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Protein

50S ribosomal protein L39e

Gene

rpl39e

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the 23S rRNA. Forms part of the polypeptide exit tunnel.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-KW
  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

BioCyciHMAR272569:GJDH-2791-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L39e
Alternative name(s):
Hl39e
Hl46e
Gene namesi
Name:rpl39e
Ordered Locus Names:rrnAC3112
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
ProteomesiUP000001169 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 504950S ribosomal protein L39ePRO_0000127047Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts weakly with protein L23.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC3112.

Structurei

Secondary structure

1
50
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813Combined sources
Helixi24 – 296Combined sources
Turni30 – 323Combined sources
Turni43 – 453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40Y2-50[»]
1JJ2X-ray2.4012-49[»]
1K73X-ray3.0132-49[»]
1K8AX-ray3.0032-49[»]
1K9MX-ray3.0032-49[»]
1KC8X-ray3.0132-49[»]
1KD1X-ray3.0032-49[»]
1KQSX-ray3.1012-49[»]
1M1KX-ray3.2032-49[»]
1M90X-ray2.8032-49[»]
1N8RX-ray3.0032-49[»]
1NJIX-ray3.0032-49[»]
1Q7YX-ray3.2032-49[»]
1Q81X-ray2.9532-49[»]
1Q82X-ray2.9832-49[»]
1Q86X-ray3.0032-49[»]
1QVFX-ray3.1012-49[»]
1QVGX-ray2.9012-49[»]
1S72X-ray2.4021-50[»]
1VQ4X-ray2.7021-50[»]
1VQ5X-ray2.6021-50[»]
1VQ6X-ray2.7021-50[»]
1VQ7X-ray2.5021-50[»]
1VQ8X-ray2.2021-50[»]
1VQ9X-ray2.4021-50[»]
1VQKX-ray2.3021-50[»]
1VQLX-ray2.3021-50[»]
1VQMX-ray2.3021-50[»]
1VQNX-ray2.4021-50[»]
1VQOX-ray2.2021-50[»]
1VQPX-ray2.2521-50[»]
1W2BX-ray3.5012-49[»]
1YHQX-ray2.4021-50[»]
1YI2X-ray2.6521-50[»]
1YIJX-ray2.6021-50[»]
1YITX-ray2.8021-50[»]
1YJ9X-ray2.9021-50[»]
1YJNX-ray3.0021-50[»]
1YJWX-ray2.9021-50[»]
2OTJX-ray2.9021-50[»]
2OTLX-ray2.7021-50[»]
2QA4X-ray3.0021-50[»]
2QEXX-ray2.9021-50[»]
3CC2X-ray2.4021-50[»]
3CC4X-ray2.7021-50[»]
3CC7X-ray2.7021-50[»]
3CCEX-ray2.7521-50[»]
3CCJX-ray2.7021-50[»]
3CCLX-ray2.9021-50[»]
3CCMX-ray2.5521-50[»]
3CCQX-ray2.9021-50[»]
3CCRX-ray3.0021-50[»]
3CCSX-ray2.9521-50[»]
3CCUX-ray2.8021-50[»]
3CCVX-ray2.9021-50[»]
3CD6X-ray2.7521-50[»]
3CMAX-ray2.8021-50[»]
3CMEX-ray2.9521-50[»]
3CPWX-ray2.7011-50[»]
3CXCX-ray3.0012-50[»]
3G4SX-ray3.2021-50[»]
3G6EX-ray2.7021-50[»]
3G71X-ray2.8521-50[»]
3I55X-ray3.1121-50[»]
3I56X-ray2.9021-50[»]
3OW2X-ray2.7012-50[»]
4ADXelectron microscopy6.6021-50[»]
4V9FX-ray2.4021-50[»]
SMRiP22452. Positions 2-50.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22452.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L39e family.Curated

Phylogenomic databases

eggNOGiCOG2167.
HOGENOMiHOG000230627.
KOiK02924.
OMAiPAWVIMK.

