Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

50S ribosomal protein L18

Gene

rplR

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This is one of the proteins that binds and mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L18
Alternative name(s):
TL24
Gene namesi
Name:rplR
Ordered Locus Names:TTHA1676
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00001313722 – 11250S ribosomal protein L18Add BLAST111

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and probably the 23S rRNA; has been isolated in a complex with the 5S rRNA and RL25 (Ref. 2).

Protein-protein interaction databases

STRINGi300852.TTHA1676.

Structurei

Secondary structure

1112
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 19Combined sources4
Beta strandi25 – 30Combined sources6
Beta strandi35 – 41Combined sources7
Turni42 – 45Combined sources4
Beta strandi46 – 51Combined sources6
Helixi54 – 56Combined sources3
Helixi63 – 79Combined sources17
Beta strandi102 – 104Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RS/YS1-112[»]
1VY4X-ray2.60BS/DS1-112[»]
1VY5X-ray2.55BS/DS1-112[»]
1VY6X-ray2.90BS/DS1-112[»]
1VY7X-ray2.80BS/DS1-112[»]
4L47X-ray3.22RS/YS1-112[»]
4L71X-ray3.90RS/YS1-112[»]
4LELX-ray3.90RS/YS1-112[»]
4LFZX-ray3.92RS/YS1-112[»]
4LNTX-ray2.94RS/YS1-112[»]
4LSKX-ray3.48RS/YS1-112[»]
4LT8X-ray3.14RS/YS1-112[»]
4P6FX-ray3.60RS/YS1-112[»]
4P70X-ray3.68RS/YS1-112[»]
4TUAX-ray3.60RS/YS1-112[»]
4TUBX-ray3.60RS/YS1-112[»]
4TUCX-ray3.60RS/YS1-112[»]
4TUDX-ray3.60RS/YS1-112[»]
4TUEX-ray3.50RS/YS1-112[»]
4V42X-ray5.50BQ1-112[»]
4V4PX-ray5.50Q1-112[»]
4V4XX-ray5.00BR1-112[»]
4V4YX-ray5.50BR1-112[»]
4V4ZX-ray4.51BR1-112[»]
4V51X-ray2.80BS/DS2-112[»]
4V5AX-ray3.50BS/DS2-112[»]
4V5CX-ray3.30BS/DS1-112[»]
4V5DX-ray3.50BS/DS1-112[»]
4V5EX-ray3.45BS/DS1-112[»]
4V5FX-ray3.60BS/DS1-112[»]
4V5GX-ray3.60BS/DS1-112[»]
4V5JX-ray3.10BS/DS1-112[»]
4V5KX-ray3.20BS/DS1-112[»]
4V5LX-ray3.10BS1-112[»]
4V5Melectron microscopy7.80BS1-112[»]
4V5Nelectron microscopy7.60BS1-112[»]
4V5PX-ray3.10BS/DS1-112[»]
4V5QX-ray3.10BS/DS1-112[»]
4V5RX-ray3.10BS/DS1-112[»]
4V5SX-ray3.10BS/DS1-112[»]
4V68electron microscopy6.40BS11-109[»]
4V6AX-ray3.10BS/DS1-112[»]
4V6FX-ray3.10AQ/DQ1-112[»]
4V6GX-ray3.50BQ/DQ1-112[»]
4V7JX-ray3.30AS/BS1-112[»]
4V7KX-ray3.60AS/BS1-112[»]
4V7LX-ray3.00BS/DS1-112[»]
4V7MX-ray3.45BS/DS1-112[»]
4V7WX-ray3.00BS/DS1-112[»]
4V7XX-ray3.00BS/DS1-112[»]
4V7YX-ray3.00BS/DS1-112[»]
4V7ZX-ray3.10BS/DS1-112[»]
4V87X-ray3.10AQ/DQ2-112[»]
