CAZyme Information: PV10_08399-t45_1-p1

Basic Information

• Species: Exophiala mesophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
• CAZyme ID: PV10_08399-t45_1-p1
• CAZy Family: GT35
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
655	KN847525|CGC4	71132.36	4.2638

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EmesophilaCBS40295	9237	N/A	56	9181

• Gene Location: location=KN847525:1377370-1379558(+)

Full Sequence      

MLWPTALTTALLASVAVSSPSLHLRQQQENVLANLSLADFVAQERTIALQGVLANIGGLN
SSLVEGASPGVVVASPSTVNPNYFFTWTRDSALTYIMLIDELIFGNTSLKGTIEDYTSAQ
AFLQTVTNPSGSLYPAGDGLGEPKFYTNLTRFDGTWGRPQRDGPALRAIAFMNLAPVLFA
LNETDEFRRIYWPLVTNDLLYTSQYWNQACHDKLILSTRLIRTGYDLWEEVHGNSFFTVA
AQHRALVQGALLAEEIGEECEFCQQADQILCLLSNNFWNETGGYITADINVNNVNRSGIN
ADPLLAAITNFDYNATCDSVYQPCNSRILATHKVVVDAFRNLYPINKNATAPKAVLIGRY
PEDTYFKGGAWPLCTFAAAELLYDAAAQLNEIGTLSIDEDSLAFFQDLYPDANVSDYTGN
ELRVITGAMTTYADGFISAVQQYILPNGSISEQINTTSGASYSASKLTWSFASFITASQR
RARQYPPSWGAWTDLAHGNLTSSQCESSSYNATGQYLPATGAGAPNITNLTSLCYSEVIF
SVNATTSFGTNVFLAGNVSQLGGALDDPEKIILPLNPGNYSSTNPVWYVDIWLEAGEGVE
YQYILQQSNGTFRFEGGQLRNLTVGGCGSGNVTRVNDVFNTTMGTNANANASVSA

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	64	477	4.4e-70	0.9529085872576177

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	5.56e-109	47	479	2	417	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	1.41e-22	538	634	9	103	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	1.23e-17	538	633	3	94	Starch binding domain.
119437	CBM20	8.73e-16	538	633	2	93	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	1.22e-13	536	640	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
APA13257.1|CBM20|GH15	1.42e-169	5	630	7	597
CAA47945.1|CBM20|GH15|3.2.1.3	4.53e-168	10	633	13	601
CAA48243.1|CBM20|GH15|3.2.1.3	4.53e-168	10	633	13	601
CAY05396.1|CBM20|GH15|3.2.1.3	4.53e-168	10	633	13	601
ATZ55778.1|CBM20|GH15	6.21e-168	36	639	31	605

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FHW_A	1.57e-169	10	633	13	601	Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
6FRV_A	4.76e-148	36	633	2	610	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	3.80e-147	36	620	7	574	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
2VN4_A	6.91e-140	36	624	1	582	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
3EQA_A	1.62e-135	36	527	2	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	8.06e-169	10	633	13	601	Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1
sp|P69328|AMYG_ASPNG	3.63e-147	30	633	19	634	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	3.63e-147	30	633	19	634	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P22832|AMYG_ASPUS	4.98e-147	36	633	26	633	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	1.11e-145	30	633	19	633	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
0.000626	0.999356	CS pos: 25-26. Pr: 0.8183

TMHMM  Annotations     

There is no transmembrane helices in PV10_08399-t45_1-p1.