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P14122 (RL11_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 110. 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 L11
Alternative name(s):
Hmal11
Gene names
Name:rpl11
Ordered Locus Names:rrnAC1414
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 length162 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. HAMAP-Rule MF_00736

Subunit structure

Part of the 50S ribosomal subunit. Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated spine to which 3 L12 dimers bind in a sequential fashion Probable. Ref.6

Sequence similarities

Belongs to the ribosomal protein L11P 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: UniProtKB-HAMAP

   Cellular_componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionLSU rRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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.3
Chain2 – 16216150S ribosomal protein L11 HAMAP-Rule MF_00736
PRO_0000104431

Secondary structure

.............................. 162
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14122 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E64E6802B49208B8

FASTA16217,089
        10         20         30         40         50         60 
MAGTIEVLVP GGEANPGPPL GPELGPTPVD VQAVVQEIND QTAAFDGTEV PVTVKYDDDG 

        70         80         90        100        110        120 
SFEIEVGVPP TAELIKDEAG FETGSGEPQE DFVADLSVDQ VKQIAEQKHP DLLSYDLTNA 

       130        140        150        160 
AKEVVGTCTS LGVTIEGENP REFKERIDAG EYDDVFAAEA QA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the genes encoding the L11, L1, L10 and L12 equivalent ribosomal proteins from the archaebacterium Halobacterium marismortui."
Arndt E., Weigel C.
Nucleic Acids Res. 18:1285-1285(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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.
[3]"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 2-28.
[4]"Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit."
Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A.
Nature 400:841-847(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[5]"Structure of the base of the L7/L12 stalk of the Haloarcula marismortui large ribosomal subunit: analysis of L11 movements."
Kavran J.M., Steitz T.A.
J. Mol. Biol. 371:1047-1059(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), RRNA-BINDING, INTERACTION WITH L10.
[6]"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
X51430 Genomic DNA. Translation: CAA35793.1.
AY596297 Genomic DNA. Translation: AAV46342.1.
PIRR5HS11. S08420.
RefSeqYP_136048.1. NC_006396.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C04X-ray5.00C79-88[»]
1S72X-ray2.40I1-162[»]
1VQ4X-ray2.70I1-162[»]
1VQ5X-ray2.60I1-162[»]
1VQ6X-ray2.70I1-162[»]
1VQ7X-ray2.50I1-162[»]
1VQ8X-ray2.20I1-162[»]
1VQ9X-ray2.40I1-162[»]
1VQKX-ray2.30I1-162[»]
1VQLX-ray2.30I1-162[»]
1VQMX-ray2.30I1-162[»]
1VQNX-ray2.40I1-162[»]
1VQOX-ray2.20I1-162[»]
1VQPX-ray2.25I1-162[»]
1YHQX-ray2.40I1-162[»]
1YI2X-ray2.65I1-162[»]
1YIJX-ray2.60I1-162[»]
1YITX-ray2.80I1-162[»]
1YJ9X-ray2.90I1-162[»]
1YJNX-ray3.00I1-162[»]
1YJWX-ray2.90I1-162[»]
2OTJX-ray2.90I2-162[»]
2OTLX-ray2.70I1-162[»]
2QA4X-ray3.00I1-162[»]
2QEXX-ray2.90I1-162[»]
3CC2X-ray2.40I1-162[»]
3CC4X-ray2.70I1-162[»]
3CC7X-ray2.70I1-162[»]
3CCEX-ray2.75I1-162[»]
3CCJX-ray2.70I1-162[»]
3CCLX-ray2.90I1-162[»]
3CCMX-ray2.55I1-162[»]
3CCQX-ray2.90I1-162[»]
3CCRX-ray3.00I1-162[»]
3CCSX-ray2.95I1-162[»]
3CCUX-ray2.80I1-162[»]
3CCVX-ray2.90I1-162[»]
3CD6X-ray2.75I1-162[»]
3CMAX-ray2.80I1-162[»]
3CMEX-ray2.95I1-162[»]
3G4SX-ray3.20I67-136[»]
3G6EX-ray2.70I67-136[»]
3G71X-ray2.85I67-136[»]
3I55X-ray3.11I1-162[»]
3I56X-ray2.90I1-162[»]
4HUBX-ray2.40I1-162[»]
ProteinModelPortalP14122.
SMRP14122. Positions 5-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC1414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46342; AAV46342; rrnAC1414.
GeneID3128412.
KEGGhma:rrnAC1414.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0080.
HOGENOMHOG000082124.
KOK02867.
OMALKIARMK.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1277-MONOMER.

Family and domain databases

Gene3D1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPMF_00736. Ribosomal_L11.
InterProIPR000911. Ribosomal_L11/L12.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view]
PANTHERPTHR11661. PTHR11661. 1 hit.
PfamPF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]
SMARTSM00649. RL11. 1 hit.
[Graphical view]
SUPFAMSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
PROSITEPS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14122.

Entry information

Entry nameRL11_HALMA
AccessionPrimary (citable) accession number: P14122
Secondary accession number(s): Q5V2B0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 110 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