4V8AX-ray3.20AS/BS1-112[»]
4V8BX-ray3.00BQ/DQ1-112[»]
4V8CX-ray3.30AQ/BQ1-112[»]
4V8DX-ray3.00BQ/DQ1-112[»]
4V8EX-ray3.30AQ/CQ1-112[»]
4V8FX-ray3.30AQ/DQ1-112[»]
4V8GX-ray3.00BS/DS1-112[»]
4V8HX-ray3.10BS/DS1-112[»]
4V8IX-ray2.70BS/DS1-112[»]
4V8JX-ray3.90BS/DS1-112[»]
4V8NX-ray3.10BS/DS1-112[»]
4V8OX-ray3.80BS1-112[»]
4V8QX-ray3.10AS1-112[»]
4V8UX-ray3.70BS/DS1-112[»]
4V8XX-ray3.35BS/DS1-112[»]
4V90X-ray2.95BS2-112[»]
4V95X-ray3.20BS/DS1-112[»]
4V97X-ray3.52BS/DS1-112[»]
4V9AX-ray3.30BQ/DQ1-112[»]
4V9BX-ray3.10BQ/DQ1-112[»]
4V9HX-ray2.86BS1-112[»]
4V9IX-ray3.30BS/DS11-108[»]
4V9RX-ray3.00BS/DS1-112[»]
4V9SX-ray3.10BS/DS1-112[»]
4W2EX-ray2.90S1-112[»]
4W2FX-ray2.40BS/DS1-112[»]
4W2GX-ray2.55BS/DS1-112[»]
4W2HX-ray2.70BS/DS1-112[»]
4W2IX-ray2.70BS/DS1-112[»]
4W4GX-ray3.30RS/YS1-112[»]
4WPOX-ray2.80AS/CS1-112[»]
4WQ1X-ray3.1065/A82-112[»]
4WQFX-ray2.80AS/CS1-112[»]
4WQRX-ray3.1565/A81-112[»]
4WQUX-ray2.80AS/CS1-112[»]
4WQYX-ray2.80AS/CS1-112[»]
4WR6X-ray3.0565/A81-112[»]
4WRAX-ray3.0565/A81-112[»]
4WROX-ray3.05A81-112[»]
4WSDX-ray2.9565/A81-112[»]
4WSMX-ray3.3065/A81-112[»]
4WT1X-ray3.0565/A81-112[»]
4WT8X-ray3.40CR/DR11-108[»]
4WU1X-ray3.2065/A81-112[»]
4WZDX-ray3.1065/A81-112[»]
4WZOX-ray3.3065/A81-112[»]
4Y4OX-ray2.301S/2S1-112[»]
4Y4PX-ray2.501S/2S1-112[»]
4YPBX-ray3.40RS/YS1-112[»]
4YZVX-ray3.10RS/YS1-112[»]
4Z3SX-ray2.651S/2S1-112[»]
4Z8CX-ray2.901S/2S1-112[»]
4ZERX-ray3.101S/2S3-112[»]
4ZSNX-ray3.60RS/YS1-112[»]
5A9Zelectron microscopy4.70AP3-112[»]
5AA0electron microscopy5.00AP3-112[»]
5CZPX-ray3.30RS/YS1-112[»]
5D8BX-ray3.63IB/M1-112[»]
5DFEX-ray3.10RS/YS1-112[»]
5DOXX-ray3.101S/2S1-112[»]
5DOYX-ray2.601S/2S1-112[»]
5E7KX-ray3.2065/A81-112[»]
5E81X-ray2.9565/A81-112[»]
5EL4X-ray3.1565/A81-112[»]
5EL5X-ray3.1565/A81-112[»]
5EL6X-ray3.1065/A81-112[»]
5EL7X-ray3.1565/A81-112[»]
5F8KX-ray2.801S/2S3-112[»]
5FDUX-ray2.901S/2S3-112[»]
5FDVX-ray2.801S/2S3-112[»]
5HAUX-ray3.001Q/2Q1-112[»]
5HCPX-ray2.891S/2S1-112[»]
5HCQX-ray2.801S/2S1-112[»]
5HCRX-ray2.801S/2S1-112[»]
5HD1X-ray2.701S/2S1-112[»]
5IB7X-ray2.9965/A81-112[»]
5IB8X-ray3.1365/A81-112[»]
5IBBX-ray2.9665/A81-112[»]
5IMQelectron microscopy3.80k1-112[»]
5IMRelectron microscopy-k1-112[»]
5J30X-ray3.20RS/YS1-112[»]
5J3CX-ray3.04RS/YS1-112[»]
5J4BX-ray2.601S/2S1-112[»]
5J4CX-ray2.801S/2S1-112[»]
5J8BX-ray2.60S1-112[»]
ProteinModelPortaliQ5SHQ4.
SMRiQ5SHQ4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHQ4.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18P family.Curated

