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P14121

- RL30_HALMA

UniProt

P14121 - RL30_HALMA

Protein

50S ribosomal protein L30P

Gene

rpl30p

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 112 (01 Oct 2014)
      Sequence version 2 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    This is one of 5 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit, stabilizing the orientation of adjacent RNA domains.

    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-1447-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L30PUniRule annotation
    Alternative name(s):
    Hl16
    Hl20
    Hmal30
    Gene namesi
    Name:rpl30pUniRule annotation
    Ordered Locus Names:rrnAC1591
    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
    Chaini1 – 15415450S ribosomal protein L30PPRO_0000104622Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Binds 5S rRNA.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    STRINGi272569.rrnAC1591.

    Structurei

    Secondary structure

    1
    154
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Helixi15 – 239
    Beta strandi31 – 355
    Helixi39 – 479
    Helixi49 – 513
    Beta strandi52 – 554
    Helixi59 – 6911
    Beta strandi72 – 754
    Helixi81 – 877
    Beta strandi88 – 925
    Helixi93 – 1019
    Helixi108 – 1103
    Beta strandi114 – 1174
    Beta strandi128 – 1314
    Helixi132 – 1343
    Beta strandi137 – 1404
    Helixi143 – 15210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FFKX-ray2.40T1-154[»]
    1JJ2X-ray2.40V1-154[»]
    1K73X-ray3.01X1-154[»]
    1K8AX-ray3.00X1-154[»]
    1K9MX-ray3.00X1-154[»]
    1KC8X-ray3.01X1-154[»]
    1KD1X-ray3.00X1-154[»]
    1KQSX-ray3.10V1-154[»]
    1M1KX-ray3.20X1-154[»]
    1M90X-ray2.80X1-154[»]
    1N8RX-ray3.00X1-154[»]
    1NJIX-ray3.00X1-154[»]
    1Q7YX-ray3.20X1-154[»]
    1Q81X-ray2.95X1-154[»]
    1Q82X-ray2.98X1-154[»]
    1Q86X-ray3.00X1-154[»]
    1QVFX-ray3.10V1-154[»]
    1QVGX-ray2.90V1-154[»]
    1S72X-ray2.40W1-154[»]
    1VQ4X-ray2.70W1-154[»]
    1VQ5X-ray2.60W1-154[»]
    1VQ6X-ray2.70W1-154[»]
    1VQ7X-ray2.50W1-154[»]
    1VQ8X-ray2.20W1-154[»]
    1VQ9X-ray2.40W1-154[»]
    1VQKX-ray2.30W1-154[»]
    1VQLX-ray2.30W1-154[»]
    1VQMX-ray2.30W1-154[»]
    1VQNX-ray2.40W1-154[»]
    1VQOX-ray2.20W1-154[»]
    1VQPX-ray2.25W1-154[»]
    1W2BX-ray3.50V1-154[»]
    1YHQX-ray2.40W1-154[»]
    1YI2X-ray2.65W1-154[»]
    1YIJX-ray2.60W1-154[»]
    1YITX-ray2.80W1-154[»]
    1YJ9X-ray2.90W1-154[»]
    1YJNX-ray3.00W1-154[»]
    1YJWX-ray2.90W1-154[»]
    2OTJX-ray2.90W1-154[»]
    2OTLX-ray2.70W1-154[»]
    2QA4X-ray3.00W1-154[»]
    2QEXX-ray2.90W1-154[»]
    3CC2X-ray2.40W1-154[»]
    3CC4X-ray2.70W1-154[»]
    3CC7X-ray2.70W1-154[»]
    3CCEX-ray2.75W1-154[»]
    3CCJX-ray2.70W1-154[»]
    3CCLX-ray2.90W1-154[»]
    3CCMX-ray2.55W1-154[»]
    3CCQX-ray2.90W1-154[»]
    3CCRX-ray3.00W1-154[»]
    3CCSX-ray2.95W1-154[»]
    3CCUX-ray2.80W1-154[»]
    3CCVX-ray2.90W1-154[»]
    3CD6X-ray2.75W1-154[»]
    3CMAX-ray2.80W1-154[»]
    3CMEX-ray2.95W1-154[»]
    3CPWX-ray2.70V1-154[»]
    3CXCX-ray3.00V1-154[»]
    3G4SX-ray3.20W1-154[»]
    3G6EX-ray2.70W1-154[»]
    3G71X-ray2.85W1-154[»]
    3I55X-ray3.11W1-154[»]
    3I56X-ray2.90W1-154[»]
    3OW2X-ray2.70V1-154[»]
    4ADXelectron microscopy6.60W1-154[»]
    4HUBX-ray2.40W1-154[»]
    ProteinModelPortaliP14121.
    SMRiP14121. Positions 1-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14121.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L30P family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1841.
    HOGENOMiHOG000170918.
    KOiK02907.
    OMAiAIEMESA.

