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P12733

- RL18E_HALMA

UniProt

P12733 - RL18E_HALMA

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Protein

50S ribosomal protein L18e

Gene
rpl18e, rrnAC0064
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

Functioni

Stabilizes the tertiary rRNA structure within the 23S rRNA domain (domain II) to which it binds.UniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-60-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L18e
Alternative name(s):
Hl29
L19
Gene namesi
Name:rpl18e
Ordered Locus Names:rrnAC0064
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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 11611550S ribosomal protein L18eUniRule annotationPRO_0000132787Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts weakly with proteins L4 and L15. Has been cross-linked to L4.9 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC0064.

Structurei

Secondary structure

1
116
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2116
Helixi25 – 3410
Helixi38 – 403
Beta strandi41 – 455
Helixi46 – 527
Beta strandi57 – 6610
Beta strandi76 – 827
Helixi84 – 9310
Beta strandi94 – 985
Helixi99 – 1057
Beta strandi111 – 1144

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40L2-116[»]
1JJ2X-ray2.40N2-116[»]
1K73X-ray3.01P2-116[»]
1K8AX-ray3.00P2-116[»]
1K9MX-ray3.00P2-116[»]
1KC8X-ray3.01P2-116[»]
1KD1X-ray3.00P2-116[»]
1KQSX-ray3.10N2-116[»]
1M1KX-ray3.20P2-116[»]
1M90X-ray2.80P2-116[»]
1N8RX-ray3.00P2-116[»]
1NJIX-ray3.00P2-116[»]
1Q7YX-ray3.20P2-116[»]
1Q81X-ray2.95P2-116[»]
1Q82X-ray2.98P2-116[»]
1Q86X-ray3.00P2-116[»]
1QVFX-ray3.10N2-116[»]
1QVGX-ray2.90N2-116[»]
1S72X-ray2.40O1-116[»]
1VQ4X-ray2.70O1-116[»]
1VQ5X-ray2.60O1-116[»]
1VQ6X-ray2.70O1-116[»]
1VQ7X-ray2.50O1-116[»]
1VQ8X-ray2.20O1-116[»]
1VQ9X-ray2.40O1-116[»]
1VQKX-ray2.30O1-116[»]
1VQLX-ray2.30O1-116[»]
1VQMX-ray2.30O1-116[»]
1VQNX-ray2.40O1-116[»]
1VQOX-ray2.20O1-116[»]
1VQPX-ray2.25O1-116[»]
1W2BX-ray3.50N2-116[»]
1YHQX-ray2.40O1-116[»]
1YI2X-ray2.65O1-116[»]
1YIJX-ray2.60O1-116[»]
1YITX-ray2.80O1-116[»]
1YJ9X-ray2.90O1-116[»]
1YJNX-ray3.00O1-116[»]
1YJWX-ray2.90O1-116[»]
2OTJX-ray2.90O1-116[»]
2OTLX-ray2.70O1-116[»]
2QA4X-ray3.00O1-116[»]
2QEXX-ray2.90O1-116[»]
3CC2X-ray2.40O1-116[»]
3CC4X-ray2.70O1-116[»]
3CC7X-ray2.70O1-116[»]
3CCEX-ray2.75O1-116[»]
3CCJX-ray2.70O1-116[»]
3CCLX-ray2.90O1-116[»]
3CCMX-ray2.55O1-116[»]
3CCQX-ray2.90O1-116[»]
3CCRX-ray3.00O1-116[»]
3CCSX-ray2.95O1-116[»]
3CCUX-ray2.80O1-116[»]
3CCVX-ray2.90O1-116[»]
3CD6X-ray2.75O1-116[»]
3CMAX-ray2.80O1-116[»]
3CMEX-ray2.95O1-116[»]
3CPWX-ray2.70N1-116[»]
3CXCX-ray3.00N2-116[»]
3G4SX-ray3.20O2-116[»]
3G6EX-ray2.70O2-116[»]
3G71X-ray2.85O2-116[»]
3I55X-ray3.11O1-116[»]
3I56X-ray2.90O1-116[»]
3OW2X-ray2.70N2-116[»]
4ADXelectron microscopy6.60O1-116[»]
4HUBX-ray2.40O1-116[»]
ProteinModelPortaliP12733.
SMRiP12733. Positions 2-116.