Phylogenomic databases

eggNOGiENOG4105K4C. Bacteria.
COG0256. LUCA.
HOGENOMiHOG000248742.
KOiK02881.
OMAiKSTRSHI.
PhylomeDBiQ5SHQ4.

Family and domain databases

HAMAPiMF_01337_B. Ribosomal_L18_B. 1 hit.
InterProiIPR005484. Ribosomal_L18.
IPR004389. Ribosomal_L18_bac-type.
[Graphical view]
PfamiPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00060. L18_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5SHQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLTAYERR KFRVRNRIKR TGRLRLSVFR SLKHIYAQII DDEKGVTLVS
60 70 80 90 100
ASSLALKLKG NKTEVARQVG RALAEKALAL GIKQVAFDRG PYKYHGRVKA
110
LAEGAREGGL EF
Length:112
Mass (Da):12,612
Last modified:January 23, 2007 - v3
Checksum:iEA2AB016AEDB0638
GO

Mass spectrometryi

Molecular mass is 12481 Da from positions 2 - 112. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71499.1.
RefSeqiWP_008633391.1. NC_006461.1.
YP_144942.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71499; BAD71499; BAD71499.
GeneIDi3169978.
KEGGittj:TTHA1676.
PATRICi23958307. VBITheThe93045_1646.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71499.1.
RefSeqiWP_008633391.1. NC_006461.1.
YP_144942.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RS/YS1-112[»]
1VY4X-ray2.60BS/DS1-112[»]
1VY5X-ray2.55BS/DS1-112[»]
1VY6X-ray2.90BS/DS1-112[»]
1VY7X-ray2.80BS/DS1-112[»]
4L47X-ray3.22RS/YS1-112[»]
4L71X-ray3.90RS/YS1-112[»]
4LELX-ray3.90RS/YS1-112[»]
4LFZX-ray3.92RS/YS1-112[»]
4LNTX-ray2.94RS/YS1-112[»]
4LSKX-ray3.48RS/YS1-112[»]
4LT8X-ray3.14RS/YS1-112[»]
4P6FX-ray3.60RS/YS1-112[»]
4P70X-ray3.68RS/YS1-112[»]
4TUAX-ray3.60RS/YS1-112[»]
4TUBX-ray3.60RS/YS1-112[»]
4TUCX-ray3.60RS/YS1-112[»]
4TUDX-ray3.60RS/YS1-112[»]
4TUEX-ray3.50RS/YS1-112[»]
4V42X-ray5.50BQ1-112[»]
4V4PX-ray5.50Q1-112[»]
4V4XX-ray5.00BR1-112[»]
4V4YX-ray5.50BR1-112[»]
4V4ZX-ray4.51BR1-112[»]
4V51X-ray2.80BS/DS2-112[»]
4V5AX-ray3.50BS/DS2-112[»]
4V5CX-ray3.30BS/DS1-112[»]
4V5DX-ray3.50BS/DS1-112[»]
4V5EX-ray3.45BS/DS1-112[»]
4V5FX-ray3.60BS/DS1-112[»]
4V5GX-ray3.60BS/DS1-112[»]
4V5JX-ray3.10BS/DS1-112[»]
4V5KX-ray3.20BS/DS1-112[»]
4V5LX-ray3.10BS1-112[»]
4V5Melectron microscopy7.80BS1-112[»]
4V5Nelectron microscopy7.60BS1-112[»]
4V5PX-ray3.10BS/DS1-112[»]
4V5QX-ray3.10BS/DS1-112[»]
4V5RX-ray3.10BS/DS1-112[»]
4V5SX-ray3.10BS/DS1-112[»]
4V68electron microscopy6.40BS11-109[»]
4V6AX-ray3.10BS/DS1-112[»]
4V6FX-ray3.10AQ/DQ1-112[»]
4V6GX-ray3.50BQ/DQ1-112[»]
4V7JX-ray3.30AS/BS1-112[»]
4V7KX-ray3.60AS/BS1-112[»]
4V7LX-ray3.00BS/DS1-112[»]
4V7MX-ray3.45BS/DS1-112[»]
4V7WX-ray3.00BS/DS1-112[»]
4V7XX-ray3.00BS/DS1-112[»]
4V7YX-ray3.00BS/DS1-112[»]
4V7ZX-ray3.10BS/DS1-112[»]
4V87X-ray3.10AQ/DQ2-112[»]
4V8AX-ray3.20AS/BS1-112[»]
4V8BX-ray3.00BQ/DQ1-112[»]
4V8CX-ray3.30AQ/BQ1-112[»]
4V8DX-ray3.00BQ/DQ1-112[»]
4V8EX-ray3.30AQ/CQ1-112[»]
4V8FX-ray3.30AQ/DQ1-112[»]
4V8GX-ray3.00BS/DS1-112[»]
4V8HX-ray3.10BS/DS1-112[»]
