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CAZyme Information: FFUJ_13796-t31_1-p1

You are here: Home > Sequence: FFUJ_13796-t31_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 Fusarium fujikuroi
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium fujikuroi
CAZyme ID FFUJ_13796-t31_1-p1
CAZy Family GT24
CAZyme Description related to alpha-galactosidase precursor
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
409 HF679030|CGC17 44767.74 7.8682
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FfujikuroiIMI58289 15099 1279085 286 14813
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in FFUJ_13796-t31_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 130 366 7.7e-69 0.9213973799126638

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 1.05e-136 35 314 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.
166449 PLN02808 9.00e-92 12 358 9 331
alpha-galactosidase
177874 PLN02229 4.52e-91 35 345 63 351
alpha-galactosidase
178295 PLN02692 3.44e-88 23 357 44 354
alpha-galactosidase
374582 Melibiase_2 3.21e-77 35 314 2 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 409 1 409
0.0 1 409 1 409
0.0 1 409 1 409
0.0 1 409 1 409
5.62e-315 1 409 1 409

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.54e-87 32 406 9 410
Chain A, alpha-galactosidase [Trichoderma reesei],1T0O_A Chain A, alpha-galactosidase [Trichoderma reesei]
2.59e-80 35 358 9 332
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
1.06e-79 31 404 5 358
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
4.10e-79 31 409 5 362
Chain A, alpha-galactosidase [Oryza sativa]
5.95e-77 11 364 11 370
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
1.79e-96 8 406 6 444
Probable alpha-galactosidase B OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=aglB PE=3 SV=1
2.42e-96 7 404 4 429
Probable alpha-galactosidase B OS=Penicillium simplicissimum OX=69488 GN=agl1 PE=2 SV=1
8.68e-96 13 404 5 437
Probable alpha-galactosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglB PE=3 SV=1
3.45e-95 13 404 5 437
Probable alpha-galactosidase B OS=Aspergillus niger OX=5061 GN=aglB PE=2 SV=1
2.18e-94 5 404 2 441
Probable alpha-galactosidase B OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=aglB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000286 0.999703 CS pos: 29-30. Pr: 0.7292

TMHMM  Annotations      help

There is no transmembrane helices in FFUJ_13796-t31_1-p1.