Skip Header

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

P18138

- RL31_HALMA

UniProt

P18138 - RL31_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 L31e

Gene

rpl31e

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Binds to the 23S rRNA. Located at the polypeptide exit tunnel on the outside of the subunit.

GO - Molecular functioni

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

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-2792-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L31e
Alternative name(s):
Hl30
L34
Gene namesi
Name:rpl31e
Ordered Locus Names:rrnAC3113
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 – 929150S ribosomal protein L31ePRO_0000153791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC3113.

Structurei

Secondary structure

1
92
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 146Combined sources
Helixi16 – 205Combined sources
Helixi23 – 253Combined sources
Helixi26 – 4116Combined sources
Helixi46 – 483Combined sources
Beta strandi49 – 513Combined sources
Helixi53 – 597Combined sources
Turni60 – 623Combined sources
Turni63 – 653Combined sources
Beta strandi69 – 7810Combined sources
Turni79 – 824Combined sources
Beta strandi83 – 875Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40U2-92[»]
1JJ2X-ray2.40W2-92[»]
1K73X-ray3.01Y2-92[»]
1K8AX-ray3.00Y2-92[»]
1K9MX-ray3.00Y2-92[»]
1KC8X-ray3.01Y2-92[»]
1KD1X-ray3.00Y2-92[»]
1KQSX-ray3.10W2-92[»]
1M1KX-ray3.20Y2-92[»]
1M90X-ray2.80Y2-92[»]
1N8RX-ray3.00Y2-92[»]
1NJIX-ray3.00Y2-92[»]
1Q7YX-ray3.20Y2-92[»]
1Q81X-ray2.95Y2-92[»]
1Q82X-ray2.98Y2-92[»]
1Q86X-ray3.00Y2-92[»]
1QVFX-ray3.10W2-92[»]
1QVGX-ray2.90W2-92[»]
1S72X-ray2.40X1-92[»]
1VQ4X-ray2.70X1-92[»]
1VQ5X-ray2.60X1-92[»]
1VQ6X-ray2.70X1-92[»]
1VQ7X-ray2.50X1-92[»]
1VQ8X-ray2.20X1-92[»]
1VQ9X-ray2.40X1-92[»]
1VQKX-ray2.30X1-92[»]
1VQLX-ray2.30X1-92[»]
1VQMX-ray2.30X1-92[»]
1VQNX-ray2.40X1-92[»]
1VQOX-ray2.20X1-92[»]
1VQPX-ray2.25X1-92[»]
1W2BX-ray3.50W2-92[»]
1YHQX-ray2.40X1-92[»]
1YI2X-ray2.65X1-92[»]
1YIJX-ray2.60X1-92[»]
1YITX-ray2.80X1-92[»]
1YJ9X-ray2.90X1-92[»]
1YJNX-ray3.00X1-92[»]
1YJWX-ray2.90X1-92[»]
2OTJX-ray2.90X1-92[»]
2OTLX-ray2.70X1-92[»]
2QA4X-ray3.00X1-92[»]
2QEXX-ray2.90X1-92[»]
3CC2X-ray2.40X1-92[»]
3CC4X-ray2.70X1-92[»]
3CC7X-ray2.70X1-92[»]
3CCEX-ray2.75X1-92[»]
3CCJX-ray2.70X1-92[»]
3CCLX-ray2.90X1-92[»]
3CCMX-ray2.55X1-92[»]
3CCQX-ray2.90X1-92[»]
3CCRX-ray3.00X1-92[»]
3CCSX-ray2.95X1-92[»]
3CCUX-ray2.80X1-92[»]
3CCVX-ray2.90X1-92[»]
3CD6X-ray2.75X1-92[»]
3CMAX-ray2.80X1-92[»]
3CMEX-ray2.95X1-92[»]
3CPWX-ray2.70W1-92[»]
3CXCX-ray3.00W2-92[»]
3G4SX-ray3.20X8-89[»]
3G6EX-ray2.70X8-89[»]
3G71X-ray2.85X8-89[»]
3I55X-ray3.11X1-92[»]
3I56X-ray2.90X1-92[»]
3OW2X-ray2.70W8-89[»]
4ADXelectron microscopy6.60X1-92[»]
4HUBX-ray2.40X1-92[»]
ProteinModelPortaliP18138.
SMRiP18138. Positions 8-89.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18138.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L31e family.Curated

Phylogenomic databases

eggNOGiCOG2097.
HOGENOMiHOG000230616.
KOiK02910.
OMAiSHENTFI.

