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CAZyme Information: MGYG000003165_00269
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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 sp900548315 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus sp900548315 | |||||||||||
| CAZyme ID | MGYG000003165_00269 | |||||||||||
| CAZy Family | CBM4 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 5805; End: 8093 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH9 | 329 | 759 | 3e-112 | 0.9952153110047847 |
| CBM4 | 77 | 200 | 2.2e-25 | 0.9761904761904762 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam00759 | Glyco_hydro_9 | 2.17e-97 | 331 | 758 | 1 | 374 | Glycosyl hydrolase family 9. |
| cd02850 | E_set_Cellulase_N | 1.02e-21 | 241 | 324 | 2 | 86 | N-terminal Early set domain associated with the catalytic domain of cellulase. E or "early" set domains are associated with the catalytic domain of cellulases at the N-terminal end. Cellulases are O-glycosyl hydrolases (GHs) that hydrolyze beta 1-4 glucosidic bonds in cellulose. They are usually categorized into either exoglucanases, which sequentially release terminal sugar units from the cellulose chain, or endoglucanases, which also attack the chain internally. The N-terminal domain of cellulase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others. |
| PLN02909 | PLN02909 | 3.56e-19 | 377 | 699 | 77 | 413 | Endoglucanase |
| PLN02345 | PLN02345 | 4.81e-19 | 367 | 759 | 29 | 456 | endoglucanase |
| PLN02613 | PLN02613 | 6.35e-18 | 477 | 755 | 168 | 472 | endoglucanase |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CBK83282.1 | 0.0 | 1 | 762 | 1 | 757 |
| QWT52372.1 | 1.30e-255 | 3 | 762 | 3 | 767 |
| QNL99669.1 | 2.27e-255 | 3 | 762 | 3 | 765 |
| ADU86915.1 | 1.22e-225 | 74 | 762 | 66 | 784 |
| AHF24789.1 | 2.66e-222 | 65 | 759 | 65 | 771 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3EZ8_A | 1.65e-100 | 238 | 759 | 6 | 529 | CrystalStructure of endoglucanase Cel9A from the thermoacidophilic Alicyclobacillus acidocaldarius [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3GZK_A Structure of A. Acidocaldarius Cellulase CelA [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3H2W_A Structure of A. acidocaldarius cellulase CelA in complex with cellobiose [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3H3K_A Structure of A. acidocaldarius cellulase CelA in complex with cellotetraose [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3RX5_A structure of AaCel9A in complex with cellotriose-like isofagomine [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3RX7_A Structure of AaCel9A in complex with cellotetraose-like isofagomine [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3RX8_A structure of AaCel9A in complex with cellobiose-like isofagomine [Alicyclobacillus acidocaldarius subsp. acidocaldarius] |
| 5E2J_A | 5.80e-100 | 238 | 759 | 29 | 552 | Crystalstructure of single mutant thermostable endoglucanase (D468A) from Alicyclobacillus acidocaldarius [Alicyclobacillus acidocaldarius subsp. acidocaldarius],5E2J_B Crystal structure of single mutant thermostable endoglucanase (D468A) from Alicyclobacillus acidocaldarius [Alicyclobacillus acidocaldarius subsp. acidocaldarius] |
| 4CJ0_A | 3.15e-85 | 227 | 759 | 16 | 545 | ChainA, ENDOGLUCANASE D [Acetivibrio thermocellus],4CJ1_A Chain A, ENDOGLUCANASE D [Acetivibrio thermocellus] |
| 1CLC_A | 4.39e-85 | 227 | 759 | 30 | 559 | ChainA, ENDOGLUCANASE CELD; EC: 3.2.1.4 [Acetivibrio thermocellus] |
| 3X17_A | 1.34e-81 | 243 | 760 | 20 | 555 | Crystalstructure of metagenome-derived glycoside hydrolase family 9 endoglucanase [uncultured bacterium],3X17_B Crystal structure of metagenome-derived glycoside hydrolase family 9 endoglucanase [uncultured bacterium] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P23658 | 1.48e-89 | 239 | 761 | 2 | 545 | Cellodextrinase OS=Butyrivibrio fibrisolvens OX=831 GN=ced1 PE=1 SV=1 |
| P0C2S4 | 1.72e-84 | 227 | 759 | 16 | 545 | Endoglucanase D (Fragment) OS=Acetivibrio thermocellus OX=1515 GN=celD PE=1 SV=1 |
| A3DDN1 | 3.04e-84 | 227 | 759 | 40 | 569 | Endoglucanase D OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celD PE=1 SV=1 |
| P14090 | 3.71e-80 | 97 | 757 | 201 | 903 | Endoglucanase C OS=Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) OX=590998 GN=cenC PE=1 SV=2 |
| A7LXT3 | 1.11e-76 | 241 | 761 | 32 | 578 | Xyloglucan-specific endo-beta-1,4-glucanase BoGH9A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02649 PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as LIPO
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000000 | 0.000001 | 1.000072 | 0.000000 | 0.000000 | 0.000000 |