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CAZyme Information: EJT51541.1

You are here: Home > Sequence: EJT51541.1

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 Trichosporon asahii
Lineage Basidiomycota; Tremellomycetes; ; Trichosporonaceae; Trichosporon; Trichosporon asahii
CAZyme ID EJT51541.1
CAZy Family GT3
CAZyme Description Chitobiosyldiphosphodolichol beta-mannosyltransferase [Source:UniProtKB/TrEMBL;Acc:J5TLZ8]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
487 JH977542|CGC1 54326.80 8.9862
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_TasahiiCBS2479 8834 1186058 523 8311
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.142:10 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT33 48 462 3.6e-129 0.9905882352941177

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
340843 GT33_ALG1-like 2.03e-173 47 462 3 408
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins. This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.
215155 PLN02275 1.74e-124 46 412 4 371
transferase, transferring glycosyl groups
223515 RfaB 2.95e-11 55 431 14 356
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340831 GT4_PimA-like 8.45e-10 59 413 15 332
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.
340816 Glycosyltransferase_GTB-type 4.57e-08 158 398 3 235
glycosyltransferase family 1 and related proteins with GTB topology. 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. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.60e-176 23 467 24 502
5.60e-176 23 467 24 502
7.40e-174 23 467 24 502
5.99e-173 23 467 24 502
1.71e-172 23 467 24 502

PDB Hits      help

EJT51541.1 has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.44e-80 45 461 30 457
Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Mus musculus OX=10090 GN=Alg1 PE=1 SV=3
6.69e-77 29 467 16 463
Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Pongo abelii OX=9601 GN=ALG1 PE=2 SV=1
1.02e-75 29 467 16 463
Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Homo sapiens OX=9606 GN=ALG1 PE=1 SV=2
4.41e-74 52 416 9 421
UDP-glycosyltransferase TURAN OS=Arabidopsis thaliana OX=3702 GN=TUN PE=2 SV=1
1.11e-69 40 461 18 416
Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg1 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000081 0.000003

TMHMM  Annotations      download full data without filtering help

Start End
15 37
128 150