AC MF_00856; DC Protein; auto TR HAMAP; MF_00856; -; 1; level=0 XX Names: Raf1 XX ID RAF1 DE RecName: Full=RuBisCO accumulation factor 1; GN Name=raf1; XX CC -!- FUNCTION: A major RuBisCO chaperone. Acts after GroEL-GroES chaperonin CC to fold and/or assemble the large subunit of RuBisCO (ccbL, rbcL). CC Cooperates with RbcX in RbcL folding, plays the major role in assembly CC of dimers into RbcL(8)-Raf1(8) intermediate complexes. RbcS replaces CC Raf1, leading to holoenzyme formation. CC -!- SUBUNIT: Homodimer. Forms an RbcL(8)-Raf1(8) complex. Forms complexes of CC many stoichiometries with RbcL with and without RbcS. RbcX and Raf1 can CC bind simultaneously to RbcL. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DOMAIN: Has 3 domains, the N-terminal alpha-helical domain, an extended CC flexible linker and the C-terminal beta-sheet domain. The 2 C-terminal CC beta-sheet domains are swapped and pack against each other to form the CC dimer interface. CC -!- SIMILARITY: Belongs to the RAF family. XX DR Pfam; PF18087; RuBisCo_chap_C; 1; trigger=no DR Pfam; PF18578; Raf1_N; 1; trigger=no DR Pfam; PF18579; Raf1_HTH; 1; trigger=no XX KW Carbon dioxide fixation KW Chaperone KW Cytoplasm KW Photosynthesis XX GO GO:0015977; P:carbon fixation GO GO:0005737; C:cytoplasm GO GO:0110102; P:ribulose bisphosphate carboxylase complex assembly XX FT From: RAF1_NOSS1 (Q8YLP6) FT REGION 16..197 FT /note="N-terminal alpha-helix" FT REGION 221..347 FT /note="C-terminal beta-sheet" XX Size: 335-380; Related: None; Template: Q8YLP6; Q31Q05; Q8DI26; Scope: Bacteria; Cyanobacteriota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.3 2023/02/17 //