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P32411 (RL44E_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 94. 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 L44e
Alternative name(s):
HLA
La
Gene names
Name:rpl44e
Ordered Locus Names:rrnAC3514
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 length92 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the 23S rRNA. Binds deacetylated tRNA in the E site; when the tRNA binds a stretch of 7 amino acids are displaced to allow binding. HAMAP-Rule MF_01476

Cofactor

Binds 1 zinc ion per subunit Probable. Ref.3

Subunit structure

Part of the 50S ribosomal subunit. Interacts weakly with protein L15e. Binds the E site tRNA. Ref.1 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 L44e family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 929250S ribosomal protein L44e HAMAP-Rule MF_01476
PRO_0000149150

Regions

Zinc finger11 – 7464C4-type Probable

Sites

Metal binding111Zinc Probable
Metal binding141Zinc Probable
Metal binding711Zinc Probable
Metal binding741Zinc Probable

Secondary structure

..................... 92
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32411 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 14197AA6AE7AC07A

FASTA9210,791
        10         20         30         40         50         60 
MQMPRRFNTY CPHCNEHQEH EVEKVRSGRQ TGMKWIDRQR ERNSGIGNDG KFSKVPGGDK 

        70         80         90 
PTKKTDLKYR CGECGKAHLR EGWRAGRLEF QE 

« Hide

References

« Hide 'large scale' references
[1]"HL35e and HLA: primary structure of two very basic and cysteine-rich ribosomal proteins from Haloarcula marismortui."
Bergmann U., Wittmann-Liebold B.
Biochim. Biophys. Acta 1173:195-200(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, SUBUNIT.
[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, SUBUNIT, RRNA-BINDING, PROBABLE COFACTOR.
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, RRNA-BINDING, TRNA-BINDING.
[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
AY596297 Genomic DNA. Translation: AAV48183.1.
PIRS33790.
RefSeqYP_137889.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40Z1-92[»]
1JJ2X-ray2.4021-92[»]
1K73X-ray3.0141-92[»]
1K8AX-ray3.0041-92[»]
1K9MX-ray3.0041-92[»]
1KC8X-ray3.0141-92[»]
1KD1X-ray3.0041-92[»]
1KQSX-ray3.1021-92[»]
1M1KX-ray3.2041-92[»]
1M90X-ray2.8041-92[»]
1N8RX-ray3.0041-92[»]
1NJIX-ray3.0041-92[»]
1Q7YX-ray3.2041-92[»]
1Q81X-ray2.9541-92[»]
1Q82X-ray2.9841-92[»]
1Q86X-ray3.0041-92[»]
1QVFX-ray3.1021-92[»]
1QVGX-ray2.9021-92[»]
1S72X-ray2.4031-92[»]
1VQ4X-ray2.7031-92[»]
1VQ5X-ray2.6031-92[»]
1VQ6X-ray2.7031-92[»]
1VQ7X-ray2.5031-92[»]
1VQ8X-ray2.2031-92[»]
1VQ9X-ray2.4031-92[»]
1VQKX-ray2.3031-92[»]
1VQLX-ray2.3031-92[»]
1VQMX-ray2.3031-92[»]
1VQNX-ray2.4031-92[»]
1VQOX-ray2.2031-92[»]
1VQPX-ray2.2531-92[»]
1W2BX-ray3.5021-92[»]
1YHQX-ray2.4031-92[»]
1YI2X-ray2.6531-92[»]
1YIJX-ray2.6031-92[»]
1YITX-ray2.8031-92[»]
1YJ9X-ray2.9031-92[»]
1YJNX-ray3.0031-92[»]
1YJWX-ray2.9031-92[»]
2OTJX-ray2.9031-92[»]
2OTLX-ray2.7031-92[»]
2QA4X-ray3.0031-92[»]
2QEXX-ray2.9031-92[»]
3CC2X-ray2.4031-92[»]
3CC4X-ray2.7031-92[»]
3CC7X-ray2.7031-92[»]
3CCEX-ray2.7531-92[»]
3CCJX-ray2.7031-92[»]
3CCLX-ray2.9031-92[»]
3CCMX-ray2.5531-92[»]
3CCQX-ray2.9031-92[»]
3CCRX-ray3.0031-92[»]
3CCSX-ray2.9531-92[»]
3CCUX-ray2.8031-92[»]
3CCVX-ray2.9031-92[»]
3CD6X-ray2.7531-92[»]
3CMAX-ray2.8031-92[»]
3CMEX-ray2.9531-92[»]
3CPWX-ray2.7021-92[»]
3CXCX-ray3.0021-92[»]
3G4SX-ray3.2031-92[»]
3G6EX-ray2.7031-92[»]
3G71X-ray2.8531-92[»]
3I55X-ray3.1131-92[»]
3I56X-ray2.9031-92[»]
3OW2X-ray2.7021-92[»]
4HUBX-ray2.4031-92[»]
ProteinModelPortalP32411.
SMRP32411. Positions 1-92.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC3514.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV48183; AAV48183; rrnAC3514.
GeneID3129532.
KEGGhma:rrnAC3514.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1631.
HOGENOMHOG000224988.
KOK02929.
OMAYRGYPRP.
ProtClustDBPRK05767.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-3155-MONOMER.

Family and domain databases

Gene3D3.10.450.80. 1 hit.
HAMAPMF_01476. Ribosomal_L44e.
InterProIPR000552. Ribosomal_L44e.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERPTHR10369. PTHR10369. 1 hit.
PfamPF00935. Ribosomal_L44. 1 hit.
[Graphical view]
ProDomPD002841. Ribosomal_L44e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF57829. SSF57829. 1 hit.
PROSITEPS01172. RIBOSOMAL_L44E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32411.

Entry information

Entry nameRL44E_HALMA
AccessionPrimary (citable) accession number: P32411
Secondary accession number(s): Q5UX20
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: February 19, 2014
This is version 94 of the entry and version 1 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