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P12734 (RL21_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 108. 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 L21e
Alternative name(s):
Hl31
Gene names
Name:rpl21e
Ordered Locus Names:rrnAC0260
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 length96 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00369

Subunit structure

Part of the 50S ribosomal subunit. Interacts with protein L18 and binds the 5S rRNA. Has been cross-linked to L18. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the ribosomal protein L21e 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 – 969550S ribosomal protein L21e HAMAP-Rule MF_00369
PRO_0000149686

Secondary structure

...................... 96
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12734 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DE6DE036844EF1F2

FASTA9610,548
        10         20         30         40         50         60 
MPSSNGPLEG TRGKLKNKPR DRGTSPPQRA VEEFDDGEKV HLKIDPSVPN GRFHPRFDGQ 

        70         80         90 
TGTVEGKQGD AYKVDIVDGG KEKTIIVTAA HLRRQE 

« 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]"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 2-96.
[3]"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: CROSS-LINKING TO L18.
[4]"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.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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: AAV45317.1.
PIRR5HS31. S00370.
RefSeqYP_135023.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40N2-96[»]
1JJ2X-ray2.40P2-96[»]
1K73X-ray3.01R2-96[»]
1K8AX-ray3.00R2-96[»]
1K9MX-ray3.00R2-96[»]
1KC8X-ray3.01R2-96[»]
1KD1X-ray3.00R2-96[»]
1KQSX-ray3.10P2-96[»]
1M1KX-ray3.20R2-96[»]
1M90X-ray2.80R2-96[»]
1N8RX-ray3.00R2-96[»]
1NJIX-ray3.00R2-96[»]
1Q7YX-ray3.20R2-96[»]
1Q81X-ray2.95R2-96[»]
1Q82X-ray2.98R2-96[»]
1Q86X-ray3.00R2-96[»]
1QVFX-ray3.10P2-96[»]
1QVGX-ray2.90P2-96[»]
1S72X-ray2.40Q1-96[»]
1VQ4X-ray2.70Q1-96[»]
1VQ5X-ray2.60Q1-96[»]
1VQ6X-ray2.70Q1-96[»]
1VQ7X-ray2.50Q1-96[»]
1VQ8X-ray2.20Q1-96[»]
1VQ9X-ray2.40Q1-96[»]
1VQKX-ray2.30Q1-96[»]
1VQLX-ray2.30Q1-96[»]
1VQMX-ray2.30Q1-96[»]
1VQNX-ray2.40Q1-96[»]
1VQOX-ray2.20Q1-96[»]
1VQPX-ray2.25Q1-96[»]
1W2BX-ray3.50P2-95[»]
1YHQX-ray2.40Q1-96[»]
1YI2X-ray2.65Q1-96[»]
1YIJX-ray2.60Q1-96[»]
1YITX-ray2.80Q1-96[»]
1YJ9X-ray2.90Q1-96[»]
1YJNX-ray3.00Q1-96[»]
1YJWX-ray2.90Q1-96[»]
2OTJX-ray2.90Q1-96[»]
2OTLX-ray2.70Q1-96[»]
2QA4X-ray3.00Q1-96[»]
2QEXX-ray2.90Q1-96[»]
3CC2X-ray2.40Q1-96[»]
3CC4X-ray2.70Q1-96[»]
3CC7X-ray2.70Q1-96[»]
3CCEX-ray2.75Q1-96[»]
3CCJX-ray2.70Q1-96[»]
3CCLX-ray2.90Q1-96[»]
3CCMX-ray2.55Q1-96[»]
3CCQX-ray2.90Q1-96[»]
3CCRX-ray3.00Q1-96[»]
3CCSX-ray2.95Q1-96[»]
3CCUX-ray2.80Q1-96[»]
3CCVX-ray2.90Q1-96[»]
3CD6X-ray2.75Q1-96[»]
3CMAX-ray2.80Q1-96[»]
3CMEX-ray2.95Q1-96[»]
3CPWX-ray2.70P1-96[»]
3CXCX-ray3.00P2-95[»]
3G4SX-ray3.20Q2-96[»]
3G6EX-ray2.70Q2-96[»]
3G71X-ray2.85Q2-96[»]
3I55X-ray3.11Q1-96[»]
3I56X-ray2.90Q1-96[»]
3OW2X-ray2.70P2-96[»]
4HUBX-ray2.40Q1-96[»]
ProteinModelPortalP12734.
SMRP12734. Positions 2-96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC0260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV45317; AAV45317; rrnAC0260.
GeneID3129654.
KEGGhma:rrnAC0260.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2139.
HOGENOMHOG000106438.
KOK02889.
OMAPRFHGRT.
ProtClustDBPRK04306.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-236-MONOMER.

Family and domain databases

Gene3D2.30.30.70. 1 hit.
HAMAPMF_00369. Ribosomal_L21e.
InterProIPR001147. Ribosomal_L21e.
IPR022856. Ribosomal_L21e_arc.
IPR018259. Ribosomal_L21e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamPF01157. Ribosomal_L21e. 1 hit.
[Graphical view]
SUPFAMSSF50104. SSF50104. 1 hit.
PROSITEPS01171. RIBOSOMAL_L21E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12734.

Entry information

Entry nameRL21_HALMA
AccessionPrimary (citable) accession number: P12734
Secondary accession number(s): Q5V585
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 108 of the entry and version 2 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