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Protein

50S ribosomal protein L18

Gene

rpl18

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This is one of 5 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit, where it forms part of the central protuberance and stabilizes the orientation of adjacent RNA domains.

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):
Hl12
Hmal18
Gene namesi
Name:rpl18
Ordered Locus Names:rrnAC1593
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
Proteomesi
  • UP000001169 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001314002 – 18750S ribosomal protein L18Add BLAST186

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts with proteins L5 and L21e, and attaches the 5S rRNA to the 23S rRNA. Has been cross-linked to L21e.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1593.

Structurei

Secondary structure

1187
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Helixi12 – 15Combined sources4
Helixi21 – 28Combined sources8
Beta strandi34 – 39Combined sources6
Beta strandi44 – 50Combined sources7
Beta strandi53 – 55Combined sources3
Beta strandi57 – 64Combined sources8
Helixi65 – 70Combined sources6
Beta strandi76 – 78Combined sources3
Helixi79 – 95Combined sources17
Beta strandi102 – 104Combined sources3
Helixi115 – 125Combined sources11
Helixi134 – 136Combined sources3
Helixi140 – 144Combined sources5
Helixi146 – 153Combined sources8
Beta strandi159 – 162Combined sources4
Helixi170 – 181Combined sources12
Beta strandi182 – 185Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40K2-186[»]
1JJ2X-ray2.40M2-187[»]
1K73X-ray3.01O2-187[»]
1K8AX-ray3.00O2-187[»]
1K9MX-ray3.00O2-187[»]
1KC8X-ray3.01O2-187[»]
1KD1X-ray3.00O2-187[»]
1KQSX-ray3.10M2-187[»]
1M1KX-ray3.20O2-187[»]
1M90X-ray2.80O2-187[»]
1N8RX-ray3.00O2-187[»]
1NJIX-ray3.00O2-187[»]
1Q7YX-ray3.20O2-187[»]
1Q81X-ray2.95O2-187[»]
1Q82X-ray2.98O2-187[»]
1Q86X-ray3.00O2-187[»]
1QVFX-ray3.10M2-187[»]
1QVGX-ray2.90M2-187[»]
1S72X-ray2.40N1-187[»]
1VQ4X-ray2.70N1-187[»]
1VQ5X-ray2.60N1-187[»]
1VQ6X-ray2.70N1-187[»]
1VQ7X-ray2.50N1-187[»]
1VQ8X-ray2.20N1-187[»]
1VQ9X-ray2.40N1-187[»]
1VQKX-ray2.30N1-187[»]
1VQLX-ray2.30N1-187[»]
1VQMX-ray2.30N1-187[»]
1VQNX-ray2.40N1-187[»]
1VQOX-ray2.20N1-187[»]
1VQPX-ray2.25N1-187[»]
1W2BX-ray3.50M2-187[»]
1YHQX-ray2.40N1-187[»]
1YI2X-ray2.65N1-187[»]
1YIJX-ray2.60N1-187[»]
1YITX-ray2.80N1-187[»]
1YJ9X-ray2.90N1-187[»]
1YJNX-ray3.00N1-187[»]
1YJWX-ray2.90N1-187[»]
2OTJX-ray2.90N1-187[»]
2OTLX-ray2.70N1-187[»]
2QA4X-ray3.00N1-187[»]
2QEXX-ray2.90N1-187[»]
3CC2X-ray2.40N1-187[»]
3CC4X-ray2.70N1-187[»]
3CC7X-ray2.70N1-187[»]
3CCEX-ray2.75N1-187[»]
3CCJX-ray2.70N1-187[»]
3CCLX-ray2.90N1-187[»]
3CCMX-ray2.55N1-187[»]
3CCQX-ray2.90N1-187[»]
3CCRX-ray3.00N1-187[»]
3CCSX-ray2.95N1-187[»]
3CCUX-ray2.80N1-187[»]
3CCVX-ray2.90N1-187[»]
3CD6X-ray2.75N1-187[»]
3CMAX-ray2.80N1-187[»]
3CMEX-ray2.95N1-187[»]
3CPWX-ray2.70M1-187[»]
3CXCX-ray3.00M2-187[»]
3G4SX-ray3.20N2-187[»]
3G6EX-ray2.70N2-187[»]
3G71X-ray2.85N2-187[»]
3I55X-ray3.11N1-187[»]
3I56X-ray2.90N1-187[»]
3OW2X-ray2.70M2-187[»]
4ADXelectron microscopy6.60N1-187[»]
4V4RX-ray5.90S2-187[»]
4V4SX-ray6.76S2-187[»]
4V4TX-ray6.46S2-187[»]
4V9FX-ray2.40N1-187[»]
ProteinModelPortaliP14123.
SMRiP14123.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14123.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18P family.Curated

Phylogenomic databases

eggNOGiarCOG04088. Archaea.
COG0256. LUCA.
HOGENOMiHOG000105947.
KOiK02881.
OMAiGNKVFAV.

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A. 1 hit.
InterProiIPR005485. Rbsml_L5_euk/L18_arc.
[Graphical view]
PANTHERiPTHR23410. PTHR23410. 1 hit.
PfamiPF17144. Ribosomal_L5e. 2 hits.
[Graphical view]
PRINTSiPR00058. RIBOSOMALL5.

Sequencei

Sequence statusi: Complete.

