CAZyme Information: MGYG000003929_02742

Basic Information

• Species: CAG-590 sp900544905
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-590; CAG-590 sp900544905
• CAZyme ID: MGYG000003929_02742
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1144	MGYG000003929_12|CGC1	126077.92	4.697

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003929	3094552	MAG	United Kingdom	Europe

• Gene Location: Start: 42826; End: 46260 Strand: +

Full Sequence      

MGNVMKKIIAFMMAVVLVMGTISIDSQAASKKKAVKSISITNLETKTLVLKPKKTFKLKT
KVKVSGRVSKKVTYSSSNKKVATVSKTGKIKAVKKGTAKITVKSAANKKKKVTIKVIVGT
PVKKVTLNKKSAKAYVGDTIKLKATISPKKPSVKKLKYNSSNTAVAKVSSKGVVTCLAEG
KAKITVKATDGSGKKAVCNVTVQKKTTEEPTTEKKQDTSTTEDKKPDKTTTEDKKPDKDT
TEEKKDLSYSGYELKWMDDFDGTALNRDNWNVETHEPGWVNSELQEYVDSDENIYVKDGN
LIIKPVKTVDEDGNVSYTSGRVNTQNKQDFTYGLFEVRAKVPEGQGYLPAFWMMPTNENL
YGQWPRCGEIDIMEVMGQENNKAYGTIHYGNPHSESQGIHVLNQGNYTDSYHVFSCEWEP
GKIRWYVDGILYHEESDWYSTTAGQGTVSYPAPFDQPFYMILNLAVGGSWVGNPNDSTDF
ENAAFVIDYVKAYQKDSYDENVSKPEKEVVLRDPDANGNYVNNGDFAAAESLTDDEDWKF
MTALEGEAEAAIENNSIKVTTSNAGTVDYSVQLVQAGIPFEKGATYTVSFDARATAARTM
KTAIKAPDHGYSEYMTAKTVDLTTENQTYSYEFKMTSDSDANGRLEFNIGAAGSTEDIYI
SNVSIKKTQEANPDEKEEKTILADGNYVYNGSFQEGEGRLGYWEITNNADASVSVTNANT
DRKLKVTVDKDGTEAGDVLVAQSDLAIEGGGTYALSFDAQADSARNMKIVVAGQELTANL
TEESNSYSFKITTAEELTDKNIVFYMGEKGTVYLDNVRLVEDALIKNGSFNAGFAGYEWY
VDSSADAANVVDSLSEDNAADFTIKDTGDQDWKIQLKQNNVELEKGQWYKLSFKAKSSLP
RKIRVIMQGTEAKNYAVYSGENTVTLDTDYQTYEKTFQMTAETDTQAFLSICLGKIDERI
TTQHRVCVDDIVLEKVEAPEIPEVEPGENILKNGDFSDGSTSWENAVTSPGEASVSFDDN
KAVYDITNVGTADWNVQLKQNDIMLEKGCKYKISFKACSTEARTIKLAMLSSTYAWYGGA
DIALEKDVEKDVVIEFTMEADTDAATTMVVSMGQIFEADNVTEIDTPASTITLSDFVLEK
VATE

Enzyme Prediction     

No EC number prediction in MGYG000003929_02742.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	256	493	1.6e-80	0.9956521739130435
CBM4	519	650	2.6e-36	0.9920634920634921
CBM4	824	954	5.7e-31	0.9841269841269841
CBM4	989	1113	3.6e-29	0.9920634920634921
CBM4	686	807	3.2e-21	0.9920634920634921

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	1.75e-98	256	493	1	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.
cd08024	GH16_CCF	4.13e-56	256	494	3	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.
cd02182	GH16_Strep_laminarinase_like	8.18e-50	251	494	1	259	Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel.
cd00413	Glyco_hydrolase_16	1.71e-41	258	493	1	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.
cd02179	GH16_beta_GRP	1.04e-35	258	493	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAA34888.1	0.0	247	1140	332	1220
QWT52878.1	0.0	247	1141	244	1135
QQQ91210.1	0.0	246	1125	256	1146
ASU30685.1	0.0	246	1125	256	1146
ANU77877.1	0.0	246	1125	256	1146

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VY0_A	2.70e-55	252	493	13	259	TheX-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus],2VY0_B The X-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus]
3AZX_A	1.66e-52	252	506	10	266	Crystalstructure 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	1.95e-52	252	494	18	263	Structureof 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]
3ATG_A	1.25e-49	253	505	4	250	endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
2HYK_A	5.76e-49	254	494	9	243	Thecrystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23903	5.55e-53	246	495	417	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
C1IE32	2.69e-42	248	493	16	267	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
P45798	4.17e-42	252	494	40	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q9ZG90	2.61e-31	252	494	56	288	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1
Q27082	5.33e-30	252	505	25	260	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000431	0.998827	0.000230	0.000163	0.000159	0.000154

TMHMM  Annotations     

start	end
7	29