CAZyme Information: TRIREDRAFT_55886.P177

Basic Information

• Species: Trichoderma reesei
• Lineage: Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma reesei
• CAZyme ID: TRIREDRAFT_55886.P177
• CAZy Family: GH27
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
767	GL985057|CGC3	85018.88	4.2867

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TreeseiQM6a	9138	431241	7	9131

• Gene Location: location=GL985057:945560-948152(-)

Full Sequence      

MAYHLTTSYAGEALLSGFNWFNGVDPSHGFVSYQSRRDAEAMGLYSIDERSGVVRLGVDS
TNEYSLSDRGRPSIRIESKATYDHGLFIADFLHMPPSHCGLWPAFWTYGDNWPYDGEIDI
IEGVNTAHTNILSAHTADGCTQSPTIDGLYSGQLINTECAVGENNIGCGFHPSAEDTSSY
GDGFNAAHGGVYAMEWDSVHIRIWHFARGEIPRDIEEKKPDPETWGLPIAVFGGESCDVD
EYFKRMRLVLNINFCGDYGNAVWGITDQCNAFASTCPEYVASHPEAFANAYWDVRYIDAY
QLRIGGHRPHPGHPKNPDRPHHSDQPDQPDQPDEWNQPDHPDQWDRPDHPSDPDSWRNEQ
VTTTTMTTRWTETVTAYATGYHPHDPQDVDSNDGWRDHVPAHTTAAIEPVATRAPVNPVK
INDYSYLGCFYSSTDFPCFTEVADSLDMTLETCIELCRPRTYAAVFDSHCFCADDLDAGT
RAAKREGLCNRECPGNKLEQCGGLIGPRDNDGPREKFVTDETPRHALTVYAFVAEEKPEQ
PPAMAPGSNGPWRNEGDNWESEDEGTATEVEEVAVFPVSEEDDSKWKGGDWEHDGGDGYA
WSEQWGDWKESQTEKQVKPDITEVVVSVTETVVDCPEGTPTKEAIVIPTWLPPVESKPWV
PSDPSDPPSPPSPPPPEHNDDDYFHHDAAPPPHEDYDQSHHDPLPPPPPPPPAHNGTNNH
FHPSSTSPDSPVNTFVLVAAASMVYGEVGRYFAIMGSGILVVVMGLL

Enzyme Prediction     

No EC number prediction in TRIREDRAFT_55886.P177.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	51	280	5.9e-81	0.9563318777292577

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185690	GH16_fungal_Lam16A_glucanase	5.18e-142	2	301	1	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).
396406	WSC	1.19e-13	427	503	1	80	WSC domain. This domain may be involved in carbohydrate binding.
185693	GH16_laminarinase_like	5.12e-11	96	204	89	175	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.
214616	WSC	4.75e-08	423	503	1	85	present in yeast cell wall integrity and stress response component proteins. Domain present in WSC proteins, polycystin and fungal exoglucanase
185691	GH16_Strep_laminarinase_like	1.77e-06	73	135	70	148	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYS93645.1|GH16_1	3.49e-300	1	764	1	764
UKZ47266.1|GH16_1	3.05e-297	1	664	1	682
UKZ73836.1|GH16_1	3.47e-282	1	595	1	543
UKZ85129.1|GH16_1	2.26e-266	1	663	1	658
UKZ60234.1|GH16_1	5.79e-266	1	664	1	644

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JVV_A	1.04e-80	2	300	2	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']
3WDU_A	2.77e-80	3	300	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	2.86e-80	3	300	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	2.01e-79	3	300	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	2.14e-79	3	300	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']

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B8N7S7|EGLX_ASPFN	5.32e-79	3	305	31	330	Probable endo-1,3(4)-beta-glucanase AFLA_105200 OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=AFLA_105200 PE=3 SV=1
sp|Q2UIE6|EGLX_ASPOR	7.39e-79	3	305	31	330	Probable endo-1,3(4)-beta-glucanase AO090023000083 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=AO090023000083 PE=3 SV=1
sp|D4AJR9|EGLX_ARTBC	4.95e-73	3	309	20	323	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|Q9USW3|YHZ7_SCHPO	1.30e-71	3	301	129	418	Probable glycosidase C21B10.07 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPBC21B10.07 PE=3 SV=1
sp|Q5BAP5|EGLX_EMENI	2.85e-71	3	302	29	325	Endo-1,3(4)-beta-glucanase xgeA OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=xgeA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000028	0.000004

TMHMM  Annotations     

There is no transmembrane helices in TRIREDRAFT_55886.P177.