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CAZyme Information: EXJ76042.1

You are here: Home > Sequence: EXJ76042.1

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 EXJ76042.1
CAZy Family GT50
CAZyme Description Alpha-galactosidase [Source:UniProtKB/TrEMBL;Acc:W9X6D6]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
492 53417.92 4.6852
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 132 406 8.1e-66 0.9737991266375546

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 3.08e-114 38 327 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.
166449 PLN02808 4.54e-87 29 412 23 364
alpha-galactosidase
177874 PLN02229 3.15e-86 32 419 57 407
alpha-galactosidase
178295 PLN02692 5.31e-82 32 410 50 386
alpha-galactosidase
374582 Melibiase_2 1.28e-62 37 327 1 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.69e-160 30 492 29 498
4.38e-159 30 492 42 507
2.12e-158 32 492 23 502
2.12e-158 32 492 23 502
8.52e-158 32 492 23 502

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.80e-147 21 491 13 479
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRL_A Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae]
7.75e-146 21 491 13 479
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]
9.49e-129 32 410 3 369
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
4.52e-71 32 409 3 338
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
2.42e-70 32 370 3 305
Chain A, alpha-galactosidase [Oryza sativa]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.18e-154 20 480 12 468
Alpha-galactosidase OS=Zygotorulaspora mrakii OX=42260 GN=MEL PE=3 SV=1
2.58e-151 24 480 15 467
Alpha-galactosidase OS=Lachancea cidri OX=29831 GN=MEL PE=3 SV=1
3.16e-150 27 482 19 470
Alpha-galactosidase OS=Saccharomyces mikatae OX=114525 GN=MEL PE=3 SV=1
1.02e-148 24 482 16 470
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
1.89e-146 21 483 13 471
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
0.000297 0.999673 CS pos: 26-27. Pr: 0.9778

TMHMM  Annotations      help

There is no transmembrane helices in EXJ76042.1.