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P20279 (RL3_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 107. 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

Names and origin

Protein namesRecommended name:
50S ribosomal protein L3
Alternative name(s):
Hl1
Hmal3
Gene names
Name:rpl3
Ordered Locus Names:rrnAC1611
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit By similarity. HAMAP-Rule MF_01325_A

Subunit structure

Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L24e. Interacts weakly with protein L13. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Sequence similarities

Belongs to the ribosomal protein L3P family.

Ontologies

Keywords
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_01325_A
Chain2 – 33833750S ribosomal protein L3 HAMAP-Rule MF_01325_A
PRO_0000077207

Experimental info

Sequence conflict3111R → P in AAA86859. Ref.1
Sequence conflict3121F → FF AA sequence Ref.1

Secondary structure

............................................................ 338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20279 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 996D3BE503F4DBD4

FASTA33837,341
        10         20         30         40         50         60 
MPQPSRPRKG SLGFGPRKRS TSETPRFNSW PSDDGQPGVQ GFAGYKAGMT HVVLVNDEPN 

        70         80         90        100        110        120 
SPREGMEETV PVTVIETPPM RAVALRAYED TPYGQRPLTE VWTDEFHSEL DRTLDVPEDH 

       130        140        150        160        170        180 
DPDAAEEQIR DAHEAGDLGD LRLITHTVPD AVPSVPKKKP DVMETRVGGG SVSDRLDHAL 

       190        200        210        220        230        240 
DIVEDGGEHA MNDIFRAGEY ADVAGVTKGK GTQGPVKRWG VQKRKGKHAR QGWRRRIGNL 

       250        260        270        280        290        300 
GPWNPSRVRS TVPQQGQTGY HQRTELNKRL IDIGEGDEPT VDGGFVNYGE VDGPYTLVKG 

       310        320        330 
SVPGPDKRLV RFRPAVRPND QPRLDPEVRY VSNESNQG 

« Hide

References

« Hide 'large scale' references
[1]"Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui."
Arndt E., Kroemer W., Hatakeyama T.
J. Biol. Chem. 265:3034-3039(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[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]"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] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05222 Genomic DNA. Translation: AAA86859.1.
AY596297 Genomic DNA. Translation: AAV46528.1.
PIRR5HS3L. C35063.
RefSeqYP_136234.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40B2-338[»]
1JJ2X-ray2.40B2-338[»]
1K73X-ray3.01D2-338[»]
1K8AX-ray3.00D2-338[»]
1K9MX-ray3.00D2-338[»]
1KC8X-ray3.01D2-338[»]
1KD1X-ray3.00D2-338[»]
1KQSX-ray3.10B2-338[»]
1M1KX-ray3.20D2-338[»]
1M90X-ray2.80D2-338[»]
1ML5electron microscopy14.00e2-311[»]
e312-338[»]
1N8RX-ray3.00D2-338[»]
1NJIX-ray3.00D2-338[»]
1Q7YX-ray3.20D2-338[»]
1Q81X-ray2.95D2-338[»]
1Q82X-ray2.98D2-338[»]
1Q86X-ray3.00D2-338[»]
1QVFX-ray3.10B2-338[»]
1QVGX-ray2.90B2-338[»]
1S72X-ray2.40B1-338[»]
1VQ4X-ray2.70B1-338[»]
1VQ5X-ray2.60B1-338[»]
1VQ6X-ray2.70B1-338[»]
1VQ7X-ray2.50B1-338[»]
1VQ8X-ray2.20B1-338[»]
1VQ9X-ray2.40B1-338[»]
1VQKX-ray2.30B1-338[»]
1VQLX-ray2.30B1-338[»]
1VQMX-ray2.30B1-338[»]
1VQNX-ray2.40B1-338[»]
1VQOX-ray2.20B1-338[»]
1VQPX-ray2.25B1-338[»]
1W2BX-ray3.50B2-338[»]
1YHQX-ray2.40B1-338[»]
1YI2X-ray2.65B1-338[»]
1YIJX-ray2.60B1-338[»]
1YITX-ray2.80B1-338[»]
1YJ9X-ray2.90B1-338[»]
1YJNX-ray3.00B1-338[»]
1YJWX-ray2.90B1-338[»]
2B9PX-ray6.46E2-338[»]
2OTJX-ray2.90B1-338[»]
2OTLX-ray2.70B2-338[»]
2QA4X-ray3.00B1-338[»]
2QEXX-ray2.90B1-338[»]
3CC2X-ray2.40B1-338[»]
3CC4X-ray2.70B1-338[»]
3CC7X-ray2.70B1-338[»]
3CCEX-ray2.75B1-338[»]
3CCJX-ray2.70B1-338[»]
3CCLX-ray2.90B1-338[»]
3CCMX-ray2.55B1-338[»]
3CCQX-ray2.90B1-338[»]
3CCRX-ray3.00B1-338[»]
3CCSX-ray2.95B1-338[»]
3CCUX-ray2.80B1-338[»]
3CCVX-ray2.90B1-338[»]
3CD6X-ray2.75B1-338[»]
3CMAX-ray2.80B1-338[»]
3CMEX-ray2.95B1-338[»]
3CPWX-ray2.70B1-338[»]
3CXCX-ray3.00B2-338[»]
3G4SX-ray3.20B2-338[»]
3G6EX-ray2.70B2-338[»]
3G71X-ray2.85B2-338[»]
3I55X-ray3.11B1-338[»]
3I56X-ray2.90B1-338[»]
3OW2X-ray2.70B2-338[»]
4HUBX-ray2.40B1-338[»]
ProteinModelPortalP20279.
SMRP20279. Positions 2-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC1611.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46528; AAV46528; rrnAC1611.
GeneID3128366.
KEGGhma:rrnAC1611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0087.
HOGENOMHOG000107320.
KOK02906.
OMAEITPKGG.
ProtClustDBPRK04231.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1467-MONOMER.

Family and domain databases

HAMAPMF_01325_A. Ribosomal_L3_A.
InterProIPR000597. Ribosomal_L3.
IPR019928. Ribosomal_L3_arc.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMSSF50447. SSF50447. 1 hit.
TIGRFAMsTIGR03626. L3_arch. 1 hit.
PROSITEPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20279.

Entry information

Entry nameRL3_HALMA
AccessionPrimary (citable) accession number: P20279
Secondary accession number(s): Q5V1S4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 107 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references