    Family and domain databases

    Gene3Di1.10.15.30. 1 hit.
    3.30.1390.20. 2 hits.
    HAMAPiMF_01371_A. Ribosomal_L30_A.
    InterProiIPR005997. Ribosomal_L30_arc.
    IPR023106. Ribosomal_L30_central_dom_arc.
    IPR018038. Ribosomal_L30_CS.
    IPR016082. Ribosomal_L30_ferredoxin-like.
    [Graphical view]
    PfamiPF00327. Ribosomal_L30. 1 hit.
    [Graphical view]
    SUPFAMiSSF55129. SSF55129. 1 hit.
    TIGRFAMsiTIGR01309. L30P_arch. 1 hit.
    PROSITEiPS00634. RIBOSOMAL_L30. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14121-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHALVQLRGE VNMHTDIQDT LEMLNIHHVN HCTLVPETDA YRGMVAKVND    50
    FVAFGEPSQE TLETVLATRA EPLEGDADVD DEWVAEHTDY DDISGLAFAL 100
    LSEETTLREQ GLSPTLRLHP PRGGHDGVKH PVKEGGQLGK HDTEGIDDLL 150
    EAMR 154
    Length:154
    Mass (Da):17,042
    Last modified:August 1, 1992 - v2
    Checksum:iED673F036E974C14
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831W → L AA sequence (PubMed:2591382)Curated
    Sequence conflicti148 – 1481Missing AA sequence (PubMed:2591382)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58395 Genomic DNA. Translation: CAA41292.1.
    AY596297 Genomic DNA. Translation: AAV46509.1.
    PIRiS16543. R5HS30.
    RefSeqiYP_136215.1. NC_006396.1.

