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Protein

50S ribosomal protein L24e

Gene

rpl24e

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the 23S rRNA.

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi7 – 71ZincCurated
Metal bindingi10 – 101ZincCurated
Metal bindingi33 – 331ZincCurated
Metal bindingi37 – 371ZincCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3731C4-typeCuratedAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, RNA-binding, rRNA-binding, Zinc

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-97-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L24e
Alternative name(s):
Hl21/Hl22
Gene namesi
Name:rpl24e
Ordered Locus Names:rrnAC0104
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

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 676650S ribosomal protein L24ePRO_0000136913Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L14.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC0104.

Structurei

Secondary structure

1
67
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 103Combined sources
Beta strandi20 – 234Combined sources
Beta strandi25 – 273Combined sources
Beta strandi29 – 335Combined sources
Helixi35 – 428Combined sources
Helixi47 – 493Combined sources
Beta strandi50 – 534Combined sources
Turni54 – 563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40R2-67[»]
1JJ2X-ray2.40T2-67[»]
1K73X-ray3.01V2-67[»]
1K8AX-ray3.00V2-67[»]
1K9MX-ray3.00V2-67[»]
1KC8X-ray3.01V2-67[»]
1KD1X-ray3.00V2-67[»]
1KQSX-ray3.10T2-67[»]
1M1KX-ray3.20V2-67[»]
1M90X-ray2.80V2-67[»]
1ML5electron microscopy14.00r2-67[»]
1N8RX-ray3.00V2-67[»]
1NJIX-ray3.00V2-67[»]
1Q7YX-ray3.20V2-67[»]
1Q81X-ray2.95V2-67[»]
1Q82X-ray2.98V2-67[»]
1Q86X-ray3.00V2-67[»]
1QVFX-ray3.10T2-67[»]
1QVGX-ray2.90T2-67[»]
1S72X-ray2.40U2-67[»]
1VQ4X-ray2.70U2-67[»]
1VQ5X-ray2.60U2-67[»]
1VQ6X-ray2.70U2-67[»]
1VQ7X-ray2.50U2-67[»]
1VQ8X-ray2.20U2-67[»]
1VQ9X-ray2.40U2-67[»]
1VQKX-ray2.30U2-67[»]
1VQLX-ray2.30U2-67[»]
1VQMX-ray2.30U2-67[»]
1VQNX-ray2.40U2-67[»]
1VQOX-ray2.20U2-67[»]
1VQPX-ray2.25U2-67[»]
1W2BX-ray3.50T2-67[»]
1YHQX-ray2.40U2-67[»]
1YI2X-ray2.65U2-67[»]
1YIJX-ray2.60U2-67[»]
1YITX-ray2.80U2-67[»]
1YJ9X-ray2.80U2-67[»]
1YJNX-ray3.00U2-67[»]
1YJWX-ray2.90U2-67[»]
2OTJX-ray2.90U2-67[»]
2OTLX-ray2.70U2-67[»]
2QA4X-ray3.00U1-67[»]
2QEXX-ray2.90U1-67[»]
3CC2X-ray2.40U1-67[»]
3CC4X-ray2.70U1-67[»]
3CC7X-ray2.70U1-67[»]
3CCEX-ray2.75U1-67[»]
3CCJX-ray2.70U1-67[»]
3CCLX-ray2.90U1-67[»]
3CCMX-ray2.55U1-67[»]
3CCQX-ray2.90U1-67[»]
3CCRX-ray3.00U1-67[»]
3CCSX-ray2.95U1-67[»]
3CCUX-ray2.80U1-67[»]
3CCVX-ray2.90U1-67[»]
3CD6X-ray2.75U1-67[»]
3CMAX-ray2.80U1-67[»]
3CMEX-ray2.95U1-67[»]
3CPWX-ray2.70T1-67[»]
3CXCX-ray3.00T2-67[»]
3G4SX-ray3.20U5-57[»]
3G6EX-ray2.70U5-57[»]
3G71X-ray2.85U5-57[»]
3I55X-ray3.11U2-67[»]
3I56X-ray2.90U2-67[»]
3OW2X-ray2.70T5-57[»]
4ADXelectron microscopy6.60U1-67[»]
4V42X-ray5.50BR2-67[»]
4V4RX-ray5.90T2-67[»]
4V4SX-ray6.76T2-67[»]
4V4TX-ray6.46T2-67[»]
4V9FX-ray2.40U1-67[»]
ProteinModelPortaliP14116.
SMRiP14116. Positions 5-57.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14116.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L24e family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3731C4-typeCuratedAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG2075.
HOGENOMiHOG000156057.
KOiK02896.

