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P60618 (RL15E_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L15e
Alternative name(s):
50S ribosomal protein LC12
Gene names
Name:rpl15e
Ordered Locus Names:rrnAC2065
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Part of the 50S ribosomal subunit. Interacts with protein L7Ae and weakly with L44e. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Sequence similarities

Belongs to the ribosomal protein L15e family.

Ontologies

Keywords
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 19619550S ribosomal protein L15e HAMAP-Rule MF_00256
PRO_0000127570

Experimental info

Sequence conflict131W → T AA sequence Ref.2

Secondary structure

..................................... 196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60618 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 502449E0A6BC23BB

FASTA19622,355
        10         20         30         40         50         60 
MARSAYSYIR DAWKNPGDGQ LAELQWQRQQ EWRNEGAVER IERPTRLDKA RSQGYKAKQG 

        70         80         90        100        110        120 
VIVARVSVRK GSARKRRHKA GRRSKRQGVT RITRRKDIQR VAEERASRTF PNLRVLNSYS 

       130        140        150        160        170        180 
VGQDGRQKWH EVILIDPNHP AIQNDDDLSW ICADDQADRV FRGLTGAGRR NRGLSGKGKG 

       190 
SEKTRPSLRS NGGKGK 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[2]"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 2-21.
[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]"Structural insights into peptide bond formation."
Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.
Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY596297 Genomic DNA. Translation: AAV46920.1.
PIRH28949.
RefSeqYP_136626.1. NC_006396.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40I37-194[»]
1JJ2X-ray2.40L2-194[»]
1K73X-ray3.01N2-194[»]
1K8AX-ray3.00N2-194[»]
1K9MX-ray3.00N2-194[»]
1KC8X-ray3.01N2-194[»]
1KD1X-ray3.00N2-194[»]
1KQSX-ray3.10L2-194[»]
1M1KX-ray3.20N2-194[»]
1M90X-ray2.80N2-194[»]
1N8RX-ray3.00N2-194[»]
1NJIX-ray3.00N2-194[»]
1Q7YX-ray3.20N2-194[»]
1Q81X-ray2.95N2-194[»]
1Q82X-ray2.98N2-194[»]
1Q86X-ray3.00N2-194[»]
1QVFX-ray3.10L2-194[»]
1QVGX-ray2.90L2-194[»]
1S72X-ray2.40M2-194[»]
1VQ4X-ray2.70M2-194[»]
1VQ5X-ray2.60M2-194[»]
1VQ6X-ray2.70M2-194[»]
1VQ7X-ray2.50M2-194[»]
1VQ8X-ray2.20M2-194[»]
1VQ9X-ray2.40M1-194[»]
1VQKX-ray2.30M1-194[»]
1VQLX-ray2.30M1-194[»]
1VQMX-ray2.30M1-194[»]
1VQNX-ray2.40M2-194[»]
1VQOX-ray2.20M1-194[»]
1VQPX-ray2.25M1-194[»]
1W2BX-ray3.50L2-194[»]
1YHQX-ray2.40M2-195[»]
1YI2X-ray2.65M1-195[»]
1YIJX-ray2.60M1-195[»]
1YITX-ray2.80M1-195[»]
1YJ9X-ray2.90M1-195[»]
1YJNX-ray3.00M1-195[»]
1YJWX-ray2.90M1-195[»]
2OTJX-ray2.90M2-194[»]
2OTLX-ray2.70M2-194[»]
2QA4X-ray3.00M1-194[»]
2QEXX-ray2.90M1-194[»]
3CC2X-ray2.40M1-196[»]
3CC4X-ray2.70M1-196[»]
3CC7X-ray2.70M1-196[»]
3CCEX-ray2.75M1-196[»]
3CCJX-ray2.70M1-196[»]
3CCLX-ray2.90M1-196[»]
3CCMX-ray2.55M1-196[»]
3CCQX-ray2.90M1-196[»]
3CCRX-ray3.00M1-196[»]
3CCSX-ray2.95M1-196[»]
3CCUX-ray2.80M1-196[»]
3CCVX-ray2.90M1-196[»]
3CD6X-ray2.75M1-196[»]
3CMAX-ray2.80M1-196[»]
3CMEX-ray2.95M1-196[»]
3CPWX-ray2.70L1-196[»]
3G4SX-ray3.20M2-195[»]
3G6EX-ray2.70M2-195[»]
3G71X-ray2.85M2-195[»]
3I55X-ray3.11M2-194[»]
3I56X-ray2.90M2-194[»]
4ADXelectron microscopy6.60M1-196[»]
4HUBX-ray2.40M1-196[»]
ProteinModelPortalP60618.
SMRP60618. Positions 2-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC2065.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46920; AAV46920; rrnAC2065.
GeneID3129041.
KEGGhma:rrnAC2065.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1632.
HOGENOMHOG000229584.
KOK02877.
OMASHIKDAW.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1864-MONOMER.

Family and domain databases

Gene3D3.40.1120.10. 1 hit.
HAMAPMF_00256. Ribosomal_L15e.
InterProIPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020926. Ribosomal_L15e_arc.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
[Graphical view]
PANTHERPTHR11847. PTHR11847. 1 hit.
PfamPF00827. Ribosomal_L15e. 1 hit.
[Graphical view]
SUPFAMSSF54189. SSF54189. 1 hit.
PROSITEPS01194. RIBOSOMAL_L15E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60618.

Entry information

Entry nameRL15E_HALMA
AccessionPrimary (citable) accession number: P60618
Secondary accession number(s): P12740, Q5V0N3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 82 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references