dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: Bcin10g04190.1:RNA-p1

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Basic Information help

Species

Botrytis cinerea

Lineage

Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Botrytis; Botrytis cinerea

CAZyme ID

Bcin10g04190.1:RNA-p1

CAZy Family

GH55

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
713		78782.90	5.5182

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BcinereaB05-10	12073	332648	366	11707

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	1.1.3.9:34	1.1.3.13:3	1.1.3.-:1	1.1.3.7:1	1.1.3.47:1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA5	7	502	3.8e-128	0.37158469945355194

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
199882	E_set_GO_C	3.44e-32	391	490	1	103	C-terminal Early set domain associated with the catalytic domain of galactose oxidase. E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.
401164	DUF1929	2.32e-23	402	485	2	86	Domain of unknown function (DUF1929). Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. Their precise function, has not, as yet, been defined, though they are mostly found in sugar-utilising enzymes, such as galactose oxidase.
276965	Kelch	5.67e-07	235	371	1	131	Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.
276965	Kelch	3.69e-05	92	202	10	111	Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.
276965	Kelch	1.25e-04	189	338	1	137	Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
0.0	1	713	1	713
1.53e-73	8	503	36	517
1.78e-72	8	498	27	509
2.25e-61	3	497	110	585
8.66e-57	8	488	101	565

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
9.93e-42	8	485	4	475	Novel fungal alcohol oxidase with catalytic diversity among the AA5 family, apo form [Colletotrichum graminicola M1.001],5C92_A Novel fungal alcohol oxidase with catalytic diversity among the AA5 family, in complex with copper [Colletotrichum graminicola M1.001]
2.22e-37	3	485	198	684	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
2.22e-37	3	485	198	684	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
2.22e-37	3	485	198	684	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001],6STX_C Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
1.12e-36	107	485	233	609	Structure of Galactose Oxidase homologue from Streptomyces lividans [Streptomyces lividans],4UNM_B Structure of Galactose Oxidase homologue from Streptomyces lividans [Streptomyces lividans]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.41e-33	8	485	200	673	Galactose oxidase OS=Gibberella zeae OX=5518 GN=GAOA PE=1 SV=1
4.31e-33	8	485	200	673	Galactose oxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GAOA PE=3 SV=1
2.16e-26	54	492	75	523	Aldehyde oxidase GLOX OS=Vitis pseudoreticulata OX=231512 GN=GLOX PE=2 SV=1
1.32e-24	75	493	476	906	WSC domain-containing protein ARB_07867 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07867 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000075	0.000001

TMHMM Annotations help

There is no transmembrane helices in Bcin10g04190.1:RNA-p1.