Difference between revisions of "Sequence-based predictions TSD"
From Bioinformatikpedia
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== Secondary structure == |
== Secondary structure == |
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| + | Proteins |
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| + | <figtable id="tab:gopetgo"> |
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| + | {| class="wikitable", style="width:100%; border-collapse: collapse; border-style: solid; border-width:0px; border-color: #000" |
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| + | |- |
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| + | ! style="text-align:left; border-style: solid; border-width: 0 0 2px 0" | ID |
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| + | ! style="text-align:left; border-style: solid; border-width: 0 0 2px 0" | [http://www.uniprot.org/uniprot/P10775 P10775 ] |
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| + | ! style="text-align:left; border-style: solid; border-width: 0 0 2px 0" | [http://www.uniprot.org/uniprot/Q9X0E6 Q9X0E6 ] |
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| + | ! style="text-align:left; border-style: solid; border-width: 0 0 2px 0" | [http://www.uniprot.org/uniprot/Q08209 Q08209] |
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| + | |- |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Protein name (organism) |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Ribonuclease inhibitor (sus scrofa) |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Divalent-cation tolerance protein CutA (Thermotoga maritima) |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (Human) |
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| + | |- |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Function |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis. |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Involved in resistance toward heavy metals. |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1. |
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| + | |- |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Subcellular location |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Cytoplasm |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Cytoplasm |
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| + | | style="border-style: solid; border-width: 0 0 0 0" | Nucleus |
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| + | |- |
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| + | |} |
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| + | '''Table TODO''': |
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| + | </figtable> |
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== Disorder == |
== Disorder == |
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== Transmembrane helices == |
== Transmembrane helices == |
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Revision as of 11:56, 14 May 2012
Thor: He's my brother
Natasha Romanoff: He killed 80 people in 2 days
Thor: ...He's adopted
If not noted otherwise, the sequence for all predictions is the HEXA Reference sequence. A protocol for this task can be found here.
Contents
Secondary structure
Proteins
<figtable id="tab:gopetgo">
| ID | P10775 | Q9X0E6 | Q08209 |
|---|---|---|---|
| Protein name (organism) | Ribonuclease inhibitor (sus scrofa) | Divalent-cation tolerance protein CutA (Thermotoga maritima) | Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (Human) |
| Function | Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis. | Involved in resistance toward heavy metals. | Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1. |
| Subcellular location | Cytoplasm | Cytoplasm | Nucleus |
Table TODO: </figtable>
Disorder
Transmembrane helices
Signal peptides
GO terms
GOpet
<figtable id="tab:gopetgo">
| GO-Term ID | Type | Confidence | GO-Term description |
|---|---|---|---|
| GO:0003824 | Molecular function | 97% | catalytic activity |
| GO:0004563 | Molecular function | 96% | beta-N-acetylhexosaminidase activity |
| GO:0015929 | Molecular function | 96% | hexosaminidase activity |
| GO:0016787 | Molecular function | 96% | hydrolase activity |
| GO:0016798 | Molecular function | 96% | hydrolase activity acting on glycosyl bonds |
| GO:0004553 | Molecular function | 96% | hydrolase activity hydrolyzing O-glycosyl compounds |
| GO:0016799 | Molecular function | 77% | hydrolase activity hydrolyzing N-glycosyl compounds |
| GO:0046982 | Molecular function | 61% | protein heterodimerization activity |
Table TODO: </figtable>
