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P20279

- RL3_HALMA

UniProt

P20279 - RL3_HALMA

Protein

50S ribosomal protein L3

Gene

rpl3

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 109 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      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

    BioCyciHMAR272569:GJDH-1467-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L3
    Alternative name(s):
    Hl1
    Hmal3
    Gene namesi
    Name:rpl3
    Ordered Locus Names:rrnAC1611
    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. ribosome Source: UniProtKB-KW

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 33833750S ribosomal protein L3PRO_0000077207Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L24e. Interacts weakly with protein L13.2 Publications

    Protein-protein interaction databases

    STRINGi272569.rrnAC1611.

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 143
    Beta strandi35 – 395
    Beta strandi42 – 5514
    Beta strandi59 – 613
    Turni62 – 654
    Beta strandi66 – 7611
    Beta strandi80 – 9112
    Beta strandi94 – 1029
    Helixi110 – 1123
    Helixi122 – 13514
    Beta strandi138 – 1469
    Helixi149 – 1513
    Beta strandi153 – 1553
    Beta strandi162 – 1687
    Helixi172 – 18514
    Beta strandi187 – 1893
    Turni192 – 1943
    Beta strandi200 – 2067
    Beta strandi209 – 2135
    Helixi215 – 2195
    Helixi226 – 2294
    Beta strandi230 – 2323
    Beta strandi234 – 2363
    Beta strandi243 – 2475
    Beta strandi250 – 2523
    Beta strandi256 – 2594
    Beta strandi262 – 27918
    Turni286 – 2883
    Beta strandi293 – 3008
    Beta strandi309 – 3146
    Beta strandi328 – 3314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FFKX-ray2.40B2-338[»]
    1JJ2X-ray2.40B2-338[»]
    1K73X-ray3.01D2-338[»]
    1K8AX-ray3.00D2-338[»]
    1K9MX-ray3.00D2-338[»]
    1KC8X-ray3.01D2-338[»]
    1KD1X-ray3.00D2-338[»]
    1KQSX-ray3.10B2-338[»]
    1M1KX-ray3.20D2-338[»]
    1M90X-ray2.80D2-338[»]
    1ML5electron microscopy14.00e2-311[»]
    e312-338[»]
    1N8RX-ray3.00D2-338[»]
    1NJIX-ray3.00D2-338[»]
    1Q7YX-ray3.20D2-338[»]
    1Q81X-ray2.95D2-338[»]
    1Q82X-ray2.98D2-338[»]
    1Q86X-ray3.00D2-338[»]
    1QVFX-ray3.10B2-338[»]
    1QVGX-ray2.90B2-338[»]
    1S72X-ray2.40B1-338[»]
    1VQ4X-ray2.70B1-338[»]
    1VQ5X-ray2.60B1-338[»]
    1VQ6X-ray2.70B1-338[»]
    1VQ7X-ray2.50B1-338[»]
    1VQ8X-ray2.20B1-338[»]
    1VQ9X-ray2.40B1-338[»]
    1VQKX-ray2.30B1-338[»]
    1VQLX-ray2.30B1-338[»]
    1VQMX-ray2.30B1-338[»]
    1VQNX-ray2.40B1-338[»]
    1VQOX-ray2.20B1-338[»]
    1VQPX-ray2.25B1-338[»]
    1W2BX-ray3.50B2-338[»]
    1YHQX-ray2.40B1-338[»]
    1YI2X-ray2.65B1-338[»]
    1YIJX-ray2.60B1-338[»]
    1YITX-ray2.80B1-338[»]
    1YJ9X-ray2.90B1-338[»]
    1YJNX-ray3.00B1-338[»]
    1YJWX-ray2.90B1-338[»]
    2B9PX-ray6.46E2-338[»]
    2OTJX-ray2.90B1-338[»]
    2OTLX-ray2.70B2-338[»]
    2QA4X-ray3.00B1-338[»]
    2QEXX-ray2.90B1-338[»]
    3CC2X-ray2.40B1-338[»]
    3CC4X-ray2.70B1-338[»]
    3CC7X-ray2.70B1-338[»]
    3CCEX-ray2.75B1-338[»]
    3CCJX-ray2.70B1-338[»]
    3CCLX-ray2.90B1-338[»]
    3CCMX-ray2.55B1-338[»]
    3CCQX-ray2.90B1-338[»]
    3CCRX-ray3.00B1-338[»]
    3CCSX-ray2.95B1-338[»]
    3CCUX-ray2.80B1-338[»]
    3CCVX-ray2.90B1-338[»]
    3CD6X-ray2.75B1-338[»]
    3CMAX-ray2.80B1-338[»]
    3CMEX-ray2.95B1-338[»]
    3CPWX-ray2.70B1-338[»]
    3CXCX-ray3.00B2-338[»]
    3G4SX-ray3.20B2-338[»]
    3G6EX-ray2.70B2-338[»]
    3G71X-ray2.85B2-338[»]
    3I55X-ray3.11B1-338[»]
    3I56X-ray2.90B1-338[»]
    3OW2X-ray2.70B2-338[»]
    4ADXelectron microscopy6.60B1-338[»]
    4HUBX-ray2.40B1-338[»]
    ProteinModelPortaliP20279.
    SMRiP20279. Positions 2-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20279.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L3P family.Curated

