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CAZyme Information: FPRO_05588-t41_1-p1

You are here: Home > Sequence: FPRO_05588-t41_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 Fusarium proliferatum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
CAZyme ID FPRO_05588-t41_1-p1
CAZy Family PL4
CAZyme Description uncharacterized protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
445 FJOF01000003|CGC19 49837.00 6.1930
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FproliferatumET1 16509 1227346 366 16143
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in FPRO_05588-t41_1-p1.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
340850 GT4_ExpE7-like 1.57e-17 137 417 87 339
glycosyltransferase ExpE7 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
340831 GT4_PimA-like 8.49e-11 76 414 15 342
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.
223515 RfaB 8.18e-10 149 422 88 359
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
404563 Glyco_trans_1_4 6.02e-07 259 405 6 138
Glycosyl transferases group 1.
340816 Glycosyltransferase_GTB-type 9.20e-07 233 361 83 224
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
3.61e-279 1 445 1 448
8.00e-195 1 439 30 471
6.10e-111 1 441 24 461
4.33e-110 1 439 2 410
8.66e-109 1 439 12 417

PDB Hits      help

FPRO_05588-t41_1-p1 has no PDB hit.

Swiss-Prot Hits      help

FPRO_05588-t41_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000056 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in FPRO_05588-t41_1-p1.