CAZyme Information: FPRN_10470-t42_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRN_10470-t42_1-p1
• CAZy Family: GH3
• CAZyme Description: related to xyloglucan endo-transglycosylase-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
298	FCQG01000008|CGC2	32788.62	5.5106

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FproliferatumNRRL62905	15602	N/A	348	15254

• Gene Location: location=FCQG01000008:83730-84813(+)

Full Sequence      

MILPLTHLLATARLVSGACECGYSIKNPQGESQIVFTDRLETKFSQLHSISEGHDWLAQN
FTVSAADGRGNFSKAFLPNNVNTHGTKSGDGSGLELRYFNDTQEIDIEFLSQDFDHDNGI
YPINLVVQSKKSLEAGYDASKTGSFKRVKLDFDPTDAFHEYRFDYLPGQVLFYADGNLLA
HMKGGDMPSSGGHLILQHWSNGNPLWSGGPPKEDATVTVSYVKAYFNSSNSERQSQLVRR
CHESSKENPVCAINDSDNDEIDSAGASPRRIAQVNSVCVLIVGLVMPLLQLSHVFLVV

Enzyme Prediction     

No EC number prediction in FPRN_10470-t42_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	98	225	5.3e-64	0.6614583333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185683	Glyco_hydrolase_16	5.64e-27	101	225	97	210	glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.
185684	GH16_lichenase	3.08e-09	98	221	94	205	lichenase, member of glycosyl hydrolase family 16. Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure.
395585	Glyco_hydro_16	2.15e-06	39	223	24	168	Glycosyl hydrolases family 16.
178706	PLN03161	0.008	104	176	101	161	Probable xyloglucan endotransglucosylase/hydrolase protein; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCT71404.1|GH16_23	3.64e-214	1	298	1	298
QGI84375.1|GH16_23	3.64e-214	1	298	1	298
QGI98026.1|GH16_23	3.64e-214	1	298	1	298
QGI67140.1|GH16_23	3.64e-214	1	298	1	298
QKD58555.1|GH16_23	5.59e-193	1	298	1	298

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1CPN_A	1.27e-08	104	233	47	174	NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS [Paenibacillus macerans]
1MAC_A	6.10e-08	104	208	103	192	Crystal Structure And Site-Directed Mutagenesis Of Bacillus Macerans Endo-1,3-1,4-Beta-Glucanase [Paenibacillus macerans],1MAC_B Crystal Structure And Site-Directed Mutagenesis Of Bacillus Macerans Endo-1,3-1,4-Beta-Glucanase [Paenibacillus macerans]
1AJK_A	6.23e-08	104	208	22	111	Circularly Permuted (1-3,1-4)-Beta-D-Glucan 4- Glucanohydrolase Cpa16m-84 [Paenibacillus macerans],1AJK_B Circularly Permuted (1-3,1-4)-Beta-D-Glucan 4- Glucanohydrolase Cpa16m-84 [Paenibacillus macerans]
1BYH_A	6.23e-08	104	208	105	194	MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE [synthetic construct],1GLH_A Cation Binding To A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity And Effect On Protein Stability [Paenibacillus macerans],2AYH_A Crystal And Molecular Structure At 1.6 Angstroms Resolution Of The Hybrid Bacillus Endo-1,3-1,4-Beta-D-Glucan 4- Glucanohydrolase H(A16-M) [hybrid]
1CPM_A	6.23e-08	104	208	47	136	NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS [Paenibacillus macerans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23904|GUB_PAEMA	4.01e-07	104	208	128	217	Beta-glucanase OS=Paenibacillus macerans OX=44252 PE=1 SV=2
sp|P45797|GUB_PAEPO	1.81e-06	104	208	129	218	Beta-glucanase OS=Paenibacillus polymyxa OX=1406 GN=gluB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.848919	0.151111

TMHMM  Annotations     

There is no transmembrane helices in FPRN_10470-t42_1-p1.