CAZyme Information: APA12357.1

Basic Information

• Species: Sclerotinia sclerotiorum
• Lineage: Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Sclerotinia; Sclerotinia sclerotiorum
• CAZyme ID: APA12357.1
• CAZy Family: GH51
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
679	CP017822|CGC7	71962.75	5.2399

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ssclerotiorum1980UF-70	11368	665079	238	11130

• Gene Location: location=CP017822:900120-902412(-)

Full Sequence      

MASSLLSALTSLNSISNFNSTLVLRAVQPIMHTFTPLLLAGSLALQSIHAFPNPSRVEER
DGEILKRSVDSFIATESPIAMRNLLCNIGSSGSCAAGASSGIVIASPDKVNPDYFYTWTR
DSALVFKNLVDTFISSTYSPSLQQQIEDYISAQAGLQTVSNPSGGFSSGGLGEPKFNVDK
TAFTGAWGRPQRDGPALRATAMIAYSKWLIANGYTSTVQTIVWPIIRNDLSYVTQYWNQT
GFDLWEEVQGSSFFTIAAQHRALVEGSALASQIGQSCTYCDSQAPQVLCFLQSFWSSSSG
YIISNINENNGRSGKDANSILSTIQTFDPTASCDSSTFQPCSDRALANHKVVTDSFRSIY
SINSGIAEGVAVSVGRYPEDSYQGGNPWYLNTLAAAEQLYDALYTWNKQGSITVTSTSLA
FFRDFSSSVTAGTYSSSTSTYTTLYNAIKTYADGYMNIVATYAQANGSLSEQFNRAGGAP
LSAYDLTWSYAAFLTAAARRAGVVPYSWGEPSANSVPGSCYATSAYGTYSTATATSFPAS
QTPNGSGSVPAPSTTATTTKTGSSTTTTASSCPIATSVAVTFNELKTTVYGQTIKIAGSI
SQLGSWAPASAVALSASKYTSSNPLWSVTINLPAGTAIQYKFINVASDGTVTWEADPNRS
YTVPVSCATSATVSGSWQS

Enzyme Prediction     

EC	3.2.1.3:94	1.14.99.55:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	93	497	1.5e-79	0.961218836565097
CBM20	578	668	1.3e-27	0.9666666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	2.98e-136	78	497	1	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	1.49e-57	572	677	1	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	6.06e-41	578	673	1	95	Starch binding domain.
99883	CBM20_alpha_amylase	1.54e-33	578	677	1	94	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.
215006	CBM_2	3.31e-26	578	664	1	87	Starch binding domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA12357.1|CBM20|GH15	0.0	1	679	1	679
ATZ49247.1|CBM20|GH15	0.0	1	677	1	672
ATZ49248.1|CBM20|GH15	0.0	1	677	1	672
QSZ31699.1|CBM20|GH15	0.0	1	679	1	677
CCD49819.2|CBM20|GH15	0.0	31	677	1	645

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	5.01e-258	68	679	1	599	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	2.66e-247	68	678	2	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1AGM_A	2.97e-214	68	539	2	467	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	3.08e-214	68	539	2	467	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1GAI_A	3.19e-214	68	539	2	467	GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P14804|AMYG_NEUCR	2.00e-268	31	678	1	626	Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
sp|P22832|AMYG_ASPUS	2.68e-247	66	678	24	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	3.79e-247	66	678	24	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P69327|AMYG_ASPAW	2.25e-246	66	678	24	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	2.25e-246	66	678	24	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.976276	0.023727

TMHMM  Annotations     

There is no transmembrane helices in APA12357.1.