    Phylogenomic databases

    eggNOGiCOG0087.
    HOGENOMiHOG000107320.
    KOiK02906.
    OMAiTYISTES.

    Family and domain databases

    HAMAPiMF_01325_A. Ribosomal_L3_A.
    InterProiIPR000597. Ribosomal_L3.
    IPR019928. Ribosomal_L3_arc.
    IPR019926. Ribosomal_L3_CS.
    IPR009000. Transl_B-barrel.
    [Graphical view]
    PfamiPF00297. Ribosomal_L3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    TIGRFAMsiTIGR03626. L3_arch. 1 hit.
    PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P20279-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPQPSRPRKG SLGFGPRKRS TSETPRFNSW PSDDGQPGVQ GFAGYKAGMT    50
    HVVLVNDEPN SPREGMEETV PVTVIETPPM RAVALRAYED TPYGQRPLTE 100
    VWTDEFHSEL DRTLDVPEDH DPDAAEEQIR DAHEAGDLGD LRLITHTVPD 150
    AVPSVPKKKP DVMETRVGGG SVSDRLDHAL DIVEDGGEHA MNDIFRAGEY 200
    ADVAGVTKGK GTQGPVKRWG VQKRKGKHAR QGWRRRIGNL GPWNPSRVRS 250
    TVPQQGQTGY HQRTELNKRL IDIGEGDEPT VDGGFVNYGE VDGPYTLVKG 300
    SVPGPDKRLV RFRPAVRPND QPRLDPEVRY VSNESNQG 338
    Length:338
    Mass (Da):37,341
    Last modified:January 23, 2007 - v5
    Checksum:i996D3BE503F4DBD4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti311 – 3111R → P in AAA86859. (PubMed:2406244)Curated
    Sequence conflicti312 – 3121F → FF AA sequence (PubMed:2406244)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05222 Genomic DNA. Translation: AAA86859.1.
    AY596297 Genomic DNA. Translation: AAV46528.1.
    PIRiC35063. R5HS3L.
    RefSeqiYP_136234.1. NC_006396.1.

