Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9P7W9

Entry ID Method Resolution Chain Position Source
AF-Q9P7W9-F1 Predicted AlphaFoldDB

No variants for Q9P7W9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9P7W9

No associated diseases with Q9P7W9

No regional properties for Q9P7W9

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9P7W9

Functions

Description
EC Number 3.1.26.5 Endoribonucleases producing 5'-phosphomonoesters
Subcellular Localization
  • Nucleus, nucleolus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
nucleolar ribonuclease P complex A ribonuclease P complex located in the nucleolus of a eukaryotic cell, where it catalyzes the 5' endonucleolytic cleavage of precursor tRNAs to yield mature tRNAs. Eukaryotic nucleolar ribonuclease P complexes generally contain a single RNA molecule that is necessary but not sufficient for catalysis, and several protein molecules.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
ribonuclease MRP complex A ribonucleoprotein complex that contains an RNA molecule of the snoRNA family, and cleaves the rRNA precursor as part of rRNA transcript processing. It also has other roles: In S. cerevisiae it is involved in cell cycle-regulated degradation of daughter cell-specific mRNAs, while in mammalian cells it also enters the mitochondria and processes RNAs to create RNA primers for DNA replication.
ribonuclease P complex A ribonucleoprotein complex that catalyzes cleavage of the leader sequence of precursor tRNAs (pre-tRNAs), generating the mature 5' end of tRNAs.

2 GO annotations of molecular function

Name Definition
ribonuclease P activity Catalysis of the endonucleolytic cleavage of RNA, removing 5' extra nucleotides from tRNA precursor.
ribonuclease P RNA binding Binding to RNA subunit of ribonuclease P.

4 GO annotations of biological process

Name Definition
endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Endonucleolytic cleavage between the SSU-rRNA and the 5.8S rRNA of an rRNA molecule originally produced as a tricistronic rRNA transcript that contained the Small SubUnit (SSU) rRNA, the 5.8S rRNA, and the Large SubUnit (LSU) rRNA, in that order, from 5' to 3' along the primary transcript.
endonucleolytic cleavage involved in tRNA processing Any endonucleolytic RNA phosphodiester bond hydrolysis that is involved in tRNA processing.
rRNA processing Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules.
tRNA 5'-leader removal Generation of the mature 5'-end of the tRNA, usually via an endonucleolytic cleavage by RNase P.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MADPLYSSLK TVNSTSKVTP ESLVFQTKIL TPEEAKNVIN EKIAFKPLLL VPSLNLEKQG
70 80 90 100 110 120
DRKESVASKK RKKLSSKEKK KLQLNVVPKI ADYSQFKHLH SMWCSYILEV IAGCTGESLM
130 140 150 160 170 180
AKLAKAEYQG AYMQVLRSKS TTRVGLEGIC IHESKHMLSL ITKENRVVRV PKQDSVMKVI
190 200 210
VDVPQRKLVF ELYTQHLLLR AGDRSNKRFK SKNTIDL