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Protein

50S ribosomal protein L3

Gene

rplC

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.By similarity

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1731-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L3
Gene namesi
Name:rplC
Ordered Locus Names:TTHA1692
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20620650S ribosomal protein L3PRO_0000077180Add
BLAST

Post-translational modificationi

The mass differences between the observed and calculated masses are suggested to be due to methylation, which is known to occur in the E.coli and R.palustris orthologs.

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19.

Protein-protein interaction databases

STRINGi300852.TTHA1692.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1614Combined sources
Beta strandi19 – 279Combined sources
Beta strandi31 – 377Combined sources
Turni39 – 424Combined sources
Beta strandi46 – 538Combined sources
Helixi56 – 583Combined sources
Helixi61 – 688Combined sources
Turni69 – 713Combined sources
Beta strandi75 – 828Combined sources
Beta strandi87 – 915Combined sources
Helixi93 – 953Combined sources
Beta strandi101 – 1077Combined sources
Beta strandi112 – 1143Combined sources
Helixi116 – 1205Combined sources
Beta strandi127 – 1304Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1373Combined sources
Turni145 – 1473Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi161 – 17616Combined sources
Helixi177 – 1793Combined sources
Beta strandi181 – 1866Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi195 – 2006Combined sources
Turni202 – 2043Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RE/YE1-206[»]
1VY4X-ray2.60BE/DE1-206[»]
1VY5X-ray2.55BE/DE1-206[»]
1VY6X-ray2.90BE/DE1-206[»]
1VY7X-ray2.80BE/DE1-206[»]
4L47X-ray3.22RE/YE1-206[»]
4L71X-ray3.90RE/YE1-206[»]
4LELX-ray3.90RE/YE1-206[»]
4LFZX-ray3.92RE/YE1-206[»]
4LNTX-ray2.94RE/YE1-206[»]
4LSKX-ray3.48RE/YE1-206[»]
4LT8X-ray3.14RE/YE1-206[»]
4P6FX-ray3.60RE/YE1-206[»]
4P70X-ray3.68RE/YE1-206[»]
4V42X-ray5.50BE1-206[»]
4V4PX-ray5.50E21-26[»]
4V4XX-ray5.00E1-206[»]
4V4YX-ray5.50E1-206[»]
4V4ZX-ray4.51E1-206[»]
4V51X-ray2.80BE/DE1-206[»]
4V5AX-ray3.50BE/DE1-206[»]
4V5CX-ray3.30BE/DE1-206[»]
4V5DX-ray3.50BE/DE1-206[»]
4V5EX-ray3.45BE/DE1-206[»]
4V5FX-ray3.60BE/DE1-206[»]
4V5GX-ray3.60BE/DE1-206[»]
4V5JX-ray3.10BE/DE1-206[»]
4V5KX-ray3.20BE/DE1-206[»]
4V5LX-ray3.10BE1-206[»]
4V5Melectron microscopy7.80BE1-206[»]
4V5Nelectron microscopy7.60BE1-206[»]
4V5PX-ray3.10BE/DE1-206[»]
4V5QX-ray3.10BE/DE1-206[»]
4V5RX-ray3.10BE/DE1-206[»]
4V5SX-ray3.10BE/DE1-206[»]
4V68electron microscopy6.40BE1-205[»]
4V6AX-ray3.10BE/DE1-206[»]
4V6FX-ray3.10AE/DE1-206[»]
4V6GX-ray3.50BE/DE1-206[»]
4V7JX-ray3.30AE/BE1-206[»]
4V7KX-ray3.60AE/BE1-206[»]
4V7LX-ray3.00BE/DE1-206[»]
4V7MX-ray3.45BE/DE1-206[»]
4V7WX-ray3.00BE/DE1-206[»]
4V7XX-ray3.00BE/DE1-206[»]
4V7YX-ray3.00BE/DE1-206[»]
4V7ZX-ray3.10BE/DE1-206[»]
4V87X-ray3.10AE/DE1-205[»]
4V8AX-ray3.20AE/BE1-206[»]
4V8BX-ray3.00BE/DE1-206[»]
4V8CX-ray3.30AE/BE1-206[»]
4V8DX-ray3.00BE/DE1-206[»]
4V8EX-ray3.30AE/CE1-206[»]
4V8FX-ray3.30AE/DE1-206[»]
4V8GX-ray3.00BE/DE1-206[»]
4V8HX-ray3.10BE/DE1-206[»]
4V8IX-ray2.70BE/DE1-206[»]
4V8JX-ray3.90BE/DE1-206[»]
4V8NX-ray3.10BE/DE1-206[»]
4V8OX-ray3.80BE1-206[»]
4V8QX-ray3.10AE1-206[»]
4V8UX-ray3.70BE/DE1-206[»]
4V8XX-ray3.35BE/DE1-206[»]
4V90X-ray2.95BE1-206[»]
4V95X-ray3.20BE/DE1-206[»]
4V97X-ray3.52BE/DE1-206[»]
4V9AX-ray3.30BE/DE1-206[»]
4V9BX-ray3.10BE/DE1-206[»]
4V9HX-ray2.86BE1-206[»]
4V9IX-ray3.30BE/DE1-204[»]
4V9RX-ray3.00BE/DE1-206[»]
4V9SX-ray3.10BE/DE1-206[»]
4W2EX-ray2.90E1-206[»]
4W2FX-ray2.40BE/DE1-206[»]
4W2GX-ray2.55BE/DE1-206[»]
4W2HX-ray2.70BE/DE1-206[»]
4W2IX-ray2.70BE/DE1-206[»]
ProteinModelPortaliQ5SHN8.
SMRiQ5SHN8. Positions 1-206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHN8.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

