Protein: | RIBA2_ORYSJ |
Organism: | Oryza sativa Japonica Group |
Length: | 553 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 RIBA2_ORYSJ.
Description | E-value | Query Range |
Subject Range |
|
641.0 | [0..66] | [536..42] |
Region A: Residues: [1-133] |
1 11 21 31 41 51 | | | | | | 1 MASISPTSSS VAALRGHPVQ FVKGGAVSKE AKGSISFSPV ANSNNANVKF TGLRVAASLK 60 61 RDGAFPGDGY SGNDNTVLPK STSVRGQDYP TADSVLPTES IIVPEISNAG LKCVADMFSD 120 121 EDKDTEQDLD SPT |
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.
Region A: Residues: [134-345] |
1 11 21 31 41 51 | | | | | | 1 EGFSSISEAI KDIQQGKLVI VVDDESRENE GDLIMAASLV TPEAMAFVVR YGTGIVCVSM 60 61 KEEDLERLNL PLMVATKENE EKLCTAFTVT VDAKEGTTTG VSAKDRAKTV MTLASPDSKP 120 121 EDFNRPGHIF PLKYREGGVL KRAGHTEASV DLAMLAGLPP AAVLCEIVDE DGSMARLPKL 180 181 RVFAERENLK IVSIADLIRY RRKRDRLVER SS |
Detection Method: | ![]() |
Confidence: | 83.0 |
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: [346-553] |
1 11 21 31 41 51 | | | | | | 1 VARLPLRWGN VRAYCYRSVI DGIEHIAMVK GEIGDGQGVL VRVHSECLTG DIFGSARCDC 60 61 GDQLAMAMEM IEKAGRGVLV YLRGHEGRGI GLGHKLRAYN LQDDGRDTVE ANEDLGLPVD 120 121 SREYGIGAQI LRDLGVRSMK LMTNNPAKYG GLKGYGLSIV GRVPLVTPIT SENRRYLETK 180 181 RTKMGHVYGL ANGQASHQTG SNGAKGEH |
Detection Method: | ![]() |
Confidence: | 74.69897 |
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 |