Protein: | PTC3 |
Organism: | Saccharomyces cerevisiae |
Length: | 468 amino acids |
Reference: | Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076 |
Listed below are up to the top 10 sequence alignment matches, by species, for the PSI-BLAST search against the protein sequence for PTC3.
Description | E-value | Query Range |
Subject Range |
|
0.0 | [1..468] | [1..468] |
|
0.0 | [1..389] | [1..404] |
|
4.0E-99 | [1..389] | [1..404] |
|
5.0E-99 | [1..389] | [1..404] |
|
4.0E-98 | [1..360] | [1..370] |
|
7.0E-97 | [1..360] | [1..370] |
Region A: Residues: [1-303] |
1 11 21 31 41 51 | | | | | | 1 MGQILSNPII DKEHHSGTDC LTAFGLCAMQ GWRMSMEDAH IVEPNLLAES DEEHLAFYGI 60 61 FDGHGGSSVA EFCGSKMISI LKKQESFKSG MLEQCLIDTF LATDVELLKD EKLKDDHSGC 120 121 TATVILVSQL KKLLICANSG DSRTVLSTGG NSKAMSFDHK PTLLSEKSRI VAADGFVEMD 180 181 RVNGNLALSR AIGDFEFKSN TKLGPHEQVV TCVPDIICHN LNYDEDEFVI LACDGIWDCL 240 241 TSQECVDLVH YGISQGNMTL SDISSRIVDV CCSPTTEGSG IGCDNMSISI VALLKENESE 300 301 SQW |
Detection Method: | ![]() |
Confidence: | 499.85005 |
Match: | 1a6q__ |
Description: | Protein serine/threonine phosphatase 2C, C-terminal domain; Protein serine/threonine phosphatase 2C, catalytic domain |
Matching Structure (courtesy of the PDB):![]() |
Term | Confidence | Notes |
phosphoprotein phosphatase activity | 7.29765002420868 | bayes_pls_golite062009 |
phosphatase activity | 6.46633224572308 | bayes_pls_golite062009 |
phosphoric ester hydrolase activity | 6.25564034681743 | bayes_pls_golite062009 |
protein serine/threonine phosphatase activity | 5.66354576593165 | bayes_pls_golite062009 |
hydrolase activity, acting on ester bonds | 5.62997267604309 | bayes_pls_golite062009 |
hydrolase activity | 2.5631136269171 | bayes_pls_golite062009 |
binding | 1.74689317666387 | bayes_pls_golite062009 |
catalytic activity | 1.53401212718168 | bayes_pls_golite062009 |
protein binding | 0.425331902048676 | bayes_pls_golite062009 |
Region A: Residues: [304-377] |
1 11 21 31 41 51 | | | | | | 1 FERMRSKNYN IQTSFVQRRK SIFDFHDFSD DDNEVFAITT KKLQDRLNRS KDNDDMEIDD 60 61 LDTELDSSAT PSKL |
Detection Method: | ![]() |
Confidence: | 499.85005 |
Match: | 1a6q__ |
Description: | Protein serine/threonine phosphatase 2C, C-terminal domain; Protein serine/threonine phosphatase 2C, catalytic domain |
Matching Structure (courtesy of the PDB):![]() |
Region A: Residues: [378-468] |
1 11 21 31 41 51 | | | | | | 1 SGEDRTGPID LFSLEALLEA GIQIRQRPSS DSDGNTSYFH GASLSDMLAS LSNAAAGETE 60 61 PNDADDNDDN DGEENGKNEN AKKGSKIEEI E |
Shown below are all of our de novo (Rosetta) predictions for this domain.
Click here to view only most confident match.
MCM Score |
SCOP Match |
SCOP Description | ||
View | Download | 0.337 | a.4.5 | "Winged helix" DNA-binding domain |
View | Download | 0.355 | d.58.3 | Protease propeptides/inhibitors |
View | Download | 0.531 | a.46.2 | Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain |
View | Download | 0.333 | d.58.38 | Urease metallochaperone UreE, C-terminal domain |
View | Download | 0.289 | d.52.1 | Alpha-lytic protease prodomain |
View | Download | 0.250 | d.58.3 | Protease propeptides/inhibitors |
View | Download | 0.246 | c.3.1 | FAD/NAD(P)-binding domain |
View | Download | 0.242 | d.58.7 | RNA-binding domain, RBD |
View | Download | 0.235 | d.58.23 | Probable ACP-binding domain of malonyl-CoA ACP transacylase |
View | Download | 0.229 | d.211.1 | Ankyrin repeat |
View | Download | 0.227 | d.58.10 | Acylphosphatase-like |
View | Download | 0.221 | c.2.1 | NAD(P)-binding Rossmann-fold domains |
View | Download | 0.218 | d.58.11 | EF-G/eEF-2 domains III and V |
View | Download | 0.212 | d.58.48 | MTH1187-like |
View | Download | 0.202 | a.134.1 | Fungal elicitin |