CAZyme Information: NEUTE1DRAFT_72302-t26_1-p1

Basic Information

• Species: Neurospora tetrasperma
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora tetrasperma
• CAZyme ID: NEUTE1DRAFT_72302-t26_1-p1
• CAZy Family: GH76
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
396	GL891382|CGC6	44535.52	5.8211

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_NtetraspermaFGSC2508	10380	510951	0	10380

• Gene Location: location=GL891382:4807849-4809039(-)

Full Sequence      

MWKAEAALSKPWKPDDSSLAFSKRPLPPPSNETFLSSAGYKLPLRTKGRDIVDQNGKRFK
LSSVNWYGASDELFIPGGLDVQHRDVIASTIRSLGFNSVRMPYSDEMVISNPEVPLRLLA
ANQDLVGKRALDVFEATVTALTDAGLAVIVNNHITTATWCCGADPCDAGWANDFLPGSLC
RVRQTEAEWIDHWVTVMTRFVDNPLVIGADLRNEVRGLWGTMPWERWAAAAERAGNALLR
INPDWLIIVGGTESGNDLTGVRRRPVELDVANRLVYSAHVYSWSGWGSMGGRYSKRTYAS
FVKAMRQNWGYLVEENLAPVWIGEFGAPDRPGIGDANYWQNLLRYLKAIDADFGYWAINP
RKPKDNEKESYSLVEDDWVTPVLDYRMKDMTELMRQ

Enzyme Prediction     

No EC number prediction in NEUTE1DRAFT_72302-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	51	365	1.4e-156	0.9936507936507937

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395098	Cellulase	7.18e-24	52	360	1	270	Cellulase (glycosyl hydrolase family 5).
225344	BglC	1.68e-09	90	385	81	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
EAA35171.3|GH5_24	6.49e-298	1	396	83	478
AEO70062.1|GH5_24	4.73e-239	4	395	20	411
APD14599.1|GH5_24	1.29e-236	1	395	18	412
AEO53175.1|GH5_24	6.12e-229	1	395	21	415
UQC80596.1|GH5_24	1.08e-228	1	395	121	512

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ECE_A	4.53e-49	46	380	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]
1VRX_A	1.24e-48	46	380	8	338	Chain A, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]
3VVG_A	1.42e-28	61	380	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]
3W6M_A	3.69e-28	61	380	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]
2ZUM_A	3.93e-28	61	380	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23548|GUN_PAEPO	1.71e-52	37	380	32	369	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P54583|GUN1_ACIC1	1.25e-46	46	380	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	3.81e-33	35	378	22	379	Glycosyl hydrolase 5 family protein OS=Chamaecyparis obtusa OX=13415 PE=1 SV=1
sp|P50400|GUND_CELFI	3.14e-26	44	380	46	400	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
sp|P19487|GUNA_XANCP	3.62e-25	49	380	32	356	Major extracellular endoglucanase OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=engXCA PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000069	0.000001

TMHMM  Annotations     

There is no transmembrane helices in NEUTE1DRAFT_72302-t26_1-p1.