Protein profile

KP13_04392

50S ribosomal protein L25

Genome: KpKP13

Gene: AHE43540.1 rplY Structure source: AlphaFold + ColabFold UniProt A0A0H3GVK0
Amino acids 94
Annotations 5
Features 12
PDB binders 0
Druggability 0.105

Overview

Basic information about this protein and its source genome.

Accession
KP13_04392
Gene
AHE43540.1 rplY
Status
annotated
Amino acids
94
Structure source
AlphaFold + ColabFold
GO
GO:0008097 Binding to a 5S ribosomal RNA, the smallest RNA constituent of a ribosome. GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome. GO:0005840 An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins. GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome. GO:0022625 The large subunit of a ribosome located in the cytosol.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
89.362
DEG E-value
4.310000000000001e-59
Localization
Cytoplasmic
ColabFold pLDDT
95.63

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.105
Structure A0A0H3GVK0
Pocket Pocket 1
P2Rank 0.014
Structure A0A0H3GVK0
Pocket Pocket 1
ColabFold model
FPocket 0.214 · Pocket 2
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 147 / 4744 genomes with a hit
Normalized 0.031

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • GO:0008097 Binding to a 5S ribosomal RNA, the smallest RNA constituent of a ribosome.
  • GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
  • GO:0005840 An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
  • GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
  • GO:0022625 The large subunit of a ribosome located in the cytosol.

Sequence Features

Domain/signature hits from InterPro and related databases.

12 records
Show feature table
Start End DB Term Name
3 93 CDD cd00495 Ribosomal_L25_TL5_CTC
3 93 InterPro IPR029751 Ribosomal protein L25
4 91 Pfam PF01386 Ribosomal L25p family
4 91 InterPro IPR029751 Ribosomal protein L25
1 93 SUPERFAMILY SSF50715 Ribosomal protein L25-like
1 93 InterPro IPR011035 Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain superfamily
2 94 PANTHER PTHR33284 RIBOSOMAL PROTEIN L25/GLN-TRNA SYNTHETASE, ANTI-CODON-BINDING DOMAIN-CONTAINING PROTEIN
1 94 FunFam G3DSA:2.40.240.10:FF:000002 50S ribosomal protein L25
2 94 Hamap MF_01336 50S ribosomal protein L25 [rplY].
2 94 InterPro IPR020055 Ribosomal protein L25, short-form
1 94 Gene3D G3DSA:2.40.240.10 Ribosomal Protein L25; Chain P
1 94 InterPro IPR020056 Ribosomal protein L25/Gln-tRNA synthetase, N-terminal

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

Loading 3D structure...

Legend High Medium Low

Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GVK0
AlphaFold full sequence Viewing
ColabFold KP13_04392
ColabFold full sequence Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer