Literature summary for 1.17.4.1 extracted from

Kan, S.C.; Yu, L.K.; Chen, J.H.; Hu, H.Y.; Hsu, W.H.
Mutational analysis of splicing activities of ribonucleotide reductase alpha subunit protein from lytic bacteriophage P1201 (2011), Curr. Microbiol., 62, 1282-1286.

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Protein Variants

Protein Variants	Comment	Organism
G392S	temperature-sensitive protein with complete splicing activity at 17 and 28°C but not at 37°C or higher	Corynebacterium phage P1201
G392S/C539G	the cleavage at the ribonucleotide reductase RIR1 intein C-terminus is blocked, but other cleavage activities can be efficiently performed at 17°C. The mutant variant possesses the properties of low-temperature-induced cleavage at the intein N-terminus	Corynebacterium phage P1201
additional information	mutations of resiude C539, the N-terminal residue of the C-extein in the ribonucleotide reductase RIR1 protein, lead to changes of pattern and level of protein-splicing activities	Corynebacterium phage P1201

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium phage P1201	-	-	-

Synonyms

Synonyms	Comment	Organism
RIR1	-	Corynebacterium phage P1201

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Release 2023.1 (January 2023)