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CAZyme Information: MGYG000001219_01038
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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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; | |||||||||||
| CAZyme ID | MGYG000001219_01038 | |||||||||||
| CAZy Family | GH123 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1642; End: 6351 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH123 | 175 | 738 | 5.5e-171 | 0.9869888475836431 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam13320 | DUF4091 | 1.94e-21 | 624 | 692 | 1 | 66 | Domain of unknown function (DUF4091). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 70 amino acids in length. There is a single completely conserved residue G that may be functionally important. |
| sd00036 | LRR_3 | 9.19e-19 | 1453 | 1547 | 1 | 93 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
| sd00036 | LRR_3 | 1.42e-18 | 1453 | 1547 | 24 | 116 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
| sd00036 | LRR_3 | 2.47e-17 | 1453 | 1535 | 47 | 127 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
| pfam13306 | LRR_5 | 7.55e-16 | 1455 | 1535 | 1 | 77 | Leucine rich repeats (6 copies). This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BBA55846.1 | 0.0 | 12 | 1365 | 8 | 1709 |
| QTQ18982.1 | 0.0 | 12 | 1365 | 29 | 1730 |
| VEG17315.1 | 0.0 | 12 | 1365 | 29 | 1730 |
| BAQ98792.1 | 0.0 | 12 | 1365 | 8 | 1709 |
| ADP36622.1 | 0.0 | 12 | 1365 | 8 | 1709 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5FQE_A | 7.34e-110 | 176 | 754 | 30 | 610 | Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQE_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FR0_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens] |
| 5FQG_A | 9.32e-109 | 176 | 754 | 30 | 610 | Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQH_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens] |
| 5L7V_A | 7.59e-84 | 202 | 694 | 51 | 519 | ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7V_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482] |
| 5L7R_A | 1.12e-83 | 202 | 694 | 66 | 534 | ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7R_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_A Chain A, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_B Chain B, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482] |
Swiss-Prot Hits help
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 |
|---|---|---|---|---|---|
| 0.000234 | 0.999065 | 0.000178 | 0.000177 | 0.000164 | 0.000149 |