4V8IX-ray2.70BS/DS1-112[»]
4V8JX-ray3.90BS/DS1-112[»]
4V8NX-ray3.10BS/DS1-112[»]
4V8OX-ray3.80BS1-112[»]
4V8QX-ray3.10AS1-112[»]
4V8UX-ray3.70BS/DS1-112[»]
4V8XX-ray3.35BS/DS1-112[»]
4V90X-ray2.95BS2-112[»]
4V95X-ray3.20BS/DS1-112[»]
4V97X-ray3.52BS/DS1-112[»]
4V9AX-ray3.30BQ/DQ1-112[»]
4V9BX-ray3.10BQ/DQ1-112[»]
4V9HX-ray2.86BS1-112[»]
4V9IX-ray3.30BS/DS11-108[»]
4V9RX-ray3.00BS/DS1-112[»]
4V9SX-ray3.10BS/DS1-112[»]
4W2EX-ray2.90S1-112[»]
4W2FX-ray2.40BS/DS1-112[»]
4W2GX-ray2.55BS/DS1-112[»]
4W2HX-ray2.70BS/DS1-112[»]
4W2IX-ray2.70BS/DS1-112[»]
4W4GX-ray3.30RS/YS1-112[»]
4WPOX-ray2.80AS/CS1-112[»]
4WQ1X-ray3.1065/A82-112[»]
4WQFX-ray2.80AS/CS1-112[»]
4WQRX-ray3.1565/A81-112[»]
4WQUX-ray2.80AS/CS1-112[»]
4WQYX-ray2.80AS/CS1-112[»]
4WR6X-ray3.0565/A81-112[»]
4WRAX-ray3.0565/A81-112[»]
4WROX-ray3.05A81-112[»]
4WSDX-ray2.9565/A81-112[»]
4WSMX-ray3.3065/A81-112[»]
4WT1X-ray3.0565/A81-112[»]
4WT8X-ray3.40CR/DR11-108[»]
4WU1X-ray3.2065/A81-112[»]
4WZDX-ray3.1065/A81-112[»]
4WZOX-ray3.3065/A81-112[»]
4Y4OX-ray2.301S/2S1-112[»]
4Y4PX-ray2.501S/2S1-112[»]
4YPBX-ray3.40RS/YS1-112[»]
4YZVX-ray3.10RS/YS1-112[»]
4Z3SX-ray2.651S/2S1-112[»]
4Z8CX-ray2.901S/2S1-112[»]
4ZERX-ray3.101S/2S3-112[»]
4ZSNX-ray3.60RS/YS1-112[»]
5A9Zelectron microscopy4.70AP3-112[»]
5AA0electron microscopy5.00AP3-112[»]
5CZPX-ray3.30RS/YS1-112[»]
5D8BX-ray3.63IB/M1-112[»]
5DFEX-ray3.10RS/YS1-112[»]
5DOXX-ray3.101S/2S1-112[»]
5DOYX-ray2.601S/2S1-112[»]
5E7KX-ray3.2065/A81-112[»]
5E81X-ray2.9565/A81-112[»]
5EL4X-ray3.1565/A81-112[»]
5EL5X-ray3.1565/A81-112[»]
5EL6X-ray3.1065/A81-112[»]
5EL7X-ray3.1565/A81-112[»]
5F8KX-ray2.801S/2S3-112[»]
5FDUX-ray2.901S/2S3-112[»]
5FDVX-ray2.801S/2S3-112[»]
5HAUX-ray3.001Q/2Q1-112[»]
5HCPX-ray2.891S/2S1-112[»]
5HCQX-ray2.801S/2S1-112[»]
5HCRX-ray2.801S/2S1-112[»]
5HD1X-ray2.701S/2S1-112[»]
5IB7X-ray2.9965/A81-112[»]
5IB8X-ray3.1365/A81-112[»]
5IBBX-ray2.9665/A81-112[»]
5IMQelectron microscopy3.80k1-112[»]
5IMRelectron microscopy-k1-112[»]
5J30X-ray3.20RS/YS1-112[»]
5J3CX-ray3.04RS/YS1-112[»]
5J4BX-ray2.601S/2S1-112[»]
5J4CX-ray2.801S/2S1-112[»]
5J8BX-ray2.60S1-112[»]
ProteinModelPortaliQ5SHQ4.
SMRiQ5SHQ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71499; BAD71499; BAD71499.
GeneIDi3169978.
KEGGittj:TTHA1676.
PATRICi23958307. VBITheThe93045_1646.

Phylogenomic databases

eggNOGiENOG4105K4C. Bacteria.
COG0256. LUCA.
HOGENOMiHOG000248742.
KOiK02881.
OMAiKSTRSHI.
PhylomeDBiQ5SHQ4.

Miscellaneous databases

EvolutionaryTraceiQ5SHQ4.

Family and domain databases

HAMAPiMF_01337_B. Ribosomal_L18_B. 1 hit.
InterProiIPR005484. Ribosomal_L18.
IPR004389. Ribosomal_L18_bac-type.
[Graphical view]
PfamiPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00060. L18_bact. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL18_THET8
AccessioniPrimary (citable) accession number: Q5SHQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.