Family and domain databases

Gene3Di3.10.440.10. 1 hit.
HAMAPiMF_00410. Ribosomal_L31e.
InterProiIPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
IPR023621. Ribosomal_L31e_dom.
[Graphical view]
PfamiPF01198. Ribosomal_L31e. 1 hit.
[Graphical view]
ProDomiPD006030. Ribosomal_L31e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54575. SSF54575. 1 hit.
PROSITEiPS01144. RIBOSOMAL_L31E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P18138-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSASDFEERV VTIPLRDARA EPNHKRADKA MILIREHLAK HFSVDEDAVR
60 70 80 90
LDPSINEAAW ARGRANTPSK IRVRAARFEE EGEAIVEAET AE
Length:92
Mass (Da):10,367
Last modified:January 23, 2007 - v2
Checksum:i0FF505E03E8F6C4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55007 Genomic DNA. Translation: CAA38751.1.
AY596297 Genomic DNA. Translation: AAV47824.1.
PIRiS13067. R5HSER.
RefSeqiYP_137530.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV47824; AAV47824; rrnAC3113.
GeneIDi3128100.
KEGGihma:rrnAC3113.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55007 Genomic DNA. Translation: CAA38751.1 .
AY596297 Genomic DNA. Translation: AAV47824.1 .
PIRi S13067. R5HSER.
RefSeqi YP_137530.1. 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 U 2-92 [» ]
1JJ2 X-ray 2.40 W 2-92 [» ]
1K73 X-ray 3.01 Y 2-92 [» ]
1K8A X-ray 3.00 Y 2-92 [» ]
1K9M X-ray 3.00 Y 2-92 [» ]
1KC8 X-ray 3.01 Y 2-92 [» ]
1KD1 X-ray 3.00 Y 2-92 [» ]
1KQS X-ray 3.10 W 2-92 [» ]
1M1K X-ray 3.20 Y 2-92 [» ]
1M90 X-ray 2.80 Y 2-92 [» ]
1N8R X-ray 3.00 Y 2-92 [» ]
1NJI X-ray 3.00 Y 2-92 [» ]
1Q7Y X-ray 3.20 Y 2-92 [» ]
1Q81 X-ray 2.95 Y 2-92 [» ]
1Q82 X-ray 2.98 Y 2-92 [» ]
1Q86 X-ray 3.00 Y 2-92 [» ]
1QVF X-ray 3.10 W 2-92 [» ]
1QVG X-ray 2.90 W 2-92 [» ]
1S72 X-ray 2.40 X 1-92 [» ]
1VQ4 X-ray 2.70 X 1-92 [» ]
1VQ5 X-ray 2.60 X 1-92 [» ]
1VQ6 X-ray 2.70 X 1-92 [» ]
1VQ7 X-ray 2.50 X 1-92 [» ]
1VQ8 X-ray 2.20 X 1-92 [» ]
1VQ9 X-ray 2.40 X 1-92 [» ]
1VQK X-ray 2.30 X 1-92 [» ]
1VQL X-ray 2.30 X 1-92 [» ]
1VQM X-ray 2.30 X 1-92 [» ]
1VQN X-ray 2.40 X 1-92 [» ]
1VQO X-ray 2.20 X 1-92 [» ]
1VQP X-ray 2.25 X 1-92 [» ]
1W2B X-ray 3.50 W 2-92 [» ]
1YHQ X-ray 2.40 X 1-92 [» ]
1YI2 X-ray 2.65 X 1-92 [» ]
1YIJ X-ray 2.60 X 1-92 [» ]
1YIT X-ray 2.80 X 1-92 [» ]
1YJ9 X-ray 2.90 X 1-92 [» ]
1YJN X-ray 3.00 X 1-92 [» ]
1YJW X-ray 2.90 X 1-92 [» ]
2OTJ X-ray 2.90 X 1-92 [» ]
2OTL X-ray 2.70 X 1-92 [» ]
2QA4 X-ray 3.00 X 1-92 [» ]
2QEX X-ray 2.90 X 1-92 [» ]
3CC2 X-ray 2.40 X 1-92 [» ]
3CC4 X-ray 2.70 X 1-92 [» ]
3CC7 X-ray 2.70 X 1-92 [» ]
3CCE X-ray 2.75 X 1-92 [» ]
3CCJ X-ray 2.70 X 1-92 [» ]
3CCL X-ray 2.90 X 1-92 [» ]
3CCM X-ray 2.55 X 1-92 [» ]
3CCQ X-ray 2.90 X 1-92 [» ]
3CCR X-ray 3.00 X 1-92 [» ]
3CCS X-ray 2.95 X 1-92 [» ]
3CCU X-ray 2.80 X 1-92 [» ]
3CCV X-ray 2.90 X 1-92 [» ]
3CD6 X-ray 2.75 X 1-92 [» ]
3CMA X-ray 2.80 X 1-92 [» ]
3CME X-ray 2.95 X 1-92 [» ]
3CPW X-ray 2.70 W 1-92 [» ]
3CXC X-ray 3.00 W 2-92 [» ]
3G4S X-ray 3.20 X 8-89 [» ]
3G6E X-ray 2.70 X 8-89 [» ]
3G71 X-ray 2.85 X 8-89 [» ]
3I55 X-ray 3.11 X 1-92 [» ]
3I56 X-ray 2.90 X 1-92 [» ]
3OW2 X-ray 2.70 W 8-89 [» ]
4ADX electron microscopy 6.60 X 1-92 [» ]
4HUB X-ray 2.40 X 1-92 [» ]
ProteinModelPortali P18138.
SMRi P18138. Positions 8-89.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272569.rrnAC3113.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV47824 ; AAV47824 ; rrnAC3113 .
GeneIDi 3128100.
KEGGi hma:rrnAC3113.

Phylogenomic databases

eggNOGi COG2097.
HOGENOMi HOG000230616.
KOi K02910.
OMAi SHENTFI.

Enzyme and pathway databases

BioCyci HMAR272569:GJDH-2792-MONOMER.

Miscellaneous databases

EvolutionaryTracei P18138.

Family and domain databases

Gene3Di 3.10.440.10. 1 hit.
HAMAPi MF_00410. Ribosomal_L31e.
InterProi IPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
IPR023621. Ribosomal_L31e_dom.
[Graphical view ]
Pfami PF01198. Ribosomal_L31e. 1 hit.
[Graphical view ]
ProDomi PD006030. Ribosomal_L31e. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF54575. SSF54575. 1 hit.
PROSITEi PS01144. RIBOSOMAL_L31E. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Evidence for an additional archaebacterial gene cluster in Halobacterium marismortui encoding ribosomal proteins HL46e and HL30."
    Bergmann U., Arndt E.
    Biochim. Biophys. Acta 1050:56-60(1990) [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. "Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacterium Halobacterium marismortui."
    Hatakeyama T., Hatakeyama T.
    Biochim. Biophys. Acta 1039:343-347(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-92.
  4. "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.
  5. "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.
  6. "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.
  7. "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.
  8. "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.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  10. "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.
  11. "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.
  12. "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 nameiRL31_HALMA
AccessioniPrimary (citable) accession number: P18138
Secondary accession number(s): Q5UY29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 110 of the entry and version 2 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