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P15825 (RLA0_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L10E
Short name=Ribosomal protein L10
Alternative name(s):
Acidic ribosomal protein P0 homolog
HMal10
L10E
Gene names
Name:rplP0
Synonyms:rpl10e
Ordered Locus Names:rrnAC1417
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ribosomal protein L10e is the functional equivalent of E.coli protein L10. HAMAP MF_00280

Subunit structure

Part of the 50S ribosomal subunit. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Sequence similarities

Belongs to the ribosomal protein L10P family.

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processribosome biogenesis

Inferred from electronic annotation. Source: InterPro

translation

Inferred from electronic annotation. Source: InterPro

   Cellular componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionstructural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 34834850S ribosomal protein L10E HAMAP MF_00280
PRO_0000154789

Experimental info

Sequence conflict2481A → D in CAA35795. Ref.1

Secondary structure

1 ..... 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15825 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 4063B1C9D2FCB164

FASTA34837,150
        10         20         30         40         50         60 
MSAESERKTE TIPEWKQEEV DAIVEMIESY ESVGVVNIAG IPSRQLQDMR RDLHGTAELR 

        70         80         90        100        110        120 
VSRNTLLERA LDDVDDGLED LNGYITGQVG LIGTDDNPFS LFQELEASKT PAPIGAGEVA 

       130        140        150        160        170        180 
PNDIVIPEGD TGVDPGPFVG ELQSVGADAR IQEGSIQVLS DSTVLDTGEE VSQELSNVLN 

       190        200        210        220        230        240 
ELGIEPKEVG LDLRAVFADG VLFEPEELEL DIDEYRSDIQ AAAGRAFNLS VNADYPTATT 

       250        260        270        280        290        300 
APTMLQSARG NAKSLALQAA IEDPEVVPDL VSKADAQVRA LASQIDDEEA LPEELQGVEA 

       310        320        330        340 
DVATEEPTDD QDDDTASEDD ADADDAAEEA DDDDDDDEDA GDALGAMF

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the genes encoding the L11, L1, L10 and L12 equivalent ribosomal proteins from the archaebacterium Halobacterium marismortui."
Arndt E., Weigel C.
Nucleic Acids Res. 18:1285-1285(1990) [PubMed: 2320419] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed: 15520287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[3]"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: 11483524] [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 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: 12150912] [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.
[5]"Structural insights into peptide bond formation."
Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.
Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002) [PubMed: 12185246] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[6]"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: 12860128] [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.
[7]"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: 14561884] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT E SITE SUBSTRATES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X51430 Genomic DNA. Translation: CAA35795.1.
AY596297 Genomic DNA. Translation: AAV46344.1.
PIRR5HS10. S08422.
RefSeqYP_136050.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JJ2X-ray2.40G1-348[»]
1K73X-ray3.01I1-348[»]
1K8AX-ray3.00I1-348[»]
1K9MX-ray3.00I1-348[»]
1KC8X-ray3.01I1-348[»]
1KD1X-ray3.00I1-348[»]
1KQSX-ray3.10G1-348[»]
1M1KX-ray3.20I1-348[»]
1M90X-ray2.80I1-348[»]
1N8RX-ray3.00I1-348[»]
1NJIX-ray3.00I1-348[»]
1Q7YX-ray3.20I1-348[»]
1Q81X-ray2.95I1-348[»]
1Q82X-ray2.98I1-348[»]
1Q86X-ray3.00I1-348[»]
1QVFX-ray3.10G1-348[»]
1QVGX-ray2.90G1-348[»]
1S72X-ray2.40G1-348[»]
1VQ4X-ray2.70G1-348[»]
1VQ5X-ray2.60G1-348[»]
1VQ6X-ray2.70G1-348[»]
1VQ7X-ray2.50G1-348[»]
1VQ8X-ray2.20G1-348[»]
1VQ9X-ray2.40G1-348[»]
1VQKX-ray2.30G1-348[»]
1VQLX-ray2.30G1-348[»]
1VQMX-ray2.30G1-348[»]
1VQNX-ray2.40G1-348[»]
1VQOX-ray2.20G1-348[»]
1VQPX-ray2.25G1-348[»]
1W2BX-ray3.50G1-348[»]
1YHQX-ray2.40G1-348[»]
1YI2X-ray2.65G1-348[»]
1YIJX-ray2.60G1-348[»]
1YITX-ray2.80G1-348[»]
1YJ9X-ray2.90G1-348[»]
1YJNX-ray3.00G1-348[»]
1YJWX-ray2.90G1-348[»]
1ZB4model-A1-130[»]
2OTJX-ray2.90G1-348[»]
2OTLX-ray2.70G1-348[»]
2QA4X-ray3.00G1-348[»]
2QEXX-ray2.90G1-348[»]
3CC2X-ray2.40G1-348[»]
3CC4X-ray2.70G1-348[»]
3CC7X-ray2.70G1-348[»]
3CCEX-ray2.75G1-348[»]
3CCJX-ray2.70G1-348[»]
3CCLX-ray2.90G1-348[»]
3CCMX-ray2.55G1-348[»]
3CCQX-ray2.90G1-348[»]
3CCRX-ray3.00G1-348[»]
3CCSX-ray2.95G1-348[»]
3CCUX-ray2.80G1-348[»]
3CCVX-ray2.90G1-348[»]
3CD6X-ray2.75G1-348[»]
3CMAX-ray2.80G1-348[»]
3CMEX-ray2.95G1-348[»]
3CPWX-ray2.70G1-348[»]
3CXCX-ray3.00G1-348[»]
3G4SX-ray3.20G1-348[»]
3G6EX-ray2.70G1-348[»]
3G71X-ray2.85G1-348[»]
3I55X-ray3.11G1-348[»]
3I56X-ray2.90G1-348[»]
ProteinModelPortalP15825.
SMRP15825. Positions 7-132.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3128417.
GenomeReviewsGene locus rrnAC1417 in contig AY596297_GR.
KEGGhma:rrnAC1417.
NMPDRfig|272569.1.peg.1316.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG731512.
OMAYVFLFDL.
PhylomeDBP15825.
ProtClustDBPRK04019.

Enzyme and pathway databases

BioCycHMAR272569:RRNAC1417-MONOMER.

Family and domain databases

HAMAPMF_00280. Ribosomal_L10e_acid.
[Tree]
InterProIPR001790. Ribosomal_L10/acidic_P0.
IPR013522. Ribosomal_L10_N_arc.
IPR022909. Ribosome_L10_arc.
[Graphical view]
Gene3DG3DSA:1.10.10.380. Ribosomal_L10_N_arc. 2 hits.
KOK02864.
PfamPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRLA0_HALMA
AccessionPrimary (citable) accession number: P15825
Secondary accession number(s): Q5V2A8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 4, 2005
Last modified: December 14, 2011
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents