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CAZyme Information: MGYG000000014_01918
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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 | Clostridium butyricum | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium butyricum | |||||||||||
| CAZyme ID | MGYG000000014_01918 | |||||||||||
| CAZy Family | CBM27 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 204055; End: 207858 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH26 | 295 | 644 | 1.2e-58 | 0.9306930693069307 |
| CBM23 | 780 | 948 | 2.5e-41 | 0.9876543209876543 |
| CBM27 | 104 | 259 | 5.2e-22 | 0.9761904761904762 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| NF033930 | pneumo_PspA | 3.35e-46 | 1119 | 1264 | 476 | 620 | pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus. |
| NF033930 | pneumo_PspA | 7.91e-44 | 1118 | 1266 | 515 | 660 | pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus. |
| NF033838 | PspC_subgroup_1 | 1.08e-43 | 1118 | 1266 | 518 | 683 | pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. |
| NF033930 | pneumo_PspA | 1.40e-43 | 1126 | 1264 | 443 | 580 | pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus. |
| NF033930 | pneumo_PspA | 1.58e-42 | 1121 | 1264 | 458 | 600 | pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AXB85606.1 | 0.0 | 1 | 1267 | 1 | 1267 |
| QGH21752.1 | 0.0 | 1 | 1267 | 1 | 1267 |
| QGH25791.1 | 0.0 | 1 | 1267 | 1 | 1267 |
| QSX03803.1 | 0.0 | 1 | 1267 | 1 | 1444 |
| QJU44978.1 | 0.0 | 1 | 1267 | 1 | 1444 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4YN5_A | 5.18e-64 | 293 | 661 | 50 | 414 | Catalyticdomain of Bacillus sp. JAMB-750 GH26 Endo-beta-1,4-mannanase [Bacillus sp. JAMB750] |
| 2BVT_A | 1.59e-54 | 292 | 726 | 6 | 420 | Thestructure of a modular endo-beta-1,4-mannanase from Cellulomonas fimi explains the product specificity of glycoside hydrolase family 26 mannanases. [Cellulomonas fimi],2BVT_B The structure of a modular endo-beta-1,4-mannanase from Cellulomonas fimi explains the product specificity of glycoside hydrolase family 26 mannanases. [Cellulomonas fimi],2BVY_A The structure and characterization of a modular endo-beta-1,4-mannanase from Cellulomonas fimi [Cellulomonas fimi] |
| 1J9Y_A | 2.77e-54 | 289 | 661 | 6 | 369 | Crystalstructure of mannanase 26A from Pseudomonas cellulosa [Cellvibrio japonicus] |
| 1R7O_A | 3.58e-54 | 289 | 661 | 16 | 379 | CrystalStructure of apo-mannanase 26A from Psudomonas cellulosa [Cellvibrio japonicus] |
| 2WHM_A | 5.11e-54 | 289 | 661 | 6 | 369 | Cellvibriojaponicus Man26A E121A and E320G double mutant in complex with mannobiose [Cellvibrio japonicus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P49424 | 3.95e-53 | 289 | 661 | 44 | 407 | Mannan endo-1,4-beta-mannosidase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=manA PE=1 SV=2 |
| A1A278 | 6.84e-53 | 290 | 947 | 38 | 697 | Mannan endo-1,4-beta-mannosidase OS=Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) OX=367928 GN=BAD_1030 PE=1 SV=1 |
| P16699 | 1.52e-18 | 285 | 549 | 22 | 274 | Mannan endo-1,4-beta-mannosidase A and B OS=Caldalkalibacillus mannanilyticus (strain DSM 16130 / CIP 109019 / JCM 10596 / AM-001) OX=1236954 PE=1 SV=1 |
| P55278 | 1.41e-14 | 449 | 564 | 167 | 284 | Mannan endo-1,4-beta-mannosidase OS=Bacillus subtilis OX=1423 PE=3 SV=1 |
| Q5AWB7 | 3.20e-14 | 419 | 612 | 151 | 324 | Probable mannan endo-1,4-beta-mannosidase E OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=manE PE=3 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 |
|---|---|---|---|---|---|
| 0.023596 | 0.759972 | 0.213318 | 0.001895 | 0.000729 | 0.000458 |