| Protein: | CCS |
| Organism: | Homo sapiens |
| Length: | 274 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.
| Description | E-value | Query Range |
Subject Range |
|
|
5.0E-80 | [1..274] | [1..274] |
|
|
6.0E-80 | [1..274] | [1..274] |
|
|
8.0E-80 | [1..274] | [1..274] |
|
|
1.0E-78 | [1..274] | [1..274] |
|
|
2.0E-77 | [1..274] | [1..274] |
|
|
5.0E-77 | [1..274] | [1..274] |
|
|
1.0E-73 | [20..274] | [1..255] |
|
|
2.0E-66 | [13..272] | [8..267] |
|
|
1.0E-65 | [3..274] | [2..274] |
|
Region A: Residues: [1-85] |
1 11 21 31 41 51
| | | | | |
1 MASDSGNQGT LCTLEFAVQM TCQSCVDAVR KSLQGVAGVQ DVEVHLEDQM VLVHTTLPSQ 60
61 EVQALLEGTG RQAVLKGMGS GQLQN
|
| Detection Method: |  |
| Confidence: | 10.39794 |
| Match: | 2crlA |
| Description: | The apo form of HMA domain of copper chaperone for superoxide dismutase |
Matching Structure (courtesy of the PDB): |
|
|
Region A: Residues: [86-274] |
1 11 21 31 41 51
| | | | | |
1 LGAAVAILGG PGTVQGVVRF LQLTPERCLI EGTIDGLEPG LHGLHVHQYG DLTNNCNSCG 60
61 NHFNPDGASH GGPQDSDRHR GDLGNVRADA DGRAIFRMED EQLKVWDVIG RSLIIDEGED 120
121 DLGRGGHPLS KITGNSGERL ACGIIARSAG LFQNPKQICS CDGLTIWEER GRPIAGKGRK 180
181 ESAQPPAHL
|
| Detection Method: | |
| Confidence: | 40.09691 |
| 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 |
