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P10972

- RL24_HALMA

UniProt

P10972 - RL24_HALMA

Protein

50S ribosomal protein L24P

Gene

rpl24p

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.By similarity
    Stabilizes the tertiary rRNA structure within the 23S rRNA domain (domain I) to which it binds. Located at the polypeptide exit tunnel on the outside of the subunit.

    GO - Molecular functioni

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

    GO - Biological processi

    1. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciHMAR272569:GJDH-1457-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L24P
    Alternative name(s):
    Hl15
    Hl16
    Hmal24
    Gene namesi
    Name:rpl24p
    Ordered Locus Names:rrnAC1601
    OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
    Taxonomic identifieri272569 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
    ProteomesiUP000001169: Chromosome I

    Subcellular locationi

    GO - Cellular componenti

    1. large ribosomal subunit Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 12011950S ribosomal protein L24PPRO_0000130767Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Interacts weakly with protein L4.2 Publications

    Protein-protein interaction databases

    STRINGi272569.rrnAC1601.

    Structurei

    Secondary structure

    1
    120
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 139
    Helixi17 – 193
    Helixi21 – 244
    Beta strandi25 – 284
    Helixi30 – 367
    Beta strandi39 – 424
    Beta strandi48 – 514
    Turni55 – 584
    Beta strandi60 – 678
    Turni68 – 714
    Beta strandi72 – 754
    Beta strandi79 – 813
    Beta strandi83 – 853
    Beta strandi87 – 893
    Helixi94 – 963
    Beta strandi97 – 1015
    Helixi107 – 1148
    Beta strandi116 – 1183

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FFKX-ray2.40Q2-120[»]
    1JJ2X-ray2.40S2-120[»]
    1K73X-ray3.01U2-120[»]
    1K8AX-ray3.00U2-120[»]
    1K9MX-ray3.00U2-120[»]
    1KC8X-ray3.01U2-120[»]
    1KD1X-ray3.00U2-120[»]
    1KQSX-ray3.10S2-120[»]
    1M1KX-ray3.20U2-120[»]
    1M90X-ray2.80U2-120[»]
    1N8RX-ray3.00U2-120[»]
    1NJIX-ray3.00U2-120[»]
    1Q7YX-ray3.20U2-120[»]
    1Q81X-ray2.95U2-120[»]
    1Q82X-ray2.98U2-120[»]
    1Q86X-ray3.00U2-120[»]
    1QVFX-ray3.10S2-120[»]
    1QVGX-ray2.90S2-120[»]
    1S72X-ray2.40T1-120[»]
    1VQ4X-ray2.70T1-120[»]
    1VQ5X-ray2.60T1-120[»]
    1VQ6X-ray2.70T1-120[»]
    1VQ7X-ray2.50T1-120[»]
    1VQ8X-ray2.20T1-120[»]
    1VQ9X-ray2.40T1-120[»]
    1VQKX-ray2.30T1-120[»]
    1VQLX-ray2.30T1-120[»]
    1VQMX-ray2.30T1-120[»]
    1VQNX-ray2.40T1-120[»]
    1VQOX-ray2.20T1-120[»]
    1VQPX-ray2.25T1-120[»]
    1W2BX-ray3.50S2-120[»]
    1YHQX-ray2.40T1-120[»]
    1YI2X-ray2.65T1-120[»]
    1YIJX-ray2.60T1-120[»]
    1YITX-ray2.80T1-120[»]
    1YJ9X-ray2.90T1-120[»]
    1YJNX-ray3.00T1-120[»]
    1YJWX-ray2.90T1-120[»]
    2B66X-ray5.90Y2-120[»]
    2B9PX-ray6.46Y2-120[»]
    2OTJX-ray2.90T1-120[»]
    2OTLX-ray2.70T1-120[»]
    2QA4X-ray3.00T1-120[»]
    2QEXX-ray2.90T1-120[»]
    3CC2X-ray2.40T1-120[»]
    3CC4X-ray2.70T1-120[»]
    3CC7X-ray2.70T1-120[»]
    3CCEX-ray2.75T1-120[»]
    3CCJX-ray2.70T1-120[»]
    3CCLX-ray2.90T1-120[»]
    3CCMX-ray2.55T1-120[»]
    3CCQX-ray2.90T1-120[»]
    3CCRX-ray3.00T1-120[»]
    3CCSX-ray2.95T1-120[»]
    3CCUX-ray2.80T1-120[»]
    3CCVX-ray2.90T1-120[»]
    3CD6X-ray2.75T1-120[»]
    3CMAX-ray2.80T1-120[»]
    3CMEX-ray2.95T1-120[»]
    3CPWX-ray2.70S1-120[»]
    3CXCX-ray3.00S2-120[»]
    3G4SX-ray3.20T2-120[»]
    3G6EX-ray2.70T2-120[»]
    3G71X-ray2.85T2-120[»]
    3I55X-ray3.11T1-120[»]
    3I56X-ray2.90T1-120[»]
    3OW2X-ray2.70S2-120[»]
    4ADXelectron microscopy6.60T1-120[»]
    4HUBX-ray2.40T1-120[»]
    ProteinModelPortaliP10972.
    SMRiP10972. Positions 2-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10972.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L24P family.Curated

    Phylogenomic databases

    eggNOGiCOG0198.
    HOGENOMiHOG000216571.
    KOiK02895.
    OMAiHKIMSAT.

