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CAZyme Information: RAK73005.1

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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 fijiensis
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fijiensis
CAZyme ID RAK73005.1
CAZy Family AA7
CAZyme Description putative glucoamylase precursor
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
515 54990.17 4.6995
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AfijiensisCBS313.89 12336 1448319 318 12018
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.3:94

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH15 45 466 9e-74 0.9861495844875346

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395586 Glyco_hydro_15 3.42e-135 39 465 1 415
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
273702 oligosac_amyl 1.64e-12 193 463 370 607
oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.
225922 SGA1 6.25e-09 61 465 261 600
Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.88e-222 30 506 30 493
1.88e-222 30 506 30 493
1.88e-222 30 506 30 493
1.88e-222 30 506 30 493
7.62e-222 30 506 30 493

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.80e-185 29 506 2 466
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
5.42e-183 29 506 2 465
Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori]
5.61e-183 29 506 2 465
GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
5.81e-183 29 506 2 465
GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]
8.23e-183 29 506 2 466
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.57e-185 29 506 36 501
Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
2.31e-182 4 506 4 490
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
2.31e-182 4 506 4 490
Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
1.34e-178 4 506 4 489
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
3.80e-178 4 506 4 489
Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.025284 0.974697 CS pos: 18-19. Pr: 0.9408

TMHMM  Annotations      help

There is no transmembrane helices in RAK73005.1.