dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Aspergillus lentulus

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus

CAZyme ID

GAQ02996.1

CAZy Family

AA3

CAZyme Description

glucan 1,3-beta-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1433	BCLY01000001\|CGC42	155485.08	4.7278

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlentulusIFM54703	9916	N/A	259	9657

Gene Location

Enzyme Prediction help

No EC number prediction in GAQ02996.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH55	142	901	1.5e-252	0.9702702702702702

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
176558	PI-PLCXDc_like_2	2.48e-81	1105	1400	1	293	Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.
403800	Pectate_lyase_3	9.81e-73	170	411	1	213	Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
176529	PI-PLCXDc_like	7.21e-44	1106	1417	2	288	Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and similar proteins. This family corresponds to the catalytic domain present in phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs mainly found in eukaryota. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs and their bacterial homologs contain a single TIM-barrel type catalytic domain, X domain, which is more closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs.
176500	PI-PLCc_bacteria_like	7.63e-27	1106	1394	2	259	Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins. This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11), which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.
403800	Pectate_lyase_3	7.66e-11	543	656	1	122	Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.

CAZyme Hits help

E-Value	Query Start	Query End	Hit Start
45	1432	54	1445
45	1430	63	1428
335	1432	8	1106
32	916	393	1267
20	918	404	1297

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.07e-169	146	897	4	736	Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
2.38e-167	148	902	26	743	Chain A, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQN_B Chain B, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQO_A Chain A, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQO_B Chain B, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium]
3.07e-08	157	268	13	110	Structure of the Streptococcus pneumoniae surface protein and adhesin PfbA [Streptococcus pneumoniae TIGR4]
5.53e-08	172	268	117	202	Crystal structure of PfbA, a surface adhesin of Streptococcus pneumoniae [Streptococcus pneumoniae R6],4MR0_B Crystal structure of PfbA, a surface adhesin of Streptococcus pneumoniae [Streptococcus pneumoniae R6]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
7.56e-175	139	902	34	862	Probable glucan endo-1,3-beta-glucosidase ARB_02077 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02077 PE=1 SV=1
3.31e-137	131	905	34	776	Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
3.74e-49	141	867	30	708	Glucan endo-1,3-beta-glucosidase BGN13.1 OS=Trichoderma harzianum OX=5544 GN=bgn13.1 PE=1 SV=1
3.01e-07	172	268	153	238	Plasmin and fibronectin-binding protein A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pfbA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000212	0.999781	CS pos: 22-23. Pr: 0.9799

TMHMM Annotations help

There is no transmembrane helices in GAQ02996.1.

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