CAZyme Information: CC1G_05516-t26_1-p1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: CC1G_05516-t26_1-p1
• CAZy Family: GH10
• CAZyme Description: alpha amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
780	AACS02000011|CGC8	85775.92	6.8593

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccinereaokay7-130	13657	240176	301	13356

Full Sequence      

MKLPQLWTVSLSLFGLFLALTYASPAPQHVKRAPQVSLINHSYSNAVLSGTINVQNIAYS
KVVEVVWAVGDSWSDSQIIPATYTSSGSNNFETWAFSGRASGATQFYIRYTVSGQTYYDP
GNYQNHQVNRPPSNSQPPVVTSSTAVVPPPTSTTAPAPPPTGTVAPGNLPPIIPANIPYE
APATPPTGCNNFNGLDNCQGNSHEMAASSERRRWQTPPRGDPAHEESFQDYSHLVGYADI
QYNSARNAAVVTVNAAHKEGATLTYSFNGAEQSSPIFQVTNSLQTALAITVTSSDGKKLV
LEPINFFWQHQSLSAAQSSFNNGQKGGIVELFGWPWNDIAKECEFLGKAGYMGVKVWAPN
EHVWGSHYYEPDGQFRPWYFVYQPVSYRLQSRMGTREELRNMINSCRRAGVRVYADAVIN
HMSGQGTDIQNHRVGNCELYSGHNATENSPYYTSGNTFLINPFTGTRPTLEFPAVPYGPT
DFHCERSLNSWTDGIVVTKGWLVGLTDLNTSKPYVQDRIATYLTDLLSIGFSGFRVDAAK
HIGPQDMAQILARLKNKMGGSLPDDFITWMEVIIGGEAALMACSGGEWSWYTNFDNKMRA
AGLSNEDIQKVKIWSSDYPKEMPICGHWILPPSRFAIQNDDHDQQNDGSSSRDMADKGSV
LIKEKNVAAHRNFEVNLFARRDNDWHIKLILSSYMFMPNGGSGFPDGLSDCSLHYTGNQN
INGCKGVPKDTAYVANACGYTMQPGKYTRPHRDISIINAMRGWVGLGPTNANALGIPGCQ

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	350	649	9.3e-53	0.9182156133828996
CBM21	38	128	9.4e-16	0.9345794392523364

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	1.34e-142	325	766	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	7.47e-35	332	576	8	213	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	1.68e-21	319	426	6	99	Alpha-amylase domain.
397445	CBM_21	2.03e-17	32	129	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.
236518	PRK09441	9.12e-12	392	545	76	241	cytoplasmic alpha-amylase; Reviewed

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EGX42980.1|CBM21|GH13	EGX42980.1|CBM21|GH13	0.0	31	780	37	790
QRW16798.1|CBM21|GH13	QRW16798.1|CBM21|GH13	4.63e-255	35	779	34	783
QRV88491.1|CBM21|GH13	QRV88491.1|CBM21|GH13	1.99e-253	36	777	79	840
QRV73700.1|CBM21|GH13	QRV73700.1|CBM21|GH13	2.81e-253	36	777	79	840
QRW02641.1|CBM21|GH13	QRW02641.1|CBM21|GH13	2.81e-253	36	777	79	840

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Q4N_X	1Q4N_X	2.12e-44	321	645	4	302	Chain X, Alpha-amylase, salivary [Homo sapiens]
3DHP_A	3DHP_A	9.86e-44	321	645	4	302	Chain A, Alpha-amylase 1 [Homo sapiens]
1JXK_A	1JXK_A	4.20e-43	321	645	4	302	Role of ethe mobile loop in the mehanism of human salivary amylase [Homo sapiens],1MFU_A Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant [Homo sapiens]
1C8Q_A	1C8Q_A	4.58e-43	321	645	4	302	STRUCTURE SOLUTION AND REFINEMENT OF THE RECOMBINANT HUMAN SALIVARY AMYLASE [Homo sapiens],1MFV_A Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme [Homo sapiens],1SMD_A HUMAN SALIVARY AMYLASE [Homo sapiens],1XV8_A Crystal Structure of Human Salivary Alpha-Amylase Dimer [Homo sapiens],1XV8_B Crystal Structure of Human Salivary Alpha-Amylase Dimer [Homo sapiens]
3BLK_A	3BLK_A	4.58e-43	321	645	4	302	Chain A, Alpha-amylase 1 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P19961|AMY2B_HUMAN	sp|P19961|AMY2B_HUMAN	5.62e-44	299	645	5	317	Alpha-amylase 2B OS=Homo sapiens OX=9606 GN=AMY2B PE=1 SV=1
sp|P04746|AMYP_HUMAN	sp|P04746|AMYP_HUMAN	4.83e-43	299	645	5	317	Pancreatic alpha-amylase OS=Homo sapiens OX=9606 GN=AMY2A PE=1 SV=2
sp|P00688|AMYP_MOUSE	sp|P00688|AMYP_MOUSE	6.24e-43	299	645	5	314	Pancreatic alpha-amylase OS=Mus musculus OX=10090 GN=Amy2 PE=1 SV=2
sp|P0DTE7|AMY1B_HUMAN	sp|P0DTE7|AMY1B_HUMAN	8.92e-43	300	645	6	317	Alpha-amylase 1B OS=Homo sapiens OX=9606 GN=AMY1B PE=1 SV=1
sp|P0DTE8|AMY1C_HUMAN	sp|P0DTE8|AMY1C_HUMAN	8.92e-43	300	645	6	317	Alpha-amylase 1C OS=Homo sapiens OX=9606 GN=AMY1C PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000188	0.999820	CS pos: 32-33. Pr: 0.7407

TMHMM  Annotations     

There is no transmembrane helices in CC1G_05516-t26_1-p1.