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CAZyme Information: P168DRAFT_241942-t37_1-p1

You are here: Home > Sequence: P168DRAFT_241942-t37_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Aspergillus campestris
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus campestris
CAZyme ID P168DRAFT_241942-t37_1-p1
CAZy Family AA7
CAZyme Description cellulase family protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
414 MSFM01000011|CGC5 45797.18 4.6785
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AcampestrisIBT28561 9929 1392248 173 9756
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in P168DRAFT_241942-t37_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 26 365 8.5e-113 0.9968051118210862

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395098 Cellulase 2.12e-11 56 365 24 268
Cellulase (glycosyl hydrolase family 5).
200477 AmyAc_CMD 0.008 128 187 103 155
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.05e-186 2 411 3 407
6.33e-179 8 411 11 409
2.05e-175 19 411 27 420
4.67e-171 19 411 29 427
5.41e-159 19 411 32 422

PDB Hits      help

P168DRAFT_241942-t37_1-p1 has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.71e-70 5 411 17 401
Glycosyl hydrolase 5 family protein OS=Chamaecyparis obtusa OX=13415 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000243 0.999711 CS pos: 17-18. Pr: 0.9786

TMHMM  Annotations      help

There is no transmembrane helices in P168DRAFT_241942-t37_1-p1.