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Protein

50S ribosomal protein L3

Gene

rpl3

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L3
Alternative name(s):
Hl1
Hmal3
Gene namesi
Name:rpl3
Ordered Locus Names:rrnAC1611
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
Proteomesi
  • UP000001169 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000772072 – 33850S ribosomal protein L3Add BLAST337

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L24e. Interacts weakly with protein L13.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1611.

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 14Combined sources3
Beta strandi35 – 39Combined sources5
Beta strandi42 – 55Combined sources14
Beta strandi59 – 61Combined sources3
Turni62 – 65Combined sources4
Beta strandi66 – 76Combined sources11
Beta strandi80 – 91Combined sources12
Beta strandi94 – 102Combined sources9
Helixi110 – 112Combined sources3
Helixi122 – 135Combined sources14
Beta strandi138 – 146Combined sources9
Helixi149 – 151Combined sources3
Beta strandi153 – 155Combined sources3
Beta strandi162 – 168Combined sources7
Helixi172 – 185Combined sources14
Beta strandi187 – 189Combined sources3
Turni192 – 194Combined sources3
Beta strandi200 – 206Combined sources7
Beta strandi209 – 213Combined sources5
Helixi215 – 219Combined sources5
Helixi226 – 229Combined sources4
Beta strandi230 – 232Combined sources3
Beta strandi234 – 236Combined sources3
Beta strandi243 – 247Combined sources5
Beta strandi250 – 252Combined sources3
Beta strandi256 – 259Combined sources4
Beta strandi262 – 279Combined sources18
Turni286 – 288Combined sources3
Beta strandi293 – 300Combined sources8
Beta strandi309 – 314Combined sources6
Beta strandi328 – 331Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40B2-338[»]
1JJ2X-ray2.40B2-338[»]
1K73X-ray3.01D2-338[»]
1K8AX-ray3.00D2-338[»]
1K9MX-ray3.00D2-338[»]
1KC8X-ray3.01D2-338[»]
1KD1X-ray3.00D2-338[»]
1KQSX-ray3.10B2-338[»]
1M1KX-ray3.20D2-338[»]
1M90X-ray2.80D2-338[»]
1ML5electron microscopy14.00e2-311[»]
e312-338[»]
1N8RX-ray3.00D2-338[»]
1NJIX-ray3.00D2-338[»]
1Q7YX-ray3.20D2-338[»]
1Q81X-ray2.95D2-338[»]
1Q82X-ray2.98D2-338[»]
1Q86X-ray3.00D2-338[»]
1QVFX-ray3.10B2-338[»]
1QVGX-ray2.90B2-338[»]
1S72X-ray2.40B1-338[»]
1VQ4X-ray2.70B1-338[»]
1VQ5X-ray2.60B1-338[»]
1VQ6X-ray2.70B1-338[»]
1VQ7X-ray2.50B1-338[»]
1VQ8X-ray2.20B1-338[»]
1VQ9X-ray2.40B1-338[»]
1VQKX-ray2.30B1-338[»]
1VQLX-ray2.30B1-338[»]
1VQMX-ray2.30B1-338[»]
1VQNX-ray2.40B1-338[»]
1VQOX-ray2.20B1-338[»]
1VQPX-ray2.25B1-338[»]
1W2BX-ray3.50B2-338[»]
1YHQX-ray2.40B1-338[»]
1YI2X-ray2.65B1-338[»]
1YIJX-ray2.60B1-338[»]
1YITX-ray2.80B1-338[»]
1YJ9X-ray2.90B1-338[»]
1YJNX-ray3.00B1-338[»]
1YJWX-ray2.90B1-338[»]
2OTJX-ray2.90B1-338[»]
2OTLX-ray2.70B2-338[»]
2QA4X-ray3.00B1-338[»]
2QEXX-ray2.90B1-338[»]
3CC2X-ray2.40B1-338[»]
3CC4X-ray2.70B1-338[»]
3CC7X-ray2.70B1-338[»]
3CCEX-ray2.75B1-338[»]
3CCJX-ray2.70B1-338[»]
3CCLX-ray2.90B1-338[»]
3CCMX-ray2.55B1-338[»]
3CCQX-ray2.90B1-338[»]
3CCRX-ray3.00B1-338[»]
3CCSX-ray2.95B1-338[»]
3CCUX-ray2.80B1-338[»]
3CCVX-ray2.90B1-338[»]
3CD6X-ray2.75B1-338[»]
3CMAX-ray2.80B1-338[»]
3CMEX-ray2.95B1-338[»]
3CPWX-ray2.70B1-338[»]
3CXCX-ray3.00B2-338[»]
3G4SX-ray3.20B2-338[»]
3G6EX-ray2.70B2-338[»]
3G71X-ray2.85B2-338[»]
3I55X-ray3.11B1-338[»]
3I56X-ray2.90B1-338[»]
3OW2X-ray2.70B2-338[»]
4ADXelectron microscopy6.60B1-338[»]
4V4TX-ray6.46E2-338[»]
4V9FX-ray2.40B1-338[»]
ProteinModelPortaliP20279.
SMRiP20279.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20279.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

eggNOGiarCOG04070. Archaea.
COG0087. LUCA.
HOGENOMiHOG000107320.
KOiK02906.
OMAiVPRIRSW.

