HAMAP annotation rule: MF_01318
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Accession MF_01318
Dates 22-JUL-2003 (Created)
9-FEB-2012 (Last updated, Version 25)
Data class Protein

case <OC:Bacteria> or <OG:Chloroplast>
end case


case <OC:Archaea>
end case

Names Ribosomal_L1




case <OC:Bacteria> and not <OC:Cyanobacteria>
Identifier RL1
Protein name
RecName: Full=50S ribosomal protein L1;
Gene name rplA

else case <OC:Cyanobacteria>
Identifier RL1
Protein name
RecName: Full=50S ribosomal protein L1;
Gene name rplA, rpl1

else case <OC:Archaea>
Identifier RL1
Protein name
RecName: Full=50S ribosomal protein L1P;
Gene name rpl1p

else case <OG:Chloroplast>
Identifier RK1
Protein name
RecName: Full=50S ribosomal protein L1, chloroplastic;
Gene name rpl1
end case


case <OC:Bacteria>
FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity).
FUNCTION: Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).

else case <OC:Archaea>
FUNCTION: Binds directly to 23S rRNA. Probably involved in E site tRNA release (By similarity).
FUNCTION: Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA (By similarity).
end case

SUBUNIT: Part of the 50S ribosomal subunit (By similarity).

case <OG:Chloroplast>
FUNCTION: Binds directly to 23S rRNA. Might be involved in E site tRNA release (Potential).
SUBCELLULAR LOCATION: Plastid, chloroplast.
end case

SIMILARITY: Belongs to the ribosomal protein L1P family.
Pfam PF00687; Ribosomal_L1; 1;
TIGRFAMs TIGR01169; RplA_bact; 1;
PROSITE PS01199; RIBOSOMAL_L1; 1;

case not <OG:Chloroplast>
end case

GO:0019843; Molecular function: rRNA binding.
GO:0006412; Biological process: translation.

case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
end case




Size range: 209-253 amino acids
Related UniRules: None
Template: P0A7L0 (RL1_ECOLI); Q5SLP7 (RL1_THET8); P27150 (RL1_THETH); P54050 (RL1_METJA); O52704 (RL1_METTL); P35024 (RL1_SULAC): [Recover all]
Scope: Bacteria
Archaea
Plastid
Fusion: Nter: None; Cter: <Unknown>
Duplicate: in RHOS1
Plasmid encoded: None
Comments: C-terminal fusion in MYCPE, quite atypical in NANEQ and NEOSM. Some of the Rickettsiales are about 15 residues shorter at the N-terminus. L1 proteins from thermophilic organisms have an approximately 10-fold higher affinity for their binding sites on both 23S rRNA and mRNA than do their mesophilic counterparts, maybe helping to explain the ribosome's greater stability in thermophiles. See: PubMed=9746351; Kohrer C., Mayer C., Neumair O., Grobner P., Piendl W.; "Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA."; Eur. J. Biochem. 256:97-105(1998).

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