CAZyme Information: KIS67016.1

Basic Information

• Species: Ustilago maydis
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Ustilago; Ustilago maydis
• CAZyme ID: KIS67016.1
• CAZy Family: CE9
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
486		54665.40	8.3146

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Umaydis521	6910	237631	145	6765

• Gene Location: location=CM003154:660-2120(-)

Full Sequence      

MLFRKNKKSKAQLDSVLPPSGSQDNVSAETKSSDDGHSTDSRPVTIDCLPITKAAQRDLL
QPPHGFVSRRIDIDTWTPPNLWSLSKRGKRSKRMDYLFVLFGILVGVLASGAVIGLGIFS
FMSDQHKYCLALDEQFDGPLNTNIWSREVQVGGFGNKEFEWTTASSNNSYTKDGKLYITP
TLTADAIGEGAVTNGYTVNLTQSGECTAPRVPWMDRTDSEDIRMASIRNADVNCQISSNS
TLGTVIPPVQSARLTTNASFSMRYGRVEVRARMPTGDWLWPAVWMMPRDSVYGEWPKSGE
IDLFEGKGNQARSRTEQLSNTMRSALHWGNDATTDQYLKTNQVSTLWRNLWNDEFHTFGL
EWDEHGIWTWRDSRARRVLNVRFKEPFINQMPKVQLQNGGGMVPAPNPWSKSTNNGAPFD
QDFYLILNLAVGGTNGYFADVGQPWSNDDPRAAATFWSQRASWLPSWGSVEKRSMVIDYV
KAWKRC

Enzyme Prediction     

EC	3.2.1.39:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	135	483	1.8e-106	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185694	GH16_CCF	2.35e-144	130	484	1	330	Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
185688	GH16_beta_GRP	1.32e-61	134	483	5	320	beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16. Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
185693	GH16_laminarinase_like	1.23e-52	133	483	3	235	Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
225182	BglS	1.48e-14	251	424	105	260	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
185683	Glyco_hydrolase_16	8.05e-12	247	483	51	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SJX63888.1|GH16_4	3.52e-139	77	486	160	555
CDU25158.1|GH16_4	2.93e-136	65	486	44	451
CBQ68259.1|GH16_4	7.93e-135	78	486	160	554
CDU25173.1|GH16_4	3.54e-129	68	486	59	461
CDR88142.1|GH16_4	1.38e-128	66	486	166	571

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ILN_A	1.08e-19	251	436	72	225	Chain A, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
3AZX_A	9.79e-19	122	433	1	230	Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZX_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZZ_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3B00_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B01_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8]
4DFS_A	1.22e-18	251	433	91	238	Structure of the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4DFS_B Structure of the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1]
2HYK_A	1.53e-18	130	433	9	218	The crystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]
3ATG_A	1.57e-17	130	433	5	214	endo-1,3-beta-glucanase from Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8N0N3|BGBP_PENMO	3.00e-66	129	484	31	360	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1
sp|Q9NL89|BGBP_BOMMO	2.92e-37	130	481	185	491	Beta-1,3-glucan-binding protein OS=Bombyx mori OX=7091 PE=1 SV=1
sp|Q0E666|BGBP1_GALME	8.13e-35	130	483	179	488	Beta-1,3-glucan-binding protein 1 OS=Galleria mellonella OX=7137 GN=bgrp1 PE=1 SV=1
sp|Q76DI2|BGBP_TENMO	5.25e-32	140	481	177	477	Beta-1,3-glucan-binding protein OS=Tenebrio molitor OX=7067 GN=GRP PE=1 SV=1
sp|Q9NJ98|BGBP1_MANSE	4.33e-30	130	483	173	485	Beta-1,3-glucan-binding protein 1 OS=Manduca sexta OX=7130 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000051	0.000000

TMHMM  Annotations     

Start	End
96	118