eggNOGiCOG0087.
HOGENOMiHOG000100368.
KOiK02906.
OMAiKRMAGRY.
OrthoDBiEOG6WDSMH.
PhylomeDBiQ5SHN8.

Family and domain databases

HAMAPiMF_01325_B. Ribosomal_L3_B.
InterProiIPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERiPTHR11229. PTHR11229. 1 hit.
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03625. L3_bact. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SHN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGILGVKVG MTRIFRDDRA VPVTVILAGP CPVVQRRTPE KDGYTAVQLG
60 70 80 90 100
FLPQNPKRVN RPLKGHFAKA GVEPVRILRE IRDFNPEGDT VTVEIFKPGE
110 120 130 140 150
RVDVTGTSKG RGFAGVMKRW NFAGGPDSHG AHKIHRHPGS IGNRKTPGRV
160 170 180 190 200
YKGKKMAGHY GAERVTVMNL EVVDVIPEEN LLLVKGAVPG PNGGLVIVRE

TKKAAK
Length:206
Mass (Da):22,408
Last modified:December 21, 2004 - v1
Checksum:iA920741478CB6028
GO

Mass spectrometryi

Molecular mass is 22437 Da from positions 1 - 206. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71515.1.
RefSeqiYP_144958.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71515; BAD71515; BAD71515.
GeneIDi3167929.
KEGGittj:TTHA1692.
PATRICi23958339. VBITheThe93045_1662.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71515.1.
RefSeqiYP_144958.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RE/YE1-206[»]
1VY4X-ray2.60BE/DE1-206[»]
1VY5X-ray2.55BE/DE1-206[»]
1VY6X-ray2.90BE/DE1-206[»]
1VY7X-ray2.80BE/DE1-206[»]
4L47X-ray3.22RE/YE1-206[»]
4L71X-ray3.90RE/YE1-206[»]
4LELX-ray3.90RE/YE1-206[»]
4LFZX-ray3.92RE/YE1-206[»]
4LNTX-ray2.94RE/YE1-206[»]
4LSKX-ray3.48RE/YE1-206[»]
4LT8X-ray3.14RE/YE1-206[»]
4P6FX-ray3.60RE/YE1-206[»]
4P70X-ray3.68RE/YE1-206[»]
4V42X-ray5.50BE1-206[»]
4V4PX-ray5.50E21-26[»]
4V4XX-ray5.00E1-206[»]
4V4YX-ray5.50E1-206[»]
4V4ZX-ray4.51E1-206[»]
4V51X-ray2.80BE/DE1-206[»]
4V5AX-ray3.50BE/DE1-206[»]
4V5CX-ray3.30BE/DE1-206[»]
4V5DX-ray3.50BE/DE1-206[»]
4V5EX-ray3.45BE/DE1-206[»]
4V5FX-ray3.60BE/DE1-206[»]
4V5GX-ray3.60BE/DE1-206[»]
4V5JX-ray3.10BE/DE1-206[»]
4V5KX-ray3.20BE/DE1-206[»]
4V5LX-ray3.10BE1-206[»]
4V5Melectron microscopy7.80BE1-206[»]
4V5Nelectron microscopy7.60BE1-206[»]
4V5PX-ray3.10BE/DE1-206[»]
4V5QX-ray3.10BE/DE1-206[»]
4V5RX-ray3.10BE/DE1-206[»]
4V5SX-ray3.10BE/DE1-206[»]
4V68electron microscopy6.40BE1-205[»]
4V6AX-ray3.10BE/DE1-206[»]
4V6FX-ray3.10AE/DE1-206[»]
4V6GX-ray3.50BE/DE1-206[»]
4V7JX-ray3.30AE/BE1-206[»]
4V7KX-ray3.60AE/BE1-206[»]
4V7LX-ray3.00BE/DE1-206[»]
4V7MX-ray3.45BE/DE1-206[»]
4V7WX-ray3.00BE/DE1-206[»]
4V7XX-ray3.00BE/DE1-206[»]
4V7YX-ray3.00BE/DE1-206[»]
