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Protein

Ribonuclease P/MRP protein subunit POP5

Gene

POP5

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP (By similarity).By similarity

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB-EC

GO - Biological processi

  1. tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P/MRP protein subunit POP5 (EC:3.1.26.5)
Gene namesi
Name:POP5
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

Nucleusnucleolus By similarity

GO - Cellular componenti

  1. nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170170Ribonuclease P/MRP protein subunit POP5PRO_0000327379Add
BLAST

Proteomic databases

PRIDEiQ1JQ92.

Interactioni

Subunit structurei

Component of nuclear RNase P and RNase MRP ribonucleoproteins. RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. RNase MRP consists of an RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007083.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1369.
HOGENOMiHOG000293345.
HOVERGENiHBG082157.
InParanoidiQ1JQ92.
KOiK03537.

Family and domain databases

InterProiIPR016819. RNase_P/MRP_POP5.
IPR002759. RNase_P/MRP_subunit.
[Graphical view]
PANTHERiPTHR13004:SF8. PTHR13004:SF8. 1 hit.
PfamiPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
PIRSFiPIRSF023803. Ribonuclease_P_prd. 1 hit.

Sequencei

Sequence statusi: Complete.

Q1JQ92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRFKHRYLL CEVVSDDPRC RLTLEDRVLG TLVRDTIARV HGTFGAAACS
60 70 80 90 100
IGFAVRYLNA YTGIVLLRCR KEFYRLVWSA LPFITSLENK GHRYPCFLNT
110 120 130 140 150
LHVGGTIRTC QKFLIQYNRR QLLILLQNCT DEGEREAIQK SVTKSCLLEE
160 170
ESAGEELSDS GGEETAEPME
Length:170
Mass (Da):19,351
Last modified:June 13, 2006 - v1
Checksum:i712668C4F7745A8C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC116153 mRNA. Translation: AAI16154.1.
RefSeqiNP_001068780.1. NM_001075312.2.
UniGeneiBt.10352.

Genome annotation databases

GeneIDi507410.
KEGGibta:507410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC116153 mRNA. Translation: AAI16154.1.
RefSeqiNP_001068780.1. NM_001075312.2.
UniGeneiBt.10352.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007083.

Proteomic databases

PRIDEiQ1JQ92.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi507410.
KEGGibta:507410.

Organism-specific databases

CTDi51367.

Phylogenomic databases

eggNOGiCOG1369.
HOGENOMiHOG000293345.
HOVERGENiHBG082157.
InParanoidiQ1JQ92.
KOiK03537.

Miscellaneous databases

NextBioi20868044.

Family and domain databases

InterProiIPR016819. RNase_P/MRP_POP5.
IPR002759. RNase_P/MRP_subunit.
[Graphical view]
PANTHERiPTHR13004:SF8. PTHR13004:SF8. 1 hit.
PfamiPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
PIRSFiPIRSF023803. Ribonuclease_P_prd. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal cerebellum.

Entry informationi

Entry nameiPOP5_BOVIN
AccessioniPrimary (citable) accession number: Q1JQ92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 13, 2006
Last modified: April 1, 2015
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The last C-terminal 19 amino acids are not required for complex association and RNase activity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.