You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000002267_04376
You are here: Home > Sequence: MGYG000002267_04376
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 | Eisenbergiella sp003478085 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp003478085 | |||||||||||
| CAZyme ID | MGYG000002267_04376 | |||||||||||
| CAZy Family | GH5 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 42608; End: 43942 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH5 | 46 | 329 | 1.5e-88 | 0.993006993006993 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam00150 | Cellulase | 2.02e-27 | 69 | 330 | 24 | 271 | Cellulase (glycosyl hydrolase family 5). |
| COG2730 | BglC | 3.49e-16 | 39 | 328 | 40 | 363 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]. |
| pfam02449 | Glyco_hydro_42 | 0.003 | 73 | 188 | 14 | 138 | Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BBF45252.1 | 7.31e-152 | 1 | 440 | 1 | 438 |
| BCN30880.1 | 6.71e-137 | 1 | 441 | 1 | 438 |
| CUS27061.1 | 2.11e-100 | 127 | 442 | 1 | 314 |
| QHW32866.1 | 1.09e-79 | 1 | 440 | 1 | 460 |
| EGX46484.1 | 6.45e-75 | 4 | 428 | 10 | 463 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1CEC_A | 1.05e-24 | 21 | 328 | 6 | 316 | ChainA, ENDOGLUCANASE CELC [Acetivibrio thermocellus] |
| 1CEN_A | 2.68e-24 | 21 | 328 | 6 | 316 | ChainA, CELLULASE CELC [Acetivibrio thermocellus],1CEO_A Chain A, CELLULASE CELC [Acetivibrio thermocellus] |
| 7EC9_A | 2.56e-14 | 73 | 328 | 40 | 307 | ChainA, Endoglucanase [Thermotoga maritima MSB8],7EC9_B Chain B, Endoglucanase [Thermotoga maritima MSB8],7EFZ_A Chain A, Endoglucanase [Thermotoga maritima MSB8],7EFZ_B Chain B, Endoglucanase [Thermotoga maritima MSB8] |
| 1VJZ_A | 6.17e-14 | 73 | 328 | 40 | 307 | Crystalstructure of Endoglucanase (TM1752) from Thermotoga maritima at 2.05 A resolution [Thermotoga maritima] |
| 3AMC_A | 2.94e-13 | 73 | 327 | 37 | 288 | Crystalstructures of Thermotoga maritima Cel5A, apo form and dimer/au [Thermotoga maritima MSB8],3AMC_B Crystal structures of Thermotoga maritima Cel5A, apo form and dimer/au [Thermotoga maritima MSB8],3AMD_A Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_B Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_C Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_D Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3MMU_A Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_B Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_C Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_D Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_E Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_F Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_G Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_H Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_A Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_B Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_C Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_D Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| W8QRE4 | 1.88e-73 | 1 | 428 | 1 | 455 | Beta-xylosidase OS=Phanerodontia chrysosporium OX=2822231 GN=Xyl5 PE=1 SV=2 |
| P23340 | 2.26e-24 | 21 | 328 | 6 | 316 | Endoglucanase C307 OS=Clostridium sp. (strain F1) OX=1508 GN=celC307 PE=1 SV=1 |
| A3DJ77 | 2.26e-24 | 21 | 328 | 6 | 316 | Endoglucanase C OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celC PE=3 SV=1 |
| P0C2S3 | 5.77e-24 | 21 | 328 | 6 | 316 | Endoglucanase C OS=Acetivibrio thermocellus OX=1515 GN=celC PE=1 SV=1 |
| Q875R9 | 2.44e-14 | 1 | 261 | 29 | 304 | Glucan 1,3-beta-glucosidase OS=Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651) OX=226302 GN=EXG1 PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000052 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |