GO_REF:0000033

Annotation inferences using phylogenetic trees

PAINT node PTN001005190 (eukaryote-wide PRORP clade) carries ribonuclease P activity and tRNA 5'-leader removal, seeded by Arabidopsis PRORP1/2/3 and animal PRORPs; the tobacco protein inherits both.

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

Automated ARBA/EC/PANTHER pipeline assigns ribonuclease P activity and tRNA 5'-leader removal, the same claims as the IBA rows.

file:TOBAC/A0A1S3Y076/A0A1S3Y076-deep-research-falcon.md

Deep research report on A0A1S3Y076 PRORP in Nicotiana tabacum

Ungrounded summary describing the protein as a PRORP with PPR and NYN domains; predicts organellar localisation, which this review does not accept.

PMID:26655022

Nuclear Protein-Only Ribonuclease P2 Structure and Biochemical Characterization Provide Insight into the Conserved Properties of tRNA 5' End Processing Enzymes.

Arabidopsis PRORP2 is nuclear, Mg2+-dependent and processes nuclear pre-tRNAs.

"PRORP2 and PRORP3 localize to the nucleus and PRORP1 localizes to the chloroplast and the mitochondria"

PMID:22549728

PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis.

Protein-only RNase P supports nuclear and organellar RNase P activity in Arabidopsis.

"protein-only RNase P enzymes called PRORP (for proteinaceous RNase P) support RNase P activity in vivo in both organelles and the nucleus in Arabidopsis."

PMID:37945696

A tRNA-modifying enzyme facilitates RNase P activity in Arabidopsis nuclei.

Arabidopsis nuclear PRORP2 forms a complex with tRNA methyltransferases TRM1A/TRM1B.

"PRORP2 occurs in a complex with the tRNA methyl transferases TRM1A and TRM1B in vivo"

PMID:20473316

A single Arabidopsis organellar protein has RNase P activity.

PMID:28499021

Protein-only RNase P function in Escherichia coli: viability, processing defects and differences between PRORP isoenzymes.

file:TOBAC/A0A1S3Y076/A0A1S3Y076-bioinformatics/RESULTS-rereview.md

Pairwise comparison of A0A1S3Y076 with Arabidopsis PRORP1/2/3 and catalytic-site mapping

57-59% identity to the nuclear PRORP2/PRORP3 vs 50% to organellar PRORP1; all eight PRORP1 Zn/Mn ligands conserved; no transit-peptide extension.