    Family and domain databases

    Gene3Di2.30.30.30. 1 hit.
    HAMAPiMF_01326_A. Ribosomal_L24_A.
    InterProiIPR005824. KOW.
    IPR014722. Rib_L2_dom2.
    IPR005825. Ribosomal_L24/26_CS.
    IPR005756. Ribosomal_L26/L24P_euk/arc.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view]
    PANTHERiPTHR11143. PTHR11143. 1 hit.
    PfamiPF00467. KOW. 1 hit.
    [Graphical view]
    SMARTiSM00739. KOW. 1 hit.
    [Graphical view]
    SUPFAMiSSF50104. SSF50104. 1 hit.
    TIGRFAMsiTIGR01080. rplX_A_E. 1 hit.
    PROSITEiPS01108. RIBOSOMAL_L24. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10972-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKQPDKQRK SQRRAPLHER HKQVRATLSA DLREEYGQRN VRVNAGDTVE    50
    VLRGDFAGEE GEVINVDLDK AVIHVEDVTL EKTDGEEVPR PLDTSNVRVT 100
    DLDLEDEKRE ARLESEDDSA 120
    Length:120
    Mass (Da):13,648
    Last modified:January 23, 2007 - v3
    Checksum:iBDEEF21DE1587096
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211H → R AA sequence (PubMed:3191994)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55311 Genomic DNA. Translation: CAA39019.1.
    AY596297 Genomic DNA. Translation: AAV46518.1.
    PIRiS10735. R5HS24.
    RefSeqiYP_136224.1. NC_006396.1.

    Genome annotation databases

    EnsemblBacteriaiAAV46518; AAV46518; rrnAC1601.
    GeneIDi3128440.
    KEGGihma:rrnAC1601.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55311 Genomic DNA. Translation: CAA39019.1 .
    AY596297 Genomic DNA. Translation: AAV46518.1 .
    PIRi S10735. R5HS24.
    RefSeqi YP_136224.1. NC_006396.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FFK X-ray 2.40 Q 2-120 [» ]
    1JJ2 X-ray 2.40 S 2-120 [» ]
    1K73 X-ray 3.01 U 2-120 [» ]
    1K8A X-ray 3.00 U 2-120 [» ]
    1K9M X-ray 3.00 U 2-120 [» ]
    1KC8 X-ray 3.01 U 2-120 [» ]
    1KD1 X-ray 3.00 U 2-120 [» ]
    1KQS X-ray 3.10 S 2-120 [» ]
    1M1K X-ray 3.20 U 2-120 [» ]
    1M90 X-ray 2.80 U 2-120 [» ]
    1N8R X-ray 3.00 U 2-120 [» ]
    1NJI X-ray 3.00 U 2-120 [» ]
    1Q7Y X-ray 3.20 U 2-120 [» ]
    1Q81 X-ray 2.95 U 2-120 [» ]
    1Q82 X-ray 2.98 U 2-120 [» ]
    1Q86 X-ray 3.00 U 2-120 [» ]
    1QVF X-ray 3.10 S 2-120 [» ]
    1QVG X-ray 2.90 S 2-120 [» ]
    1S72 X-ray 2.40 T 1-120 [» ]
    1VQ4 X-ray 2.70 T 1-120 [» ]
    1VQ5 X-ray 2.60 T 1-120 [» ]
    1VQ6 X-ray 2.70 T 1-120 [» ]
    1VQ7 X-ray 2.50 T 1-120 [» ]
    1VQ8 X-ray 2.20 T 1-120 [» ]
    1VQ9 X-ray 2.40 T 1-120 [» ]
    1VQK X-ray 2.30 T 1-120 [» ]
    1VQL X-ray 2.30 T 1-120 [» ]
    1VQM X-ray 2.30 T 1-120 [» ]
    1VQN X-ray 2.40 T 1-120 [» ]
    1VQO X-ray 2.20 T 1-120 [» ]
    1VQP X-ray 2.25 T 1-120 [» ]
    1W2B X-ray 3.50 S 2-120 [» ]
    1YHQ X-ray 2.40 T 1-120 [» ]
    1YI2 X-ray 2.65 T 1-120 [» ]
    1YIJ X-ray 2.60 T 1-120 [» ]
    1YIT X-ray 2.80 T 1-120 [» ]
    1YJ9 X-ray 2.90 T 1-120 [» ]
    1YJN X-ray 3.00 T 1-120 [» ]
    1YJW X-ray 2.90 T 1-120 [» ]
    2B66 X-ray 5.90 Y 2-120 [» ]
    2B9P X-ray 6.46 Y 2-120 [» ]
    2OTJ X-ray 2.90 T 1-120 [» ]
    2OTL X-ray 2.70 T 1-120 [» ]
    2QA4 X-ray 3.00 T 1-120 [» ]
    2QEX X-ray 2.90 T 1-120 [» ]
    3CC2 X-ray 2.40 T 1-120 [» ]
    3CC4 X-ray 2.70 T 1-120 [» ]
    3CC7 X-ray 2.70 T 1-120 [» ]
    3CCE X-ray 2.75 T 1-120 [» ]
    3CCJ X-ray 2.70 T 1-120 [» ]
    3CCL X-ray 2.90 T 1-120 [» ]
    3CCM X-ray 2.55 T 1-120 [» ]
    3CCQ X-ray 2.90 T 1-120 [» ]
    3CCR X-ray 3.00 T 1-120 [» ]
    3CCS X-ray 2.95 T 1-120 [» ]
    3CCU X-ray 2.80 T 1-120 [» ]
    3CCV X-ray 2.90 T 1-120 [» ]
    3CD6 X-ray 2.75 T 1-120 [» ]
    3CMA X-ray 2.80 T 1-120 [» ]
    3CME X-ray 2.95 T 1-120 [» ]
    3CPW X-ray 2.70 S 1-120 [» ]
    3CXC X-ray 3.00 S 2-120 [» ]
    3G4S X-ray 3.20 T 2-120 [» ]
    3G6E X-ray 2.70 T 2-120 [» ]
    3G71 X-ray 2.85 T 2-120 [» ]
    3I55 X-ray 3.11 T 1-120 [» ]
    3I56 X-ray 2.90 T 1-120 [» ]
    3OW2 X-ray 2.70 S 2-120 [» ]
    4ADX electron microscopy 6.60 T 1-120 [» ]
    4HUB X-ray 2.40 T 1-120 [» ]
    ProteinModelPortali P10972.
    SMRi P10972. Positions 2-120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272569.rrnAC1601.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV46518 ; AAV46518 ; rrnAC1601 .
    GeneIDi 3128440.
    KEGGi hma:rrnAC1601.

