CAZyme Information: CPAG_03935-t26_1-p1

Basic Information

• Species: Coccidioides posadasii
• Lineage: Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides posadasii
• CAZyme ID: CPAG_03935-t26_1-p1
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
355		39591.73	5.3393

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CposadasiiRMSCC3488	10016	454284	119	9897

• Gene Location: location=DS268110:2828575-2829667(+)

Full Sequence      

MNSTILSMVQVRYYISLRLYQSSLFFVYPMVNIFLLFVSALLWHEAVAVYELVDSYAGNT
FFSNFTFFTEPDPTQGFVKYIGEPEARKNGLIGFSSSYSGDNMAWMSVDRTNVAPMGRES
VRITSKKVYNQGLFIVDIAHVPTTTCGTWPAFWMYGPDWPHGGEIDIYEGVNLEYQNSMT
LHTGPGCTVSRHAESTGRMTTTNCDVAAAGQKPNEGCKVRSQDPLSFGAGLNAVAGGMYA
TEWTVDAIKIWFFPRTFQIPYDITQGTPDPNTWGLPTAHFAGNCSFTNSFKDLRIVINTT
FCGQWAGQVWGKSPCASVTSTCEEFVANYPEAFLQSYWAINSIKVYEKKPGWESA

Enzyme Prediction     

No EC number prediction in CPAG_03935-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	100	326	5e-87	0.9606986899563319

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185690	GH16_fungal_Lam16A_glucanase	1.81e-152	50	346	2	292	fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Group of fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Lam16A belongs to the 'nonspecific' 1,3(4)-beta-glucanase subfamily, although beta-1,6 branching and beta-1,4 bonds specifically define where Lam16A hydrolyzes its substrates, like curdlan (beta-1,3-glucan), lichenin (beta-1,3-1,4-mixed linkage glucan), and laminarin (beta-1,6-branched-1,3-glucan).
185693	GH16_laminarinase_like	2.65e-12	120	314	66	222	Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
185691	GH16_Strep_laminarinase_like	6.30e-08	147	204	106	169	Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel.
185694	GH16_CCF	3.52e-04	149	273	130	239	Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
395585	Glyco_hydro_16	0.002	122	167	24	67	Glycosyl hydrolases family 16.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVM11556.1|GH16_1	1.05e-236	30	335	1	306
BCS08185.1|GH16_1	3.35e-119	48	347	20	315
BCR95648.1|GH16_1	3.35e-119	48	347	20	315
CAK36992.1|GH16_1	1.76e-116	48	347	24	318
AUW31128.1|GH16_1	1.07e-114	38	348	5	314

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WDU_A	1.27e-97	50	346	2	295	The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_B The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_C The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_D The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila']
3WDT_A	1.31e-97	50	346	3	296	The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_B The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_C The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_D The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDV_A The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_B The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_C The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_D The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila']
3WDY_A	9.89e-97	50	346	1	294	The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_B The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_C The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_D The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila']
3WDW_A	1.06e-96	50	346	3	296	The apo-form structure of E113A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDW_B The apo-form structure of E113A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDX_A The complex structure of E113A with glucotriose [Paecilomyces sp. 'thermophila'],3WDX_B The complex structure of E113A with glucotriose [Paecilomyces sp. 'thermophila']
5JVV_A	3.68e-81	50	346	3	297	Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase [Paecilomyces sp. 'thermophila'],5JVV_B Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase [Paecilomyces sp. 'thermophila']

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4AJR9|EGLX_ARTBC	3.01e-90	48	348	18	316	Endo-1,3(4)-beta-glucanase ARB_04519 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_04519 PE=3 SV=1
sp|A1C7B5|EGLX_ASPCL	3.10e-85	50	347	33	328	Probable endo-1,3(4)-beta-glucanase ACLA_073210 OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=ACLA_073210 PE=3 SV=1
sp|A1DHY9|EGLX_NEOFI	2.40e-83	50	347	32	327	Probable endo-1,3(4)-beta-glucanase NFIA_089530 OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=NFIA_089530 PE=3 SV=1
sp|B0XTU6|EGLX_ASPFC	6.80e-83	50	347	32	327	Probable endo-1,3(4)-beta-glucanase AFUB_029980 OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=AFUB_029980 PE=3 SV=1
sp|Q4X084|EGLX_ASPFU	6.80e-83	50	347	32	327	Probable endo-1,3(4)-beta-glucanase AFUA_2G14360 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=AFUA_2G14360 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000032	0.000003

TMHMM  Annotations     

Start	End
21	43