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CAZyme Information: AN7657-T-p1

You are here: Home > Sequence: AN7657-T-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 Aspergillus nidulans
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus nidulans
CAZyme ID AN7657-T-p1
CAZy Family GH95
CAZyme Description Putative 1,3-beta-glucanosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
455 48882.98 4.4390
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AnidulansFGSCA4 10988 227321 276 10712
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.-:26

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH72 27 326 7.5e-131 0.9871794871794872

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
397351 Glyco_hydro_72 4.27e-176 24 328 4 315
Glucanosyltransferase. This is a family of glycosylphosphatidylinositol-anchored beta(1-3)glucanosyltransferases. The active site residues in the Aspergillus fumigatus example are the two glutamate residues at 160 and 261.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 455 1 455
1.01e-262 1 455 1 453
3.12e-238 1 453 1 450
3.12e-238 1 453 1 450
3.12e-238 1 453 1 450

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.75e-73 32 332 36 347
Saccharomyces cerevisiae Gas2p in complex with laminaripentaose [Saccharomyces cerevisiae],2W63_A Saccharomyces Cerevisiae Gas2p In Complex With Laminaritriose And Laminaritetraose [Saccharomyces cerevisiae],5O9O_A Crystal structure of ScGas2 in complex with compound 7. [Saccharomyces cerevisiae S288C],5O9P_A Crystal structure of Gas2 in complex with compound 10 [Saccharomyces cerevisiae S288C],5O9Q_A Crystal structure of ScGas2 in complex with compound 6 [Saccharomyces cerevisiae S288C],5O9R_A Crystal structure of ScGas2 in complex with compound 9 [Saccharomyces cerevisiae S288C],5O9Y_A Crystal structure of ScGas2 in complex with compound 11 [Saccharomyces cerevisiae S288C],5OA2_A Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA2_B Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA2_C Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA6_A Crystal structure of ScGas2 in complex with compound 12 [Saccharomyces cerevisiae S288C]
1.86e-72 32 332 36 347
Saccharomyces cerevisiae Gas2p apostructure (E176Q mutant) [Saccharomyces cerevisiae]
1.86e-72 32 332 36 347
SACCHAROMYCES CEREVISIAE GAS2P (E176Q MUTANT) IN COMPLEX WITH LAMINARITETRAOSE AND LAMINARIPENTAOSE [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.36e-239 1 453 1 450
1,3-beta-glucanosyltransferase gel1 OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=gel1 PE=1 SV=1
2.25e-238 1 453 1 450
1,3-beta-glucanosyltransferase gel1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=gel1 PE=3 SV=1
5.94e-136 5 377 5 378
1,3-beta-glucanosyltransferase GAS5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GAS5 PE=1 SV=1
6.87e-132 29 373 19 364
1,3-beta-glucanosyltransferase PGA4 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=PGA4 PE=1 SV=1
3.25e-131 31 385 27 387
1,3-beta-glucanosyltransferase gas4 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=gas4 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000546 0.999423 CS pos: 26-27. Pr: 0.6188

TMHMM  Annotations      download full data without filtering help

Start End
432 454