    Genome annotation databases

    EnsemblBacteriaiAAV46509; AAV46509; rrnAC1591.
    GeneIDi3127531.
    KEGGihma:rrnAC1591.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58395 Genomic DNA. Translation: CAA41292.1 .
    AY596297 Genomic DNA. Translation: AAV46509.1 .
    PIRi S16543. R5HS30.
    RefSeqi YP_136215.1. 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 T 1-154 [» ]
    1JJ2 X-ray 2.40 V 1-154 [» ]
    1K73 X-ray 3.01 X 1-154 [» ]
    1K8A X-ray 3.00 X 1-154 [» ]
    1K9M X-ray 3.00 X 1-154 [» ]
    1KC8 X-ray 3.01 X 1-154 [» ]
    1KD1 X-ray 3.00 X 1-154 [» ]
    1KQS X-ray 3.10 V 1-154 [» ]
    1M1K X-ray 3.20 X 1-154 [» ]
    1M90 X-ray 2.80 X 1-154 [» ]
    1N8R X-ray 3.00 X 1-154 [» ]
    1NJI X-ray 3.00 X 1-154 [» ]
    1Q7Y X-ray 3.20 X 1-154 [» ]
    1Q81 X-ray 2.95 X 1-154 [» ]
    1Q82 X-ray 2.98 X 1-154 [» ]
    1Q86 X-ray 3.00 X 1-154 [» ]
    1QVF X-ray 3.10 V 1-154 [» ]
    1QVG X-ray 2.90 V 1-154 [» ]
    1S72 X-ray 2.40 W 1-154 [» ]
    1VQ4 X-ray 2.70 W 1-154 [» ]
    1VQ5 X-ray 2.60 W 1-154 [» ]
    1VQ6 X-ray 2.70 W 1-154 [» ]
    1VQ7 X-ray 2.50 W 1-154 [» ]
    1VQ8 X-ray 2.20 W 1-154 [» ]
    1VQ9 X-ray 2.40 W 1-154 [» ]
    1VQK X-ray 2.30 W 1-154 [» ]
    1VQL X-ray 2.30 W 1-154 [» ]
    1VQM X-ray 2.30 W 1-154 [» ]
    1VQN X-ray 2.40 W 1-154 [» ]
    1VQO X-ray 2.20 W 1-154 [» ]
    1VQP X-ray 2.25 W 1-154 [» ]
    1W2B X-ray 3.50 V 1-154 [» ]
    1YHQ X-ray 2.40 W 1-154 [» ]
    1YI2 X-ray 2.65 W 1-154 [» ]
    1YIJ X-ray 2.60 W 1-154 [» ]
    1YIT X-ray 2.80 W 1-154 [» ]
    1YJ9 X-ray 2.90 W 1-154 [» ]
    1YJN X-ray 3.00 W 1-154 [» ]
    1YJW X-ray 2.90 W 1-154 [» ]
    2OTJ X-ray 2.90 W 1-154 [» ]
    2OTL X-ray 2.70 W 1-154 [» ]
    2QA4 X-ray 3.00 W 1-154 [» ]
    2QEX X-ray 2.90 W 1-154 [» ]
    3CC2 X-ray 2.40 W 1-154 [» ]
    3CC4 X-ray 2.70 W 1-154 [» ]
    3CC7 X-ray 2.70 W 1-154 [» ]
    3CCE X-ray 2.75 W 1-154 [» ]
    3CCJ X-ray 2.70 W 1-154 [» ]
    3CCL X-ray 2.90 W 1-154 [» ]
    3CCM X-ray 2.55 W 1-154 [» ]
    3CCQ X-ray 2.90 W 1-154 [» ]
    3CCR X-ray 3.00 W 1-154 [» ]
    3CCS X-ray 2.95 W 1-154 [» ]
    3CCU X-ray 2.80 W 1-154 [» ]
    3CCV X-ray 2.90 W 1-154 [» ]
    3CD6 X-ray 2.75 W 1-154 [» ]
    3CMA X-ray 2.80 W 1-154 [» ]
    3CME X-ray 2.95 W 1-154 [» ]
    3CPW X-ray 2.70 V 1-154 [» ]
    3CXC X-ray 3.00 V 1-154 [» ]
    3G4S X-ray 3.20 W 1-154 [» ]
    3G6E X-ray 2.70 W 1-154 [» ]
    3G71 X-ray 2.85 W 1-154 [» ]
    3I55 X-ray 3.11 W 1-154 [» ]
    3I56 X-ray 2.90 W 1-154 [» ]
    3OW2 X-ray 2.70 V 1-154 [» ]
    4ADX electron microscopy 6.60 W 1-154 [» ]
    4HUB X-ray 2.40 W 1-154 [» ]
    ProteinModelPortali P14121.
    SMRi P14121. Positions 1-154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272569.rrnAC1591.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV46509 ; AAV46509 ; rrnAC1591 .
    GeneIDi 3127531.
    KEGGi hma:rrnAC1591.

    Phylogenomic databases

    eggNOGi COG1841.
    HOGENOMi HOG000170918.
    KOi K02907.
    OMAi AIEMESA.

    Enzyme and pathway databases

    BioCyci HMAR272569:GJDH-1447-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P14121.

    Family and domain databases

    Gene3Di 1.10.15.30. 1 hit.
    3.30.1390.20. 2 hits.
    HAMAPi MF_01371_A. Ribosomal_L30_A.
    InterProi IPR005997. Ribosomal_L30_arc.
    IPR023106. Ribosomal_L30_central_dom_arc.
    IPR018038. Ribosomal_L30_CS.
    IPR016082. Ribosomal_L30_ferredoxin-like.
    [Graphical view ]
    Pfami PF00327. Ribosomal_L30. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55129. SSF55129. 1 hit.
    TIGRFAMsi TIGR01309. L30P_arch. 1 hit.
    PROSITEi PS00634. RIBOSOMAL_L30. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins."
      Hatakeyama T., Kaufmann F., Schroeter B., Hatakeyama T.
      Eur. J. Biochem. 185:685-693(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Organization and nucleotide sequence of ten ribosomal protein genes from the region equivalent to the spectinomycin operon in the archaebacterium Halobacterium marismortui."
      Scholzen T., Arndt E.
      Mol. Gen. Genet. 228:70-80(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    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 1-30.
    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 nameiRL30_HALMA
    AccessioniPrimary (citable) accession number: P14121
    Secondary accession number(s): Q5V1U3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 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