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

P14123-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATGPRYKVP MRRRREARTD YHQRLRLLKS GKPRLVARKS NKHVRAQLVT
60 70 80 90 100
LGPNGDDTLA SAHSSDLAEY GWEAPTGNMP SAYLTGLLAG LRAQEAGVEE
110 120 130 140 150
AVLDIGLNSP TPGSKVFAIQ EGAIDAGLDI PHNDDVLADW QRTRGAHIAE
160 170 180
YDEQLEEPLY SGDFDAADLP EHFDELRETL LDGDIEL
Length:187
Mass (Da):20,614
Last modified:January 23, 2007 - v3
Checksum:i60E9AF3CB64E7CA5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18R → A AA sequence (PubMed:3196689).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58395 Genomic DNA. Translation: CAA41290.1.
AY596297 Genomic DNA. Translation: AAV46511.1.
PIRiS16541. R5HS18.
RefSeqiWP_011223738.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46511; AAV46511; rrnAC1593.
GeneIDi3127918.
KEGGihma:rrnAC1593.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58395 Genomic DNA. Translation: CAA41290.1.
AY596297 Genomic DNA. Translation: AAV46511.1.
PIRiS16541. R5HS18.
RefSeqiWP_011223738.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40K2-186[»]
1JJ2X-ray2.40M2-187[»]
1K73X-ray3.01O2-187[»]
1K8AX-ray3.00O2-187[»]
1K9MX-ray3.00O2-187[»]
1KC8X-ray3.01O2-187[»]
1KD1X-ray3.00O2-187[»]
1KQSX-ray3.10M2-187[»]
1M1KX-ray3.20O2-187[»]
1M90X-ray2.80O2-187[»]
1N8RX-ray3.00O2-187[»]
1NJIX-ray3.00O2-187[»]
1Q7YX-ray3.20O2-187[»]
1Q81X-ray2.95O2-187[»]
1Q82X-ray2.98O2-187[»]
1Q86X-ray3.00O2-187[»]
1QVFX-ray3.10M2-187[»]
1QVGX-ray2.90M2-187[»]
1S72X-ray2.40N1-187[»]
1VQ4X-ray2.70N1-187[»]
1VQ5X-ray2.60N1-187[»]
1VQ6X-ray2.70N1-187[»]
1VQ7X-ray2.50N1-187[»]
1VQ8X-ray2.20N1-187[»]
1VQ9X-ray2.40N1-187[»]
1VQKX-ray2.30N1-187[»]
1VQLX-ray2.30N1-187[»]
1VQMX-ray2.30N1-187[»]
1VQNX-ray2.40N1-187[»]
1VQOX-ray2.20N1-187[»]
1VQPX-ray2.25N1-187[»]
1W2BX-ray3.50M2-187[»]
1YHQX-ray2.40N1-187[»]
1YI2X-ray2.65N1-187[»]
1YIJX-ray2.60N1-187[»]
1YITX-ray2.80N1-187[»]
1YJ9X-ray2.90N1-187[»]
1YJNX-ray3.00N1-187[»]
1YJWX-ray2.90N1-187[»]
2OTJX-ray2.90N1-187[»]
2OTLX-ray2.70N1-187[»]
2QA4X-ray3.00N1-187[»]
2QEXX-ray2.90N1-187[»]
3CC2X-ray2.40N1-187[»]
3CC4X-ray2.70N1-187[»]
3CC7X-ray2.70N1-187[»]
3CCEX-ray2.75N1-187[»]
3CCJX-ray2.70N1-187[»]
3CCLX-ray2.90N1-187[»]
3CCMX-ray2.55N1-187[»]
3CCQX-ray2.90N1-187[»]
3CCRX-ray3.00N1-187[»]
3CCSX-ray2.95N1-187[»]
3CCUX-ray2.80N1-187[»]
3CCVX-ray2.90N1-187[»]
3CD6X-ray2.75N1-187[»]
3CMAX-ray2.80N1-187[»]
3CMEX-ray2.95N1-187[»]
3CPWX-ray2.70M1-187[»]
3CXCX-ray3.00M2-187[»]
3G4SX-ray3.20N2-187[»]
3G6EX-ray2.70N2-187[»]
3G71X-ray2.85N2-187[»]
3I55X-ray3.11N1-187[»]
3I56X-ray2.90N1-187[»]
3OW2X-ray2.70M2-187[»]
4ADXelectron microscopy6.60N1-187[»]
4V4RX-ray5.90S2-187[»]
4V4SX-ray6.76S2-187[»]
4V4TX-ray6.46S2-187[»]
4V9FX-ray2.40N1-187[»]
ProteinModelPortaliP14123.
SMRiP14123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC1593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV46511; AAV46511; rrnAC1593.
GeneIDi3127918.
KEGGihma:rrnAC1593.

Phylogenomic databases

eggNOGiarCOG04088. Archaea.
COG0256. LUCA.
HOGENOMiHOG000105947.
KOiK02881.
OMAiGNKVFAV.

Miscellaneous databases

EvolutionaryTraceiP14123.

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A. 1 hit.
InterProiIPR005485. Rbsml_L5_euk/L18_arc.
[Graphical view]
PANTHERiPTHR23410. PTHR23410. 1 hit.
PfamiPF17144. Ribosomal_L5e. 2 hits.
[Graphical view]
PRINTSiPR00058. RIBOSOMALL5.
ProtoNetiSearch...

Entry informationi

Entry nameiRL18_HALMA
AccessioniPrimary (citable) accession number: P14123
Secondary accession number(s): Q5V1U1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 131 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.