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CAZyme Information: PV07_09920-t44_1-p1

You are here: Home > Sequence: PV07_09920-t44_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 Cladophialophora immunda
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora immunda
CAZyme ID PV07_09920-t44_1-p1
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
483 54400.33 5.3016
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CimmundaCBS83496 12879 N/A 49 12830
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 120 396 2e-70 0.9650655021834061

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 7.53e-125 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 3.62e-106 8 395 43 390
alpha-galactosidase
166449 PLN02808 1.02e-103 17 407 24 369
alpha-galactosidase
178295 PLN02692 1.31e-96 19 395 50 381
alpha-galactosidase
374582 Melibiase_2 1.11e-72 24 314 1 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.60e-223 8 483 12 497
4.81e-220 8 483 11 496
9.41e-213 14 471 16 482
1.08e-212 27 472 1 468
6.25e-211 14 471 16 482

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.76e-174 19 467 24 468
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRL_A Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae]
9.39e-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]
5.39e-131 18 395 2 364
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
1.46e-90 19 396 3 335
Chain A, alpha-galactosidase [Oryza sativa]
1.60e-83 17 407 1 346
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
2.24e-178 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
3.30e-176 9 470 12 472
Alpha-galactosidase OS=Torulaspora delbrueckii OX=4950 GN=MEL PE=3 SV=1
5.77e-176 19 467 24 468
Alpha-galactosidase OS=Zygotorulaspora mrakii OX=42260 GN=MEL PE=3 SV=1
2.41e-175 19 470 24 471
Alpha-galactosidase OS=Saccharomyces paradoxus OX=27291 GN=MEL PE=3 SV=1
9.74e-175 19 467 24 468
Alpha-galactosidase 6 OS=Saccharomyces cerevisiae OX=4932 GN=MEL6 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000385 0.999602 CS pos: 16-17. Pr: 0.9676

TMHMM  Annotations      help

There is no transmembrane helices in PV07_09920-t44_1-p1.