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CAZyme Information: EEP82810.1

You are here: Home > Sequence: EEP82810.1

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 Uncinocarpus reesii
Lineage Ascomycota; Eurotiomycetes; ; Onygenaceae; Uncinocarpus; Uncinocarpus reesii
CAZyme ID EEP82810.1
CAZy Family GT66
CAZyme Description conserved hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
485 54786.03 9.9977
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ureesii1704 7856 336963 96 7760
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EEP82810.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT90 108 343 2.3e-18 0.972

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
310354 Glyco_transf_90 9.58e-23 144 334 122 312
Glycosyl transferase family 90. This family of glycosyl transferases are specifically (mannosyl) glucuronoxylomannan/galactoxylomannan -beta 1,2-xylosyltransferases, EC:2.4.2.-.
214773 CAP10 6.32e-19 108 342 3 250
Putative lipopolysaccharide-modifying enzyme.
340831 GT4_PimA-like 0.005 285 330 313 359
phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.61e-158 1 369 31 447
4.95e-151 1 368 38 450
4.95e-151 1 368 38 450
5.66e-150 1 368 38 450
5.66e-150 1 368 38 450

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.37e-07 79 337 110 371
Crystal structure of Drosophila Poglut1 (Rumi) complexed with its glycoprotein product (glucosylated EGF repeat) and UDP [Drosophila melanogaster],5F85_A Crystal structure of Drosophila Poglut1 (Rumi) complexed with its substrate protein (EGF repeat) and UDP [Drosophila melanogaster],5F86_A Crystal structure of Drosophila Poglut1 (Rumi) complexed with its substrate protein (EGF repeat) [Drosophila melanogaster],5F87_A Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster],5F87_B Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster],5F87_C Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster],5F87_D Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster],5F87_E Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster],5F87_F Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.97e-07 144 346 177 387
O-glucosyltransferase rumi homolog OS=Anopheles gambiae OX=7165 GN=AGAP004267 PE=3 SV=1
7.16e-07 79 344 120 388
O-glucosyltransferase rumi OS=Drosophila pseudoobscura pseudoobscura OX=46245 GN=rumi PE=3 SV=1
7.19e-07 79 337 122 383
O-glucosyltransferase rumi OS=Drosophila melanogaster OX=7227 GN=rumi PE=1 SV=1
1.96e-06 94 344 216 466
Protein O-glucosyltransferase 2 OS=Mus musculus OX=10090 GN=Poglut2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000040 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in EEP82810.1.