Family and domain databases

Gene3Di1.10.1620.10. 1 hit.
HAMAPiMF_00629. Ribosomal_L39e.
InterProiIPR000077. Ribosomal_L39.
IPR020083. Ribosomal_L39_CS.
IPR023626. Ribosomal_L39e_dom.
[Graphical view]
PANTHERiPTHR19970. PTHR19970. 1 hit.
PfamiPF00832. Ribosomal_L39. 1 hit.
[Graphical view]
SUPFAMiSSF48662. SSF48662. 1 hit.
PROSITEiPS00051. RIBOSOMAL_L39E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P22452-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKSKATKK RLAKLDNQNS RVPAWVMLKT DREVQRNHKR RHWRRNDTDE
Length:50
Mass (Da):6,115
Last modified:January 22, 2007 - v2
Checksum:i4999D410AB7B331A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55007 Genomic DNA. Translation: CAA38750.1.
AY596297 Genomic DNA. Translation: AAV47823.1.
PIRiS13066. R6HS39.
RefSeqiYP_137529.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV47823; AAV47823; rrnAC3112.
GeneIDi3130549.
KEGGihma:rrnAC3112.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55007 Genomic DNA. Translation: CAA38750.1.
AY596297 Genomic DNA. Translation: AAV47823.1.
PIRiS13066. R6HS39.
RefSeqiYP_137529.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40Y2-50[»]
1JJ2X-ray2.4012-49[»]
1K73X-ray3.0132-49[»]
1K8AX-ray3.0032-49[»]
1K9MX-ray3.0032-49[»]
1KC8X-ray3.0132-49[»]
1KD1X-ray3.0032-49[»]
1KQSX-ray3.1012-49[»]
1M1KX-ray3.2032-49[»]
1M90X-ray2.8032-49[»]
1N8RX-ray3.0032-49[»]
1NJIX-ray3.0032-49[»]
1Q7YX-ray3.2032-49[»]
1Q81X-ray2.9532-49[»]
1Q82X-ray2.9832-49[»]
1Q86X-ray3.0032-49[»]
1QVFX-ray3.1012-49[»]
1QVGX-ray2.9012-49[»]
1S72X-ray2.4021-50[»]
1VQ4X-ray2.7021-50[»]
1VQ5X-ray2.6021-50[»]
1VQ6X-ray2.7021-50[»]
1VQ7X-ray2.5021-50[»]
1VQ8X-ray2.2021-50[»]
1VQ9X-ray2.4021-50[»]
1VQKX-ray2.3021-50[»]
1VQLX-ray2.3021-50[»]
1VQMX-ray2.3021-50[»]
1VQNX-ray2.4021-50[»]
1VQOX-ray2.2021-50[»]
1VQPX-ray2.2521-50[»]
1W2BX-ray3.5012-49[»]
1YHQX-ray2.4021-50[»]
1YI2X-ray2.6521-50[»]
1YIJX-ray2.6021-50[»]
1YITX-ray2.8021-50[»]
1YJ9X-ray2.9021-50[»]
1YJNX-ray3.0021-50[»]
1YJWX-ray2.9021-50[»]
2OTJX-ray2.9021-50[»]
2OTLX-ray2.7021-50[»]
2QA4X-ray3.0021-50[»]
2QEXX-ray2.9021-50[»]
3CC2X-ray2.4021-50[»]
3CC4X-ray2.7021-50[»]
3CC7X-ray2.7021-50[»]
3CCEX-ray2.7521-50[»]
3CCJX-ray2.7021-50[»]
3CCLX-ray2.9021-50[»]
3CCMX-ray2.5521-50[»]
3CCQX-ray2.9021-50[»]
3CCRX-ray3.0021-50[»]
3CCSX-ray2.9521-50[»]
3CCUX-ray2.8021-50[»]
3CCVX-ray2.9021-50[»]
3CD6X-ray2.7521-50[»]
3CMAX-ray2.8021-50[»]
3CMEX-ray2.9521-50[»]
3CPWX-ray2.7011-50[»]
3CXCX-ray3.0012-50[»]
3G4SX-ray3.2021-50[»]
3G6EX-ray2.7021-50[»]
3G71X-ray2.8521-50[»]
3I55X-ray3.1121-50[»]
3I56X-ray2.9021-50[»]
3OW2X-ray2.7012-50[»]
4ADXelectron microscopy6.6021-50[»]
4V9FX-ray2.4021-50[»]
SMRiP22452. Positions 2-50.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC3112.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV47823; AAV47823; rrnAC3112.
GeneIDi3130549.
KEGGihma:rrnAC3112.

Phylogenomic databases

eggNOGiCOG2167.
HOGENOMiHOG000230627.
KOiK02924.
OMAiPAWVIMK.

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-2791-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP22452.

Family and domain databases

Gene3Di1.10.1620.10. 1 hit.
HAMAPiMF_00629. Ribosomal_L39e.
InterProiIPR000077. Ribosomal_L39.
IPR020083. Ribosomal_L39_CS.
IPR023626. Ribosomal_L39e_dom.
[Graphical view]
PANTHERiPTHR19970. PTHR19970. 1 hit.
PfamiPF00832. Ribosomal_L39. 1 hit.
[Graphical view]
SUPFAMiSSF48662. SSF48662. 1 hit.
PROSITEiPS00051. RIBOSOMAL_L39E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evidence for an additional archaebacterial gene cluster in Halobacterium marismortui encoding ribosomal proteins HL46e and HL30."
    Bergmann U., Arndt E.
    Biochim. Biophys. Acta 1050:56-60(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-50.
  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(1999) [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(1999) [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(2001) [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(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.
  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(2001) [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(2002) [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(2002) [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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.

Entry informationi

Entry nameiRL39_HALMA
AccessioniPrimary (citable) accession number: P22452
Secondary accession number(s): Q5UY30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1991
Last sequence update: January 22, 2007
Last modified: March 31, 2015
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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.