTLDFVQPHASRRFEYK
FADFPTKNASMVVPNPKDIVTEGIGSIPALRTAMQATLLDIMLGQWTNGSVSDAAQAYSV
PVFLLMQAIDDMETAKKLGAEEKKEEEEEEKRKKDFILLIVSVVLMFVPVIGEEAAAAAG
LADLARGIAIAGEAGNGALALYDTVEDPSSAVVNIIGMLFGVGSIAKVARDGKGLASVAK
LRREMSANEVASLGSIFKENDVVLQTIMKVCRE

Enzyme Prediction     

EC	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	115	467	3.9e-52	0.9391891891891891

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	0.0	115	464	1	344	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	2.03e-55	115	464	1	333	Glyco_18 domain.
395573	Glyco_hydro_18	2.54e-47	115	463	1	305	Glycosyl hydrolases family 18.
119365	GH18_chitinase	5.06e-43	117	361	2	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.
119351	GH18_chitolectin_chitotriosidase	4.47e-40	119	464	4	340	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX55440.1|CBM18|GH18	0.0	46	872	1	820
BCS30629.1|CBM18|CBM50|GH18	0.0	2	872	104	980
UPK95779.1|CBM18|CBM50|GH18	1.98e-192	2	869	389	1251
QKX54053.1|CBM18|CBM50|GH18	9.48e-192	2	869	358	1233
QGA13088.1|CBM18|CBM50|GH18	4.31e-189	2	869	415	1289

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUS_A	3.31e-27	119	475	7	352	Crystal structure of a insect group III chitinase (CAD2) from Ostrinia furnacalis [Ostrinia furnacalis],5WVH_A Crystal structure of an insect group III chitinase complex with (GlcNAc)6 (CAD2-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
1HKK_A	4.90e-27	115	464	2	341	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	4.99e-27	115	464	2	341	Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]
1LG1_A	6.72e-27	115	464	2	341	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	6.84e-27	115	464	2	341	Structure of human chitotriosidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	3.38e-87	2	463	288	710	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|Q13231|CHIT1_HUMAN	4.39e-26	112	464	20	362	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	8.52e-26	112	464	20	364	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q6RY07|CHIA_RAT	6.55e-25	112	464	20	364	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q9BZP6|CHIA_HUMAN	9.04e-25	119	478	27	381	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000039	0.000003

TMHMM  Annotations     

There is no transmembrane helices in ASPCADRAFT_2151-t33_1-p1.