CAZyme Information: CIMG_11964-t26_1-p1

Basic Information

• Species: Coccidioides immitis
• Lineage: Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides immitis
• CAZyme ID: CIMG_11964-t26_1-p1
• CAZy Family: GT62
• CAZyme Description: (Trans)glycosidases superfamily protein, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
269	GG704912|CGC17	30317.60	6.0727

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CimmitisRS	9905	246410	148	9757

• Gene Location: location=GG704912:5204426-5205357(+)

Full Sequence      

MQQCNKIDPENINMDGLTHLFLAFAGINPSNFEVSLANPAHEDLCTRLVHKNSNICEIWI
ALGGWAFTDVDTTKKTWSELASCSNSHQRFIASVKVFMAKYKLKGIDIDWEYPGTPERNG
QPDDTKNLVSLVKEMHAAFRTMEDYVDFFGLITYDLHGAWNNSGYYGHKIAGHINISEIQ
NMISLLWYAKINPAKINLGLAYYGQGYTLQDPSCNWAGCQWTGLSDAGSCTMTRGVMLLQ
EIETLISEKGIQLQLLQKKMMKQITFGDQ

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	7	234	8.4e-33	0.6385135135135135

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.23e-43	2	246	11	279	Glyco_18 domain.
119357	GH18_zymocin_alpha	2.48e-42	4	250	15	291	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	2.14e-41	6	242	17	282	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	8.70e-36	15	215	21	235	Glycosyl hydrolases family 18.
119365	GH18_chitinase	4.09e-31	9	210	18	272	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
EGX44068.1|GH18	5.48e-70	4	269	120	408
CDP30264.1|CBM18|GH18	1.95e-65	4	269	232	522
CAP65874.1|CBM18|GH18	1.95e-65	4	269	232	522
CEI60137.1|CBM18|GH18	1.23e-64	4	269	186	476
CAE7012155.1|CBM18|GH18	2.82e-64	4	269	84	373

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2YBT_A	2.16e-22	9	252	26	299	Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_B Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_C Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_D Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_E Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_F Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBU_A Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_B Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_C Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_D Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_E Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_F Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens]
6JM7_A	2.42e-22	6	250	22	297	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
3FXY_A	2.46e-22	9	252	22	295	Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_B Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_C Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_D Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FY1_A The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3FY1_B The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3RM4_A AMCase in complex with Compound 1 [Homo sapiens],3RM4_B AMCase in complex with Compound 1 [Homo sapiens],3RM8_A AMCase in complex with Compound 2 [Homo sapiens],3RM8_B AMCase in complex with Compound 2 [Homo sapiens],3RM9_A AMCase in complex with Compound 3 [Homo sapiens],3RM9_B AMCase in complex with Compound 3 [Homo sapiens],3RME_A AMCase in complex with Compound 5 [Homo sapiens],3RME_B AMCase in complex with Compound 5 [Homo sapiens]
6JM8_A	3.05e-21	6	250	22	297	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
1HKK_A	5.08e-19	9	242	22	285	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|Q6RY07|CHIA_RAT	9.49e-23	9	252	43	316	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q91XA9|CHIA_MOUSE	1.30e-22	9	246	43	310	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q9BZP6|CHIA_HUMAN	7.48e-21	9	252	43	316	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
sp|Q91Z98|CHIL4_MOUSE	3.45e-18	9	248	43	312	Chitinase-like protein 4 OS=Mus musculus OX=10090 GN=Chil4 PE=1 SV=2
sp|Q13231|CHIT1_HUMAN	4.61e-18	9	242	43	306	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
1.000073	0.000003

TMHMM  Annotations     

There is no transmembrane helices in CIMG_11964-t26_1-p1.