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CAZyme Information: MGYG000000045_00533
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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 | Faecalibacillus intestinalis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Faecalibacillus; Faecalibacillus intestinalis | |||||||||||
| CAZyme ID | MGYG000000045_00533 | |||||||||||
| CAZy Family | GH55 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 105981; End: 110240 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH55 | 844 | 1093 | 2.1e-61 | 0.40675675675675677 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam07554 | FIVAR | 7.50e-07 | 1284 | 1345 | 4 | 68 | FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures. |
| pfam00041 | fn3 | 8.50e-06 | 342 | 420 | 1 | 81 | Fibronectin type III domain. |
| cd00063 | FN3 | 2.37e-05 | 352 | 419 | 10 | 81 | Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases. |
| smart00060 | FN3 | 5.59e-04 | 352 | 410 | 10 | 72 | Fibronectin type 3 domain. One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins. |
| pfam07554 | FIVAR | 0.001 | 1223 | 1279 | 13 | 69 | FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCL56920.1 | 0.0 | 1 | 1419 | 1 | 1417 |
| QMW75525.1 | 0.0 | 5 | 1345 | 7 | 1329 |
| QPS14140.1 | 0.0 | 5 | 1345 | 7 | 1329 |
| QQY27036.1 | 0.0 | 5 | 1345 | 7 | 1329 |
| QQV06003.1 | 0.0 | 5 | 1345 | 7 | 1329 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4PEW_A | 1.11e-118 | 545 | 1162 | 21 | 548 | Structureof sacteLam55A from Streptomyces sp. SirexAA-E [Streptomyces sp. SirexAA-E],4PEW_B Structure of sacteLam55A from Streptomyces sp. SirexAA-E [Streptomyces sp. SirexAA-E] |
| 4TZ1_A | 1.48e-118 | 545 | 1162 | 9 | 536 | Ensemblerefinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritriose [Streptomyces sp. SirexAA-E],4TZ3_A Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritetraose [Streptomyces sp. SirexAA-E],4TZ5_A Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E],4TZ5_B Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E] |
| 4TYV_A | 1.57e-118 | 545 | 1162 | 11 | 538 | Ensemblerefinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E],4TYV_B Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E] |
| 4PEX_A | 2.13e-118 | 545 | 1162 | 21 | 548 | Structureof the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E],4PEX_B Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E],4PEY_A Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritriose [Streptomyces sp. SirexAA-E],4PEZ_A Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritetraose [Streptomyces sp. SirexAA-E],4PF0_A Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E],4PF0_B Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| G2NFJ9 | 6.15e-118 | 545 | 1162 | 65 | 592 | Exo-beta-1,3-glucanase OS=Streptomyces sp. (strain SirexAA-E / ActE) OX=862751 GN=SACTE_4363 PE=1 SV=1 |
| A0A3R0A696 | 5.16e-06 | 1281 | 1417 | 933 | 1064 | Alpha-L-arabinofuranosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=blArafA PE=1 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 |
|---|---|---|---|---|---|
| 0.000349 | 0.998915 | 0.000225 | 0.000178 | 0.000153 | 0.000151 |
