50S ribosomal protein L24P - Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

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P10972 (RL24_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. 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 L24P

Alternative name(s):
Hl15
Hl16
Hmal24

Gene names

Name:	rpl24p
Ordered Locus Names:	rrnAC1601

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	120 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

One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit By similarity. HAMAP-Rule MF_01326_A

Stabilizes the tertiary rRNA structure within the 23S rRNA domain (domain I) to which it binds. Located at the polypeptide exit tunnel on the outside of the subunit. HAMAP-Rule MF_01326_A

Subunit structure

Part of the 50S ribosomal subunit. Interacts weakly with protein L4. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the ribosomal protein L24P 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	large ribosomal subunit Inferred from electronic annotation. Source: InterPro
Molecular_function	rRNA binding Inferred from electronic annotation. Source: HAMAP 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.3 Ref.4

Chain

2 – 120

119

50S ribosomal protein L24P HAMAP-Rule MF_01326_A

PRO_0000130767

Experimental info

Sequence conflict

H → R AA sequence Ref.3

Secondary structure

120

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P10972 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BDEEF21DE1587096
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FASTA

120

13,648

        10         20         30         40         50         60 
MSKQPDKQRK SQRRAPLHER HKQVRATLSA DLREEYGQRN VRVNAGDTVE VLRGDFAGEE 

        70         80         90        100        110        120 
GEVINVDLDK AVIHVEDVTL EKTDGEEVPR PLDTSNVRVT DLDLEDEKRE ARLESEDDSA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of four genes encoding ribosomal proteins from the 'S10 and spectinomycin' operon equivalent region in the archaebacterium Halobacterium marismortui." Arndt E. FEBS Lett. 267:193-198(1990) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[3]	"The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui." Hatakeyama T., Hatakeyama T., Kimura M. FEBS Lett. 240:21-28(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-120.
[4]	"Extended N-terminal sequencing of proteins of archaebacterial ribosomes blotted from two-dimensional gels onto glass fiber and poly(vinylidene difluoride) membrane." Walsh M.J., McDougall J., Wittmann-Liebold B. Biochemistry 27:6867-6876(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-18.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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

X55311 Genomic DNA. Translation: CAA39019.1.
AY596297 Genomic DNA. Translation: AAV46518.1.

PIR

R5HS24. S10735.

