dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Fusarium proliferatum

Lineage

Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum

CAZyme ID

FPRO_09787-t41_1-p1

CAZy Family

GH20

CAZyme Description

related to glucan 1,3-beta-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
854	FJOF01000006\|CGC14	94070.28	9.2794

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

Enzyme Prediction help

EC	3.2.1.39:20

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH81	171	847	9.4e-210	0.9839228295819936

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
227785	Acf2	0.0	106	852	20	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	1.43e-144	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	6.46e-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.
200437	ADF_drebrin_like	0.004	340	397	21	84	ADF homology domain of drebrin and actin-binding protein 1 (abp1). Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Many of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. Abp1 and drebrin (developmentally regulated brain protein) are multidomain proteins with an N-terminal ADF homology domain and one or more C-terminal SH3 domains. They have been shown to interact with polymeric F-actin, but not with monomeric G-actin, and do not appear to promote the disassembly of actin filaments. Drebrin rather stabilizes actin filaments by inducing changes in the helical twist and may promote or interfere with the interactions of other proteins with actin filaments.

CAZyme Hits help

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

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
7.08e-84	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]
1.15e-83	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]
1.32e-82	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]
1.53e-24	460	828	285	637	Chain A, Glycoside hydrolase family 81 [Acetivibrio thermocellus ATCC 27405]
8.12e-17	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
5.42e-224	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
8.67e-173	147	852	7	703	Ascus wall endo-1,3(4)-beta-glucanase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=eng2 PE=1 SV=1
4.93e-151	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
1.62e-141	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
1.32e-140	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
0.000193	0.999790	CS pos: 21-22. Pr: 0.9817

TMHMM Annotations help

There is no transmembrane helices in FPRO_09787-t41_1-p1.

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