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Protein

50S ribosomal protein L15e

Gene

rpl15e

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

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-KW
  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-1864-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L15e
Alternative name(s):
50S ribosomal protein LC12
Gene namesi
Name:rpl15e
Ordered Locus Names:rrnAC2065
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
ProteomesiUP000001169 Componenti: 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 – 11Removed1 Publication
Chaini2 – 19619550S ribosomal protein L15ePRO_0000127570Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts with protein L7Ae and weakly with L44e.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC2065.

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 127Combined sources
Helixi19 – 3214Combined sources
Beta strandi33 – 353Combined sources
Beta strandi37 – 437Combined sources
Helixi47 – 537Combined sources
Beta strandi61 – 699Combined sources
Helixi84 – 863Combined sources
Beta strandi89 – 913Combined sources
Helixi98 – 10912Combined sources
Beta strandi114 – 12411Combined sources
Beta strandi127 – 1359Combined sources
Helixi140 – 1434Combined sources
Turni146 – 1483Combined sources
Helixi149 – 1524Combined sources
Helixi154 – 1563Combined sources
Helixi159 – 1624Combined sources
Helixi166 – 1716Combined sources
Turni182 – 1843Combined sources
Turni188 – 1925Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4V9FX-ray2.40M1-196[»]
SMRiP60618. Positions 2-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60618.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15e family.Curated

Phylogenomic databases

eggNOGiCOG1632.
HOGENOMiHOG000229584.
KOiK02877.
OMAiYIGELYK.

Family and domain databases

Gene3Di3.40.1120.10. 1 hit.
HAMAPiMF_00256. Ribosomal_L15e.
InterProiIPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020926. Ribosomal_L15e_arc.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
[Graphical view]
PANTHERiPTHR11847. PTHR11847. 1 hit.
PfamiPF00827. Ribosomal_L15e. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS01194. RIBOSOMAL_L15E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P60618-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARSAYSYIR DAWKNPGDGQ LAELQWQRQQ EWRNEGAVER IERPTRLDKA
60 70 80 90 100
RSQGYKAKQG VIVARVSVRK GSARKRRHKA GRRSKRQGVT RITRRKDIQR
110 120 130 140 150
VAEERASRTF PNLRVLNSYS VGQDGRQKWH EVILIDPNHP AIQNDDDLSW
160 170 180 190
ICADDQADRV FRGLTGAGRR NRGLSGKGKG SEKTRPSLRS NGGKGK
Length:196
Mass (Da):22,355
Last modified:January 23, 2007 - v3
Checksum:i502449E0A6BC23BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131W → T AA sequence (PubMed:3196689).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY596297 Genomic DNA. Translation: AAV46920.1.
PIRiH28949.
RefSeqiYP_136626.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46920; AAV46920; rrnAC2065.
GeneIDi3129041.
KEGGihma:rrnAC2065.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY596297 Genomic DNA. Translation: AAV46920.1.
PIRiH28949.
RefSeqiYP_136626.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4V9FX-ray2.40M1-196[»]
SMRiP60618. Positions 2-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC2065.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV46920; AAV46920; rrnAC2065.
GeneIDi3129041.
KEGGihma:rrnAC2065.

Phylogenomic databases

eggNOGiCOG1632.
HOGENOMiHOG000229584.
KOiK02877.
OMAiYIGELYK.

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1864-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60618.

Family and domain databases

Gene3Di3.40.1120.10. 1 hit.
HAMAPiMF_00256. Ribosomal_L15e.
InterProiIPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020926. Ribosomal_L15e_arc.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
[Graphical view]
PANTHERiPTHR11847. PTHR11847. 1 hit.
PfamiPF00827. Ribosomal_L15e. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS01194. RIBOSOMAL_L15E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.

Entry informationi

Entry nameiRL15E_HALMA
AccessioniPrimary (citable) accession number: P60618
Secondary accession number(s): P12740, Q5V0N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 87 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.