Transcription Factor
| Accessions: | 3clc_A (3D-footprint 20231221), 3clc_D (3D-footprint 20231221), 3s8q_A (3D-footprint 20231221), 3ufd_A (3D-footprint 20231221), 3ufd_E (3D-footprint 20231221), 4iwr_B (3D-footprint 20231221), 4iwr_F (3D-footprint 20231221), 4x4b_A (3D-footprint 20231221), 4x4b_D (3D-footprint 20231221), 4x4c_A (3D-footprint 20231221), 4x4c_D (3D-footprint 20231221), 4x4d_A (3D-footprint 20231221), 4x4d_D (3D-footprint 20231221), 4x4e_A (3D-footprint 20231221), 4x4e_D (3D-footprint 20231221), 4x4f_A (3D-footprint 20231221), 4x4f_D (3D-footprint 20231221), 4x4g_A (3D-footprint 20231221), 4x4g_D (3D-footprint 20231221), 4x4h_A (3D-footprint 20231221), 4x4h_D (3D-footprint 20231221), 4x4i_A (3D-footprint 20231221), 4x4i_D (3D-footprint 20231221) |
| Names: | Q8GGH0_9ENTR, Regulatory protein, R-M CONTROLLER PROTEIN |
| Organisms: | Enterobacter sp. RFL1396 |
| Libraries: | 3D-footprint 20231221 1 1 Contreras-Moreira B. 3D-footprint: a database for the structural analysis of protein-DNA complexes. Nucleic acids research 38:D91-7 (2010). [Pubmed] |
| Uniprot: | Q8GGH0 |
| Length: | 76 |
| Pfam Domains: | 12-62 Helix-turn-helix domain 12-62 Helix-turn-helix |
| Sequence: (in bold interface residues) | 1 ESFLLSKVSFVIKKIRLEKGMTQEDLAYKSNLDRTYISGIERNSRNLTIKSLELIMKGLE 60 61 VSDVVFFEMLIKEILK |
| Interface Residues: | 24, 33, 34, 35, 36, 38, 39, 42, 44, 45 |
| 3D-footprint Homologues: | 3zkc_A, 8ity_P, 3s8q_A, 3u3w_B |
| Binding Motifs: | 3clc_ABCD TGTnGACnnnnGnCACACGGnCnnnnATTCACA 3s8q_A TGTGACnta 3s8q_AB TGTGACnTAtAGTCCG 3ufd_AB TGTCGACTATAGTCTACA 3ufd_E TGTAGAC 4iwr_AB TGTGACnnnnnnTCcG 4iwr_EF CGGAmnnnnnGTCACA 4iwr_F gTCcG 4x4b_ABCD TGTnGAcnnnnTnCACrCnGannnnnAGTcACA 4x4c_ABCD TGTGACTnnnnnTCnGCGTGnAnnnnGTCnACA 4x4d_ABCD TGTGACTnnnnntCnGyGTGnAnnnngTCnACA 4x4e_ABCD TGTnGACnnnnTnCACRCnGannnnnAGTcACA 4x4f_ABCD TGTGACTnnnnntCnGyGTGnAnnnnGTCnACA 4x4g_ABCD TGTnGACnnnnTnCACRCnGAnnnnnAGTCACA 4x4h_ABCD TGTGACTnnnnntCnGyGTGnAnnnngTCnACA 4x4i_ABCD TGTGACTnnnnnTCnGYGTGnAnnnnGTCnACA |
| Binding Sites: | 3clc_E / 4x4b_E / 4x4c_E / 4x4d_E / 4x4e_E / 4x4f_E / 4x4g_E / 4x4h_E / 4x4i_E 3clc_F / 4x4b_F / 4x4c_F / 4x4d_F / 4x4e_F / 4x4f_F / 4x4g_F / 4x4h_F / 4x4i_F 3s8q_C 3s8q_D 3ufd_G 3ufd_H 4iwr_C 4iwr_D 4iwr_G 4iwr_H |
| Publications: | McGeehan J.E, Streeter S.D, Thresh S.J, Ball N, Ravelli R.B, Kneale G.G. Structural analysis of the genetic switch that regulates the expression of restriction-modification genes. Nucleic acids research 36:4778-87 (2008). [Pubmed] McGeehan J.E, Ball N.J, Streeter S.D, Thresh S.J, Kneale G.G. Recognition of dual symmetry by the controller protein C.Esp1396I based on the structure of the transcriptional activation complex. Nucleic acids research 40:4158-67 (2012). [Pubmed] Ball N.J, McGeehan J.E, Streeter S.D, Thresh S.J, Kneale G.G. The structural basis of differential DNA sequence recognition by restriction-modification controller proteins. Nucleic acids research 40:10532-42 (2012). [Pubmed] Martin RN, McGeehan JE, Ball NJ, Streeter SD, Thresh SJ, Kneale GG. Structural analysis of DNA-protein complexes regulating the restriction-modification system Esp1396I. Acta Crystallogr Sect F Struct Biol Cryst Commun : (2013). [Pubmed] Bury C, Garman EF, Ginn HM, Ravelli RB, Carmichael I, Kneale G, McGeehan JE. Radiation damage to nucleoprotein complexes in macromolecular crystallography. J Synchrotron Radiat 22:213-24 (2015). [Pubmed] |
| Related annotations: | PaperBLAST |
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