50S ribosomal protein L31e - Haloarcula marismortui

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Reviewed, UniProtKB/Swiss-Prot P18138 (RL31_HALMA)

Last modified November 3, 2009. Version 79. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
    50S ribosomal protein L31e
Alternative name(s):
    L34
    Hl30

Gene names

Name:	rpl31e
Ordered Locus Names:	rrnAC3113

Organism

Haloarcula marismortui (Halobacterium marismortui) [Complete proteome] [HAMAP]

Taxonomic identifier

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula

Protein attributes

Sequence length	92 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	Binds to the 23S rRNA. Located at the polypeptide exit tunnel on the outside of the subunit. HAMAP MF_00410
Subunit structure	Part of the 50S ribosomal subunit. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Sequence similarities	Belongs to the ribosomal protein L31e family.

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation
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

1

Removed Ref.3

Chain

91

50S ribosomal protein L31e HAMAP MF_00410

PRO_0000153791

Amino acid modifications

Modified residue

1

N-acetylserine HAMAP MF_00410

Secondary structure

1

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92

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P18138-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0FF505E03E8F6C4A
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92

10,367

        10         20         30         40         50         60 
MSASDFEERV VTIPLRDARA EPNHKRADKA MILIREHLAK HFSVDEDAVR LDPSINEAAW 

        70         80         90 
ARGRANTPSK IRVRAARFEE EGEAIVEAET AE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for an additional archaebacterial gene cluster in Halobacterium marismortui encoding ribosomal proteins HL46e and HL30." Bergmann U., Arndt E. Biochim. Biophys. Acta 1050:56-60(1990) [PubMed: 2207169] [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: 15520287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[3]	"Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacterium Halobacterium marismortui." Hatakeyama T., Hatakeyama T. Biochim. Biophys. Acta 1039:343-347(1990) [PubMed: 2198942] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-92.
[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: 10937989] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[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: 10937990] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[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: 11828326] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[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: 11483524] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[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: 12150912] [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.
[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: 12185246] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[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: 12860128] [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.
[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: 14561884] [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

X55007 Genomic DNA. Translation: CAA38751.1.
AY596297 Genomic DNA. Translation: AAV47824.1.

PIR

R5HSER. S13067.

RefSeq

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFK	X-ray	2.40	U	2-92	[»]
1JJ2	X-ray	2.40	W	2-92	[»]
1K73	X-ray	3.01	Y	2-92	[»]
1K8A	X-ray	3.00	Y	2-92	[»]
1K9M	X-ray	3.00	Y	2-92	[»]
1KC8	X-ray	3.01	Y	2-92	[»]
1KD1	X-ray	3.00	Y	2-92	[»]
1KQS	X-ray	3.10	W	2-92	[»]
1M1K	X-ray	3.20	Y	2-92	[»]
1M90	X-ray	2.80	Y	2-92	[»]
1N8R	X-ray	3.00	Y	2-92	[»]
1NJI	X-ray	3.00	Y	2-92	[»]
1Q7Y	X-ray	3.20	Y	2-92	[»]
1Q81	X-ray	2.95	Y	2-92	[»]
1Q82	X-ray	2.98	Y	2-92	[»]
1Q86	X-ray	3.00	Y	2-92	[»]
1QVF	X-ray	3.10	W	2-92	[»]
1QVG	X-ray	2.90	W	2-92	[»]
1S72	X-ray	2.40	X	1-92	[»]
1VQ4	X-ray	2.70	X	1-92	[»]
1VQ5	X-ray	2.60	X	1-92	[»]
1VQ6	X-ray	2.70	X	1-92	[»]
1VQ7	X-ray	2.50	X	1-92	[»]
1VQ8	X-ray	2.20	X	1-92	[»]
1VQ9	X-ray	2.40	X	1-92	[»]
1VQK	X-ray	2.30	X	1-92	[»]
1VQL	X-ray	2.30	X	1-92	[»]
1VQM	X-ray	2.30	X	1-92	[»]
1VQN	X-ray	2.40	X	1-92	[»]
1VQO	X-ray	2.20	X	1-92	[»]
1VQP	X-ray	2.25	X	1-92	[»]
1W2B	X-ray	3.50	W	2-91	[»]
1YHQ	X-ray	2.40	X	1-92	[»]
1YI2	X-ray	2.65	X	1-92	[»]
1YIJ	X-ray	2.60	X	1-92	[»]
1YIT	X-ray	2.80	X	1-92	[»]
1YJ9	X-ray	2.90	X	1-92	[»]
1YJN	X-ray	3.00	X	1-92	[»]
1YJW	X-ray	2.90	X	1-92	[»]
2OTJ	X-ray	2.90	X	1-92	[»]
2OTL	X-ray	2.70	X	1-92	[»]
2QA4	X-ray	3.00	X	1-92	[»]
2QEX	X-ray	2.90	X	1-92	[»]
3CC2	X-ray	2.40	X	1-92	[»]
3CC4	X-ray	2.70	X	1-92	[»]
3CC7	X-ray	2.70	X	1-92	[»]
3CCE	X-ray	2.75	X	1-92	[»]
3CCJ	X-ray	2.70	X	1-92	[»]
3CCL	X-ray	2.90	X	1-92	[»]
3CCM	X-ray	2.55	X	1-92	[»]
3CCQ	X-ray	2.90	X	1-92	[»]
3CCR	X-ray	3.00	X	1-92	[»]
3CCS	X-ray	2.95	X	1-92	[»]
3CCU	X-ray	2.80	X	1-92	[»]
3CCV	X-ray	2.90	X	1-92	[»]
3CD6	X-ray	2.75	X	1-92	[»]
3CMA	X-ray	2.80	X	1-92	[»]
3CME	X-ray	2.95	X	1-92	[»]
3CPW	X-ray	2.70	W	1-92	[»]
3CXC	X-ray	3.00	W	2-91	[»]
3G4S	X-ray	3.20	X	8-89	[»]
3G6E	X-ray	2.70	X	8-89	[»]
3G71	X-ray	2.85	X	8-89	[»]

ModBase

Genome annotation databases

GeneID

GenomeReviews

Gene locus rrnAC3113 in contig AY596297_GR.

KEGG

NMPDR

fig|272569.1.peg.2820.

Organism-specific databases

CMR

Phylogenomic databases

HOGENOM

OMA

Enzyme and pathway databases

BioCyc

HMAR272569:RRNAC3113-MON.

Family and domain databases

HAMAP

MF_00410.
[Tree]

InterPro

IPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
[Graphical view]

Gene3D

G3DSA:3.10.440.10. Ribosomal_L31e. 1 hit.

PANTHER

PTHR10956. Ribosomal_L31e. 1 hit.

Pfam

PF01198. Ribosomal_L31e. 1 hit.
[Graphical view]

ProDom

PD006030. Ribosomal_L31e. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS01144. RIBOSOMAL_L31E. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

RL31_HALMA

Accession

Primary (citable) accession number: P18138
Secondary accession number(s): Q5UY29

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents