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Protein

50S ribosomal protein L44e

Gene

rpl44e

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111ZincCurated
Metal bindingi14 – 141ZincCurated
Metal bindingi71 – 711ZincCurated
Metal bindingi74 – 741ZincCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri11 – 7464C4-typeCuratedAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, RNA-binding, rRNA-binding, tRNA-binding, Zinc

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-3155-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L44eUniRule annotation
Alternative name(s):
HLA
La
Gene namesi
Name:rpl44eUniRule annotation
Ordered Locus Names:rrnAC3514
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
ProteomesiUP000001169 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 929250S ribosomal protein L44ePRO_0000149150Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts weakly with protein L15e. Binds the E site tRNA.UniRule annotation4 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC3514.

Structurei

Secondary structure

1
92
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1110Combined sources
Turni12 – 154Combined sources
Beta strandi16 – 249Combined sources
Beta strandi32 – 343Combined sources
Helixi35 – 439Combined sources
Beta strandi45 – 473Combined sources
Helixi50 – 534Combined sources
Beta strandi61 – 633Combined sources
Beta strandi67 – 715Combined sources
Turni72 – 743Combined sources
Beta strandi77 – 793Combined sources
Beta strandi89 – 913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4ADXelectron microscopy6.6031-92[»]
4V9FX-ray2.4031-92[»]
ProteinModelPortaliP32411.
SMRiP32411. Positions 1-92.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32411.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L44e family.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri11 – 7464C4-typeCuratedAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG1631.
HOGENOMiHOG000224988.
KOiK02929.
OMAiYRGYPRP.

Family and domain databases

Gene3Di3.10.450.80. 1 hit.
HAMAPiMF_01476. Ribosomal_L44e.
InterProiIPR000552. Ribosomal_L44e.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR10369. PTHR10369. 1 hit.
PfamiPF00935. Ribosomal_L44. 1 hit.
[Graphical view]
ProDomiPD002841. Ribosomal_L44e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01172. RIBOSOMAL_L44E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQMPRRFNTY CPHCNEHQEH EVEKVRSGRQ TGMKWIDRQR ERNSGIGNDG
60 70 80 90
KFSKVPGGDK PTKKTDLKYR CGECGKAHLR EGWRAGRLEF QE
Length:92
Mass (Da):10,791
Last modified:October 1, 1993 - v1
Checksum:i14197AA6AE7AC07A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY596297 Genomic DNA. Translation: AAV48183.1.
PIRiS33790.
RefSeqiWP_004593654.1. NC_006396.1.
YP_137889.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV48183; AAV48183; rrnAC3514.
GeneIDi23805216.
3129532.
KEGGihma:rrnAC3514.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY596297 Genomic DNA. Translation: AAV48183.1.
PIRiS33790.
RefSeqiWP_004593654.1. NC_006396.1.
YP_137889.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4ADXelectron microscopy6.6031-92[»]
4V9FX-ray2.4031-92[»]
ProteinModelPortaliP32411.
SMRiP32411. Positions 1-92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC3514.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV48183; AAV48183; rrnAC3514.
GeneIDi23805216.
3129532.
KEGGihma:rrnAC3514.

Phylogenomic databases

eggNOGiCOG1631.
HOGENOMiHOG000224988.
KOiK02929.
OMAiYRGYPRP.

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-3155-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32411.

Family and domain databases

Gene3Di3.10.450.80. 1 hit.
HAMAPiMF_01476. Ribosomal_L44e.
InterProiIPR000552. Ribosomal_L44e.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR10369. PTHR10369. 1 hit.
PfamiPF00935. Ribosomal_L44. 1 hit.
[Graphical view]
ProDomiPD002841. Ribosomal_L44e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01172. RIBOSOMAL_L44E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiRL44E_HALMA
AccessioniPrimary (citable) accession number: P32411
Secondary accession number(s): Q5UX20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 27, 2015
This is version 101 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.