Protein: | CCS-PB |
Organism: | Drosophila melanogaster |
Length: | 264 amino acids |
Reference: | Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16 |
Listed below are up to the top 10 sequence alignment matches, by species, for the PSI-BLAST search against the protein sequence for CCS-PB.
Description | E-value | Query Range |
Subject Range |
|
288.0 | [0..7] | [262..15] |
|
286.0 | [0..5] | [262..13] |
|
286.0 | [0..5] | [262..13] |
|
282.0 | [0..5] | [262..13] |
|
281.0 | [0..1] | [264..1] |
|
280.0 | [0..7] | [262..15] |
|
276.0 | [0..7] | [262..15] |
|
272.0 | [0..16] | [262..3] |
|
271.0 | [0..5] | [262..8] |
Region A: Residues: [1-70] |
1 11 21 31 41 51 | | | | | | 1 MSSIKIEFAV QMRRGDESYA GALRSALDGV GQVEIDTQEG RVIIQTQRPW SEIQDKIEAT 60 61 GVRAVLSGFG |
Detection Method: | ![]() |
Confidence: | 9.154902 |
Match: | 2crlA |
Description: | The apo form of HMA domain of copper chaperone for superoxide dismutase |
Matching Structure (courtesy of the PDB):![]() |
Region A: Residues: [71-264] |
1 11 21 31 41 51 | | | | | | 1 GQSAVALINT TGSVVDKTPI QGVVRFTTIT ADKKPGVVVD GVVDGLSPGL HGLHIHESGD 60 61 TSAGCSSVGE HYNPRQSPHG SPAAGAEERH AGDLGNIRAD ENGRATFRFV DPVLEVWDII 120 121 GRAVVLTANA DDLGRGGNDQ SLIDGNSGER IACGIIARSA GILENFKRIC ACDGVTLWDE 180 181 RNKPLAGKER SQKL |
Detection Method: | ![]() |
Confidence: | 43.30103 |
Match: | 1do5A |
Description: | Copper chaperone for superoxide dismutase, C-terminal domain |
Matching Structure (courtesy of the PDB):![]() |
Term | Confidence | Notes |
protein phosphatase 2B binding | 13.5719110466797 | bayes_pls_golite062009 |
superoxide dismutase activity | 12.1093323949609 | bayes_pls_golite062009 |
oxidoreductase activity, acting on superoxide radicals as acceptor | 12.1093323949609 | bayes_pls_golite062009 |
superoxide dismutase copper chaperone activity | 5.30724557593005 | bayes_pls_golite062009 |
chaperone binding | 5.11696266714142 | bayes_pls_golite062009 |
copper ion binding | 4.51765925795625 | bayes_pls_golite062009 |
copper chaperone activity | 3.53752588768671 | bayes_pls_golite062009 |
protein phosphatase binding | 3.26481550276071 | bayes_pls_golite062009 |
phosphatase binding | 3.1414149853516 | bayes_pls_golite062009 |
metallochaperone activity | 2.82622922333955 | bayes_pls_golite062009 |
copper ion transmembrane transporter activity | 2.53311528765098 | bayes_pls_golite062009 |
ion transmembrane transporter activity | 2.46331862428318 | bayes_pls_golite062009 |
transition metal ion binding | 2.451533032488 | bayes_pls_golite062009 |
cation transmembrane transporter activity | 2.41954384727602 | bayes_pls_golite062009 |
substrate-specific transmembrane transporter activity | 2.30916666149383 | bayes_pls_golite062009 |
binding | 2.28211284921339 | bayes_pls_golite062009 |
metal ion transmembrane transporter activity | 2.0278666635337 | bayes_pls_golite062009 |
protein binding | 1.96660745768497 | bayes_pls_golite062009 |
enzyme binding | 1.82618630359051 | bayes_pls_golite062009 |
metal ion binding | 1.79413011653575 | bayes_pls_golite062009 |
cation binding | 1.79413011653575 | bayes_pls_golite062009 |
ion binding | 1.78699219376941 | bayes_pls_golite062009 |
transition metal ion transmembrane transporter activity | 1.64083855886256 | bayes_pls_golite062009 |
inorganic cation transmembrane transporter activity | 1.63756992236587 | bayes_pls_golite062009 |
transporter activity | 1.33910763967058 | bayes_pls_golite062009 |
transmembrane transporter activity | 1.12504351752996 | bayes_pls_golite062009 |
catalytic activity | 1.09233965765942 | bayes_pls_golite062009 |
di-, tri-valent inorganic cation transmembrane transporter activity | 0.704985452118462 | bayes_pls_golite062009 |
substrate-specific transporter activity | 0.618042428454534 | bayes_pls_golite062009 |
zinc ion binding | 0.25600715352161 | bayes_pls_golite062009 |
antioxidant activity | 0.240491838042064 | bayes_pls_golite062009 |