CAZyme Information: TRIREDRAFT_53731-t26_1-p1

Basic Information

• Species: Trichoderma reesei
• Lineage: Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma reesei
• CAZyme ID: TRIREDRAFT_53731-t26_1-p1
• CAZy Family: GH2
• CAZyme Description: glycoside hydrolase family 16

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
407	GL985056|CGC18	46444.20	6.1816

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=GL985056:417719-418942(+)

Full Sequence      

MLFLLLPAVLYLVFLWLREQDLNAKWQPDRESLLFNRKPLPAPLERTWISSYKLPLRTEG
RSIVDTDGRRFKLSSINWYGASDELFVPGGLDVQHRSVIAETIKKMGFNSVRLPYADELV
MKNPVIEPGLVLANPDLQGLRAMDILEAVTTALTDAGIAVIINNHITRATWCCGADPCDA
GWANDHLGPLCAVKQTEEEWIQHWEEVMGRFVHNPLVIGADLRNEVRGLWGTMPWSKWAA
AAENCGNRLLKMKSDWLIIVEGTESANDVSGALDRPVRLDVENRVVYSAHGYKWSGWGSW
QGRFAQRSYKSFVKTMRRNWAYLLEVDIAPVWFGELGAPSNPSVGDVHYWSNLMRYLKSI
DADLGYWALNPRKPKGNEKETYSLVEDDWVTPVLDYRMKDLQELIRQ

Enzyme Prediction     

No EC number prediction in TRIREDRAFT_53731-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	63	377	1.1e-158	0.9968253968253968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395098	Cellulase	8.10e-26	99	371	29	270	Cellulase (glycosyl hydrolase family 5).
225344	BglC	4.43e-13	101	396	80	383	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ55077.1|GH5_24	1.75e-282	1	407	91	497
QYT00999.1|GH5_24	1.61e-280	1	407	90	496
UKZ59514.1|GH5_24	5.03e-277	1	407	99	505
UKZ85745.1|GH5_24	1.95e-274	1	407	99	505
UKZ80856.1|GH5_24	3.64e-257	1	407	91	471

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1VRX_A	1.09e-41	58	391	8	338	Chain A, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]
1ECE_A	1.53e-41	58	391	8	338	Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus],1ECE_B Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus]
3VVG_A	3.69e-26	73	391	30	363	The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_B The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_C The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3W6L_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
2ZUM_A	9.12e-26	73	391	63	396	Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_A Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_B Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_C Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]
3W6M_A	9.47e-26	73	391	30	363	Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23548|GUN_PAEPO	2.36e-43	50	391	33	369	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P54583|GUN1_ACIC1	2.37e-39	58	391	49	379	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|C0HLA0|GH5FP_CHAOB	7.85e-32	51	406	26	399	Glycosyl hydrolase 5 family protein OS=Chamaecyparis obtusa OX=13415 PE=1 SV=1
sp|P50400|GUND_CELFI	1.55e-26	56	391	46	400	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
sp|P10474|GUNB_CALSA	1.17e-24	56	391	630	984	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.991053	0.008961

TMHMM  Annotations     

There is no transmembrane helices in TRIREDRAFT_53731-t26_1-p1.