4V7ZX-ray3.10BE/DE1-206[»]
4V87X-ray3.10AE/DE1-205[»]
4V8AX-ray3.20AE/BE1-206[»]
4V8BX-ray3.00BE/DE1-206[»]
4V8CX-ray3.30AE/BE1-206[»]
4V8DX-ray3.00BE/DE1-206[»]
4V8EX-ray3.30AE/CE1-206[»]
4V8FX-ray3.30AE/DE1-206[»]
4V8GX-ray3.00BE/DE1-206[»]
4V8HX-ray3.10BE/DE1-206[»]
4V8IX-ray2.70BE/DE1-206[»]
4V8JX-ray3.90BE/DE1-206[»]
4V8NX-ray3.10BE/DE1-206[»]
4V8OX-ray3.80BE1-206[»]
4V8QX-ray3.10AE1-206[»]
4V8UX-ray3.70BE/DE1-206[»]
4V8XX-ray3.35BE/DE1-206[»]
4V90X-ray2.95BE1-206[»]
4V95X-ray3.20BE/DE1-206[»]
4V97X-ray3.52BE/DE1-206[»]
4V9AX-ray3.30BE/DE1-206[»]
4V9BX-ray3.10BE/DE1-206[»]
4V9HX-ray2.86BE1-206[»]
4V9IX-ray3.30BE/DE1-204[»]
4V9RX-ray3.00BE/DE1-206[»]
4V9SX-ray3.10BE/DE1-206[»]
4W2EX-ray2.90E1-206[»]
4W2FX-ray2.40BE/DE1-206[»]
4W2GX-ray2.55BE/DE1-206[»]
4W2HX-ray2.70BE/DE1-206[»]
4W2IX-ray2.70BE/DE1-206[»]
ProteinModelPortaliQ5SHN8.
SMRiQ5SHN8. Positions 1-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71515; BAD71515; BAD71515.
GeneIDi3167929.
KEGGittj:TTHA1692.
PATRICi23958339. VBITheThe93045_1662.

Phylogenomic databases

eggNOGiCOG0087.
HOGENOMiHOG000100368.
KOiK02906.
OMAiKRMAGRY.
OrthoDBiEOG6WDSMH.
PhylomeDBiQ5SHN8.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1731-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SHN8.

Family and domain databases

HAMAPiMF_01325_B. Ribosomal_L3_B.
InterProiIPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERiPTHR11229. PTHR11229. 1 hit.
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03625. L3_bact. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus."
    Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T.
    Biol. Chem. 381:1079-1087(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-21.
  3. "Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry."
    Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.
    Proteomics 5:4818-4831(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  4. "The path of messenger RNA through the ribosome."
    Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.
    Cell 106:233-241(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.

Entry informationi

Entry nameiRL3_THET8
AccessioniPrimary (citable) accession number: Q5SHN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: March 4, 2015
This is version 85 of the entry and version 1 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

External Data

Dasty 3

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 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.