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CAZyme Information: MGYG000002331_03139
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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 | Vibrio parahaemolyticus | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio parahaemolyticus | |||||||||||
| CAZyme ID | MGYG000002331_03139 | |||||||||||
| CAZy Family | CBM73 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1523478; End: 1525028 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CBM73 | 464 | 513 | 1.5e-21 | 0.9259259259259259 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00190 | Tryp_SPc | 2.91e-67 | 34 | 261 | 1 | 230 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. |
| smart00020 | Tryp_SPc | 5.89e-67 | 33 | 260 | 1 | 229 | Trypsin-like serine protease. Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues. |
| pfam00089 | Trypsin | 8.65e-44 | 34 | 260 | 1 | 219 | Trypsin. |
| COG5640 | COG5640 | 1.25e-41 | 30 | 370 | 29 | 374 | Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]. |
| cd12215 | ChiC_BD | 6.04e-17 | 391 | 433 | 1 | 41 | Chitin-binding domain of chitinase C. Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QQC97343.1 | 0.0 | 1 | 516 | 1 | 516 |
| ATI48083.1 | 0.0 | 1 | 516 | 1 | 516 |
| QLE36019.1 | 0.0 | 1 | 516 | 1 | 516 |
| AHI99679.1 | 0.0 | 1 | 516 | 1 | 516 |
| AUT87227.1 | 0.0 | 1 | 516 | 1 | 516 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4M7G_A | 3.56e-47 | 34 | 255 | 1 | 213 | StreptomycesErythraeus Trypsin [Saccharopolyspora erythraea] |
| 5DJ7_A | 3.89e-47 | 34 | 255 | 1 | 213 | S.erythraea trypsin acyl-enzyme [Saccharopolyspora erythraea],5DKM_A S. erythraea trypsin Michaelis-Menten complex [Saccharopolyspora erythraea],5KWM_A S. erythraea trypsin long construct apoenzyme [Saccharopolyspora erythraea] |
| 5DK1_A | 7.58e-47 | 34 | 255 | 1 | 213 | S.erythraea trypsin mixed catalytic intermediate [Saccharopolyspora erythraea] |
| 6BQM_A | 4.69e-46 | 30 | 362 | 7 | 339 | Secretedserine protease VesC from Vibrio cholerae [Vibrio cholerae O395] |
| 1FN8_A | 1.78e-45 | 34 | 261 | 1 | 221 | ChainA, TRYPSIN [Fusarium oxysporum],1FY5_A Chain A, TRYPSIN [Fusarium oxysporum],1GDQ_A Chain A, TRYPSIN [Fusarium oxysporum],1GDU_A Chain A, TRYPSIN [Fusarium oxysporum],1PQ5_A Trypsin at pH 5, 0.85 A [Fusarium oxysporum],1PQ7_A Trypsin at 0.8 A, pH5 / borax [Fusarium oxysporum],1PQ8_A Trypsin at pH 4 at atomic resolution [Fusarium oxysporum],1TRY_A STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMS [Fusarium oxysporum],2G51_A anomalous substructure of trypsin (p1) [Fusarium oxysporum],2G52_A Anomalous substructure of trypsin (P21) [Fusarium oxysporum],2VU8_E Crystal structure of an insect inhibitor with a fungal trypsin [Fusarium oxysporum] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P35049 | 1.89e-45 | 32 | 261 | 23 | 245 | Trypsin OS=Fusarium oxysporum OX=5507 PE=1 SV=1 |
| P24664 | 2.01e-45 | 34 | 255 | 1 | 213 | Trypsin OS=Saccharopolyspora erythraea OX=1836 PE=1 SV=1 |
| Q07943 | 6.05e-38 | 33 | 261 | 27 | 249 | Vitellin-degrading protease OS=Bombyx mori OX=7091 PE=1 SV=1 |
| P35038 | 8.02e-38 | 22 | 265 | 37 | 274 | Trypsin-4 OS=Anopheles gambiae OX=7165 GN=TRYP4 PE=2 SV=2 |
| P35035 | 1.50e-37 | 23 | 260 | 37 | 268 | Trypsin-1 OS=Anopheles gambiae OX=7165 GN=TRYP1 PE=2 SV=3 |
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 |
|---|---|---|---|---|---|
| 0.000260 | 0.999038 | 0.000201 | 0.000171 | 0.000153 | 0.000147 |