CAZyme Information: ATY66444.1

Basic Information

• Species: Cordyceps militaris
• Lineage: Ascomycota; Sordariomycetes; ; Cordycipitaceae; Cordyceps; Cordyceps militaris
• CAZyme ID: ATY66444.1
• CAZy Family: GT22
• CAZyme Description: bacteriodes thetaiotaomicron symbiotic

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
808	CP023327|CGC6	88202.93	4.9918

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CmilitarisATCC34164	9362	N/A	75	9287

• Gene Location: location=CP023327:2474358-2477165(+)

Full Sequence      

MAPRSFTQVARLLALAATQLSFAHSLVNNNTHSLAQNNTHHNETHAQNSVSKTSASRLGL
HGLDAAAADKPGQDDHTCGPDRPCKNKACCGKSGWCGYSPDFCGTGCQSNCDAKAECGQY
ASPQGKTCPLNVCCSEFGFCGTTTEFCAPGCQSYCNQPKPPGGSGNDVRTRVIGYWESWN
SQHPCGRMGLDEIPVELLTHLNVAFGYISEDFRITNMDGIRDDLYRNMGNVKARNPALKI
SIALGGWTFNDPGPWQNRFSQVVATENSRATFIKNLLGFLSEYGYDGVDWEYPGADDRGG
TDADPVKYVVLLKKLRAAISASGHDYIVTFTAPSSYWYLRHFRVKEMEAYVDWINLMSYD
IHGVWDGNNPIGNHILAHTNLTEIDLALDSFWRVGVAPSSIVLGLGFYGRSFTLSDTSCW
KPGCLFSGPGAAGECTATAGILSYREIQQVLQKSGATAYLDTDAAAKYVVYDKNSWISFD
DAETFELKIQYANKIGLGGLMIWAIDLDDGDLSALEAVTSVKSGVNRKFDLTALGNLFPK
ELLPPPDADVNYGLMTFGRDGQDGYSNPRDHAFGFILVAGEKHVVSSLQKRDGFPEPITF
LDCPTDIGSAPDNSTHTARVVCLNEDVKGCFQLLEGGIEGTVLQMPDECGRGSLGRAIAM
EASKDQSIPAYILAGKQATSEVFDLLFDFDVMLMRRDSEKTSIRIDVTNAADYWDSIDDS
PGIQSRDLHERFFAPESLQWKQRFDSANVSYKSDAAIKVKKDIDISYLWHSAKECTVASG
NGFIEGLAAYVSGALDILLTYGFSAIVK

Enzyme Prediction     

No EC number prediction in ATY66444.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	169	514	8.6e-67	0.9594594594594594

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	3.36e-90	171	508	1	334	Glyco_18 domain.
119357	GH18_zymocin_alpha	3.50e-84	173	508	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.
119351	GH18_chitolectin_chitotriosidase	7.26e-82	172	509	1	342	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.
395573	Glyco_hydro_18	1.97e-71	171	508	1	307	Glycosyl hydrolases family 18.
119365	GH18_chitinase	7.27e-67	172	508	1	322	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
ATY66444.1|CBM18|GH18	0.0	1	808	1	808
UKZ58390.1|CBM18|GH18	6.10e-303	64	806	74	822
QGJ02191.1|CBM18|GH18	5.34e-302	65	806	50	791
QGI71298.1|CBM18|GH18	5.34e-302	65	806	50	791
QGI88633.1|CBM18|GH18	5.34e-302	65	806	50	791

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1WAW_A	9.17e-53	171	580	2	422	Chain A, CHITOTRIOSIDASE 1 [Homo sapiens],1WB0_A specificity and affinity of natural product cyclopentapeptide inhibitor Argifin against human chitinase [Homo sapiens]
5HBF_A	1.98e-52	171	580	23	443	Crystal structure of human full-length chitotriosidase (CHIT1) [Homo sapiens],5HBF_B Crystal structure of human full-length chitotriosidase (CHIT1) [Homo sapiens]
1HKK_A	1.40e-50	171	509	2	343	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1LG1_A	1.44e-50	171	509	2	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]
1HKI_A	1.44e-50	171	509	2	343	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q13231|CHIT1_HUMAN	7.53e-52	171	580	23	443	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q6RY07|CHIA_RAT	2.72e-47	172	539	24	397	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q91XA9|CHIA_MOUSE	6.93e-47	172	509	24	366	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q9D7Q1|CHIT1_MOUSE	1.08e-46	171	572	23	433	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|Q95M17|CHIA_BOVIN	4.38e-46	171	509	23	366	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.156920	0.843036	CS pos: 23-24. Pr: 0.8149

TMHMM  Annotations     

There is no transmembrane helices in ATY66444.1.