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Protein

50S ribosomal protein L10

Gene

rpl10

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Forms the large subunit's ribosomal stalk, playing a central role in the interaction of the ribosome with elongation factors; the stalk complex of P.horikoshii binds to E.coli large subunits and confers on them the ability to interact with eukaryotic elongation factors. Each succesive L12 dimer bound along the P0 spine increases the GTPase activity of elongation factors and increases translation by reconsituted ribosomes, although the first site is the most stimulatory.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciPHOR70601:G1G39-1936-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L10UniRule annotation
Alternative name(s):
Acidic ribosomal protein P0 homologUniRule annotation
Anchor protein P0
Gene namesi
Name:rpl10UniRule annotation
Synonyms:rplP0UniRule annotation
Ordered Locus Names:PH1999
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi217 – 224LQKAYMHA → QQKAYMHQ: Binds less L12, about 50% GTPase activity, about 35% GTPase activity; when associated with 243-Q--Q250 or 272-Q--Q-279. 1 Publication8
Mutagenesisi243 – 250IQKAFLNA → QQKAFLNQ: About 65% GTPase activity; when associated with 272-Q--Q-279. About 35% GTPase activity; when associated with 217-Q--Q-224. 1 Publication8
Mutagenesisi272 – 279AFRAMLLL → QFRAMLLQ: About 65% GTPase activity; when associated with 243-Q--Q-250. About 35% GTPase activity; when associated with 217-Q--Q-224. 1 Publication8

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001548041 – 34250S ribosomal protein L10Add BLAST342

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit, binds large rRNA. Forms the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated spine to which the L12 dimers bind in a sequential fashion.2 Publications

Protein-protein interaction databases

STRINGi70601.PH1999

Structurei

Secondary structure

1342
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni8 – 10Combined sources3
Helixi11 – 19Combined sources9
Beta strandi23 – 29Combined sources7
Helixi35 – 47Combined sources13
Beta strandi50 – 54Combined sources5
Beta strandi56 – 59Combined sources4
Helixi62 – 68Combined sources7
Beta strandi78 – 80Combined sources3
Beta strandi87 – 94Combined sources8
Helixi96 – 105Combined sources10
Beta strandi190 – 196Combined sources7
Beta strandi199 – 201Combined sources3
Helixi203 – 206Combined sources4
Helixi210 – 231Combined sources22
Turni236 – 238Combined sources3
Helixi239 – 256Combined sources18
Turni262 – 264Combined sources3
Helixi265 – 280Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A1YX-ray2.13G1-284[»]
ProteinModelPortaliO74109
SMRiO74109
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO74109

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni212 – 342Required for interaction with ribosomal protein L12 dimersAdd BLAST131

Sequence similaritiesi

Belongs to the universal ribosomal protein uL10 family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04288 Archaea
COG0244 LUCA
HOGENOMiHOG000229909
KOiK02864
OMAiMAHVAEW
OrthoDBiPOG093Z06TD

Family and domain databases

HAMAPiMF_00280 Ribosomal_L10_arch, 1 hit
InterProiView protein in InterPro
IPR022909 50S_L10_arch
IPR001790 Ribosomal_L10P
PfamiView protein in Pfam
PF00466 Ribosomal_L10, 1 hit

Sequencei

Sequence statusi: Complete.

O74109-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHVAEWKKK EVEELAKLIK SYPVIALVDV SSMPAYPLSQ MRRLIRENGG
60 70 80 90 100
LLRVSRNTLI ELAIKKAAKE LGKPELEKLV EYIDRGAGIL VTNMNPFKLY
110 120 130 140 150
KFLQQNRQPA PAKPGAVVPK DVVVPAGPTP LAPGPIVGQM QALGIPARIE
160 170 180 190 200
KGKVTIQKDT TVLKAGEVIT PELANILNAL GIQPLEVGLD VLAVYEDGIV
210 220 230 240 250
YTPDVLAIDE QEYIDMLQKA YMHAFNLAVN IAYPTPETIE AIIQKAFLNA
260 270 280 290 300
KTVAIEAGYI TKETIQDIIG RAFRAMLLLA QQLPEDVLDE KTKELLSAQA
310 320 330 340
QVAVATQPSE EEKKEEEKTE EEEKEEEASE EEALAGLSAL FG
Length:342
Mass (Da):37,514
Last modified:November 1, 1998 - v1
Checksum:iA469330FC19E6195
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA Translation: BAA31126.1
PIRiG71216
RefSeqiWP_010886060.1, NC_000961.1

Genome annotation databases

EnsemblBacteriaiBAA31126; BAA31126; BAA31126
GeneIDi1442842
KEGGipho:PH1999

Similar proteinsi

Entry informationi

Entry nameiRL10_PYRHO
AccessioniPrimary (citable) accession number: O74109
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 25, 2018
This is version 102 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

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