CAZyme Information: NEUDI_83927T0-p1

Basic Information

• Species: Neurospora discreta
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora discreta
• CAZyme ID: NEUDI_83927T0-p1
• CAZy Family: GT2
• CAZyme Description: Defense-related protein containing SCP domain

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
626	NdisFGSC8579_SC010|CGC4	66759.47	6.0978

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_NdiscretaFGSC8579	10345	510953	397	9948

• Gene Location: location=NdisFGSC8579_SC010:798259-800204(-)

Full Sequence      

MHLVSSLLVVGAAFQAVLGLPDPLHEKRNSDIIKRSVDSFIQSETPVALKNLLCNIGSSG
CRVSGAASGVVVASPSKSSPDYWYTWTRDAALVTKHIVDEFTNDYNTTLQNTIQAYVAAQ
AKLQGVSNPSGSLSNGAGLAEPKFMVDLQQFTGDWGRPQRDGPPLRAIALIGYGKWLVSN
GYADTAKNIIWPIVKNDLAYTAQYWNNTGFDLWEEVNSSSFFTIAASHRALVEGSAFAKS
VGSSCSACDAIAPQILCFQQSFWSNSGYIISNFVNYRSGKDINSVLTSIHNFDPAAGCDV
NTFQPCSDRALANHKVVVDSMRFWGVNSGRTAGKAAAVGRYAEDVYYNGNPWYLATLAAA
EQLYDAIYIWKQQGSITVTSTSLAFFKDLVPSVSTGTYPSSSSTYTTIINAVATYADGFI
DVVAQYTPSDGSLAEQFDKNTGAPLSAAHLTWSYASFLSATARRAGIVPPSWGAASANSL
PGSCAASTVAGSYATATATSFPPNLTPASTTVTPPKPTGCAADHEVLVTFNEKVTTSYGQ
TVKVVGSIAALGNWDAAKGASLSINQYSSSNPLWSTTIALPQGTSFKYKYVVVNSDGSVK
WENDPDREFAVTTDCATTATINDTWR

Enzyme Prediction     

EC	3.2.1.3:94	1.14.99.55:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	57	461	8.6e-73	0.9722991689750693
CBM20	527	616	1.8e-25	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	3.48e-156	46	460	1	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	2.65e-48	520	625	1	106	Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
395557	CBM_20	7.02e-38	526	621	1	95	Starch binding domain.
99883	CBM20_alpha_amylase	9.08e-29	526	626	1	95	Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
119437	CBM20	3.06e-28	528	625	2	96	The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAB91426.1|CBM20|GH15|3.2.1.3	0.0	1	626	1	626
AAE15057.1|CBM20|GH15|3.2.1.3	0.0	1	626	1	626
AAE15056.1|CBM20|GH15|3.2.1.3	0.0	1	626	1	626
CAA47707.1|CBM20|GH15|3.2.1.3	0.0	1	626	1	625
AEO61583.1|CBM20|GH15|3.2.1.3	7.78e-284	1	626	1	628

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	7.39e-266	36	626	1	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	1.20e-234	36	626	2	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	3.30e-206	40	626	11	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
3EQA_A	8.64e-203	36	502	2	467	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1AGM_A	1.22e-202	36	502	2	466	Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P14804|AMYG_NEUCR	0.0	1	626	1	626	Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
sp|P69327|AMYG_ASPAW	7.07e-234	13	626	2	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	7.07e-234	13	626	2	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P22832|AMYG_ASPUS	1.94e-233	13	626	2	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	2.24e-232	13	626	2	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000266	0.999711	CS pos: 19-20. Pr: 0.9826

TMHMM  Annotations     

There is no transmembrane helices in NEUDI_83927T0-p1.