CAZyme Information: CLCR_11364-t43_1-p1

Basic Information

• Species: Cladophialophora carrionii
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora carrionii
• CAZyme ID: CLCR_11364-t43_1-p1
• CAZy Family: GT8
• CAZyme Description: Glucoamylase P

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
626	LGRB01000009|CGC13	67831.85	4.6623

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CcarrioniiKSF	11240	N/A	59	11181

• Gene Location: location=LGRB01000009:2825918-2827947(+)

Full Sequence      

MSWLTPALLTLTVLALGEASPFDMQNVERRQGADALSAFIAQEQAISIQGVLSNIGGLNS
SLVNGASPGVVVASPSTVNPDYFYTWTRDSALTYTMLIDELIFGNLTLRTTIEDYTAAQA
VLQTVTNPSGSLWPAGDGLGEAKFYTNLTRYDGTWGRPQRDGPALRAIAFMTLAPVLFHL
NETDLYKQIYWPLVLNDLRYVGQYWNQTGYDLWEEVHGSSFFTIANQHKALVQGALLAEQ
LNTTCRPCAQAPQLLCFLQNNFWNASGGYLTANINANQVVRSGINSDPILASISVFDANA
TCDAGDFQPCNSKVLATHKALVDSFRALYPINNNASAPNAVLVGRYPEDTYYGGNPWPLC
TFAAAEVLYDAVHQINRTGTLTVDNDSLAFFQDISPNITAGNYTGTALTGILANMTTYAD
GFVSAVQQYLPPNGSISEQFNRTTGESTSASKLTWSFASFVTMARRRAGQYPNSWGAWHP
LANTNLTATQCRATSFNATGAYTPALAAGAPNITKDCASEVIFSVNASTQFGQDVYILGN
VTKLGGALNNADNIILPLNTGNITSDSPQWYVDIWLRADQTVGYQYVLQNGSDWVFEGGP
VRTVRVPACGSGRPVRTNDSFRFPSS

Enzyme Prediction     

EC	3.2.1.3:94

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	63	464	2.4e-75	0.9556786703601108

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	3.80e-117	45	465	1	417	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	5.55e-14	521	609	9	95	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.
99883	CBM20_alpha_amylase	1.03e-12	519	622	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.
395557	CBM_20	2.94e-12	521	612	3	91	Starch binding domain.
119437	CBM20	3.24e-12	521	611	2	89	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
APA13257.1|CBM20|GH15	2.86e-191	36	612	32	597
CAA47945.1|CBM20|GH15|3.2.1.3	8.51e-188	36	624	31	609
CAA48243.1|CBM20|GH15|3.2.1.3	8.51e-188	36	624	31	609
CAY05396.1|CBM20|GH15|3.2.1.3	8.51e-188	36	624	31	609
UQC75847.1|CBM20|GH15	1.07e-184	26	621	16	604

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FHW_A	2.94e-189	36	624	31	609	Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
2VN4_A	2.67e-158	39	622	5	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FHV_A	1.29e-157	36	623	8	594	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
6FRV_A	2.35e-152	36	622	3	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
3EQA_A	3.56e-144	36	513	3	469	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q03045|AMYG_AMORE	1.51e-188	36	624	31	609	Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1
sp|P22832|AMYG_ASPUS	8.75e-152	36	622	27	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P69328|AMYG_ASPNG	1.80e-151	12	622	5	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	1.80e-151	12	622	5	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P23176|AMYG_ASPKA	1.96e-150	12	622	5	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
0.000196	0.999782	CS pos: 30-31. Pr: 0.6708

TMHMM  Annotations     

There is no transmembrane helices in CLCR_11364-t43_1-p1.