Skip Header

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

P12737

- RL15_HALMA

UniProt

P12737 - RL15_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 L15

Gene

rpl15

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

Binds to the 23S rRNA.

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-1446-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L15
Alternative name(s):
Hl9
Hmal15
Gene namesi
Name:rpl15
Ordered Locus Names:rrnAC1590
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. large ribosomal subunit Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 16516450S ribosomal protein L15PRO_0000104860Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts weakly with proteins L18e and L32e.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1590.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Turni8 – 103Combined sources
Beta strandi11 – 133Combined sources
Beta strandi16 – 183Combined sources
Beta strandi21 – 244Combined sources
Helixi25 – 284Combined sources
Turni32 – 409Combined sources
Beta strandi42 – 443Combined sources
Helixi56 – 583Combined sources
Beta strandi62 – 665Combined sources
Helixi67 – 726Combined sources
Helixi75 – 773Combined sources
Beta strandi91 – 933Combined sources
Helixi94 – 963Combined sources
Turni99 – 1035Combined sources
Beta strandi104 – 1107Combined sources
Beta strandi120 – 1267Combined sources
Helixi128 – 1369Combined sources
Beta strandi140 – 1434Combined sources
Turni145 – 1473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40J2-165[»]
1JJ2X-ray2.40K2-165[»]
1K73X-ray3.01M2-165[»]
1K8AX-ray3.00M2-165[»]
1K9MX-ray3.00M2-165[»]
1KC8X-ray3.01M2-165[»]
1KD1X-ray3.00M2-165[»]
1KQSX-ray3.10K2-165[»]
1M1KX-ray3.20M2-165[»]
1M90X-ray2.80M2-165[»]
1N8RX-ray3.00M2-165[»]
1NJIX-ray3.00M2-165[»]
1Q7YX-ray3.20M2-165[»]
1Q81X-ray2.95M2-165[»]
1Q82X-ray2.98M2-165[»]
1Q86X-ray3.00M2-165[»]
1QVFX-ray3.10K2-165[»]
1QVGX-ray2.90K2-165[»]
1S72X-ray2.40L1-165[»]
1VQ4X-ray2.70L1-165[»]
1VQ5X-ray2.60L1-165[»]
1VQ6X-ray2.70L1-165[»]
1VQ7X-ray2.50L1-165[»]
1VQ8X-ray2.20L1-165[»]
1VQ9X-ray2.40L1-165[»]
1VQKX-ray2.30L1-165[»]
1VQLX-ray2.30L1-165[»]
1VQMX-ray2.30L1-165[»]
1VQNX-ray2.40L1-165[»]
1VQOX-ray2.20L1-165[»]
1VQPX-ray2.25L1-165[»]
1W2BX-ray3.50K2-165[»]
1YHQX-ray2.40L1-165[»]
1YI2X-ray2.65L1-165[»]
1YIJX-ray2.60L1-165[»]
1YITX-ray2.80L1-165[»]
1YJ9X-ray2.90L1-165[»]
1YJNX-ray3.00L1-165[»]
1YJWX-ray2.90L1-165[»]
2B66X-ray5.90P2-165[»]
2B9NX-ray6.76P2-165[»]
2B9PX-ray6.46P2-165[»]
2OTJX-ray2.90L1-165[»]
2OTLX-ray2.70L1-165[»]
2QA4X-ray3.00L1-165[»]
2QEXX-ray2.90L1-165[»]
3CC2X-ray2.40L1-165[»]
3CC4X-ray2.70L1-165[»]
3CC7X-ray2.70L1-165[»]
3CCEX-ray2.75L1-165[»]
3CCJX-ray2.70L1-165[»]
3CCLX-ray2.90L1-165[»]
3CCMX-ray2.55L1-165[»]
3CCQX-ray2.90L1-165[»]
3CCRX-ray3.00L1-165[»]
3CCSX-ray2.95L1-165[»]
3CCUX-ray2.80L1-165[»]
3CCVX-ray2.90L1-165[»]
3CD6X-ray2.75L1-165[»]
3CMAX-ray2.80L1-165[»]
3CMEX-ray2.95L1-165[»]
3CPWX-ray2.70K1-165[»]
3CXCX-ray3.00K2-165[»]
3G4SX-ray3.20L1-165[»]
3G6EX-ray2.70L1-165[»]
3G71X-ray2.85L1-165[»]
3I55X-ray3.11L1-165[»]
3I56X-ray2.90L1-165[»]
3OW2X-ray2.70K2-151[»]
4ADXelectron microscopy6.60L1-165[»]
4HUBX-ray2.40L1-165[»]
ProteinModelPortaliP12737.
SMRiP12737. Positions 2-151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12737.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15P family.Curated