Miscellaneous databases

EvolutionaryTraceiP12733.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1727.
HOGENOMiHOG000225300.
KOiK02883.
OMAiASCHAHG.

Family and domain databases

HAMAPiMF_00329. Ribosomal_L18e.
InterProiIPR001196. Ribosomal_L15_CS.
IPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR022947. Ribosomal_L18e_arc.
IPR021132. Ribosomal_L18e_CS.
[Graphical view]
PANTHERiPTHR10934. PTHR10934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12733-1 [UniParc]FASTAAdd to Basket

« Hide

MSKTNPRLSS LIADLKSAAR SSGGAVWGDV AERLEKPRRT HAEVNLGRIE    50
RYAQEDETVV VPGKVLGSGV LQKDVTVAAV DFSGTAETKI DQVGEAVSLE 100
QAIENNPEGS HVRVIR 116
Length:116
Mass (Da):12,422
Last modified:January 23, 2007 - v2
Checksum:iBFACD702AE94474D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M76567 Genomic DNA. Translation: AAA73096.1.
AY596297 Genomic DNA. Translation: AAV45144.1.
M87833 Genomic DNA. Translation: AAA73213.1.
PIRiA41715. R5HSH9.
RefSeqiYP_134850.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV45144; AAV45144; rrnAC0064.
GeneIDi3130533.
KEGGihma:rrnAC0064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M76567 Genomic DNA. Translation: AAA73096.1 .
AY596297 Genomic DNA. Translation: AAV45144.1 .
M87833 Genomic DNA. Translation: AAA73213.1 .
PIRi A41715. R5HSH9.
RefSeqi YP_134850.1. 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 L 2-116 [» ]
1JJ2 X-ray 2.40 N 2-116 [» ]
1K73 X-ray 3.01 P 2-116 [» ]
1K8A X-ray 3.00 P 2-116 [» ]
1K9M X-ray 3.00 P 2-116 [» ]
1KC8 X-ray 3.01 P 2-116 [» ]
1KD1 X-ray 3.00 P 2-116 [» ]
1KQS X-ray 3.10 N 2-116 [» ]
1M1K X-ray 3.20 P 2-116 [» ]
1M90 X-ray 2.80 P 2-116 [» ]
1N8R X-ray 3.00 P 2-116 [» ]
1NJI X-ray 3.00 P 2-116 [» ]
1Q7Y X-ray 3.20 P 2-116 [» ]
1Q81 X-ray 2.95 P 2-116 [» ]
1Q82 X-ray 2.98 P 2-116 [» ]
1Q86 X-ray 3.00 P 2-116 [» ]
1QVF X-ray 3.10 N 2-116 [» ]
1QVG X-ray 2.90 N 2-116 [» ]
1S72 X-ray 2.40 O 1-116 [» ]
1VQ4 X-ray 2.70 O 1-116 [» ]
1VQ5 X-ray 2.60 O 1-116 [» ]
1VQ6 X-ray 2.70 O 1-116 [» ]
1VQ7 X-ray 2.50 O 1-116 [» ]
1VQ8 X-ray 2.20 O 1-116 [» ]
1VQ9 X-ray 2.40 O 1-116 [» ]
1VQK X-ray 2.30 O 1-116 [» ]
1VQL X-ray 2.30 O 1-116 [» ]
1VQM X-ray 2.30 O 1-116 [» ]
1VQN X-ray 2.40 O 1-116 [» ]
1VQO X-ray 2.20 O 1-116 [» ]
1VQP X-ray 2.25 O 1-116 [» ]
1W2B X-ray 3.50 N 2-116 [» ]
1YHQ X-ray 2.40 O 1-116 [» ]
1YI2 X-ray 2.65 O 1-116 [» ]
1YIJ X-ray 2.60 O 1-116 [» ]
1YIT X-ray 2.80 O 1-116 [» ]
1YJ9 X-ray 2.90 O 1-116 [» ]
1YJN X-ray 3.00 O 1-116 [» ]
1YJW X-ray 2.90 O 1-116 [» ]
2OTJ X-ray 2.90 O 1-116 [» ]
2OTL X-ray 2.70 O 1-116 [» ]
2QA4 X-ray 3.00 O 1-116 [» ]
2QEX X-ray 2.90 O 1-116 [» ]
3CC2 X-ray 2.40 O 1-116 [» ]
3CC4 X-ray 2.70 O 1-116 [» ]
3CC7 X-ray 2.70 O 1-116 [» ]
3CCE X-ray 2.75 O 1-116 [» ]
3CCJ X-ray 2.70 O 1-116 [» ]
3CCL X-ray 2.90 O 1-116 [» ]
3CCM X-ray 2.55 O 1-116 [» ]
3CCQ X-ray 2.90 O 1-116 [» ]
3CCR X-ray 3.00 O 1-116 [» ]
3CCS X-ray 2.95 O 1-116 [» ]
3CCU X-ray 2.80 O 1-116 [» ]
3CCV X-ray 2.90 O 1-116 [» ]
3CD6 X-ray 2.75 O 1-116 [» ]
3CMA X-ray 2.80 O 1-116 [» ]
3CME X-ray 2.95 O 1-116 [» ]
3CPW X-ray 2.70 N 1-116 [» ]
3CXC X-ray 3.00 N 2-116 [» ]
3G4S X-ray 3.20 O 2-116 [» ]
3G6E X-ray 2.70 O 2-116 [» ]
3G71 X-ray 2.85 O 2-116 [» ]
3I55 X-ray 3.11 O 1-116 [» ]
3I56 X-ray 2.90 O 1-116 [» ]
3OW2 X-ray 2.70 N 2-116 [» ]
4ADX electron microscopy 6.60 O 1-116 [» ]
4HUB X-ray 2.40 O 1-116 [» ]
ProteinModelPortali P12733.
SMRi P12733. Positions 2-116.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272569.rrnAC0064.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV45144 ; AAV45144 ; rrnAC0064 .
GeneIDi 3130533.
KEGGi hma:rrnAC0064.

