P20279 (RL3_HALMA) Reviewed, UniProtKB/Swiss-Prot

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

cellular organisms › Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula › Haloarcula marismortui

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-Rule 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: HAMAP
Cellular_component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
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

1

1

Removed HAMAP-Rule MF_01325_A

Chain

2 – 338

337

50S ribosomal protein L3P HAMAP-Rule MF_01325_A

PRO_0000077207

Experimental info

Sequence conflict

311

1

R → P in AAA86859. Ref.1

Sequence conflict

312

1

F → FF AA sequence Ref.1

Secondary structure

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338

Helix Strand Turn

Details...

Beta strand

12 – 14

3

Beta strand

35 – 39

5

Beta strand

42 – 55

14

Beta strand

59 – 61

3

Turn

62 – 65

4

Beta strand

66 – 76

11

Beta strand

80 – 91

12

Beta strand

94 – 102

9

Helix

110 – 112

3

Helix

122 – 135

14

Beta strand

138 – 146

9

Helix

149 – 151

3

Beta strand

153 – 155

3

Beta strand

162 – 168

7

Helix

172 – 185

14

Beta strand

187 – 189

3

Turn

192 – 194

3

Beta strand

200 – 206

7

Beta strand

209 – 213

5

Helix

215 – 219

5

Helix

226 – 229

4

Beta strand

230 – 232

3

Beta strand

234 – 236

3

Beta strand

243 – 247

5

Beta strand

250 – 252

3

Beta strand

256 – 259

4

Beta strand

262 – 279

18

Turn

286 – 288

3

Beta strand

293 – 300

8

Beta strand

309 – 314

6

Beta strand

328 – 331

4

Sequences

	Sequence		Length	Mass (Da)
	P20279 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 996D3BE503F4DBD4	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

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] [Europe PMC] [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] [Europe PMC] [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] [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.
[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]	"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.
[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.
+	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	[»]
3OW2	X-ray	2.70	B	2-338	[»]

ProteinModelPortal

P20279.

SMR

P20279. Positions 2-338.

ModBase

Search...

Protein-protein interaction databases

STRING

272569.rrnAC1611.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV46528; AAV46528; rrnAC1611.

GeneID

3128366.

KEGG

hma:rrnAC1611.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0087.

HOGENOM

HOG000107320.

KO

K02906.

OMA

GFHQRTE.

ProtClustDB

PRK04231.

Enzyme and pathway databases

BioCyc

HMAR272569:GJDH-1467-MONOMER.

Family and domain databases

HAMAP

MF_01325_A. Ribosomal_L3_A.

InterPro

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

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...

Other

EvolutionaryTrace

P20279.

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:	May 1, 2013
This is version 102 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program