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CAZyme Information: TRIREDRAFT_75015-t26_1-p1

You are here: Home > Sequence: TRIREDRAFT_75015-t26_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 Trichoderma reesei
Lineage Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma reesei
CAZyme ID TRIREDRAFT_75015-t26_1-p1
CAZy Family GT22
CAZyme Description glycoside hydrolase family 27
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
476 52124.57 6.5610
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_TreeseiQM6a 9138 431241 7 9131
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 184 453 4.5e-41 0.9519650655021834

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 8.15e-66 50 365 2 268
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 4.07e-15 5 458 13 401
alpha-galactosidase
166449 PLN02808 1.37e-12 52 475 35 385
alpha-galactosidase
178295 PLN02692 5.58e-11 52 458 59 392
alpha-galactosidase
374582 Melibiase_2 9.52e-11 87 360 47 276
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.12e-314 1 476 1 467
5.23e-311 1 475 1 476
1.29e-284 62 476 19 433
6.14e-237 9 476 7 473
1.24e-236 9 476 7 473

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.62e-22 52 476 28 443
Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
2.81e-21 52 476 28 443
Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus]
1.23e-12 47 474 7 361
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
4.54e-10 53 359 16 282
Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H53_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H54_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H54_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H55_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H55_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3IGU_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3IGU_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],4DO4_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO4_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO5_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO5_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO6_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO6_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens]
6.67e-10 104 474 75 430
Chain A, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.84e-139 34 475 168 622
Alpha-galactosidase 3 OS=Hypocrea jecorina OX=51453 GN=agl3 PE=1 SV=1
2.08e-93 18 436 56 477
Putative alpha-galactosidase 8 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agl8 PE=5 SV=2
8.73e-14 37 476 1 425
Probable alpha-galactosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=aglB PE=3 SV=1
1.27e-13 50 476 34 446
Probable alpha-galactosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=aglB PE=3 SV=2
1.63e-13 47 458 71 411
Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000385 0.999567 CS pos: 26-27. Pr: 0.7023

TMHMM  Annotations      help

There is no transmembrane helices in TRIREDRAFT_75015-t26_1-p1.