Phylogenomic databases

eggNOGi COG1727.
HOGENOMi HOG000225300.
KOi K02883.
OMAi ASCHAHG.

Enzyme and pathway databases

BioCyci HMAR272569:GJDH-60-MONOMER.

Miscellaneous databases

EvolutionaryTracei P12733.

Family and domain databases

HAMAPi MF_00329. Ribosomal_L18e.
InterProi IPR001196. Ribosomal_L15_CS.
IPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR022947. Ribosomal_L18e_arc.
IPR021132. Ribosomal_L18e_CS.
[Graphical view ]
PANTHERi PTHR10934. PTHR10934. 1 hit.
Pfami PF00828. Ribosomal_L18e. 1 hit.
[Graphical view ]
SUPFAMi SSF52080. SSF52080. 1 hit.
PROSITEi PS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Halobacterial S9 operon. Three ribosomal protein genes are cotranscribed with genes encoding a tRNA(Leu), the enolase, and a putative membrane protein in the archaebacterium Haloarcula (Halobacterium) marismortui."
    Kroemer W.J., Arndt E.
    J. Biol. Chem. 266:24573-24579(1991) [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. "Complete amino acid sequences of the ribosomal proteins L25, L29 and L31 from the archaebacterium Halobacterium marismortui."
    Hatakeyama T., Kimura M.
    Eur. J. Biochem. 172:703-711(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-116.
  4. "The alpha-operon equivalent genome region in the extreme halophilic archaebacterium Haloarcula (Halobacterium) marismortui."
    Scholzen T., Arndt E.
    J. Biol. Chem. 267:12123-12130(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
  5. "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 2-24.
  6. "Localization of proteins HL29 and HL31 from Haloarcula marismortui within the 50 S ribosomal subunit by chemical crosslinking."
    Bergmann U., Wittmann-Liebold B.
    J. Mol. Biol. 232:693-700(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 4-27; 37-39 AND 65-82, CROSS-LINKING TO L4.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  13. "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.
  14. "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.
  15. "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 nameiRL18E_HALMA
AccessioniPrimary (citable) accession number: P12733
Secondary accession number(s): Q5V5Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 113 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

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

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