CAZyme Information: OTA24504.1

Basic Information

• Species: Hortaea werneckii
• Lineage: Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii
• CAZyme ID: OTA24504.1
• CAZy Family: CE4
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1039	MUNK01000241|CGC1	111072.99	4.0610

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000	15649	1157616	29	15620

Full Sequence      

MSPRSTKREREPLPSCSSTIIPNRMTCSRKLFIAFAASTVHVVQAQQLKDGHPAFMSYPG
INNACETALNTTVDCPAFLQRVSVNNAILDLDQVQALCTGSCVTDLQSARSDIASACTAD
TDVIVYDNVAYPATFIADQYLFTTEVSCLRDTYTGEYCDPKFLVWSNQSFMTTNQSCSNC
WLNVQALQLGNPLAYDDSLASNFAELKASCNAKSYTYATPTVYGINATETTDTDGAKFTK
PATCTGSYVLQPGDDCNSVAKKMGVSTYSMLVSNGLDLYCQNFEAAVNSSASLCTPPTCK
IYEWNFFDECNDVANQNDVSVAHFLSWNPNFDSICRNSIIFAGYQVCVSAPGGTVESGAS
TNLSVSPGASSAVPAPTNSFPETKECGGWYTVQAGDDCAKLSVAFSMTISDFLFLNPEIY
TNCTNLLLGVSYCVFPVGDIASYSGYPAPTTLSITVPPATFSSVNTAVPSATNHPDPDFV
FQNLPKAPGTADDCTFYADHNDNTRDADSNSCTAVASAWDIELEDLLDWNPSLSTDQEAC
ATQPGRSYCVRKSTKVVYAPTGDECIAVNATEIPEGTNADCTCFTEVSGYEGTVGLDCKA
IADDSSITLVVLQDLNPWLASDCDNALFAGLGEWDHRAVCIGTNATSSSSSTRSSSSGSK
ITKAMGPTRTGTPAGCRRFYTVQSGDGCAAIEETFDITFAQLYKWNPTIGEDCANLWLGY
AYCVDASISATITTSSPTRSTPSVTTPTPTQEGMTKSCNDFYKVKSGDGCYDIASHYGIS
LEDFYTYNPAVGDDCSKLYPDNYVCVGVTSSGSCKIDVKFNTAHSTEWGESVWAVGSIPE
LGSWDVNEALMLTGSSGADGSTNWQATAELPADTQVSYKFVKVQTDGTPVWEQDPNRSFL
TSSCGGSAMQEGGSWQGSSTGSTAPSTTSPIVPTCTSLDVVFEVLAQTTYGESVYVIGSV
PALGEWSTDAAVVLAADQYTQARPLWRGTISLAVGQDVQFKFIKINLDGTYTWEADPNRI
VRIPTDCSATLTQSGTFQQ

Enzyme Prediction     

EC	-	3.2.1.3:71	3.2.1.1:13

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM20	816	905	9.7e-24	0.9555555555555556
CBM20	940	1028	1.9e-23	0.9444444444444444

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
99886	CBM20_glucoamylase	1.36e-36	933	1036	2	105	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	6.36e-32	940	1032	3	94	Starch binding domain.
99883	CBM20_alpha_amylase	1.04e-26	940	1034	3	93	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	1.06e-24	940	1032	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.
99886	CBM20_glucoamylase	2.24e-24	818	915	9	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW40759.1|CBM50	QMW40759.1|CBM50	1.39e-135	28	727	3	743
UNI22107.1|CBM50	UNI22107.1|CBM50	6.17e-134	31	724	4	686
ATY65640.1|CBM50	ATY65640.1|CBM50	5.04e-129	31	807	14	779
UKZ93577.1|CBM50	UKZ93577.1|CBM50	7.20e-121	35	641	11	601
SMQ53700.1|CBM50	SMQ53700.1|CBM50	4.76e-119	33	461	10	441

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AC0_A	1AC0_A	9.61e-24	934	1038	3	108	GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODEXTRIN, NMR, MINIMIZED AVERAGE STRUCTURE [Aspergillus niger],1ACZ_A GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODEXTRIN, NMR, 5 STRUCTURES [Aspergillus niger],1KUL_A Chain A, GLUCOAMYLASE [Aspergillus niger],1KUM_A Chain A, GLUCOAMYLASE [Aspergillus niger],5GHL_A Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_B Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_C Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_D Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger]
6FRV_A	6FRV_A	1.48e-19	942	1038	519	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2VN4_A	2VN4_A	6.94e-18	889	1038	439	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FHV_A	6FHV_A	1.60e-11	932	1027	486	582	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
6FHW_A	6FHW_A	8.61e-11	811	917	502	608	Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4AVW3|LYSM5_ARTBC	sp|D4AVW3|LYSM5_ARTBC	5.47e-36	335	724	211	534	LysM domain-containing protein ARB_00327 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_00327 PE=3 SV=2
sp|D4ALG0|LYSM1_ARTBC	sp|D4ALG0|LYSM1_ARTBC	5.76e-30	494	808	45	373	LysM domain-containing protein ARB_05157 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05157 PE=1 SV=1
sp|P23176|AMYG_ASPKA	sp|P23176|AMYG_ASPKA	1.17e-19	934	1038	534	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|D4AY86|LYSM6_ARTBC	sp|D4AY86|LYSM6_ARTBC	4.96e-19	64	437	40	422	LysM domain-containing protein ARB_01155/01156 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01155/01156 PE=3 SV=2
sp|P22832|AMYG_ASPUS	sp|P22832|AMYG_ASPUS	8.16e-19	934	1038	534	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.936076	0.063922

TMHMM  Annotations     

There is no transmembrane helices in OTA24504.1.