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Protein

50S ribosomal protein L6

Gene

rpl6

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

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

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1452-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L6UniRule annotation
Alternative name(s):
Hl10
Hmal6
Gene namesi
Name:rpl6UniRule annotation
Ordered Locus Names:rrnAC1596
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 – 17817750S ribosomal protein L6PRO_0000131083Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts weakly with protein L13.2 PublicationsUniRule annotation

Protein-protein interaction databases

STRINGi272569.rrnAC1596.

Structurei

Secondary structure

1
178
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Beta strandi13 – 175Combined sources
Beta strandi20 – 256Combined sources
Beta strandi28 – 336Combined sources
Beta strandi40 – 445Combined sources
Beta strandi47 – 515Combined sources
Helixi57 – 7721Combined sources
Beta strandi81 – 888Combined sources
Beta strandi90 – 923Combined sources
Beta strandi95 – 995Combined sources
Beta strandi102 – 1076Combined sources
Helixi108 – 1103Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi124 – 1285Combined sources
Beta strandi131 – 1377Combined sources
Helixi139 – 15113Combined sources
Beta strandi156 – 1583Combined sources
Turni160 – 1623Combined sources
Beta strandi166 – 1716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray3.50E2-178[»]
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[»]
4ADXelectron microscopy6.60E1-178[»]
4V9FX-ray2.40E1-178[»]
ProteinModelPortaliP14135.
SMRiP14135. Positions 2-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14135.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L6P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0097.
HOGENOMiHOG000039905.
KOiK02933.
OMAiTRTAKIM.

Family and domain databases

Gene3Di3.90.930.12. 2 hits.
HAMAPiMF_01365_A. Ribosomal_L6_A.
InterProiIPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR002359. Ribosomal_L6_CS2.
IPR019907. Ribosomal_L6P_arc.
[Graphical view]
PANTHERiPTHR11655. PTHR11655. 1 hit.
PfamiPF00347. Ribosomal_L6. 2 hits.
[Graphical view]
PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
SUPFAMiSSF56053. SSF56053. 2 hits.
TIGRFAMsiTIGR03653. arch_L6P. 1 hit.
PROSITEiPS00700. RIBOSOMAL_L6_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14135-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRVELEIPE DVDAEQDHLD ITVEGDNGSV TRRLWYPDID VSVDGDTVVI
60 70 80 90 100
ESDEDNAKTM STIGTFQSHI ENMFHGVTEG WEYGMEVFYS HFPMQVNVEG
110 120 130 140 150
DEVVIENFLG EKAPRRTTIH GDTDVEIDGE ELTVSGPDIE AVGQTAADIE
160 170
QLTRINDKDV RVFQDGVYIT RKPNRGDA
Length:178
Mass (Da):19,944
Last modified:January 23, 2007 - v3
Checksum:i380872452165689C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31R → S.
Natural varianti24 – 241E → S.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58395 Genomic DNA. Translation: CAA41287.1.
AY596297 Genomic DNA. Translation: AAV46514.1.
PIRiS16538. R5HS6L.
RefSeqiWP_011223740.1. NC_006396.1.
YP_136220.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46514; AAV46514; rrnAC1596.
GeneIDi3127517.
KEGGihma:rrnAC1596.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58395 Genomic DNA. Translation: CAA41287.1.
AY596297 Genomic DNA. Translation: AAV46514.1.
PIRiS16538. R5HS6L.
RefSeqiWP_011223740.1. NC_006396.1.
YP_136220.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray3.50E2-178[»]
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[»]
4ADXelectron microscopy6.60E1-178[»]
4V9FX-ray2.40E1-178[»]
ProteinModelPortaliP14135.
SMRiP14135. Positions 2-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC1596.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV46514; AAV46514; rrnAC1596.
GeneIDi3127517.
KEGGihma:rrnAC1596.

Phylogenomic databases

eggNOGiCOG0097.
HOGENOMiHOG000039905.
KOiK02933.
OMAiTRTAKIM.

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1452-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14135.

Family and domain databases

Gene3Di3.90.930.12. 2 hits.
HAMAPiMF_01365_A. Ribosomal_L6_A.
InterProiIPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR002359. Ribosomal_L6_CS2.
IPR019907. Ribosomal_L6P_arc.
[Graphical view]
PANTHERiPTHR11655. PTHR11655. 1 hit.
PfamiPF00347. Ribosomal_L6. 2 hits.
[Graphical view]
PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
SUPFAMiSSF56053. SSF56053. 2 hits.
TIGRFAMsiTIGR03653. arch_L6P. 1 hit.
PROSITEiPS00700. RIBOSOMAL_L6_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiRL6_HALMA
AccessioniPrimary (citable) accession number: P14135
Secondary accession number(s): P12739, Q5V1T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 119 of the entry and version 3 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, Reference proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.