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CAZyme Information: PHYBL_33968T0-p1

You are here: Home > Sequence: PHYBL_33968T0-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 Phycomyces blakesleeanus
Lineage Mucoromycota; Mucoromycetes; ; Phycomycetaceae; Phycomyces; Phycomyces blakesleeanus
CAZyme ID PHYBL_33968T0-p1
CAZy Family GT2
CAZyme Description Protein phosphatase, regulatory subunit PPP1R3C/D
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
598 63961.01 5.7361
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PblakesleeanusNRRL1555 16528 763407 0 16528
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC - 3.2.1.3:9

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH15 186 589 7.8e-78 0.9501385041551247
CBM21 27 125 2.6e-17 0.9719626168224299

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395586 Glyco_hydro_15 5.41e-102 177 590 5 416
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
397445 CBM_21 1.18e-16 29 125 7 112
Carbohydrate/starch-binding module (family 21). This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.
225922 SGA1 4.30e-16 175 590 249 601
Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism].
273702 oligosac_amyl 1.80e-10 328 584 401 604
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.14e-238 22 595 26 600
1.14e-238 22 595 26 600
1.14e-238 22 595 26 600
1.62e-238 22 595 26 600
1.62e-238 22 595 26 600

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.77e-78 162 597 1 432
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]
4.90e-78 162 597 1 432
GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
5.04e-78 162 597 1 432
GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]
1.96e-76 162 597 1 433
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
6.69e-75 162 597 1 433
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
4.70e-238 22 595 26 600
Glucoamylase 1 OS=Rhizopus oryzae OX=64495 PE=1 SV=2
8.96e-146 164 595 34 447
Glucoamylase amyD OS=Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) OX=246409 GN=amyD PE=1 SV=1
7.85e-83 29 596 34 611
Glucoamylase OS=Blastobotrys adeninivorans OX=409370 GN=GAA PE=3 SV=1
2.02e-75 162 597 25 456
Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
1.40e-74 179 597 40 455
Glucoamylase ARB_02327-1 OS=Schizophyllum commune (strain H4-8 / FGSC 9210) OX=578458 GN=SCHCODRAFT_57589 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000217 0.999742 CS pos: 22-23. Pr: 0.9802

TMHMM  Annotations      help

There is no transmembrane helices in PHYBL_33968T0-p1.