dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Macrophomina phaseolina

Lineage

Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina

CAZyme ID

EKG13535.1

CAZy Family

CE9

CAZyme Description

Pollen allergen/expansin

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
598		60416.10	3.7989

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MphaseolinaMS6	14712	1126212	906	13806

Gene Location

Enzyme Prediction help

No EC number prediction in EKG13535.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CBM63	512	581	4.5e-22	0.8589743589743589

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
409004	DPBB_RlpA_EXP_N-like	6.33e-27	403	499	2	94	double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains. The double-psi beta-barrel (DPBB) fold is found in a divergent group of proteins, including endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), EG45-like domain containing proteins, kiwellins, Streptomyces papain inhibitor (SPI), and the N-terminal domain of plant and bacterial expansins. RlpA may work in tandem with amidases to degrade peptidoglycan (PG) in the division septum and lateral wall to facilitate daughter cell separation. An EG45-like domain containing protein from Arabidopsis thaliana, called plant natriuretic peptide A (AtPNP-A), functions in cell volume regulation. Kiwellin proteins comprise a widespread family of plant-defense proteins that target pathogenic bacterial/fungal effectors that down-regulate plant defense responses. SPI is a stress protein produced under hyperthermal stress conditions that serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes. Some expansin family proteins display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs.
409008	DPBB_EXP_N-like	1.75e-19	403	502	2	117	N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains. The plant expansin family consists of four subfamilies, alpha-expansin (EXPA), beta-expansin (EXPB), expansin-like A (EXLA), and expansin-like B (EXLB). EXPA and EXPB display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. EXPA proteins function more efficiently on dicotyledonous cell walls, whereas EXPB proteins exhibit specificity for the cell walls of monocotyledons. Expansins also affect environmental stress responses. Expansin family proteins contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This family also includes GH45 endoglucanases from mollusks. This model represents the N-terminal domain of expansins and similar proteins, which adopts a double-psi beta-barrel (DPBB) fold.
226755	YoaJ	4.21e-15	393	582	10	209	Peptidoglycan-binding domain, expansin [Cell wall/membrane/envelope biogenesis].
409010	DPBB_SPI-like	6.32e-14	403	499	2	101	double-psi beta-barrel fold of Streptomyces papain inhibitor and similar proteins. Streptomyces papain inhibitor (SPI) adopts a rigid, thermo-resistant double-psi-beta-barrel (DPBB) fold that is stabilized by two cysteine bridges. SPI serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes, that is used to covalently and specifically link functional amines to glutamine donor sites of therapeutic proteins. SPI is a stress protein produced under hyperthermal stress conditions, and is able to inhibit the cysteine proteases, papain and bromelain, as well as the bovine serine protease trypsin.
409009	DPBB_EXLX1-like	1.44e-08	403	499	4	101	N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus subtilis EXLX1. This subfamily is composed of bacterial expansins including Bacillus subtilis EXLX1, also called expansin-YoaJ. Similar to plant expansins, EXLX1 contains an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. It strongly binds to crystalline cellulose via D2, and weakly binds soluble cellooligosaccharides. Bacterial expansins, which are present in some plant pathogens, have the ability to loosen plant cell walls, but with weaker activity compared to plant expansins. They may have a role in plant-bacterial interactions. This model represents the N-terminal domain of EXLX1 and similar bacterial expansins, which adopts a double-psi beta-barrel (DPBB) fold.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.78e-80	398	598	170	370
4.92e-75	402	598	182	378
1.05e-74	404	598	325	519
1.05e-74	404	598	325	519
1.16e-74	398	598	323	523

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.63e-19	404	580	5	180	Crystal structure of Clavibacter michiganensis expansin in complex with cellopentaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4JCW_B Crystal structure of Clavibacter michiganensis expansin in complex with cellopentaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4JJO_A crystal structure of apo-clavibacter Michiganensis expansin [Clavibacter michiganensis]
1.22e-18	404	580	5	180	Crystal structure of D78N mutant apo form of clavibacter michiganensis expansin [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4L48_A Crystal structure of d78n mutant clavibacter michiganensis expansin in complex with cellohexaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4L48_C Crystal structure of d78n mutant clavibacter michiganensis expansin in complex with cellohexaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382]
1.52e-13	404	579	9	182	Structure of an expansin like protein from Bacillus Subtilis at 1.9A resolution [Bacillus subtilis],4FER_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellohexaose [Bacillus subtilis subsp. subtilis str. 168],4FER_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellohexaose [Bacillus subtilis subsp. subtilis str. 168],4FFT_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with mixed-linkage glucan [Bacillus subtilis subsp. subtilis str. 168],4FFT_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with mixed-linkage glucan [Bacillus subtilis subsp. subtilis str. 168],4FG2_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellotetraose [Bacillus subtilis subsp. subtilis str. 168],4FG2_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellotetraose [Bacillus subtilis subsp. subtilis str. 168],4FG4_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with hemithiocellodextrin [Bacillus subtilis subsp. subtilis str. 168],4FG4_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with hemithiocellodextrin [Bacillus subtilis subsp. subtilis str. 168]