CAZyme Information: MGYG000002289_00620

Basic Information

• Species: Coprococcus sp000433075
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus sp000433075
• CAZyme ID: MGYG000002289_00620
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1222	MGYG000002289_1|CGC7	134901.36	4.345

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002289	2644240	Isolate	China	Asia

• Gene Location: Start: 736114; End: 739782 Strand: +

Full Sequence      

MVKGKKYLALFLAAGLVITAMPLGTTHATGIIDNDPVTTVNSEDVVDPSTDLSYEGYKEV
WGDEFDGTELNRDVWNVETHEKGWVNSELQAYVDNDEVLQVKDGYLNINPVKTVEHSSEA
AAIVKNADFSSGKDDWVETIADWGDPYHTVASSTVVDNGIKYTITDPGDEDWHVQLKQDN
LNLKEGHTYKVAYNVTSTAARQIKSGVQSAAYTWYGGADPVLEANVVTPVEYEFTMEADD
DTATVYFSLGKIADVETPASDITITDITFTDLSDDGEGEDVVNYTSGRISTQNKQTFTYG
LFECRAKVPAGKGYLPAFWLMANDENVYGQWPRCGEIDCMEVMGQDPDKLYGTIHYGNPH
AESQGTYEITDGASFADEFHTFACEWLPGKINWYVDGKLYHTESNWHSTTVGQGTLTYPA
PFDQPFYIILNLAVGGSWVGNPDDTTNFDNNPYVIDYVKVYQKDSYDENVQKPENNVELR
DPDVTGNYVNNGDFSVEEDLTDDTDWKFLTALGGEAAATISGNEINIDTTNEGTVDYSVQ
LVQAGVPLLKGATYKVSFDACAAEARTMHVDIKAPDHGYINYMNGTGAEVALDTEYNHYE
YEFKMKSDSDANGRLEYNIGAAGSNAQIKLKNVRIEKIADPDPNEKEEKTVLANGNYVYN
GGFQEGTGHLGYWDIAKSEGSSVSVTDYKDGRRFKAVIPEAASEYVFLSQDDMTFNEGTP
YLFSFDLEADTDTTVKAVIAGVECEAEVVKGDKKTYRFEIPPTTEFSDKSVSFTFDAAGT
YYLDNVKMVENAMIKNGSFNDGETGYTIYIDSSAKASHVVDSIKEDNALSLTIDKTGDAD
WKIQVKQEDVKLEAGKTYRLKLKAKSSVDRDIRVVMQGGEKLGWPVYSNDNVISLTSEYT
EIEDVFTMNEDTDPAAFLSICLGKVDREITDQHVVCIDDISLEEVKAEKEIPEYEVPENQ
TIHCGQTLADITLPEGFSFEEPGLELAPGISKVTLKYTPADTDKYEIVTGIEITITVEHD
YKDGVCVCGDIADGFAKVNGKWGFYKDQKIVSNYTGVVKGVIDGKSNWYYVKNGVYTKAS
GITKRVDGKGNWYYVKNGVYTKASGIAKKVDGTGNWYYVKNGVLTRTNGITKKADGSSAT
WFYVKNGVFTKATGIAKKADGSGATWYYVKNGAYTKDTCIAKKADGSSKTQYYVKTGSWA
NKFTGTIKIGKKNYKIVNGVVK

Enzyme Prediction     

No EC number prediction in MGYG000002289_00620.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	281	461	2.1e-61	0.7521739130434782
CBM4	487	620	6.6e-33	0.9920634920634921
CBM4	793	923	1.4e-28	0.9841269841269841

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	1.94e-69	274	461	54	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	7.64e-36	286	462	101	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.
cd00413	Glyco_hydrolase_16	1.97e-33	283	461	52	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.
COG2273	BglS	1.95e-31	259	465	78	269	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd02182	GH16_Strep_laminarinase_like	9.00e-30	283	462	67	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNL98962.1	0.0	3	946	3	966
QAA34888.1	1.93e-239	3	947	263	1064
QWT52878.1	1.91e-234	52	953	244	984
QQQ91210.1	2.07e-216	49	980	254	1028
QMW76264.1	2.07e-216	49	980	254	1028

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VY0_A	8.33e-43	272	461	75	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]
4DFS_A	9.06e-43	283	462	88	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]
3AZX_A	1.42e-42	283	462	80	255	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]
3ATG_A	2.67e-41	275	473	51	250	endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
2HYK_A	1.46e-39	284	462	72	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	1.34e-36	284	463	501	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
C1IE32	2.14e-34	284	459	88	265	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
P45798	2.01e-33	284	462	105	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q9ZG90	9.94e-26	280	462	115	288	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1
Q27082	1.11e-21	277	462	79	253	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
0.000297	0.998993	0.000182	0.000188	0.000174	0.000155

TMHMM  Annotations     

start	end
7	29