    Phylogenomic databases

    eggNOGi COG0198.
    HOGENOMi HOG000216571.
    KOi K02895.
    OMAi HKIMSAT.

    Enzyme and pathway databases

    BioCyci HMAR272569:GJDH-1457-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P10972.

    Family and domain databases

    Gene3Di 2.30.30.30. 1 hit.
    HAMAPi MF_01326_A. Ribosomal_L24_A.
    InterProi IPR005824. KOW.
    IPR014722. Rib_L2_dom2.
    IPR005825. Ribosomal_L24/26_CS.
    IPR005756. Ribosomal_L26/L24P_euk/arc.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view ]
    PANTHERi PTHR11143. PTHR11143. 1 hit.
    Pfami PF00467. KOW. 1 hit.
    [Graphical view ]
    SMARTi SM00739. KOW. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50104. SSF50104. 1 hit.
    TIGRFAMsi TIGR01080. rplX_A_E. 1 hit.
    PROSITEi PS01108. RIBOSOMAL_L24. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of four genes encoding ribosomal proteins from the 'S10 and spectinomycin' operon equivalent region in the archaebacterium Halobacterium marismortui."
      Arndt E.
      FEBS Lett. 267:193-198(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    3. "The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui."
      Hatakeyama T., Hatakeyama T., Kimura M.
      FEBS Lett. 240:21-28(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-120.
    4. "Extended N-terminal sequencing of proteins of archaebacterial ribosomes blotted from two-dimensional gels onto glass fiber and poly(vinylidene difluoride) membrane."
      Walsh M.J., McDougall J., Wittmann-Liebold B.
      Biochemistry 27:6867-6876(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-18.
    5. "The complete atomic structure of the large ribosomal subunit at 2.4 A resolution."
      Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A.
      Science 289:905-920(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    6. "The structural basis of ribosome activity in peptide bond synthesis."
      Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A.
      Science 289:920-930(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT.
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    7. "A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits."
      Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K., Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A.
      Nat. Struct. Biol. 9:225-230(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT.
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    8. "The kink-turn: a new RNA secondary structure motif."
      Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A.
      EMBO J. 20:4214-4221(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    9. "The structures of four macrolide antibiotics bound to the large ribosomal subunit."
      Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.
      Mol. Cell 10:117-128(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FOUR MACROLIDE ANTIBIOTICS.
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    11. "Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit."
      Hansen J.L., Moore P.B., Steitz T.A.
      J. Mol. Biol. 330:1061-1075(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER.
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    12. "Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit."
      Schmeing T.M., Moore P.B., Steitz T.A.
      RNA 9:1345-1352(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT E SITE SUBSTRATES.
    13. "Revisiting the Haloarcula marismortui 50S ribosomal subunit model."
      Gabdulkhakov A., Nikonov S., Garber M.
      Acta Crystallogr. D 69:997-1004(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.

    Entry informationi

    Entry nameiRL24_HALMA
    AccessioniPrimary (citable) accession number: P10972
    Secondary accession number(s): Q5V1T4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 121 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

    External Data

    Dasty 3