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Q5SHN8

- RL3_THET8

UniProt

Q5SHN8 - RL3_THET8

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Protein

50S ribosomal protein L3

Gene
rplC, TTHA1692
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - 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.UniRule annotation

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: 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 L3UniRule annotationPRO_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.UniRule annotation

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 – 1816
Beta strandi20 – 278
Beta strandi31 – 377
Helixi39 – 424
Beta strandi46 – 538
Helixi56 – 583
Helixi61 – 688
Turni69 – 713
Beta strandi75 – 828
Beta strandi87 – 915
Helixi93 – 953
Beta strandi101 – 1077
Beta strandi110 – 1145
Helixi116 – 1194
Beta strandi127 – 1304
Helixi132 – 1343
Beta strandi135 – 1373
Turni145 – 1473
Beta strandi157 – 1593
Beta strandi161 – 17616
Turni177 – 1804
Beta strandi181 – 1866
Beta strandi190 – 1934
Beta strandi195 – 2006
Turni202 – 2043

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GIYX-ray5.50E21-26[»]
1YL3X-ray5.50E21-26[»]
2HGJX-ray5.00E1-206[»]
2HGQX-ray5.50E1-206[»]
2HGUX-ray4.51E1-206[»]
2J01X-ray2.80E1-206[»]
2J03X-ray2.80E1-206[»]
2V47X-ray3.80E1-206[»]
2V49X-ray3.80E1-206[»]
2WDIX-ray3.30E1-206[»]
2WDJX-ray3.30E1-206[»]
2WDLX-ray3.50E1-206[»]
2WDNX-ray3.50E1-206[»]
2WH2X-ray3.45E1-206[»]
2WH4X-ray3.45E1-206[»]
2WRJX-ray3.60E1-206[»]
2WRLX-ray3.60E1-206[»]
2WROX-ray3.60E1-206[»]
2WRRX-ray3.60E1-206[»]
2X9SX-ray3.10E1-206[»]
2X9UX-ray3.10E1-206[»]
2XG0X-ray3.20E1-206[»]
2XG2X-ray3.20E1-206[»]
2XQEX-ray3.10E1-206[»]
2XTGelectron microscopy7.80E1-206[»]
2XUXelectron microscopy7.60E1-206[»]
2Y0VX-ray3.10E1-206[»]
2Y0XX-ray3.10E1-206[»]
2Y0ZX-ray3.10E1-206[»]
2Y11X-ray3.10E1-206[»]
2Y13X-ray3.10E1-206[»]
2Y15X-ray3.10E1-206[»]
2Y17X-ray3.10E1-206[»]
2Y19X-ray3.10E1-206[»]
3FINelectron microscopy6.40E1-205[»]
3HUXX-ray3.10E1-206[»]
3HUZX-ray3.10E1-206[»]
3I8FX-ray3.10E1-206[»]
3I8IX-ray3.10E1-206[»]
3I9CX-ray3.50E1-206[»]
3I9EX-ray3.50E1-206[»]
3KIRX-ray3.30E1-206[»]
3KITX-ray3.30E1-206[»]
3KIWX-ray3.60E1-206[»]
3KIYX-ray3.60E1-206[»]
3KNIX-ray3.00E1-206[»]
3KNKX-ray3.00E1-206[»]
3KNMX-ray3.45E1-206[»]
3KNOX-ray3.45E1-206[»]
3OH5X-ray3.00E1-206[»]
3OH7X-ray3.00E1-206[»]
3OHJX-ray3.00E1-206[»]
3OHKX-ray3.00E1-206[»]
3OHZX-ray3.00E1-206[»]
3OI1X-ray3.00E1-206[»]
3OI3X-ray3.10E1-206[»]
3OI5X-ray3.10E1-206[»]
3TVEX-ray3.10E1-205[»]
3TVHX-ray3.10E1-205[»]
3UXQX-ray3.20E1-206[»]
3UXRX-ray3.20E1-206[»]
3UYEX-ray3.00E1-206[»]
3UYGX-ray3.00E1-206[»]
3UZ1X-ray3.30E1-206[»]
3UZ2X-ray3.30E1-206[»]
3UZ8X-ray3.00E1-206[»]
3UZ9X-ray3.00E1-206[»]
3UZFX-ray3.30E1-206[»]
3UZHX-ray3.30E1-206[»]
3UZKX-ray3.30E1-206[»]
3UZNX-ray3.30E1-206[»]
3V23X-ray3.00E1-206[»]
3V25X-ray3.00E1-206[»]
3V27X-ray3.10E1-206[»]
3V29X-ray3.10E1-206[»]
3V2DX-ray2.70E1-206[»]
3V2FX-ray2.70E1-206[»]
3V6WX-ray3.90E1-206[»]
3V6XX-ray3.90E1-206[»]
3ZN9X-ray3.10E1-206[»]
3ZNEX-ray3.10E1-206[»]
3ZVPX-ray3.80E1-206[»]
4ABSX-ray3.10E1-206[»]
4B8GX-ray3.70E1-206[»]
4B8IX-ray3.70E1-206[»]
4BTDX-ray2.95E1-206[»]
4BYCX-ray3.35E1-206[»]
4BYEX-ray3.35E1-206[»]
4DHAX-ray3.20E1-206[»]
4DHCX-ray3.20E1-206[»]
4EJBX-ray3.52E1-206[»]
4EJCX-ray3.52E1-206[»]
4G5LX-ray3.30E1-206[»]
4G5NX-ray3.30E1-206[»]
4G5UX-ray3.10E1-206[»]
4G5WX-ray3.10E1-206[»]
4JUXX-ray2.86E1-206[»]
4K0MX-ray3.30E1-204[»]
4K0QX-ray3.30E1-204[»]
4NVVX-ray3.00E1-206[»]
4NVXX-ray3.00E1-206[»]
4NVZX-ray3.10E1-206[»]
4NW1X-ray3.10E1-206[»]
ProteinModelPortaliQ5SHN8.
SMRiQ5SHN8. Positions 1-206.