Phylogenomic databases

eggNOGiCOG0200.
HOGENOMiHOG000231263.
KOiK02876.
OMAiSHTHGWG.

Family and domain databases

Gene3Di4.10.990.10. 1 hit.
HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR027386. 50S_Rbsml_prot_L15P_N.
IPR023681. Ribosomal_L15_arc-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12737-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSKKKRQRG SRTHGGGSHK NRRGAGHRGG RGDAGRDKHE FHNHEPLGKS
60 70 80 90 100
GFKRPQKVQE EAATIDVREI DENVTLLAAD DVAEVEDGGF RVDVRDVVEE
110 120 130 140 150
ADDADYVKVL GAGQVRHELT LIADDFSEGA REKVEGAGGS VELTDLGEER
160
QAEAEETEDA DADEE
Length:165
Mass (Da):17,973
Last modified:January 23, 2007 - v4
Checksum:iAAF4318ADF0D8879
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21T → D AA sequence (PubMed:3196689)Curated
Sequence conflicti31 – 322RG → NR AA sequence (PubMed:3196689)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63127 Genomic DNA. Translation: CAA44837.1.
AY596297 Genomic DNA. Translation: AAV46508.1.
X58395 Genomic DNA. Translation: CAA41293.1.
PIRiS22349. R6HS15.
RefSeqiWP_011223737.1. NC_006396.1.
YP_136214.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46508; AAV46508; rrnAC1590.
GeneIDi3128809.
KEGGihma:rrnAC1590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63127 Genomic DNA. Translation: CAA44837.1 .
AY596297 Genomic DNA. Translation: AAV46508.1 .
X58395 Genomic DNA. Translation: CAA41293.1 .
PIRi S22349. R6HS15.
RefSeqi WP_011223737.1. NC_006396.1.
YP_136214.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FFK X-ray 2.40 J 2-165 [» ]
1JJ2 X-ray 2.40 K 2-165 [» ]
1K73 X-ray 3.01 M 2-165 [» ]
1K8A X-ray 3.00 M 2-165 [» ]
1K9M X-ray 3.00 M 2-165 [» ]
1KC8 X-ray 3.01 M 2-165 [» ]
1KD1 X-ray 3.00 M 2-165 [» ]
1KQS X-ray 3.10 K 2-165 [» ]
1M1K X-ray 3.20 M 2-165 [» ]
1M90 X-ray 2.80 M 2-165 [» ]
1N8R X-ray 3.00 M 2-165 [» ]
1NJI X-ray 3.00 M 2-165 [» ]
1Q7Y X-ray 3.20 M 2-165 [» ]
1Q81 X-ray 2.95 M 2-165 [» ]
1Q82 X-ray 2.98 M 2-165 [» ]
1Q86 X-ray 3.00 M 2-165 [» ]
1QVF X-ray 3.10 K 2-165 [» ]
1QVG X-ray 2.90 K 2-165 [» ]
1S72 X-ray 2.40 L 1-165 [» ]
1VQ4 X-ray 2.70 L 1-165 [» ]
1VQ5 X-ray 2.60 L 1-165 [» ]
1VQ6 X-ray 2.70 L 1-165 [» ]
1VQ7 X-ray 2.50 L 1-165 [» ]
1VQ8 X-ray 2.20 L 1-165 [» ]
1VQ9 X-ray 2.40 L 1-165 [» ]
1VQK X-ray 2.30 L 1-165 [» ]
1VQL X-ray 2.30 L 1-165 [» ]
1VQM X-ray 2.30 L 1-165 [» ]
1VQN X-ray 2.40 L 1-165 [» ]
1VQO X-ray 2.20 L 1-165 [» ]
1VQP X-ray 2.25 L 1-165 [» ]
1W2B X-ray 3.50 K 2-165 [» ]
1YHQ X-ray 2.40 L 1-165 [» ]
1YI2 X-ray 2.65 L 1-165 [» ]
1YIJ X-ray 2.60 L 1-165 [» ]
1YIT X-ray 2.80 L 1-165 [» ]
1YJ9 X-ray 2.90 L 1-165 [» ]
1YJN X-ray 3.00 L 1-165 [» ]
1YJW X-ray 2.90 L 1-165 [» ]
2B66 X-ray 5.90 P 2-165 [» ]
2B9N X-ray 6.76 P 2-165 [» ]
2B9P X-ray 6.46 P 2-165 [» ]
2OTJ X-ray 2.90 L 1-165 [» ]
2OTL X-ray 2.70 L 1-165 [» ]
2QA4 X-ray 3.00 L 1-165 [» ]
2QEX X-ray 2.90 L 1-165 [» ]
3CC2 X-ray 2.40 L 1-165 [» ]
3CC4 X-ray 2.70 L 1-165 [» ]
3CC7 X-ray 2.70 L 1-165 [» ]
3CCE X-ray 2.75 L 1-165 [» ]
3CCJ X-ray 2.70 L 1-165 [» ]
3CCL X-ray 2.90 L 1-165 [» ]
3CCM X-ray 2.55 L 1-165 [» ]
3CCQ X-ray 2.90 L 1-165 [» ]
3CCR X-ray 3.00 L 1-165 [» ]
3CCS X-ray 2.95 L 1-165 [» ]
3CCU X-ray 2.80 L 1-165 [» ]
3CCV X-ray 2.90 L 1-165 [» ]
3CD6 X-ray 2.75 L 1-165 [» ]
3CMA X-ray 2.80 L 1-165 [» ]
3CME X-ray 2.95 L 1-165 [» ]
3CPW X-ray 2.70 K 1-165 [» ]
3CXC X-ray 3.00 K 2-165 [» ]
3G4S X-ray 3.20 L 1-165 [» ]
3G6E X-ray 2.70 L 1-165 [» ]
3G71 X-ray 2.85 L 1-165 [» ]
3I55 X-ray 3.11 L 1-165 [» ]
3I56 X-ray 2.90 L 1-165 [» ]
3OW2 X-ray 2.70 K 2-151 [» ]
4ADX electron microscopy 6.60 L 1-165 [» ]
4HUB X-ray 2.40 L 1-165 [» ]
ProteinModelPortali P12737.
SMRi P12737. Positions 2-151.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272569.rrnAC1590.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV46508 ; AAV46508 ; rrnAC1590 .
GeneIDi 3128809.
KEGGi hma:rrnAC1590.