    Genome annotation databases

    EnsemblBacteriaiAAV46528; AAV46528; rrnAC1611.
    GeneIDi3128366.
    KEGGihma:rrnAC1611.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05222 Genomic DNA. Translation: AAA86859.1 .
    AY596297 Genomic DNA. Translation: AAV46528.1 .
    PIRi C35063. R5HS3L.
    RefSeqi YP_136234.1. 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 B 2-338 [» ]
    1JJ2 X-ray 2.40 B 2-338 [» ]
    1K73 X-ray 3.01 D 2-338 [» ]
    1K8A X-ray 3.00 D 2-338 [» ]
    1K9M X-ray 3.00 D 2-338 [» ]
    1KC8 X-ray 3.01 D 2-338 [» ]
    1KD1 X-ray 3.00 D 2-338 [» ]
    1KQS X-ray 3.10 B 2-338 [» ]
    1M1K X-ray 3.20 D 2-338 [» ]
    1M90 X-ray 2.80 D 2-338 [» ]
    1ML5 electron microscopy 14.00 e 2-311 [» ]
    e 312-338 [» ]
    1N8R X-ray 3.00 D 2-338 [» ]
    1NJI X-ray 3.00 D 2-338 [» ]
    1Q7Y X-ray 3.20 D 2-338 [» ]
    1Q81 X-ray 2.95 D 2-338 [» ]
    1Q82 X-ray 2.98 D 2-338 [» ]
    1Q86 X-ray 3.00 D 2-338 [» ]
    1QVF X-ray 3.10 B 2-338 [» ]
    1QVG X-ray 2.90 B 2-338 [» ]
    1S72 X-ray 2.40 B 1-338 [» ]
    1VQ4 X-ray 2.70 B 1-338 [» ]
    1VQ5 X-ray 2.60 B 1-338 [» ]
    1VQ6 X-ray 2.70 B 1-338 [» ]
    1VQ7 X-ray 2.50 B 1-338 [» ]
    1VQ8 X-ray 2.20 B 1-338 [» ]
    1VQ9 X-ray 2.40 B 1-338 [» ]
    1VQK X-ray 2.30 B 1-338 [» ]
    1VQL X-ray 2.30 B 1-338 [» ]
    1VQM X-ray 2.30 B 1-338 [» ]
    1VQN X-ray 2.40 B 1-338 [» ]
    1VQO X-ray 2.20 B 1-338 [» ]
    1VQP X-ray 2.25 B 1-338 [» ]
    1W2B X-ray 3.50 B 2-338 [» ]
    1YHQ X-ray 2.40 B 1-338 [» ]
    1YI2 X-ray 2.65 B 1-338 [» ]
    1YIJ X-ray 2.60 B 1-338 [» ]
    1YIT X-ray 2.80 B 1-338 [» ]
    1YJ9 X-ray 2.90 B 1-338 [» ]
    1YJN X-ray 3.00 B 1-338 [» ]
    1YJW X-ray 2.90 B 1-338 [» ]
    2B9P X-ray 6.46 E 2-338 [» ]
    2OTJ X-ray 2.90 B 1-338 [» ]
    2OTL X-ray 2.70 B 2-338 [» ]
    2QA4 X-ray 3.00 B 1-338 [» ]
    2QEX X-ray 2.90 B 1-338 [» ]
    3CC2 X-ray 2.40 B 1-338 [» ]
    3CC4 X-ray 2.70 B 1-338 [» ]
    3CC7 X-ray 2.70 B 1-338 [» ]
    3CCE X-ray 2.75 B 1-338 [» ]
    3CCJ X-ray 2.70 B 1-338 [» ]
    3CCL X-ray 2.90 B 1-338 [» ]
    3CCM X-ray 2.55 B 1-338 [» ]
    3CCQ X-ray 2.90 B 1-338 [» ]
    3CCR X-ray 3.00 B 1-338 [» ]
    3CCS X-ray 2.95 B 1-338 [» ]
    3CCU X-ray 2.80 B 1-338 [» ]
    3CCV X-ray 2.90 B 1-338 [» ]
    3CD6 X-ray 2.75 B 1-338 [» ]
    3CMA X-ray 2.80 B 1-338 [» ]
    3CME X-ray 2.95 B 1-338 [» ]
    3CPW X-ray 2.70 B 1-338 [» ]
    3CXC X-ray 3.00 B 2-338 [» ]
    3G4S X-ray 3.20 B 2-338 [» ]
    3G6E X-ray 2.70 B 2-338 [» ]
    3G71 X-ray 2.85 B 2-338 [» ]
    3I55 X-ray 3.11 B 1-338 [» ]
    3I56 X-ray 2.90 B 1-338 [» ]
    3OW2 X-ray 2.70 B 2-338 [» ]
    4ADX electron microscopy 6.60 B 1-338 [» ]
    4HUB X-ray 2.40 B 1-338 [» ]
    ProteinModelPortali P20279.
    SMRi P20279. Positions 2-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272569.rrnAC1611.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV46528 ; AAV46528 ; rrnAC1611 .
    GeneIDi 3128366.
    KEGGi hma:rrnAC1611.

    Phylogenomic databases

    eggNOGi COG0087.
    HOGENOMi HOG000107320.
    KOi K02906.
    OMAi TYISTES.

    Enzyme and pathway databases

    BioCyci HMAR272569:GJDH-1467-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P20279.

    Family and domain databases

    HAMAPi MF_01325_A. Ribosomal_L3_A.
    InterProi IPR000597. Ribosomal_L3.
    IPR019928. Ribosomal_L3_arc.
    IPR019926. Ribosomal_L3_CS.
    IPR009000. Transl_B-barrel.
    [Graphical view ]
    Pfami PF00297. Ribosomal_L3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50447. SSF50447. 1 hit.
    TIGRFAMsi TIGR03626. L3_arch. 1 hit.
    PROSITEi PS00474. RIBOSOMAL_L3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui."
      Arndt E., Kroemer W., Hatakeyama T.
      J. Biol. Chem. 265:3034-3039(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    3. "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.
    4. "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.
    5. "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.
    6. "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.
    7. "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.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    9. "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.
    10. "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.
    11. "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 nameiRL3_HALMA
    AccessioniPrimary (citable) accession number: P20279
    Secondary accession number(s): Q5V1S4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 of the entry and version 5 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