50S ribosomal protein L21e - Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

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P12734 (RL21_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
50S ribosomal protein L21e

Alternative name(s):
Hl31

Gene names

Name:	rpl21e
Ordered Locus Names:	rrnAC0260

Organism

Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]

Taxonomic identifier

272569 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula ›

Protein attributes

Sequence length	96 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is one of 5 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit, stabilizing the orientation of adjacent RNA domains. HAMAP-Rule MF_00369
Subunit structure	Part of the 50S ribosomal subunit. Interacts with protein L18 and binds the 5S rRNA. Has been cross-linked to L18. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Sequence similarities	Belongs to the ribosomal protein L21e family.

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 96

50S ribosomal protein L21e HAMAP-Rule MF_00369

PRO_0000149686

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P12734 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DE6DE036844EF1F2
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FASTA

10,548

        10         20         30         40         50         60 
MPSSNGPLEG TRGKLKNKPR DRGTSPPQRA VEEFDDGEKV HLKIDPSVPN GRFHPRFDGQ 

        70         80         90 
TGTVEGKQGD AYKVDIVDGG KEKTIIVTAA HLRRQE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"Complete amino acid sequences of the ribosomal proteins L25, L29 and L31 from the archaebacterium Halobacterium marismortui." Hatakeyama T., Kimura M. Eur. J. Biochem. 172:703-711(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-96.
[3]	"Localization of proteins HL29 and HL31 from Haloarcula marismortui within the 50 S ribosomal subunit by chemical crosslinking." Bergmann U., Wittmann-Liebold B. J. Mol. Biol. 232:693-700(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO L18.
[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]	"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.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY596297 Genomic DNA. Translation: AAV45317.1.

PIR

R5HS31. S00370.

RefSeq

YP_135023.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFK	X-ray	2.40	N	2-96	[»]
1JJ2	X-ray	2.40	P	2-96	[»]
1K73	X-ray	3.01	R	2-96	[»]
1K8A	X-ray	3.00	R	2-96	[»]
1K9M	X-ray	3.00	R	2-96	[»]
1KC8	X-ray	3.01	R	2-96	[»]
1KD1	X-ray	3.00	R	2-96	[»]
1KQS	X-ray	3.10	P	2-96	[»]
1M1K	X-ray	3.20	R	2-96	[»]
1M90	X-ray	2.80	R	2-96	[»]
1N8R	X-ray	3.00	R	2-96	[»]
1NJI	X-ray	3.00	R	2-96	[»]
1Q7Y	X-ray	3.20	R	2-96	[»]
1Q81	X-ray	2.95	R	2-96	[»]
1Q82	X-ray	2.98	R	2-96	[»]
1Q86	X-ray	3.00	R	2-96	[»]
1QVF	X-ray	3.10	P	2-96	[»]
1QVG	X-ray	2.90	P	2-96	[»]
1S72	X-ray	2.40	Q	1-96	[»]
1VQ4	X-ray	2.70	Q	1-96	[»]
1VQ5	X-ray	2.60	Q	1-96	[»]
1VQ6	X-ray	2.70	Q	1-96	[»]
1VQ7	X-ray	2.50	Q	1-96	[»]
1VQ8	X-ray	2.20	Q	1-96	[»]
1VQ9	X-ray	2.40	Q	1-96	[»]
1VQK	X-ray	2.30	Q	1-96	[»]
1VQL	X-ray	2.30	Q	1-96	[»]
1VQM	X-ray	2.30	Q	1-96	[»]
1VQN	X-ray	2.40	Q	1-96	[»]
1VQO	X-ray	2.20	Q	1-96	[»]
1VQP	X-ray	2.25	Q	1-96	[»]
1W2B	X-ray	3.50	P	2-95	[»]
1YHQ	X-ray	2.40	Q	1-96	[»]
1YI2	X-ray	2.65	Q	1-96	[»]
1YIJ	X-ray	2.60	Q	1-96	[»]
1YIT	X-ray	2.80	Q	1-96	[»]
1YJ9	X-ray	2.90	Q	1-96	[»]
1YJN	X-ray	3.00	Q	1-96	[»]
1YJW	X-ray	2.90	Q	1-96	[»]
2OTJ	X-ray	2.90	Q	1-96	[»]
2OTL	X-ray	2.70	Q	1-96	[»]
2QA4	X-ray	3.00	Q	1-96	[»]
2QEX	X-ray	2.90	Q	1-96	[»]
3CC2	X-ray	2.40	Q	1-96	[»]
3CC4	X-ray	2.70	Q	1-96	[»]
3CC7	X-ray	2.70	Q	1-96	[»]
3CCE	X-ray	2.75	Q	1-96	[»]
3CCJ	X-ray	2.70	Q	1-96	[»]
3CCL	X-ray	2.90	Q	1-96	[»]
3CCM	X-ray	2.55	Q	1-96	[»]
3CCQ	X-ray	2.90	Q	1-96	[»]
3CCR	X-ray	3.00	Q	1-96	[»]
3CCS	X-ray	2.95	Q	1-96	[»]
3CCU	X-ray	2.80	Q	1-96	[»]
3CCV	X-ray	2.90	Q	1-96	[»]
3CD6	X-ray	2.75	Q	1-96	[»]
3CMA	X-ray	2.80	Q	1-96	[»]
3CME	X-ray	2.95	Q	1-96	[»]
3CPW	X-ray	2.70	P	1-96	[»]
3CXC	X-ray	3.00	P	2-95	[»]
3G4S	X-ray	3.20	Q	2-96	[»]
3G6E	X-ray	2.70	Q	2-96	[»]
3G71	X-ray	2.85	Q	2-96	[»]
3I55	X-ray	3.11	Q	1-96	[»]
3I56	X-ray	2.90	Q	1-96	[»]
3OW2	X-ray	2.70	P	2-96	[»]

ProteinModelPortal

P12734.

SMR

P12734. Positions 2-96.

ModBase

Search...

Protein-protein interaction databases

STRING

272569.rrnAC0260.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV45317; AAV45317; rrnAC0260.

GeneID

3129654.

KEGG

hma:rrnAC0260.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG2139.

HOGENOM

HOG000106438.

K02889.

OMA

AYKVDIV.

ProtClustDB

PRK04306.

Enzyme and pathway databases

BioCyc

HMAR272569:GJDH-236-MONOMER.

Family and domain databases

HAMAP

MF_00369. Ribosomal_L21e.

InterPro

IPR001147. Ribosomal_L21e.
IPR022856. Ribosomal_L21e_arc.
IPR018259. Ribosomal_L21e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]

Pfam

PF01157. Ribosomal_L21e. 1 hit.
[Graphical view]

SUPFAM

SSF50104. Transl_SH3_like. 1 hit.

PROSITE

PS01171. RIBOSOMAL_L21E. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P12734.

Entry information

Entry name

RL21_HALMA

Accession

Primary (citable) accession number: P12734
Secondary accession number(s): Q5V585

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents