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Protein

50S ribosomal protein L1

Gene

rplA

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.By similarity
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L1UniRule annotation
Gene namesi
Name:rplAUniRule annotation
Synonyms:rpl1UniRule annotation
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001257652 – 22950S ribosomal protein L1Add BLAST228

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi262724.TTC1739.

Structurei

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 13Combined sources3
Helixi23 – 33Combined sources11
Beta strandi36 – 38Combined sources3
Beta strandi41 – 50Combined sources10
Helixi55 – 57Combined sources3
Beta strandi60 – 64Combined sources5
Beta strandi66 – 68Combined sources3
Beta strandi75 – 78Combined sources4
Helixi82 – 89Combined sources8
Beta strandi93 – 96Combined sources4
Helixi100 – 105Combined sources6
Beta strandi112 – 116Combined sources5
Helixi118 – 120Combined sources3
Helixi121 – 135Combined sources15
Helixi141 – 143Combined sources3
Beta strandi146 – 148Combined sources3
Helixi150 – 158Combined sources9
Beta strandi161 – 165Combined sources5
Beta strandi170 – 178Combined sources9
Helixi183 – 199Combined sources17
Beta strandi209 – 216Combined sources8
Beta strandi218 – 220Combined sources3
Beta strandi223 – 225Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AD2X-ray1.90A2-229[»]
1ZHOX-ray2.60A/C/E/G2-229[»]
2HW8X-ray2.10A2-229[»]
2OUMX-ray2.55A2-229[»]
2OV7X-ray2.30A/B/C2-229[»]
2VPLX-ray2.30A/C2-229[»]
3U4MX-ray2.00A1-229[»]
3U56X-ray2.10A1-229[»]
3UMYX-ray1.90A2-229[»]
4F9TX-ray1.46A1-229[»]
4QG3X-ray2.00A2-229[»]
4QGBX-ray2.60A/B14-229[»]
4QVIX-ray1.90A1-229[»]
4REOX-ray1.35A1-229[»]
5IB7X-ray2.99711-229[»]
5IB8X-ray3.13711-229[»]
5IBBX-ray2.9671/791-229[»]
5IMQelectron microscopy3.80Z1-229[»]
5IMRelectron microscopy-Z1-229[»]
5J8BX-ray2.60C2-229[»]
ProteinModelPortaliP27150.
SMRiP27150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27150.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L1P family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C64. Bacteria.
COG0081. LUCA.

Family and domain databases

CDDicd00403. Ribosomal_L1. 1 hit.
Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_B. Ribosomal_L1_B. 1 hit.
InterProiIPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01169. rplA_bact. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P27150-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKHGKRYRA LLEKVDPNKI YTIDEAAHLV KELATAKFDE TVEVHAKLGI
60 70 80 90 100
DPRRSDQNVR GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI
110 120 130 140 150
IQKILDGWMD FDAVVATPDV MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI
160 170 180 190 200
GEIIREIKAG RIEFRNDKTG AIHAPVGKAS FPPEKLADNI RAFIRALEAH
210 220
KPEGAKGTFL RSVYVTTTMG PSVRINPHS
Length:229
Mass (Da):24,826
Last modified:January 23, 2007 - v3
Checksum:i38C14B2563718175
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2P → V AA sequence (PubMed:1637860).Curated1
Sequence conflicti4 – 5HG → TN AA sequence (PubMed:1637860).Curated2
Sequence conflicti14K → F AA sequence (PubMed:1637860).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81375 Genomic DNA. Translation: CAA57139.1.
PIRiS66577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81375 Genomic DNA. Translation: CAA57139.1.
PIRiS66577.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AD2X-ray1.90A2-229[»]
1ZHOX-ray2.60A/C/E/G2-229[»]
2HW8X-ray2.10A2-229[»]
2OUMX-ray2.55A2-229[»]
2OV7X-ray2.30A/B/C2-229[»]
2VPLX-ray2.30A/C2-229[»]
3U4MX-ray2.00A1-229[»]
3U56X-ray2.10A1-229[»]
3UMYX-ray1.90A2-229[»]
4F9TX-ray1.46A1-229[»]
4QG3X-ray2.00A2-229[»]
4QGBX-ray2.60A/B14-229[»]
4QVIX-ray1.90A1-229[»]
4REOX-ray1.35A1-229[»]
5IB7X-ray2.99711-229[»]
5IB8X-ray3.13711-229[»]
5IBBX-ray2.9671/791-229[»]
5IMQelectron microscopy3.80Z1-229[»]
5IMRelectron microscopy-Z1-229[»]
5J8BX-ray2.60C2-229[»]
ProteinModelPortaliP27150.
SMRiP27150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC1739.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C64. Bacteria.
COG0081. LUCA.

Miscellaneous databases

EvolutionaryTraceiP27150.

Family and domain databases

CDDicd00403. Ribosomal_L1. 1 hit.
Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_B. Ribosomal_L1_B. 1 hit.
InterProiIPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01169. rplA_bact. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL1_THETH
AccessioniPrimary (citable) accession number: P27150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 107 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, Direct protein sequencing

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.