CAZyme Information: ACLA_049360-t26_1-p1

Basic Information

• Species: Aspergillus clavatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus
• CAZyme ID: ACLA_049360-t26_1-p1
• CAZy Family: GH20
• CAZyme Description: Glycosyl hydrolase, family 15, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
630		68618.29	5.8027

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AclavatusNRRL1	9428	344612	287	9141

• Gene Location: location=DS027054:1234260-1236452(+)

Full Sequence      

MRMKQFLTISSGLLTVVCGHLNDNPAQIVIAGGAIIPETTDPIESWLNMEIPYAFDGVLN
NIGPDGAKATGAGSGIVIASPSHSNPDYYYTWTRDAALTIKYLVESLASDDDPGLRRIIE
RYITSQAHLQTISNPSGSLSSGGLGEPKLRADGSAFHGPWGRPQRDGPALRATALIAYAN
LLIDHGKSSTAYSTVWPIIQNDLSYVTEFWNATTFDLWEEVRGSSFFTTAVQYQALVQGA
SLAQKLGDSCPHCQTQAPQILCFLQTFWTGSSILANFGSDRSGKDANSLLGTIHTFDPNA
GCDEHTFQPCSSRALANHKVVVDSFRSLYPINSDISPGQAVAIGRYPEDVYQGGHPWYLC
TLAAAEQLYDALYQWELMGNLSISDMSLVFFRDLYPSTATGTYSRGTDTFAAVTAAVKVY
ADGFLRIIQKYTPSTGALAEQFSRSDGSPLSALDLTWSYAALLTAHRARERALVLNPTTT
SPPRSPSSTIPPPLPRTCTPSSAKGPYVPVTNVTWPRPTCLTPPRTVAVRFNVLASTVFG
EDILLVGSIPELGEWDVRNQGLKLNANAYSGVTPLWYRTVMLQSGVDFEFKFVRVNRDGE
VRWEEGLNRESVVPRECGVVNATINAVWRS

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	59	465	8.3e-81	0.9806094182825484
CBM20	527	617	9.5e-23	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	9.24e-131	56	465	5	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	1.31e-37	522	628	2	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	2.73e-33	527	623	1	95	Starch binding domain.
119437	CBM20	5.25e-25	529	628	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.
99883	CBM20_alpha_amylase	2.22e-21	527	629	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAC28076.1|CBM20|GH15|3.2.1.3	3.42e-247	31	629	20	618
ABH92242.1|CBM20|GH15|3.2.1.3	3.42e-247	31	629	20	618
CAY05394.1|CBM20|GH15|3.2.1.3	3.42e-247	31	629	20	618
AAR61400.1|CBM20|GH15|3.2.1.3	3.42e-247	31	629	20	618
ABH92239.1|CBM20|GH15|3.2.1.3	8.66e-246	40	629	2	591

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FRV_A	1.12e-223	43	629	3	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1AGM_A	7.51e-200	43	516	3	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]
1GAH_A	7.79e-200	43	516	3	466	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1GAI_A	8.07e-200	43	516	3	466	GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]
6FHV_A	2.78e-198	46	629	11	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P22832|AMYG_ASPUS	1.12e-228	28	629	12	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	2.58e-227	28	629	12	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P36914|AMYG_ASPOR	1.08e-224	29	629	17	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P69327|AMYG_ASPAW	4.63e-223	28	629	12	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	4.63e-223	28	629	12	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000001	1.000052	CS pos: 17-18. Pr: 0.9852

TMHMM  Annotations     

There is no transmembrane helices in ACLA_049360-t26_1-p1.