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CAZyme Information: EXJ57715.1

You are here: Home > Sequence: EXJ57715.1

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 Cladophialophora psammophila
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora psammophila
CAZyme ID EXJ57715.1
CAZy Family AA14
CAZyme Description alpha-galactosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
483 54167.98 4.9514
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CpsammophilaCBS110553 13421 1182543 0 13421
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:15

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 120 397 2.7e-71 0.9694323144104804

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 1.30e-121 25 314 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 5.56e-105 17 395 55 390
alpha-galactosidase
166449 PLN02808 4.52e-101 15 407 22 369
alpha-galactosidase
178295 PLN02692 9.16e-95 15 395 46 381
alpha-galactosidase
374582 Melibiase_2 4.18e-71 24 314 1 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.12e-223 11 483 15 497
3.39e-220 11 483 14 496
7.03e-215 14 483 16 496
6.63e-213 14 483 16 496
8.79e-212 27 472 1 468

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.43e-174 19 467 24 468
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRL_A Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae]
2.33e-173 19 467 24 468
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRM_B Chain B, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRM_C Chain C, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRM_D Chain D, Alpha-galactosidase 1 [Saccharomyces cerevisiae]
2.47e-129 18 414 2 383
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
1.29e-88 18 396 2 335
Chain A, alpha-galactosidase [Oryza sativa]
2.87e-84 17 419 1 358
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.82e-177 19 467 24 468
Alpha-galactosidase OS=Saccharomyces pastorianus (strain ATCC 76529 / Carlsberg bottom yeast no.1 / CBS 1513 / CLIB 176 / NBRC 1167 / NCYC 396 / NRRL Y-12693) OX=1073566 GN=MEL PE=3 SV=1
5.97e-176 19 470 24 471
Alpha-galactosidase OS=Saccharomyces paradoxus OX=27291 GN=MEL PE=3 SV=1
6.64e-175 2 467 4 468
Alpha-galactosidase OS=Zygotorulaspora mrakii OX=42260 GN=MEL PE=3 SV=1
6.87e-175 19 467 24 468
Alpha-galactosidase 6 OS=Saccharomyces cerevisiae OX=4932 GN=MEL6 PE=3 SV=1
3.93e-174 19 467 24 468
Alpha-galactosidase 5 OS=Saccharomyces cerevisiae OX=4932 GN=MEL5 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000353 0.999658 CS pos: 16-17. Pr: 0.9636

TMHMM  Annotations      help

There is no transmembrane helices in EXJ57715.1.