CAZyme Information: Bcin12g03390.1:RNA-p1

Basic Information

• Species: Botrytis cinerea
• Lineage: Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Botrytis; Botrytis cinerea
• CAZyme ID: Bcin12g03390.1:RNA-p1
• CAZy Family: GH78
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
615		66972.85	5.1742

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BcinereaB05-10	12073	332648	366	11707

• Gene Location: location=bcin_chr_12:1178103-1180103(-)

Full Sequence      

MLFSRTATILSLLCVQATAISPRGSAASYSSLDSFIASERKIALQGVLNNIGPDGSKASG
AGNYVIASPSKTNPDYFYTWTRDSALTLKMLVDEFIFGNRALQPQIEKYVKAQAILQTVT
NPSGTFLPNGLGLGEPKYEVDGTRFNGAWGRPQRDGPALRAIALMAYSDWLINHNQLQRA
KLVIWPIISNDLSYIGEYWNQTGYDLWEEVLGSSFFTVQNQHRAFVEAGNLANRLGVESP
GYLNALEALCFLNQSFWNGEYIVSNINVDNGRTGLDGASILGSISIFDIDGSCDSPNLQP
CSSRALSNFRAVVNSFRFYSINAGIKNNSGIAVGRYAEDIYQGGNPWYLLTTAAAEFLYD
AVAQWRNQKKLTVDSTSINFFRDLYPSIKLKSYTNRDNEFNKILNVVTKYADSFVAIAQK
YTPSSGSLAEQFDRNTGAPISANDLTWSYAAFVTMAQRRSGQYPASWGSAAASVPPPNCA
SSSSQGVYVPAIAAGAPNVTATCQYPVRFYVNATTYYGENLYIIGNTTDLGAWNLNSALP
MNAGMYTTENPVWYVDAQLTAGEPVSYVYVREQDCGQAPIYETNNRTSVVPECGTGGSTI
RRDVWVGSGGSSGGC

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	64	456	2.1e-70	0.9362880886426593
CBM20	506	595	4e-20	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.22e-121	42	457	2	417	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	1.23e-33	505	605	7	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	1.17e-20	506	600	2	95	Starch binding domain.
99883	CBM20_alpha_amylase	2.50e-16	507	595	3	87	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	1.03e-14	507	605	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
ATZ55778.1|CBM20|GH15	0.0	1	615	1	615
CCD52574.1|CBM20|GH15	0.0	1	615	1	615
APA13257.1|CBM20|GH15	0.0	1	615	1	616
QSZ34432.1|CBM20|GH15	4.35e-280	1	615	1	617
CAA47945.1|CBM20|GH15|3.2.1.3	6.50e-277	4	615	6	616

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FHW_A	2.24e-278	4	615	6	616	Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
6FHV_A	7.12e-187	31	605	7	592	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
2VN4_A	4.60e-181	31	605	1	597	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	2.46e-174	30	605	1	615	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
3EQA_A	8.85e-156	30	488	1	458	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	1.15e-277	4	615	6	616	Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1
sp|P69328|AMYG_ASPNG	2.75e-173	30	605	25	639	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	2.75e-173	30	605	25	639	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P36914|AMYG_ASPOR	8.92e-173	30	605	28	611	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P0DN29|AMYG_ARTBC	7.62e-171	44	605	39	609	Glucoamylase ARB_02327-1 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02327-1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000345	0.999635	CS pos: 23-24. Pr: 0.6230

TMHMM  Annotations     

There is no transmembrane helices in Bcin12g03390.1:RNA-p1.