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P14135 (RL6_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 111. 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 L6
Alternative name(s):
Hl10
Hmal6
Gene names
Name:rpl6
Ordered Locus Names:rrnAC1596
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 length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. HAMAP-Rule MF_01365

Subunit structure

Part of the 50S ribosomal subunit. Interacts weakly with protein L13. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Sequence similarities

Belongs to the ribosomal protein L6P 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_functionrRNA 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 Ref.4
Chain2 – 17817750S ribosomal protein L6 HAMAP-Rule MF_01365
PRO_0000131083

Natural variations

Natural variant31R → S.
Natural variant241E → S.

Secondary structure

...................................... 178
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14135 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 380872452165689C

FASTA17819,944
        10         20         30         40         50         60 
MPRVELEIPE DVDAEQDHLD ITVEGDNGSV TRRLWYPDID VSVDGDTVVI ESDEDNAKTM 

        70         80         90        100        110        120 
STIGTFQSHI ENMFHGVTEG WEYGMEVFYS HFPMQVNVEG DEVVIENFLG EKAPRRTTIH 

       130        140        150        160        170 
GDTDVEIDGE ELTVSGPDIE AVGQTAADIE QLTRINDKDV RVFQDGVYIT RKPNRGDA 

« Hide

References

« Hide 'large scale' references
[1]"Organization and nucleotide sequence of ten ribosomal protein genes from the region equivalent to the spectinomycin operon in the archaebacterium Halobacterium marismortui."
Scholzen T., Arndt E.
Mol. Gen. Genet. 228:70-80(1991) [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]"The N-terminal sequence of ribosomal protein L10 from the archaebacterium Halobacterium marismortui and its relationship to eubacterial protein L6 and other ribosomal proteins."
Dijk J., van den Broek R., Nasiulas G., Beck A., Reinhardt R., Wittmann-Liebold B.
Biol. Chem. Hoppe-Seyler 368:921-925(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-55.
[4]"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 2-31.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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
X58395 Genomic DNA. Translation: CAA41287.1.
AY596297 Genomic DNA. Translation: AAV46514.1.
PIRR5HS6L. S16538.
RefSeqYP_136220.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C04X-ray5.00B21-25[»]
1FFKX-ray2.4012-178[»]
1JJ2X-ray2.40E2-178[»]
1K73X-ray3.01G2-178[»]
1K8AX-ray3.00G2-178[»]
1K9MX-ray3.00G2-178[»]
1KC8X-ray3.01G2-178[»]
1KD1X-ray3.00G2-178[»]
1KQSX-ray3.10E2-178[»]
1M1KX-ray3.20G2-178[»]
1M90X-ray2.80G2-178[»]
1N8RX-ray3.00G2-178[»]
1NJIX-ray3.00G2-178[»]
1Q7YX-ray3.20G2-178[»]
1Q81X-ray2.95G2-178[»]
1Q82X-ray2.98G2-178[»]
1Q86X-ray3.00G2-178[»]
1QVFX-ray3.10E2-178[»]
1QVGX-ray2.90E2-178[»]
1S72X-ray2.40E1-178[»]
1VQ4X-ray2.70E1-178[»]
1VQ5X-ray2.60E1-178[»]
1VQ6X-ray2.70E1-178[»]
1VQ7X-ray2.50E1-178[»]
1VQ8X-ray2.20E1-178[»]
1VQ9X-ray2.40E1-178[»]
1VQKX-ray2.30E1-178[»]
1VQLX-ray2.30E1-178[»]
1VQMX-ray2.30E1-178[»]
1VQNX-ray2.40E1-178[»]
1VQOX-ray2.20E1-178[»]
1VQPX-ray2.25E1-178[»]
1W2BX-ray3.50E2-177[»]
1YHQX-ray2.40E1-178[»]
1YI2X-ray2.65E1-178[»]
1YIJX-ray2.60E1-178[»]
1YITX-ray2.80E1-178[»]
1YJ9X-ray2.90E1-178[»]
1YJNX-ray3.00E1-178[»]
1YJWX-ray2.90E1-178[»]
2OTJX-ray2.90E1-178[»]
2OTLX-ray2.70E1-178[»]
2QA4X-ray3.00E1-178[»]
2QEXX-ray2.90E1-178[»]
3CC2X-ray2.40E1-178[»]
3CC4X-ray2.70E1-178[»]
3CC7X-ray2.70E1-178[»]
3CCEX-ray2.75E1-178[»]
3CCJX-ray2.70E1-178[»]
3CCLX-ray2.90E1-178[»]
3CCMX-ray2.55E1-178[»]
3CCQX-ray2.90E1-178[»]
3CCRX-ray3.00E1-178[»]
3CCSX-ray2.95E1-178[»]
3CCUX-ray2.80E1-178[»]
3CCVX-ray2.90E1-178[»]
3CD6X-ray2.75E1-178[»]
3CMAX-ray2.80E1-178[»]
3CMEX-ray2.95E1-178[»]
3CPWX-ray2.70E1-178[»]
3CXCX-ray3.00E2-178[»]
3G4SX-ray3.20E2-173[»]
3G6EX-ray2.70E2-173[»]
3G71X-ray2.85E2-173[»]
3I55X-ray3.11E1-178[»]
3I56X-ray2.90E1-178[»]
3OW2X-ray2.70E2-173[»]
4HUBX-ray2.40E1-178[»]
ProteinModelPortalP14135.
SMRP14135. Positions 2-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC1596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46514; AAV46514; rrnAC1596.
GeneID3127517.
KEGGhma:rrnAC1596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0097.
HOGENOMHOG000039905.
KOK02933.
OMAVYITQKP.
ProtClustDBPRK05518.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1452-MONOMER.

Family and domain databases

Gene3D3.90.930.12. 2 hits.
HAMAPMF_01365_A. Ribosomal_L6_A.
InterProIPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR002359. Ribosomal_L6_CS2.
IPR019907. Ribosomal_L6P_arc.
[Graphical view]
PANTHERPTHR11655. PTHR11655. 1 hit.
PTHR11655:SF1. PTHR11655:SF1. 1 hit.
PfamPF00347. Ribosomal_L6. 2 hits.
[Graphical view]
PIRSFPIRSF002162. Ribosomal_L6. 1 hit.
SUPFAMSSF56053. SSF56053. 2 hits.
TIGRFAMsTIGR03653. arch_L6P. 1 hit.
PROSITEPS00700. RIBOSOMAL_L6_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14135.

Entry information

Entry nameRL6_HALMA
AccessionPrimary (citable) accession number: P14135
Secondary accession number(s): P12739, Q5V1T8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 111 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