Phylogenomic databases

eggNOGi COG0200.
HOGENOMi HOG000231263.
KOi K02876.
OMAi SHTHGWG.

Enzyme and pathway databases

BioCyci HMAR272569:GJDH-1446-MONOMER.

Miscellaneous databases

EvolutionaryTracei P12737.

Family and domain databases

Gene3Di 4.10.990.10. 1 hit.
HAMAPi MF_01341. Ribosomal_L15.
InterProi IPR027386. 50S_Rbsml_prot_L15P_N.
IPR023681. Ribosomal_L15_arc-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view ]
Pfami PF00828. Ribosomal_L18e. 1 hit.
[Graphical view ]
SUPFAMi SSF52080. SSF52080. 1 hit.
PROSITEi PS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genes for ribosomal protein L15 and the protein equivalent to secY in the archaebacterium Haloarcula (Halobacterium) marismortui."
    Arndt E.
    Biochim. Biophys. Acta 1130:113-116(1992) [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. "Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins."
    Hatakeyama T., Kaufmann F., Schroeter B., Hatakeyama T.
    Eur. J. Biochem. 185:685-693(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-155.
  4. "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] OF 1-70.
  5. "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 2-32.
  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 nameiRL15_HALMA
AccessioniPrimary (citable) accession number: P12737
Secondary accession number(s): Q5V1U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 114 of the entry and version 4 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