CAZyme Information: KAG2008164.1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: KAG2008164.1
• CAZy Family: CBM21
• CAZyme Description: alpha amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
766		84742.37	7.0736

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccinerea326	15250	N/A	238	15012

• Gene Location: location=JAAGWA010000008:478973-481611(+)

Full Sequence      

MKLPQLWSISFALLGLVFSFASASPAMPLSDTRHVKRAPQVSLINHSYDNDVLSGTINVQ
NIAYSKVVVVHWASGDTWSDSQTIAATYSSSGSNNFETWSFSGRAPGATQFYIRYVVSGQ
TYYDPGNYQNHQISRPPGGGNPSPPGPAPTGPANLPAILPSNVPYEAPANPPSGCSNFNG
WDNCNGGNTEMVASSERRRWQTPPRGDPAYFESFQDYSHLVGYANIQYNSGRTSAVVTVN
AVHKEGAELTYSFNGVEQSSPSFEVDSSLQGTLAITVTSSDGKKLVLEPLNFFWQHQSLS
AAQSNFNNGQKGGIVELFGWPWKDIEKECEFLGKAGYMGVKVWPPTEHVWGSHHYEPDTQ
FRPWYQVYQPVSYRLTSRMGTRAELRSMINSCRRHGVRVYADAVINHMSGQGNDVQNHRN
TDCSLYSGRNATDYSPYYTNGNTYLINPFTGTRPTLEFPAVPFGPTDFHCERGINDWNNG
FLITRGWLVGLTDLNTAKPYVQDRIATFLVDLISIGFSGFRVDAAKHIGPNEMAQILGRV
KNKLGGSLPADFLTWMEVIIGGETQLNACGGGEYSWYTNFDNRLRANGFGNDDIQKVKIW
SSDYPASMPICGHWILPPSRFAVQNDDHDQQHEGSSPRWMGDKGSVLIKDKNVGAHRHFS
VNLFSRRDHDWHIKLLLSSYMFSHEGGNGFPDGLSDCNTHYTGTLPRSGCRGIGFDQAYV
ANACGYTMVPGKYTRPHRDISIINAMRGWVGLPPTNAHDLGIPGCH

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	336	634	1.9e-52	0.9144981412639405
CBM21	43	133	4.6e-16	0.9345794392523364

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	4.84e-129	311	752	1	329	Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
200454	AmyAc_bac1_AmyA	8.96e-39	318	592	8	251	Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
214758	Aamy	1.95e-20	322	412	18	99	Alpha-amylase domain.
397445	CBM_21	3.40e-17	37	134	3	113	Carbohydrate/starch-binding module (family 21). This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.
200458	AmyAc_euk_AmyA	5.78e-14	373	530	88	213	Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EGX42980.1|CBM21|GH13	0.0	19	765	16	789
QRV88491.1|CBM21|GH13	3.43e-237	41	763	79	840
QRW16798.1|CBM21|GH13	1.08e-236	1	765	1	783
QRV73700.1|CBM21|GH13	3.13e-235	41	763	79	840
QRW02641.1|CBM21|GH13	3.13e-235	41	763	79	840

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1PIF_A	1.22e-43	314	689	13	351	PIG ALPHA-AMYLASE [Sus scrofa],1PIG_A PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE OLIGOSACCHARIDE V-1532 [Sus scrofa],4X0N_A Porcine pancreatic alpha-amylase in complex with helianthamide, a novel proteinaceous inhibitor [Sus scrofa]
1BVN_P	2.26e-43	314	689	13	351	Pig Pancreatic Alpha-Amylase In Complex With The Proteinaceous Inhibitor Tendamistat [Sus scrofa]
1PPI_A	2.26e-43	314	689	13	351	THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS RESOLUTION [Sus scrofa]
1JFH_A	3.07e-43	314	689	13	351	STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION [Sus scrofa]
1KXQ_A	4.18e-43	314	689	13	351	Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_B Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_C Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_D Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_A Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_C Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_E Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXV_A Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXV_B Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O97396|AMY_PHACE	8.07e-44	298	635	16	311	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1
sp|P00688|AMYP_MOUSE	1.65e-43	285	689	5	363	Pancreatic alpha-amylase OS=Mus musculus OX=10090 GN=Amy2 PE=1 SV=2
sp|O77013|AMYR_DROKI	4.45e-43	298	682	16	350	Alpha-amylase-related protein OS=Drosophila kikkawai OX=30033 GN=Amyrel PE=3 SV=2
sp|P19961|AMY2B_HUMAN	5.96e-43	285	689	5	366	Alpha-amylase 2B OS=Homo sapiens OX=9606 GN=AMY2B PE=1 SV=1
sp|O77021|AMYR_DRODO	6.06e-43	298	682	16	350	Alpha-amylase-related protein OS=Drosophila dossoui OX=60716 GN=Amyrel PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000401	0.999570	CS pos: 23-24. Pr: 0.9764

TMHMM  Annotations     

Start	End
7	29