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CAZyme Information: ASPFODRAFT_42362-t33_1-p1

You are here: Home > Sequence: ASPFODRAFT_42362-t33_1-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 Aspergillus luchuensis
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis
CAZyme ID ASPFODRAFT_42362-t33_1-p1
CAZy Family GH43|CBM91
CAZyme Description glycoside hydrolase family 27 protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
441 KV878238|CGC23 48670.51 4.4951
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AluchuensisCBS106.47 13784 1137211 282 13502
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:58 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 124 417 1.1e-64 0.9912663755458515

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 1.57e-121 27 330 1 271
glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
177874 PLN02229 2.07e-95 21 431 57 411
alpha-galactosidase
166449 PLN02808 2.54e-93 21 430 26 376
alpha-galactosidase
178295 PLN02692 1.89e-88 21 389 50 367
alpha-galactosidase
374582 Melibiase_2 7.60e-72 26 330 1 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 441 1 442
0.0 1 441 1 442
0.0 1 441 1 443
0.0 1 441 1 443
0.0 1 441 1 443

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.69e-174 17 441 1 414
Chain A, alpha-galactosidase [Trichoderma reesei],1T0O_A Chain A, alpha-galactosidase [Trichoderma reesei]
4.00e-85 21 389 3 320
Chain A, alpha-galactosidase [Oryza sativa]
1.44e-82 21 437 3 360
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
1.11e-81 21 435 3 388
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
8.56e-76 21 374 24 361
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRL_A Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 1 441 1 443
Probable alpha-galactosidase B OS=Aspergillus niger OX=5061 GN=aglB PE=2 SV=1
0.0 1 441 1 443
Probable alpha-galactosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglB PE=3 SV=1
3.11e-260 10 441 13 442
Probable alpha-galactosidase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=aglB PE=3 SV=1
1.26e-259 10 441 13 442
Probable alpha-galactosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglB PE=3 SV=1
3.77e-253 14 441 20 447
Probable alpha-galactosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=aglB PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000255 0.999714 CS pos: 20-21. Pr: 0.7751

TMHMM  Annotations      help

There is no transmembrane helices in ASPFODRAFT_42362-t33_1-p1.