SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P60618

- RL15E_HALMA

UniProt

P60618 - RL15E_HALMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
50S ribosomal protein L15e
Gene
rpl15e, rrnAC2065
Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed - 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
Complete GO annotation...

GO - Biological processi

  1. translation Source: InterPro
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: 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 L15eUniRule annotation
PRO_0000127570Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts with protein L7Ae and weakly with L44e.9 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC2065.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
4HUBX-ray2.40M1-196[»]
ProteinModelPortaliP60618.
SMRiP60618. Positions 2-195.

Miscellaneous databases

EvolutionaryTraceiP60618.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1632.
HOGENOMiHOG000229584.
KOiK02877.
OMAiSHIKDAW.

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

MARSAYSYIR DAWKNPGDGQ LAELQWQRQQ EWRNEGAVER IERPTRLDKA    50
RSQGYKAKQG VIVARVSVRK GSARKRRHKA GRRSKRQGVT RITRRKDIQR 100
VAEERASRTF PNLRVLNSYS VGQDGRQKWH EVILIDPNHP AIQNDDDLSW 150
ICADDQADRV FRGLTGAGRR NRGLSGKGKG SEKTRPSLRS NGGKGK 196
Length:196
Mass (Da):22,355
Last modified:January 23, 2007 - v3
Checksum:i502449E0A6BC23BB
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131W → T AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AY596297 Genomic DNA. Translation: AAV46920.1 .
PIRi H28949.
RefSeqi YP_136626.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FFK X-ray 2.40 I 37-194 [» ]
1JJ2 X-ray 2.40 L 2-194 [» ]
1K73 X-ray 3.01 N 2-194 [» ]
1K8A X-ray 3.00 N 2-194 [» ]
1K9M X-ray 3.00 N 2-194 [» ]
1KC8 X-ray 3.01 N 2-194 [» ]
1KD1 X-ray 3.00 N 2-194 [» ]
1KQS X-ray 3.10 L 2-194 [» ]
1M1K X-ray 3.20 N 2-194 [» ]
1M90 X-ray 2.80 N 2-194 [» ]
1N8R X-ray 3.00 N 2-194 [» ]
1NJI X-ray 3.00 N 2-194 [» ]
1Q7Y X-ray 3.20 N 2-194 [» ]
1Q81 X-ray 2.95 N 2-194 [» ]
1Q82 X-ray 2.98 N 2-194 [» ]
1Q86 X-ray 3.00 N 2-194 [» ]
1QVF X-ray 3.10 L 2-194 [» ]
1QVG X-ray 2.90 L 2-194 [» ]
1S72 X-ray 2.40 M 2-194 [» ]
1VQ4 X-ray 2.70 M 2-194 [» ]
1VQ5 X-ray 2.60 M 2-194 [» ]
1VQ6 X-ray 2.70 M 2-194 [» ]
1VQ7 X-ray 2.50 M 2-194 [» ]
1VQ8 X-ray 2.20 M 2-194 [» ]
1VQ9 X-ray 2.40 M 1-194 [» ]
1VQK X-ray 2.30 M 1-194 [» ]
1VQL X-ray 2.30 M 1-194 [» ]
1VQM X-ray 2.30 M 1-194 [» ]
1VQN X-ray 2.40 M 2-194 [» ]
1VQO X-ray 2.20 M 1-194 [» ]
1VQP X-ray 2.25 M 1-194 [» ]
1W2B X-ray 3.50 L 2-194 [» ]
1YHQ X-ray 2.40 M 2-195 [» ]
1YI2 X-ray 2.65 M 1-195 [» ]
1YIJ X-ray 2.60 M 1-195 [» ]
1YIT X-ray 2.80 M 1-195 [» ]
1YJ9 X-ray 2.90 M 1-195 [» ]
1YJN X-ray 3.00 M 1-195 [» ]
1YJW X-ray 2.90 M 1-195 [» ]
2OTJ X-ray 2.90 M 2-194 [» ]
2OTL X-ray 2.70 M 2-194 [» ]
2QA4 X-ray 3.00 M 1-194 [» ]
2QEX X-ray 2.90 M 1-194 [» ]
3CC2 X-ray 2.40 M 1-196 [» ]
3CC4 X-ray 2.70 M 1-196 [» ]
3CC7 X-ray 2.70 M 1-196 [» ]
3CCE X-ray 2.75 M 1-196 [» ]
3CCJ X-ray 2.70 M 1-196 [» ]
3CCL X-ray 2.90 M 1-196 [» ]
3CCM X-ray 2.55 M 1-196 [» ]
3CCQ X-ray 2.90 M 1-196 [» ]
3CCR X-ray 3.00 M 1-196 [» ]
3CCS X-ray 2.95 M 1-196 [» ]
3CCU X-ray 2.80 M 1-196 [» ]
3CCV X-ray 2.90 M 1-196 [» ]
3CD6 X-ray 2.75 M 1-196 [» ]
3CMA X-ray 2.80 M 1-196 [» ]
3CME X-ray 2.95 M 1-196 [» ]
3CPW X-ray 2.70 L 1-196 [» ]
3G4S X-ray 3.20 M 2-195 [» ]
3G6E X-ray 2.70 M 2-195 [» ]
3G71 X-ray 2.85 M 2-195 [» ]
3I55 X-ray 3.11 M 2-194 [» ]
3I56 X-ray 2.90 M 2-194 [» ]
4ADX electron microscopy 6.60 M 1-196 [» ]
4HUB X-ray 2.40 M 1-196 [» ]
ProteinModelPortali P60618.
SMRi P60618. Positions 2-195.
ModBasei Search...

Protein-protein interaction databases

STRINGi 272569.rrnAC2065.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV46920 ; AAV46920 ; rrnAC2065 .
GeneIDi 3129041.
KEGGi hma:rrnAC2065.

Phylogenomic databases

eggNOGi COG1632.
HOGENOMi HOG000229584.
KOi K02877.
OMAi SHIKDAW.

Enzyme and pathway databases

BioCyci HMAR272569:GJDH-1864-MONOMER.

Miscellaneous databases

EvolutionaryTracei P60618.

Family and domain databases

Gene3Di 3.40.1120.10. 1 hit.
HAMAPi MF_00256. Ribosomal_L15e.
InterProi IPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020926. Ribosomal_L15e_arc.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
[Graphical view ]
PANTHERi PTHR11847. PTHR11847. 1 hit.
Pfami PF00827. Ribosomal_L15e. 1 hit.
[Graphical view ]
SUPFAMi SSF54189. SSF54189. 1 hit.
PROSITEi PS01194. RIBOSOMAL_L15E. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 82 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

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