popl-5 Ribonuclease P/MRP protein subunit POP5 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: popl-5
Official Full Name: Ribonuclease P/MRP protein subunit POP5
Primary source: WormBase:WBGene00013422
Locus tag: CELE_Y66A7A.2
See related: AllianceGenome:WB:WBGene00013422
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Predicted to enable ribonuclease P RNA binding activity and ribonuclease P activity. Predicted to be involved in rRNA processing and tRNA processing. Predicted to be located in nucleolus. Predicted to be part of nucleolar ribonuclease P complex and ribonuclease MRP complex. Orthologous to human POP5 (POP5 homolog, ribonuclease P/MRP subunit). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See popl-5 in Genome Data Viewer

Location:: chromosome: III

Exon count:: 4

Sequence:: Chromosome: III; NC_003281.10 (11485479..11487345, complement)

Chromosome III - NC_003281.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003281.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Y66A7A.2 (e-PCR)
- UniSTS:319806

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables ribonuclease P RNA binding	IEA Inferred from Electronic Annotation more info
enables ribonuclease P activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in rRNA processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in rRNA processing	IEA Inferred from Electronic Annotation more info
involved_in tRNA 5'-leader removal	IEA Inferred from Electronic Annotation more info
involved_in tRNA processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in tRNA processing	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of endoribonuclease complex	IEA Inferred from Electronic Annotation more info
part_of nucleolar ribonuclease P complex	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleolus	IEA Inferred from Electronic Annotation more info
located_in nucleus	IEA Inferred from Electronic Annotation more info
part_of ribonuclease MRP complex	IBA Inferred from Biological aspect of Ancestor more info
part_of ribonuclease P complex	IEA Inferred from Electronic Annotation more info
part_of ribonucleoprotein complex	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Ribonuclease P/MRP protein subunit POP5

NP_001255128.1

Confirmed by transcript evidence

NP_001255129.1

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003281.10 Reference assembly

Range

11485479..11487345 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001268199.4 → NP_001255128.1 Ribonuclease P/MRP protein subunit POP5 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_001255128.1

Status: REVIEWED

UniProtKB/TrEMBL

G5EF59

Conserved Domains (1) summary

pfam01900
Location:7 → 108

RNase_P_Rpp14; Rpp14/Pop5 family
NM_001268200.3 → NP_001255129.1 Ribonuclease P/MRP protein subunit POP5 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_001255129.1

Status: REVIEWED

UniProtKB/TrEMBL

G2HK18

Conserved Domains (1) summary

cl00281
Location:20 → 52

metallo-dependent_hydrolases; Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a ...