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CAZyme Information: VBB73719.1
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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 | Podospora comata | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora comata | |||||||||||
| CAZyme ID | VBB73719.1 | |||||||||||
| CAZy Family | AA7 | |||||||||||
| CAZyme Description | Putative Killer toxin subunits alpha/beta | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
Enzyme Prediction help
| EC | 3.2.1.14:3 | 3.2.1.14:3 | 3.2.1.14:3 |
|---|
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH18 | 497 | 858 | 8.1e-47 | 0.9256756756756757 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 119357 | GH18_zymocin_alpha | 0.0 | 497 | 859 | 1 | 344 | Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase. |
| 176558 | PI-PLCXDc_like_2 | 5.70e-109 | 1054 | 1378 | 1 | 300 | Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs. |
| 176529 | PI-PLCXDc_like | 1.37e-63 | 1054 | 1378 | 1 | 288 | Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and similar proteins. This family corresponds to the catalytic domain present in phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs mainly found in eukaryota. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs and their bacterial homologs contain a single TIM-barrel type catalytic domain, X domain, which is more closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs. |
| 214753 | Glyco_18 | 2.50e-57 | 497 | 859 | 1 | 333 | Glyco_18 domain. |
| 395573 | Glyco_hydro_18 | 1.97e-51 | 497 | 858 | 1 | 305 | Glycosyl hydrolases family 18. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 0.0 | 1 | 1478 | 1 | 1478 | |
| 4.24e-272 | 11 | 854 | 7 | 847 | |
| 4.75e-271 | 23 | 859 | 47 | 876 | |
| 6.66e-268 | 40 | 901 | 5 | 844 | |
| 1.72e-264 | 18 | 866 | 15 | 839 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2.11e-28 | 501 | 862 | 7 | 344 | Crystal structure of a insect group III chitinase (CAD2) from Ostrinia furnacalis [Ostrinia furnacalis],5WVH_A Crystal structure of an insect group III chitinase complex with (GlcNAc)6 (CAD2-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis] |
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| 3.26e-26 | 499 | 862 | 4 | 344 | High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens] |
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| 3.32e-26 | 499 | 862 | 4 | 344 | Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens] |
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| 3.32e-26 | 499 | 862 | 4 | 344 | Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens] |
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| 3.37e-26 | 499 | 862 | 4 | 344 | Structure of human chitotriosidase [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.20e-100 | 303 | 858 | 205 | 710 | Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1 |
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| 7.06e-28 | 494 | 862 | 20 | 367 | Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1 |
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| 7.69e-26 | 494 | 862 | 20 | 367 | Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1 |
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| 5.46e-25 | 494 | 862 | 20 | 365 | Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1 |
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| 3.38e-24 | 483 | 862 | 9 | 367 | Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000292 | 0.999681 | CS pos: 23-24. Pr: 0.9750 |