Family and domain databases

HAMAPiMF_01325_A. Ribosomal_L3_A. 1 hit.
InterProiIPR000597. Ribosomal_L3.
IPR019928. Ribosomal_L3_arc.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03626. L3_arch. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20279-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQPSRPRKG SLGFGPRKRS TSETPRFNSW PSDDGQPGVQ GFAGYKAGMT
60 70 80 90 100
HVVLVNDEPN SPREGMEETV PVTVIETPPM RAVALRAYED TPYGQRPLTE
110 120 130 140 150
VWTDEFHSEL DRTLDVPEDH DPDAAEEQIR DAHEAGDLGD LRLITHTVPD
160 170 180 190 200
AVPSVPKKKP DVMETRVGGG SVSDRLDHAL DIVEDGGEHA MNDIFRAGEY
210 220 230 240 250
ADVAGVTKGK GTQGPVKRWG VQKRKGKHAR QGWRRRIGNL GPWNPSRVRS
260 270 280 290 300
TVPQQGQTGY HQRTELNKRL IDIGEGDEPT VDGGFVNYGE VDGPYTLVKG
310 320 330
SVPGPDKRLV RFRPAVRPND QPRLDPEVRY VSNESNQG
Length:338
Mass (Da):37,341
Last modified:January 23, 2007 - v5
Checksum:i996D3BE503F4DBD4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti311R → P in AAA86859 (PubMed:2406244).Curated1
Sequence conflicti312F → FF AA sequence (PubMed:2406244).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05222 Genomic DNA. Translation: AAA86859.1.
AY596297 Genomic DNA. Translation: AAV46528.1.
PIRiC35063. R5HS3L.
RefSeqiWP_004957423.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46528; AAV46528; rrnAC1611.
GeneIDi3128366.
KEGGihma:rrnAC1611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05222 Genomic DNA. Translation: AAA86859.1.
AY596297 Genomic DNA. Translation: AAV46528.1.
PIRiC35063. R5HS3L.
RefSeqiWP_004957423.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40B2-338[»]
1JJ2X-ray2.40B2-338[»]
1K73X-ray3.01D2-338[»]
1K8AX-ray3.00D2-338[»]
1K9MX-ray3.00D2-338[»]
1KC8X-ray3.01D2-338[»]
1KD1X-ray3.00D2-338[»]
1KQSX-ray3.10B2-338[»]
1M1KX-ray3.20D2-338[»]
1M90X-ray2.80D2-338[»]
1ML5electron microscopy14.00e2-311[»]
e312-338[»]
1N8RX-ray3.00D2-338[»]
1NJIX-ray3.00D2-338[»]
1Q7YX-ray3.20D2-338[»]
1Q81X-ray2.95D2-338[»]
1Q82X-ray2.98D2-338[»]
1Q86X-ray3.00D2-338[»]
1QVFX-ray3.10B2-338[»]
1QVGX-ray2.90B2-338[»]
1S72X-ray2.40B1-338[»]
1VQ4X-ray2.70B1-338[»]
1VQ5X-ray2.60B1-338[»]
1VQ6X-ray2.70B1-338[»]
1VQ7X-ray2.50B1-338[»]
1VQ8X-ray2.20B1-338[»]
1VQ9X-ray2.40B1-338[»]
1VQKX-ray2.30B1-338[»]
1VQLX-ray2.30B1-338[»]
1VQMX-ray2.30B1-338[»]
1VQNX-ray2.40B1-338[»]
1VQOX-ray2.20B1-338[»]
1VQPX-ray2.25B1-338[»]
1W2BX-ray3.50B2-338[»]
1YHQX-ray2.40B1-338[»]
1YI2X-ray2.65B1-338[»]
1YIJX-ray2.60B1-338[»]
1YITX-ray2.80B1-338[»]
1YJ9X-ray2.90B1-338[»]
1YJNX-ray3.00B1-338[»]
1YJWX-ray2.90B1-338[»]
2OTJX-ray2.90B1-338[»]
2OTLX-ray2.70B2-338[»]
2QA4X-ray3.00B1-338[»]
2QEXX-ray2.90B1-338[»]
3CC2X-ray2.40B1-338[»]
3CC4X-ray2.70B1-338[»]
3CC7X-ray2.70B1-338[»]
3CCEX-ray2.75B1-338[»]
3CCJX-ray2.70B1-338[»]
3CCLX-ray2.90B1-338[»]
3CCMX-ray2.55B1-338[»]
3CCQX-ray2.90B1-338[»]
3CCRX-ray3.00B1-338[»]
3CCSX-ray2.95B1-338[»]
3CCUX-ray2.80B1-338[»]
3CCVX-ray2.90B1-338[»]
3CD6X-ray2.75B1-338[»]
3CMAX-ray2.80B1-338[»]
3CMEX-ray2.95B1-338[»]
3CPWX-ray2.70B1-338[»]
3CXCX-ray3.00B2-338[»]
3G4SX-ray3.20B2-338[»]
3G6EX-ray2.70B2-338[»]
3G71X-ray2.85B2-338[»]
3I55X-ray3.11B1-338[»]
3I56X-ray2.90B1-338[»]
3OW2X-ray2.70B2-338[»]
4ADXelectron microscopy6.60B1-338[»]
4V4TX-ray6.46E2-338[»]
4V9FX-ray2.40B1-338[»]
ProteinModelPortaliP20279.
SMRiP20279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC1611.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV46528; AAV46528; rrnAC1611.
GeneIDi3128366.
KEGGihma:rrnAC1611.

Phylogenomic databases

eggNOGiarCOG04070. Archaea.
COG0087. LUCA.
HOGENOMiHOG000107320.
KOiK02906.
OMAiVPRIRSW.

Miscellaneous databases

EvolutionaryTraceiP20279.

Family and domain databases

HAMAPiMF_01325_A. Ribosomal_L3_A. 1 hit.
InterProiIPR000597. Ribosomal_L3.
IPR019928. Ribosomal_L3_arc.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03626. L3_arch. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL3_HALMA
AccessioniPrimary (citable) accession number: P20279
Secondary accession number(s): Q5V1S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 122 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.