Miscellaneous databases

EvolutionaryTraceiQ5SHN8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0087.
HOGENOMiHOG000100368.
KOiK02906.
OMAiSMQDATH.
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

MKGILGVKVG MTRIFRDDRA VPVTVILAGP CPVVQRRTPE KDGYTAVQLG    50
FLPQNPKRVN RPLKGHFAKA GVEPVRILRE IRDFNPEGDT VTVEIFKPGE 100
RVDVTGTSKG RGFAGVMKRW NFAGGPDSHG AHKIHRHPGS IGNRKTPGRV 150
YKGKKMAGHY GAERVTVMNL EVVDVIPEEN LLLVKGAVPG PNGGLVIVRE 200
TKKAAK 206
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD71515.1 .
RefSeqi YP_144958.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GIY X-ray 5.50 E 21-26 [» ]
1YL3 X-ray 5.50 E 21-26 [» ]
2HGJ X-ray 5.00 E 1-206 [» ]
2HGQ X-ray 5.50 E 1-206 [» ]
2HGU X-ray 4.51 E 1-206 [» ]
2J01 X-ray 2.80 E 1-206 [» ]
2J03 X-ray 2.80 E 1-206 [» ]
2V47 X-ray 3.80 E 1-206 [» ]
2V49 X-ray 3.80 E 1-206 [» ]
2WDI X-ray 3.30 E 1-206 [» ]
2WDJ X-ray 3.30 E 1-206 [» ]
2WDL X-ray 3.50 E 1-206 [» ]
2WDN X-ray 3.50 E 1-206 [» ]
2WH2 X-ray 3.45 E 1-206 [» ]
2WH4 X-ray 3.45 E 1-206 [» ]
2WRJ X-ray 3.60 E 1-206 [» ]
2WRL X-ray 3.60 E 1-206 [» ]
2WRO X-ray 3.60 E 1-206 [» ]
2WRR X-ray 3.60 E 1-206 [» ]
2X9S X-ray 3.10 E 1-206 [» ]
2X9U X-ray 3.10 E 1-206 [» ]
2XG0 X-ray 3.20 E 1-206 [» ]
2XG2 X-ray 3.20 E 1-206 [» ]
2XQE X-ray 3.10 E 1-206 [» ]
2XTG electron microscopy 7.80 E 1-206 [» ]
2XUX electron microscopy 7.60 E 1-206 [» ]
2Y0V X-ray 3.10 E 1-206 [» ]
2Y0X X-ray 3.10 E 1-206 [» ]
2Y0Z X-ray 3.10 E 1-206 [» ]
2Y11 X-ray 3.10 E 1-206 [» ]
2Y13 X-ray 3.10 E 1-206 [» ]
2Y15 X-ray 3.10 E 1-206 [» ]
2Y17 X-ray 3.10 E 1-206 [» ]
2Y19 X-ray 3.10 E 1-206 [» ]
3FIN electron microscopy 6.40 E 1-205 [» ]
3HUX X-ray 3.10 E 1-206 [» ]
3HUZ X-ray 3.10 E 1-206 [» ]
3I8F X-ray 3.10 E 1-206 [» ]
3I8I X-ray 3.10 E 1-206 [» ]
3I9C X-ray 3.50 E 1-206 [» ]
3I9E X-ray 3.50 E 1-206 [» ]
3KIR X-ray 3.30 E 1-206 [» ]
3KIT X-ray 3.30 E 1-206 [» ]
3KIW X-ray 3.60 E 1-206 [» ]
3KIY X-ray 3.60 E 1-206 [» ]
3KNI X-ray 3.00 E 1-206 [» ]
3KNK X-ray 3.00 E 1-206 [» ]
3KNM X-ray 3.45 E 1-206 [» ]
3KNO X-ray 3.45 E 1-206 [» ]
3OH5 X-ray 3.00 E 1-206 [» ]
3OH7 X-ray 3.00 E 1-206 [» ]
3OHJ X-ray 3.00 E 1-206 [» ]
3OHK X-ray 3.00 E 1-206 [» ]
3OHZ X-ray 3.00 E 1-206 [» ]
3OI1 X-ray 3.00 E 1-206 [» ]
3OI3 X-ray 3.10 E 1-206 [» ]
3OI5 X-ray 3.10 E 1-206 [» ]
3TVE X-ray 3.10 E 1-205 [» ]
3TVH X-ray 3.10 E 1-205 [» ]
3UXQ X-ray 3.20 E 1-206 [» ]
3UXR X-ray 3.20 E 1-206 [» ]
3UYE X-ray 3.00 E 1-206 [» ]
