50S ribosomal protein L3P - Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

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P20279 (RL3_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 93. 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 L3P

Alternative name(s):
Hl1
Hmal3

Gene names

Name:	rpl3p
Synonyms:	rpl3
Ordered Locus Names:	rrnAC1611

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	338 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 the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit By similarity. HAMAP MF_01325_A
Subunit structure	Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L24e. Interacts weakly with protein L13. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Sequence similarities	Belongs to the ribosomal protein L3P 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: InterPro
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 HAMAP MF_01325_A

Chain

2 – 338

337

50S ribosomal protein L3P HAMAP MF_01325_A

PRO_0000077207

Experimental info

Sequence conflict

311

R → P in AAA86859. Ref.1

Sequence conflict

312

F → FF AA sequence Ref.1

Secondary structure

338

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P20279 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 996D3BE503F4DBD4
Show »

FASTA

338

37,341

        10         20         30         40         50         60 
MPQPSRPRKG SLGFGPRKRS TSETPRFNSW PSDDGQPGVQ GFAGYKAGMT HVVLVNDEPN 

        70         80         90        100        110        120 
SPREGMEETV PVTVIETPPM RAVALRAYED TPYGQRPLTE VWTDEFHSEL DRTLDVPEDH 

       130        140        150        160        170        180 
DPDAAEEQIR DAHEAGDLGD LRLITHTVPD AVPSVPKKKP DVMETRVGGG SVSDRLDHAL 

       190        200        210        220        230        240 
DIVEDGGEHA MNDIFRAGEY ADVAGVTKGK GTQGPVKRWG VQKRKGKHAR QGWRRRIGNL 

       250        260        270        280        290        300 
GPWNPSRVRS TVPQQGQTGY HQRTELNKRL IDIGEGDEPT VDGGFVNYGE VDGPYTLVKG 

       310        320        330 
SVPGPDKRLV RFRPAVRPND QPRLDPEVRY VSNESNQG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui." Arndt E., Kroemer W., Hatakeyama T. J. Biol. Chem. 265:3034-3039(1990) [PubMed: 2406244] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[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 / 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: 10937989] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. 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: 10937990] [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: 11828326] [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: 11483524] [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: 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 / 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: 12185246] [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: 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 / 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: 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

EMBL
GenBank
DDBJ

J05222 Genomic DNA. Translation: AAA86859.1.
AY596297 Genomic DNA. Translation: AAV46528.1.

PIR

R5HS3L. C35063.

RefSeq

YP_136234.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFK	X-ray	2.40	B	2-338	[»]
1JJ2	X-ray	2.40	B	2-338	[»]
1K73	X-ray	3.01	D	2-338	[»]
1K8A	X-ray	3.00	D	2-338	[»]
1K9M	X-ray	3.00	D	2-338	[»]
1KC8	X-ray	3.01	D	2-338	[»]
1KD1	X-ray	3.00	D	2-338	[»]
1KQS	X-ray	3.10	B	2-338	[»]
1M1K	X-ray	3.20	D	2-338	[»]
1M90	X-ray	2.80	D	2-338	[»]
1N8R	X-ray	3.00	D	2-338	[»]
1NJI	X-ray	3.00	D	2-338	[»]
1Q7Y	X-ray	3.20	D	2-338	[»]
1Q81	X-ray	2.95	D	2-338	[»]
1Q82	X-ray	2.98	D	2-338	[»]
1Q86	X-ray	3.00	D	2-338	[»]
1QVF	X-ray	3.10	B	2-338	[»]
1QVG	X-ray	2.90	B	2-338	[»]
1S72	X-ray	2.40	B	1-338	[»]
1VQ4	X-ray	2.70	B	1-338	[»]
1VQ5	X-ray	2.60	B	1-338	[»]
1VQ6	X-ray	2.70	B	1-338	[»]
1VQ7	X-ray	2.50	B	1-338	[»]
1VQ8	X-ray	2.20	B	1-338	[»]
1VQ9	X-ray	2.40	B	1-338	[»]
1VQK	X-ray	2.30	B	1-338	[»]
1VQL	X-ray	2.30	B	1-338	[»]
1VQM	X-ray	2.30	B	1-338	[»]
1VQN	X-ray	2.40	B	1-338	[»]
1VQO	X-ray	2.20	B	1-338	[»]
1VQP	X-ray	2.25	B	1-338	[»]
1W2B	X-ray	3.50	B	2-338	[»]
1YHQ	X-ray	2.40	B	1-338	[»]
1YI2	X-ray	2.65	B	1-338	[»]
1YIJ	X-ray	2.60	B	1-338	[»]
1YIT	X-ray	2.80	B	1-338	[»]
1YJ9	X-ray	2.90	B	1-338	[»]
1YJN	X-ray	3.00	B	1-338	[»]
1YJW	X-ray	2.90	B	1-338	[»]
2OTJ	X-ray	2.90	B	1-338	[»]
2OTL	X-ray	2.70	B	2-338	[»]
2QA4	X-ray	3.00	B	1-338	[»]
2QEX	X-ray	2.90	B	1-338	[»]
3CC2	X-ray	2.40	B	1-338	[»]
3CC4	X-ray	2.70	B	1-338	[»]
3CC7	X-ray	2.70	B	1-338	[»]
3CCE	X-ray	2.75	B	1-338	[»]
3CCJ	X-ray	2.70	B	1-338	[»]
3CCL	X-ray	2.90	B	1-338	[»]
3CCM	X-ray	2.55	B	1-338	[»]
3CCQ	X-ray	2.90	B	1-338	[»]
3CCR	X-ray	3.00	B	1-338	[»]
3CCS	X-ray	2.95	B	1-338	[»]
3CCU	X-ray	2.80	B	1-338	[»]
3CCV	X-ray	2.90	B	1-338	[»]
3CD6	X-ray	2.75	B	1-338	[»]
3CMA	X-ray	2.80	B	1-338	[»]
3CME	X-ray	2.95	B	1-338	[»]
3CPW	X-ray	2.70	B	1-338	[»]
3CXC	X-ray	3.00	B	2-338	[»]
3G4S	X-ray	3.20	B	2-338	[»]
3G6E	X-ray	2.70	B	2-338	[»]
3G71	X-ray	2.85	B	2-338	[»]
3I55	X-ray	3.11	B	1-338	[»]
3I56	X-ray	2.90	B	1-338	[»]

ProteinModelPortal

P20279.

SMR

P20279. Positions 2-338.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3128366.

GenomeReviews

Gene locus rrnAC1611 in contig AY596297_GR.

KEGG

hma:rrnAC1611.

NMPDR

fig|272569.1.peg.1502.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG297464.

OMA

WGTKKLP.

PhylomeDB

P20279.

ProtClustDB

PRK04231.

Enzyme and pathway databases

BioCyc

HMAR272569:RRNAC1611-MONOMER.

Family and domain databases

HAMAP

MF_01325_A. Ribosomal_L3_A.
[Tree]

InterPro

IPR000597. Ribosomal_L3.
IPR019928. Ribosomal_L3_arc.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]

K02906.

Pfam

PF00297. Ribosomal_L3. 1 hit.
[Graphical view]

SUPFAM

SSF50447. Translat_factor. 1 hit.

TIGRFAMs

TIGR03626. L3_arch. 1 hit.

PROSITE

PS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL3_HALMA

Accession

Primary (citable) accession number: P20279
Secondary accession number(s): Q5V1S4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 93 of the entry and version 5 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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents