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CAZyme Information: CVK91159.1

You are here: Home > Sequence: CVK91159.1

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 Fusarium mangiferae
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium mangiferae
CAZyme ID CVK91159.1
CAZy Family CE3
CAZyme Description Endo-1,3(4)-beta-glucanase [Source:UniProtKB/TrEMBL;Acc:A0A1L7SZR9]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
854 FCQH01000004|CGC1 94003.24 9.3333
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FmangiferaeMRC7560 16149 N/A 345 15804
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.39:20

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH81 172 847 1.6e-209 0.9823151125401929

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
227785 Acf2 0.0 128 852 35 756
Endoglucanase Acf2 [Carbohydrate transport and metabolism].
407548 Glyco_hydro81C 0.0 495 845 1 349
Glycosyl hydrolase family 81 C-terminal domain. Family of eukaryotic beta-1,3-glucanases. Within the Aspergillus fumigatus protein, two perfectly conserved Glu residues (E550 or E554) have been proposed as putative nucleophiles of the active site of the Engl1 endoglucanase, while the proton donor would be D475. The endo-beta-1,3-glucanase activity is essential for efficient spore release. This entry represents the helical C-terminal domain.
397619 Glyco_hydro_81 4.89e-143 167 489 1 321
Glycosyl hydrolase family 81. Family of eukaryotic beta-1,3-glucanases. Within the Aspergillus fumigatus protein ENGL1, two perfectly conserved Glu residues (E550 or E554) have been proposed as putative nucleophiles of the active site of the Engl1 endoglucanase, while the proton donor would be D475. The endo-beta-1,3-glucanase activity is essential for efficient spore release.
411776 SP2_N 1.12e-04 112 185 1 73
N-terminal domain of transcription factor Specificity Protein (SP) 2. Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 854 1 854
0.0 1 854 1 854
0.0 1 854 1 854
0.0 1 854 1 854
0.0 1 854 1 854

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.38e-86 153 831 7 703
The structure of a glycoside hydrolase family 81 endo-[beta]-1,3-glucanase [Rhizomucor miehei],4K3A_B The structure of a glycoside hydrolase family 81 endo-[beta]-1,3-glucanase [Rhizomucor miehei]
1.21e-85 153 831 32 728
Crystal structure of GH family 81 beta-1,3-glucanase from Rhizomucr miehei complexed with laminaripentaose [Rhizomucor miehei],5XBZ_B Crystal structure of GH family 81 beta-1,3-glucanase from Rhizomucr miehei complexed with laminaripentaose [Rhizomucor miehei],5XC2_A Crystal structure of GH family 81 beta-1,3-glucanase from Rhizomucr miehei complexed with laminarihexaose [Rhizomucor miehei],5XC2_B Crystal structure of GH family 81 beta-1,3-glucanase from Rhizomucr miehei complexed with laminarihexaose [Rhizomucor miehei],5XC2_C Crystal structure of GH family 81 beta-1,3-glucanase from Rhizomucr miehei complexed with laminarihexaose [Rhizomucor miehei],5XC2_D Crystal structure of GH family 81 beta-1,3-glucanase from Rhizomucr miehei complexed with laminarihexaose [Rhizomucor miehei]
2.67e-84 153 831 7 703
The structure of a glycoside hydrolase family 81 endo-[beta]-1,3-glucanase [Rhizomucor miehei],4K35_B The structure of a glycoside hydrolase family 81 endo-[beta]-1,3-glucanase [Rhizomucor miehei]
3.53e-24 460 828 285 637
Chain A, Glycoside hydrolase family 81 [Acetivibrio thermocellus ATCC 27405]
1.86e-16 526 771 361 604
Chain A, Glycoside Hydrolase [Halalkalibacterium halodurans C-125]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.41e-225 113 849 162 900
Probable endo-1,3(4)-beta-glucanase ARB_01444 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01444 PE=1 SV=1
2.14e-170 167 852 21 703
Ascus wall endo-1,3(4)-beta-glucanase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=eng2 PE=1 SV=1
1.36e-150 146 851 46 737
Primary septum endo-1,3(4)-beta-glucanase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=eng1 PE=3 SV=1
1.21e-140 146 851 401 1112
Endo-1,3(4)-beta-glucanase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DSE4 PE=1 SV=1
2.83e-139 146 850 74 777
Endo-1,3(4)-beta-glucanase 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ACF2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000195 0.999786 CS pos: 21-22. Pr: 0.9823

TMHMM  Annotations      help

There is no transmembrane helices in CVK91159.1.