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CAZyme Information: MGYG000000018_00082

You are here: Home > Sequence: MGYG000000018_00082

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Coprococcus eutactus
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus eutactus
CAZyme ID MGYG000000018_00082
CAZy Family GH16
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1211 MGYG000000018_1|CGC2 132457.67 5.2764
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000018 3280214 Isolate United Kingdom Europe
Gene Location Start: 93638;  End: 97273  Strand: +

Full Sequence      Download help

MRRLKQLVAM  MLVVCMLITL  CPSDVSARTS  KAAVKSVTVT  NLVTNKLVLK  KGTKFQVKPR60
VVVTGKISKK  VTYVSSNKKI  VTVDNKGVVK  AVKSGKAVVA  VKSAANPRVM  YKFNVYVGVP120
TKAVKLSAKA  VNMFKGTSRT  LKASIAPKNA  TYKGIQWSSS  DKRIATVSSK  GVVKAVKVGT180
VYITAKAMDG  SGKYARCKIT  VKQPVTSIKL  SAATLTITEG  SSKTLTATVA  PASATRKTLS240
WTSSNKKIAT  VSAKGVVKAI  APGTATITAK  AADGSGKKAT  CKVTVKKKVT  VENKYESQGY300
KLLWHDEFDG  TELNRDIWNV  ELHEPGWVNN  ELQAYVDSED  NIKVKNGTLI  ISSKKKVNED360
GSISYTSGRV  NTQNKQDFKY  GRVQFRAKVP  TGKGYLPAAW  MMPTNESLYG  QWPRCGEIDV420
MEVLGDNTYT  TYGTIHYGNP  HSESQGKYTL  SNGKSFADSY  HVFTCDWEPG  KITWYVDGVK480
MHEENDWYST  TAGKGTVTYP  APFDQPFYVI  LNLAVGGNWP  GNPDADADYI  NSESLYVDYV540
RVYQKDSYDE  NVTKPEREVI  IRDPDENGNY  VINGDFSETE  DLGDAENWIF  MAQNGGEGTA600
VIENNTININ  TADAGTVDYS  IQLVQPDIPV  EKGATYKLSF  DAWADEARTG  IIDVSAPTRS660
WGRYLKDTKF  DMTTEKQTFE  YEYTMTDSSD  DKGRIEFNFG  NQGSVAGVHI  TNVKLIKTNQ720
TEIVDKKTIL  ADGNLVYNGE  FQEGTGRLGY  WTVSNNCGAE  YKVTGLSDGR  RFSYKSLDES780
VDGNFILSQD  ELAYAPNTKY  VLKFDAESAT  EGKNIIITTG  DSKFAVTLDK  GIKNYVYKFE840
TGEEVTDSSI  SIDFGNSGEV  LLDNVKIMQD  SLLLNGDFSA  DFAGYDVYID  SSADADAVVD900
SQKENNAADF  TIKNSGDQNW  KIQLKQNNIK  LEKGQWYKLS  FDIKSSVSRT  VQYAIQRDGS960
THKDSTGAED  WTPYVQETVK  LDAYDQADQK  YMTVSNTFQM  ACDTDEESIF  NIALGAGGEN1020
GSAITDQHRI  CIDNIVLEKT  SAPEIDVPVG  KNLITNSEFE  MSEDGSLAGW  ENAVTAPGDA1080
TFEAGDGKIT  YSVANVGEAD  WNIQLKQMGL  SLEQGESYTL  KCTLVSDVDR  VVKVAVMTPS1140
AGYAWHGGED  VVLTAGEAKD  VTLTITPKEE  VFTDGITVDT  GAGLFFSMGY  VEGYTLGAHT1200
VSISNVSFVK  N1211

Enzyme Prediction      help

No EC number prediction in MGYG000000018_00082.

CAZyme Signature Domains help

Created with Snap60121181242302363423484544605666726787847908968102910891150304543GH16569700CBM48721015CBM410521169CBM4
Family Start End Evalue family coverage
GH16 304 543 2.9e-80 0.9956521739130435
CBM4 569 700 2.9e-34 0.9920634920634921
CBM4 872 1015 6.9e-25 0.9841269841269841
CBM4 1052 1169 2.2e-20 0.8888888888888888

CDD Domains      download full data without filtering help

Created with Snap60121181242302363423484544605666726787847908968102910891150304543GH16_laminarinase_like302544GH16_CCF299544GH16_Strep_laminarinase_like302543GH16_beta_GRP306543Glyco_hydrolase_16
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08023 GH16_laminarinase_like 6.02e-95 304 543 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 6.56e-48 302 544 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.
cd02182 GH16_Strep_laminarinase_like 2.54e-45 299 544 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.
cd02179 GH16_beta_GRP 4.65e-36 302 543 1 320
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.
cd00413 Glyco_hydrolase_16 7.02e-36 306 543 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.

CAZyme Hits      help

Created with Snap60121181242302363423484544605666726787847908968102910891150251210BCN29267.1|CBM4|GH16_32751210QAA34888.1|CBM4|GH16_32751210QMW76264.1|CBM4|GH16_32751210QIB55869.1|CBM4|GH16_32981210QJU16284.1|CBM4|GH16_3
Hit ID E-Value Query Start Query End Hit Start Hit End
BCN29267.1 0.0 25 1210 28 1201
QAA34888.1 3.88e-304 275 1210 310 1220
QMW76264.1 2.72e-282 275 1210 233 1152
QIB55869.1 2.72e-282 275 1210 233 1152
QJU16284.1 3.85e-282 298 1210 260 1152

PDB Hits      download full data without filtering help

Created with Snap601211812423023634234845446056667267878479089681029108911502965432VY0_A2915563AZX_A2905444DFS_A3025442HYK_A3025553ATG_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VY0_A 1.31e-58 296 543 9 259
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 1.72e-56 291 556 1 266
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 2.74e-56 290 544 8 263
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]
2HYK_A 1.09e-52 302 544 9 243
Thecrystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]
3ATG_A 1.12e-52 302 555 5 250
endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]

Swiss-Prot Hits      download full data without filtering help

Created with Snap60121181242302363423484544605666726787847908968102910891150299545sp|P23903|E13B_NIACI304541sp|C1IE32|E13B_CRYAT300544sp|P45798|GUB_RHOMR300587sp|Q27082|CFGA_TACTR300544sp|Q9ZG90|KSBGL_SPHMU
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P23903 1.36e-54 299 545 422 681
Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
C1IE32 1.83e-39 304 541 24 265
Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
P45798 7.05e-39 300 544 40 283
Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q27082 3.67e-33 300 587 25 288
Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q9ZG90 1.55e-31 300 544 56 288
Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000388 0.748943 0.250045 0.000212 0.000208 0.000178

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000018_00082.