dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Magnaporthiopsis poae

Lineage

Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae

CAZyme ID

KLU82346.1

CAZy Family

AA6

CAZyme Description

Expansin-like EG45 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0C4DNM7]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
222	GL876966\|CGC16	23822.99	8.8505

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MpoaeATCC64411	12363	644358	200	12163

Gene Location

Enzyme Prediction help

No EC number prediction in KLU82346.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CBM63	133	201	1.9e-16	0.8205128205128205

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	4.20e-23	27	120	3	93	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	1.23e-21	26	124	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	1.31e-18	55	178	59	184	Peptidoglycan-binding domain, expansin [Cell wall/membrane/envelope biogenesis].
178595	PLN03024	3.05e-11	23	121	20	125	Putative EG45-like domain containing protein 1; Provisional
409009	DPBB_EXLX1-like	4.20e-11	27	120	5	100	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
1.03e-61	4	222	5	223
1.64e-61	10	222	26	238
5.61e-59	27	221	176	369
4.65e-58	30	221	131	319
4.51e-57	25	221	182	377

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.53e-23	36	211	18	187	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]
2.99e-22	36	211	18	187	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]
4.11e-16	27	178	9	160	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]
1.53e-15	27	178	9	160	Crystal structure of a SeMet derivative of EXPA from Bacillus subtilis at 2.5 angstrom [Bacillus subtilis]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.16e-15	27	178	33	184	Expansin-YoaJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yoaJ PE=1 SV=1
4.10e-12	7	159	10	169	Expansin-like protein 7 OS=Dictyostelium discoideum OX=44689 GN=expl7 PE=2 SV=1
9.61e-07	62	121	53	123	Putative EG45-like domain containing protein 1 OS=Arabidopsis thaliana OX=3702 GN=EGC1 PE=3 SV=1
1.76e-06	27	212	33	241	Expansin-A8 OS=Arabidopsis thaliana OX=3702 GN=EXPA8 PE=2 SV=1
2.62e-06	57	193	54	205	Expansin-like protein 2 OS=Dictyostelium discoideum OX=44689 GN=expl2 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000782	0.999197	CS pos: 24-25. Pr: 0.9565

TMHMM Annotations help

There is no transmembrane helices in KLU82346.1.

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