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Q5SHN8

- RL3_THET8

UniProt

Q5SHN8 - RL3_THET8

Protein

50S ribosomal protein L3

Gene

rplC

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    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

    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

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SHN8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L3P family.Curated

    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

    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: October 1, 2014
    This is version 80 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