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CAZyme Information: CC1G_05454-t26_1-p1

You are here: Home > Sequence: CC1G_05454-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 Coprinopsis cinerea
Lineage Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
CAZyme ID CC1G_05454-t26_1-p1
CAZy Family GH10
CAZyme Description glycosyl transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
533 AACS02000011|CGC2 60264.19 5.0231
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ccinereaokay7-130 13657 240176 301 13356
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in CC1G_05454-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT8 224 458 5.5e-41 0.8949416342412452

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
133037 GT8_A4GalT_like 1.37e-46 232 476 1 246
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.
279798 Glyco_transf_8 6.63e-28 233 478 1 250
Glycosyl transferase family 8. This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.
224359 RfaJ 2.37e-26 232 506 3 273
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis].
404466 Methyltransf_24 6.05e-19 44 161 1 106
Methyltransferase domain. This family appears to be a methyltransferase domain.
132996 Glyco_transf_8 3.66e-17 232 458 1 243
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.45e-183 13 528 10 539
5.64e-182 13 530 10 537
5.64e-182 13 530 10 537
4.10e-175 13 499 948 1441
6.87e-27 18 205 10 197

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.53e-13 233 458 2 251
Chain A, GLYCOSYL TRANSFERASE [Neisseria meningitidis],1GA8_A Chain A, GALACTOSYL TRANSFERASE LGTC [Neisseria meningitidis]
7.42e-13 232 458 1 251
Chain A, alpha-1,4-galactosyl transferase [Neisseria meningitidis]
1.27e-08 320 511 100 280
Crystal structure of the glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVV_F Crystal structure of the glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae]
1.27e-08 320 511 100 280
Crystal structure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVW_B Crystal structure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVW_C Crystal structure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVW_D Crystal structure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.64e-10 320 452 106 231
Probable glycosyl transferase Gly OS=Streptococcus gordonii OX=1302 GN=gly PE=3 SV=2
2.74e-08 320 454 95 224
Glycosyltransferase GlyF OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyF PE=3 SV=1
6.55e-08 320 511 100 280
Glycosyltransferase GlyE OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyE PE=1 SV=1
8.76e-07 314 471 118 284
Lipopolysaccharide 1,2-glucosyltransferase OS=Escherichia coli (strain K12) OX=83333 GN=rfaJ PE=3 SV=2
3.59e-06 320 452 393 519
Glycosyltransferase GlyA OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000059 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in CC1G_05454-t26_1-p1.