3UYG X-ray 3.00 E 1-206 [» ]
3UZ1 X-ray 3.30 E 1-206 [» ]
3UZ2 X-ray 3.30 E 1-206 [» ]
3UZ8 X-ray 3.00 E 1-206 [» ]
3UZ9 X-ray 3.00 E 1-206 [» ]
3UZF X-ray 3.30 E 1-206 [» ]
3UZH X-ray 3.30 E 1-206 [» ]
3UZK X-ray 3.30 E 1-206 [» ]
3UZN X-ray 3.30 E 1-206 [» ]
3V23 X-ray 3.00 E 1-206 [» ]
3V25 X-ray 3.00 E 1-206 [» ]
3V27 X-ray 3.10 E 1-206 [» ]
3V29 X-ray 3.10 E 1-206 [» ]
3V2D X-ray 2.70 E 1-206 [» ]
3V2F X-ray 2.70 E 1-206 [» ]
3V6W X-ray 3.90 E 1-206 [» ]
3V6X X-ray 3.90 E 1-206 [» ]
3ZN9 X-ray 3.10 E 1-206 [» ]
3ZNE X-ray 3.10 E 1-206 [» ]
3ZVP X-ray 3.80 E 1-206 [» ]
4ABS X-ray 3.10 E 1-206 [» ]
4B8G X-ray 3.70 E 1-206 [» ]
4B8I X-ray 3.70 E 1-206 [» ]
4BTD X-ray 2.95 E 1-206 [» ]
4BYC X-ray 3.35 E 1-206 [» ]
4BYE X-ray 3.35 E 1-206 [» ]
4DHA X-ray 3.20 E 1-206 [» ]
4DHC X-ray 3.20 E 1-206 [» ]
4EJB X-ray 3.52 E 1-206 [» ]
4EJC X-ray 3.52 E 1-206 [» ]
4G5L X-ray 3.30 E 1-206 [» ]
4G5N X-ray 3.30 E 1-206 [» ]
4G5U X-ray 3.10 E 1-206 [» ]
4G5W X-ray 3.10 E 1-206 [» ]
4JUX X-ray 2.86 E 1-206 [» ]
4K0M X-ray 3.30 E 1-204 [» ]
4K0Q X-ray 3.30 E 1-204 [» ]
4NVV X-ray 3.00 E 1-206 [» ]
4NVX X-ray 3.00 E 1-206 [» ]
4NVZ X-ray 3.10 E 1-206 [» ]
4NW1 X-ray 3.10 E 1-206 [» ]
ProteinModelPortali Q5SHN8.
SMRi Q5SHN8. Positions 1-206.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1692.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71515 ; BAD71515 ; BAD71515 .
GeneIDi 3167929.
KEGGi ttj:TTHA1692.
PATRICi 23958339. VBITheThe93045_1662.

Phylogenomic databases

eggNOGi COG0087.
HOGENOMi HOG000100368.
KOi K02906.
OMAi SMQDATH.
OrthoDBi EOG6WDSMH.
PhylomeDBi Q5SHN8.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-1731-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5SHN8.

Family and domain databases

HAMAPi MF_01325_B. Ribosomal_L3_B.
InterProi IPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view ]
PANTHERi PTHR11229. PTHR11229. 1 hit.
Pfami PF00297. Ribosomal_L3. 1 hit.
[Graphical view ]
SUPFAMi SSF50447. SSF50447. 1 hit.
TIGRFAMsi TIGR03625. L3_bact. 1 hit.
PROSITEi PS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 (NOV-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(2000) [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(2005) [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(2001) [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: July 9, 2014
This is version 79 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

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