RefSeq

YP_136224.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFK	X-ray	2.40	Q	2-120	[»]
1JJ2	X-ray	2.40	S	2-120	[»]
1K73	X-ray	3.01	U	2-120	[»]
1K8A	X-ray	3.00	U	2-120	[»]
1K9M	X-ray	3.00	U	2-120	[»]
1KC8	X-ray	3.01	U	2-120	[»]
1KD1	X-ray	3.00	U	2-120	[»]
1KQS	X-ray	3.10	S	2-120	[»]
1M1K	X-ray	3.20	U	2-120	[»]
1M90	X-ray	2.80	U	2-120	[»]
1N8R	X-ray	3.00	U	2-120	[»]
1NJI	X-ray	3.00	U	2-120	[»]
1Q7Y	X-ray	3.20	U	2-120	[»]
1Q81	X-ray	2.95	U	2-120	[»]
1Q82	X-ray	2.98	U	2-120	[»]
1Q86	X-ray	3.00	U	2-120	[»]
1QVF	X-ray	3.10	S	2-120	[»]
1QVG	X-ray	2.90	S	2-120	[»]
1S72	X-ray	2.40	T	1-120	[»]
1VQ4	X-ray	2.70	T	1-120	[»]
1VQ5	X-ray	2.60	T	1-120	[»]
1VQ6	X-ray	2.70	T	1-120	[»]
1VQ7	X-ray	2.50	T	1-120	[»]
1VQ8	X-ray	2.20	T	1-120	[»]
1VQ9	X-ray	2.40	T	1-120	[»]
1VQK	X-ray	2.30	T	1-120	[»]
1VQL	X-ray	2.30	T	1-120	[»]
1VQM	X-ray	2.30	T	1-120	[»]
1VQN	X-ray	2.40	T	1-120	[»]
1VQO	X-ray	2.20	T	1-120	[»]
1VQP	X-ray	2.25	T	1-120	[»]
1W2B	X-ray	3.50	S	2-119	[»]
1YHQ	X-ray	2.40	T	1-120	[»]
1YI2	X-ray	2.65	T	1-120	[»]
1YIJ	X-ray	2.60	T	1-120	[»]
1YIT	X-ray	2.80	T	1-120	[»]
1YJ9	X-ray	2.90	T	1-120	[»]
1YJN	X-ray	3.00	T	1-120	[»]
1YJW	X-ray	2.90	T	1-120	[»]
2OTJ	X-ray	2.90	T	1-120	[»]
2OTL	X-ray	2.70	T	1-120	[»]
2QA4	X-ray	3.00	T	1-120	[»]
2QEX	X-ray	2.90	T	1-120	[»]
3CC2	X-ray	2.40	T	1-120	[»]
3CC4	X-ray	2.70	T	1-120	[»]
3CC7	X-ray	2.70	T	1-120	[»]
3CCE	X-ray	2.75	T	1-120	[»]
3CCJ	X-ray	2.70	T	1-120	[»]
3CCL	X-ray	2.90	T	1-120	[»]
3CCM	X-ray	2.55	T	1-120	[»]
3CCQ	X-ray	2.90	T	1-120	[»]
3CCR	X-ray	3.00	T	1-120	[»]
3CCS	X-ray	2.95	T	1-120	[»]
3CCU	X-ray	2.80	T	1-120	[»]
3CCV	X-ray	2.90	T	1-120	[»]
3CD6	X-ray	2.75	T	1-120	[»]
3CMA	X-ray	2.80	T	1-120	[»]
3CME	X-ray	2.95	T	1-120	[»]
3CPW	X-ray	2.70	S	1-120	[»]
3CXC	X-ray	3.00	S	2-119	[»]
3G4S	X-ray	3.20	T	2-120	[»]
3G6E	X-ray	2.70	T	2-120	[»]
3G71	X-ray	2.85	T	2-120	[»]
3I55	X-ray	3.11	T	1-120	[»]
3I56	X-ray	2.90	T	1-120	[»]
3OW2	X-ray	2.70	S	2-120	[»]

ProteinModelPortal

P10972.

SMR

P10972. Positions 2-120.

ModBase

Search...

Protein-protein interaction databases

STRING

272569.rrnAC1601.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV46518; AAV46518; rrnAC1601.

GeneID

3128440.

KEGG

hma:rrnAC1601.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0198.

HOGENOM

HOG000216571.

K02895.

OMA

VRIMRGD.

ProtClustDB

PRK01191.

Enzyme and pathway databases

BioCyc

HMAR272569:GJDH-1457-MONOMER.

Family and domain databases

Gene3D

2.30.30.30. 1 hit.

HAMAP

MF_01326_A. Ribosomal_L24_A.

InterPro

IPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR005825. Ribosomal_L24/26_CS.
IPR005756. Ribosomal_L26/L24P_euk/arc.
IPR008991. Translation_prot_SH3-like.
[Graphical view]

PANTHER

PTHR11143. PTHR11143. 1 hit.

Pfam

PF00467. KOW. 1 hit.
[Graphical view]

SMART

SM00739. KOW. 1 hit.
[Graphical view]

SUPFAM

SSF50104. Transl_SH3_like. 1 hit.

TIGRFAMs

TIGR01080. rplX_A_E. 1 hit.

PROSITE

PS01108. RIBOSOMAL_L24. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P10972.

Entry information

Entry name

RL24_HALMA

Accession

Primary (citable) accession number: P10972
Secondary accession number(s): Q5V1T4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 112 of the entry and version 3 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

Experimental info

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