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CAZyme Information: MGYG000002312_03338
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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 | Blautia_A sp000285855 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp000285855 | |||||||||||
| CAZyme ID | MGYG000002312_03338 | |||||||||||
| CAZy Family | GT25 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 537; End: 1148 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00702 | P4Hc | 0.006 | 36 | 202 | 1 | 164 | Prolyl 4-hydroxylase alpha subunit homologues. Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AUV58267.1 | 1.09e-143 | 3 | 203 | 689 | 889 |
| AFX92362.1 | 1.09e-143 | 3 | 203 | 689 | 889 |
| AZL89519.1 | 6.79e-142 | 3 | 203 | 689 | 889 |
| AVG46056.1 | 8.38e-142 | 3 | 203 | 670 | 870 |
| AVG47162.1 | 8.38e-142 | 3 | 203 | 670 | 870 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6AX6_A | 3.97e-72 | 3 | 203 | 38 | 235 | Thecrystal structure of a lysyl hydroxylase from Acanthamoeba polyphaga mimivirus [Acanthamoeba polyphaga mimivirus],6AX6_B The crystal structure of a lysyl hydroxylase from Acanthamoeba polyphaga mimivirus [Acanthamoeba polyphaga mimivirus],6AX7_A The crystal structure of a lysyl hydroxylase from Acanthamoeba polyphaga mimivirus [Acanthamoeba polyphaga mimivirus],6AX7_B The crystal structure of a lysyl hydroxylase from Acanthamoeba polyphaga mimivirus [Acanthamoeba polyphaga mimivirus] |
| 6FXK_A | 1.86e-47 | 26 | 203 | 540 | 714 | CrystalStructure of full-length Human Lysyl Hydroxylase LH3 [Homo sapiens],6FXM_A Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Mn2+ [Homo sapiens],6FXR_A Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP-Gal [Homo sapiens],6FXT_A Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP-Glc [Homo sapiens],6FXX_A Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP-Gal, Hg2+ Soak [Homo sapiens],6FXY_A Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP-Gal - Structure from long-wavelength S-SAD [Homo sapiens],6TE3_A Chain A, Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 [Homo sapiens],6TEC_A Chain A, Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 [Homo sapiens],6TES_A Chain A, Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 [Homo sapiens] |
| 6TEU_A | 1.86e-47 | 26 | 203 | 540 | 714 | ChainA, Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 [Homo sapiens],6TEX_A Chain A, Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 [Homo sapiens],6TEZ_A Chain A, Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q5UQC3 | 1.69e-65 | 3 | 203 | 698 | 895 | Procollagen lysyl hydroxylase and glycosyltransferase OS=Acanthamoeba polyphaga mimivirus OX=212035 GN=MIMI_L230 PE=1 SV=1 |
| P24802 | 2.50e-50 | 3 | 203 | 535 | 729 | Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 OS=Gallus gallus OX=9031 GN=PLOD1 PE=1 SV=1 |
| Q63321 | 4.71e-50 | 3 | 203 | 533 | 727 | Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 OS=Rattus norvegicus OX=10116 GN=Plod1 PE=1 SV=1 |
| Q9R0E2 | 1.24e-49 | 3 | 203 | 533 | 727 | Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 OS=Mus musculus OX=10090 GN=Plod1 PE=1 SV=1 |
| Q02809 | 3.26e-49 | 3 | 203 | 532 | 726 | Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 OS=Homo sapiens OX=9606 GN=PLOD1 PE=1 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |