| Protein: | GCH2_SYNY3, RIBA... |
| Organism: | Synechocystis sp. PCC 6803 |
| Length: | 556 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 GCH2_SYNY3, RIBA....
| Description | E-value | Query Range |
Subject Range |
|
|
859.0 | [0..1] | [548..1] |
|
|
856.0 | [0..2] | [548..11] |
|
|
855.0 | [0..2] | [547..12] |
|
|
855.0 | [0..1] | [548..37] |
|
|
835.0 | [0..1] | [549..3] |
|
|
803.0 | [0..2] | [546..11] |
|
|
797.0 | [0..2] | [543..9] |
|
|
797.0 | [0..2] | [543..9] |
|
|
778.0 | [0..2] | [550..5] |
|
|
718.0 | [0..2] | [528..24] |
|
Region A: Residues: [1-203] |
1 11 21 31 41 51
| | | | | |
1 MFDAIDAALA DIKAGKAVVV VDDENRENEG DLICAAQFAT PALVNFMAVE ARGLICLAMT 60
61 GDRLDELDLP LMVSKNTDSN QTAFTVSIDA APHLGVTTGI SAEDRARTIQ IAINPVTRPE 120
121 DLSRPGHIFP LRAKTGGVLK RAGHTEAAVD LSRLAGLYPA GVICEIQNAD GSMARLPELV 180
181 EYARKYDLKL ISIADLISYR LQH
|
| Detection Method: |  |
| Confidence: | 86.522879 |
| Match: | 1iezA |
| Description: | 3,4-dihydroxy-2-butanone 4-phosphate synthase, DHBP synthase, RibB |
Matching Structure (courtesy of the PDB): |
|
| Term | Confidence | Notes |
| 3,4-dihydroxy-2-butanone-4-phosphate synthase activity | 7.56167968780416 | bayes_pls_golite062009 |
| GTP cyclohydrolase activity | 2.51581618679202 | bayes_pls_golite062009 |
| hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines | 1.92717548101547 | bayes_pls_golite062009 |
| cyclohydrolase activity | 1.48770406828775 | bayes_pls_golite062009 |
| binding | 1.05088380360844 | bayes_pls_golite062009 |
| nucleic acid binding | 0.637633326908211 | bayes_pls_golite062009 |
| catalytic activity | 0.343636936190038 | bayes_pls_golite062009 |
| protein binding | 0.291469273637145 | bayes_pls_golite062009 |
| DNA binding | 0.21448652890147 | bayes_pls_golite062009 |
|
Region A: Residues: [204-400] |
1 11 21 31 41 51
| | | | | |
1 DRFVQRETIC EFPSQFGEFK LYAYRNLLDQ TEHIAIVKGD PSEFGQQPVM VRMHSECLTG 60
61 DALGSLRCDC RMQLQAALKM LENHGLGVVV YLRQEGRGIG LVNKLKAYSL QDLGYDTVEA 120
121 NERLGFPADL RDYGMGAQML NDLGVKQIRL ITNNPRKIAG LKGYGLEIVE RVPLLIEAND 180
181 YNSHYLTTKA EKLGHWL
|
| Detection Method: | |
| Confidence: | 81.154902 |
| Match: | 2bz0A |
| Description: | Crystal Structure of E. coli GTP cyclohydrolase II in complex with GTP analogue, GMPcPP, and Zinc |
Matching Structure (courtesy of the PDB): |
|
| Term | Confidence | Notes |
| GTP cyclohydrolase activity | 4.36867535385235 | bayes_pls_golite062009 |
| hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines | 3.7708397651039 | bayes_pls_golite062009 |
| cyclohydrolase activity | 3.33696578638249 | bayes_pls_golite062009 |
| catalytic activity | 1.40764037338379 | bayes_pls_golite062009 |
| binding | 1.32693434551075 | bayes_pls_golite062009 |
| protein binding | 0.418779722842637 | bayes_pls_golite062009 |
|
Region A: Residues: [401-556] |
1 11 21 31 41 51
| | | | | |
1 VKNYLLAIAI KFTPNVASAQ QRYEKLEKIR ALLQGTPLMV HEDNRPVAIA LFGKNSLIFH 60
61 VGLDQNLPSG QPWQKHDHSP YPALVKDFLV QLKQWPDLQA LAFLIAQGKD PMETLQVSLD 120
121 RENVSFADLT ADALNQWQPQ TVYTYSKQGS GEMTNR
|
| Detection Method: | |
Shown below is our most confident de novo (Rosetta) prediction for this domain.
Click here to view all matches.
Found no confident structure predictions for this domain.