Family and domain databases

Gene3Di2.30.170.20. 1 hit.
HAMAPiMF_00773. Ribosomal_L24e.
InterProiIPR023438. Ribosomal_L24e.
IPR000988. Ribosomal_L24e-rel.
IPR023442. Ribosomal_L24e_CS.
IPR023441. Ribosomal_L24e_dom.
IPR011017. TRASH_dom.
[Graphical view]
PANTHERiPTHR10792. PTHR10792. 1 hit.
PfamiPF01246. Ribosomal_L24e. 1 hit.
[Graphical view]
SMARTiSM00746. TRASH. 1 hit.
[Graphical view]
PROSITEiPS01073. RIBOSOMAL_L24E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRTRECDYC GTDIEPGTGT MFVHKDGATT HFCSSKCENN ADLGREARNL
60
EWTDTARGEA GEAEDEA
Length:67
Mass (Da):7,356
Last modified:January 23, 2007 - v2
Checksum:iD4FCAE00935B7305
GO

Sequence cautioni

The sequence AAV45180.1 differs from that shown. Reason: Frameshift at position 67. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY596297 Genomic DNA. Translation: AAV45180.1. Frameshift.
PIRiS06846. R6HS21.
RefSeqiYP_134886.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV45180; AAV45180; rrnAC0104.
GeneIDi3130240.
KEGGihma:rrnAC0104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY596297 Genomic DNA. Translation: AAV45180.1. Frameshift.
PIRiS06846. R6HS21.
RefSeqiYP_134886.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40R2-67[»]
1JJ2X-ray2.40T2-67[»]
1K73X-ray3.01V2-67[»]
1K8AX-ray3.00V2-67[»]
1K9MX-ray3.00V2-67[»]
1KC8X-ray3.01V2-67[»]
1KD1X-ray3.00V2-67[»]
1KQSX-ray3.10T2-67[»]
1M1KX-ray3.20V2-67[»]
1M90X-ray2.80V2-67[»]
1ML5electron microscopy14.00r2-67[»]
1N8RX-ray3.00V2-67[»]
1NJIX-ray3.00V2-67[»]
1Q7YX-ray3.20V2-67[»]
1Q81X-ray2.95V2-67[»]
1Q82X-ray2.98V2-67[»]
1Q86X-ray3.00V2-67[»]
1QVFX-ray3.10T2-67[»]
1QVGX-ray2.90T2-67[»]
1S72X-ray2.40U2-67[»]
1VQ4X-ray2.70U2-67[»]
1VQ5X-ray2.60U2-67[»]
1VQ6X-ray2.70U2-67[»]
1VQ7X-ray2.50U2-67[»]
1VQ8X-ray2.20U2-67[»]
1VQ9X-ray2.40U2-67[»]
1VQKX-ray2.30U2-67[»]
1VQLX-ray2.30U2-67[»]
1VQMX-ray2.30U2-67[»]
1VQNX-ray2.40U2-67[»]
1VQOX-ray2.20U2-67[»]
1VQPX-ray2.25U2-67[»]
1W2BX-ray3.50T2-67[»]
1YHQX-ray2.40U2-67[»]
1YI2X-ray2.65U2-67[»]
1YIJX-ray2.60U2-67[»]
1YITX-ray2.80U2-67[»]
1YJ9X-ray2.80U2-67[»]
1YJNX-ray3.00U2-67[»]
1YJWX-ray2.90U2-67[»]
2OTJX-ray2.90U2-67[»]
2OTLX-ray2.70U2-67[»]
2QA4X-ray3.00U1-67[»]
2QEXX-ray2.90U1-67[»]
3CC2X-ray2.40U1-67[»]
3CC4X-ray2.70U1-67[»]
3CC7X-ray2.70U1-67[»]
3CCEX-ray2.75U1-67[»]
3CCJX-ray2.70U1-67[»]
3CCLX-ray2.90U1-67[»]
3CCMX-ray2.55U1-67[»]
3CCQX-ray2.90U1-67[»]
3CCRX-ray3.00U1-67[»]
3CCSX-ray2.95U1-67[»]
3CCUX-ray2.80U1-67[»]
3CCVX-ray2.90U1-67[»]
3CD6X-ray2.75U1-67[»]
3CMAX-ray2.80U1-67[»]
3CMEX-ray2.95U1-67[»]
3CPWX-ray2.70T1-67[»]
3CXCX-ray3.00T2-67[»]
3G4SX-ray3.20U5-57[»]
3G6EX-ray2.70U5-57[»]
3G71X-ray2.85U5-57[»]
3I55X-ray3.11U2-67[»]
3I56X-ray2.90U2-67[»]
3OW2X-ray2.70T5-57[»]
4ADXelectron microscopy6.60U1-67[»]
4V42X-ray5.50BR2-67[»]
4V4RX-ray5.90T2-67[»]
4V4SX-ray6.76T2-67[»]
4V4TX-ray6.46T2-67[»]
4V9FX-ray2.40U1-67[»]
ProteinModelPortaliP14116.
SMRiP14116. Positions 5-57.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC0104.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV45180; AAV45180; rrnAC0104.
GeneIDi3130240.
KEGGihma:rrnAC0104.

Phylogenomic databases

eggNOGiCOG2075.
HOGENOMiHOG000156057.
KOiK02896.

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-97-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14116.

Family and domain databases

Gene3Di2.30.170.20. 1 hit.
HAMAPiMF_00773. Ribosomal_L24e.
InterProiIPR023438. Ribosomal_L24e.
IPR000988. Ribosomal_L24e-rel.
IPR023442. Ribosomal_L24e_CS.
IPR023441. Ribosomal_L24e_dom.
IPR011017. TRASH_dom.
[Graphical view]
PANTHERiPTHR10792. PTHR10792. 1 hit.
PfamiPF01246. Ribosomal_L24e. 1 hit.
[Graphical view]
SMARTiSM00746. TRASH. 1 hit.
[Graphical view]
PROSITEiPS01073. RIBOSOMAL_L24E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  2. "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 OF 2-67.
  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 nameiRL24E_HALMA
AccessioniPrimary (citable) accession number: P14116
Secondary accession number(s): Q5V5M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 117 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.