CAZyme Information: PV06_10201-t43_1-p1

Basic Information

• Species: Exophiala oligosperma
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala oligosperma
• CAZyme ID: PV06_10201-t43_1-p1
• CAZy Family: GT25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
664	KN847343.1|CGC5	72201.19	4.4450

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EoligospermaCBS72588	11938	N/A	45	11893

• Gene Location: location=KN847343.1:154049-156428(+)

Full Sequence      

MAVHSLRSQNDGGIGVLVVLFLWCFQHALAQTGSVYQLDSEYSGTNFFDGWDFFTGGDPT
GGFVTYYSRSSAQLAGMINSSSSQPTYIGSDYTTLIGNPNGAGRPSVRISTKRSWTHGLF
IGDFNHSPAGICGTWPAFWTLGPNWPYNGEIDIMEGANLNTYNGMTLHASPNCTIAGDSR
LMSGQLQSSNCAYYVSQPPNYNVGCSISDRRSQSYGTNFNTGGGGVYAMQWTSDYIAVWF
FPRGSIPADITNKTPNPSGWGLPAAEFQGSCQIDQKFQAHKIVMNNAFCGEYAGASTVWN
SSTNSCAASTGYATCNAYVAGQPGAFQNAYWSINSVRVYQLVDSGSSATSSSPYIASLQP
TSTISTTTGSTPTPTPTTALCPGYNFTVVQLGAFSYEIECGVNPGGHDIGAPYSGFQVNS
FEDCIAGCSYWNANISANYCAAVTYQFSSKACYWKKDCYAQPANAAYNGARLIYYAYPQV
TDDPRSQTLTSSSTSYVQTTPTPNTWRYIFFIKFDVERLDQPNNIDLIGITSDIVIVVDH
NCTVTVIHDGIGSGQYFINSTVGHEFHCDYRESINTGTFVFEFDNHFDIGFTFYNHSSAD
NSNSDFDYGDTAFTIKHDIGHGTQLDNDKAYAIQYDSSGGNELNDDDGVCCAVLIYYESS
PIFY

Enzyme Prediction     

EC	3.2.1.73:4	3.2.1.6:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	81	319	2.3e-82	0.9650655021834061

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185690	GH16_fungal_Lam16A_glucanase	2.85e-133	36	340	2	293	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	6.86e-12	41	295	4	216	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	2.73e-07	106	179	70	155	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	0.001	135	239	130	222	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA14232.1|GH16_1	2.14e-103	36	353	26	331
ATZ47441.1|GH16_1	4.81e-102	30	353	22	331
CCD50201.1|GH16_1	6.42e-102	30	353	22	331
ATZ47442.1|GH16_1	1.27e-101	30	353	22	331
QSZ31977.1|GH16_1	2.92e-100	16	355	7	333

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WDU_A	6.02e-82	36	339	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	6.22e-82	36	339	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	4.47e-81	36	339	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	4.77e-81	36	339	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	1.58e-72	36	339	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|B0XTU6|EGLX_ASPFC	2.71e-83	14	357	10	344	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	2.71e-83	14	357	10	344	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
sp|A1C7B5|EGLX_ASPCL	1.11e-81	29	357	26	345	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	2.02e-81	14	357	10	344	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|A2QBQ3|EGLX_ASPNC	1.83e-78	29	365	20	346	Probable endo-1,3(4)-beta-glucanase An02g00850 OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=An02g00850 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000432	0.999531	CS pos: 30-31. Pr: 0.9748

TMHMM  Annotations     

Start	End
13	30