Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

50S ribosomal protein L10

Gene

rpl10

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.Curated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1279-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L10UniRule annotation
Alternative name(s):
Acidic ribosomal protein P0 homologUniRule annotation
HMal10
L10E
Gene namesi
Name:rpl10UniRule annotation
Synonyms:rpl10e, rplP0UniRule annotation
Ordered Locus Names:rrnAC1417
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
ProteomesiUP000001169 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 34834850S ribosomal protein L10PRO_0000154789Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms part of 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 (Probable).2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1417.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2815Combined sources
Beta strandi29 – 324Combined sources
Helixi43 – 497Combined sources
Helixi64 – 718Combined sources
Beta strandi74 – 785Combined sources
Helixi79 – 835Combined sources
Beta strandi87 – 915Combined sources
Helixi100 – 1078Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi123 – 1253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JJ2X-ray2.40G1-348[»]
1K73X-ray3.01I1-348[»]
1K8AX-ray3.00I1-348[»]
1K9MX-ray3.00I1-348[»]
1KC8X-ray3.01I1-348[»]
1KD1X-ray3.00I1-348[»]
1KQSX-ray3.10G1-348[»]
1M1KX-ray3.20I1-348[»]
1M90X-ray2.80I1-348[»]
1N8RX-ray3.00I1-348[»]
1NJIX-ray3.00I1-348[»]
1Q7YX-ray3.20I1-348[»]
1Q81X-ray2.95I1-348[»]
1Q82X-ray2.98I1-348[»]
1Q86X-ray3.00I1-348[»]
1QVFX-ray3.10G1-348[»]
1QVGX-ray2.90G1-348[»]
1S72X-ray2.40G1-348[»]
1VQ4X-ray2.70G1-348[»]
1VQ5X-ray2.60G1-348[»]
1VQ6X-ray2.70G1-348[»]
1VQ7X-ray2.50G1-348[»]
1VQ8X-ray2.20G1-348[»]
1VQ9X-ray2.40G1-348[»]
1VQKX-ray2.30G1-348[»]
1VQLX-ray2.30G1-348[»]
1VQMX-ray2.30G1-348[»]
1VQNX-ray2.40G1-348[»]
1VQOX-ray2.20G1-348[»]
1VQPX-ray2.25G1-348[»]
1W2BX-ray3.50G1-348[»]
1YHQX-ray2.40G1-348[»]
1YI2X-ray2.65G1-348[»]
1YIJX-ray2.60G1-348[»]
1YITX-ray2.80G1-348[»]
1YJ9X-ray2.90G1-348[»]
1YJNX-ray3.00G1-348[»]
1YJWX-ray2.90G1-348[»]
1ZB4model-A1-130[»]
2OTJX-ray2.90G1-348[»]
2OTLX-ray2.70G1-348[»]
2QA4X-ray3.00G1-348[»]
2QEXX-ray2.90G1-348[»]
3CC2X-ray2.40G1-348[»]
3CC4X-ray2.70G1-348[»]
3CC7X-ray2.70G1-348[»]
3CCEX-ray2.75G1-348[»]
3CCJX-ray2.70G1-348[»]
3CCLX-ray2.90G1-348[»]
3CCMX-ray2.55G1-348[»]
3CCQX-ray2.90G1-348[»]
3CCRX-ray3.00G1-348[»]
3CCSX-ray2.95G1-348[»]
3CCUX-ray2.80G1-348[»]
3CCVX-ray2.90G1-348[»]
3CD6X-ray2.75G1-348[»]
3CMAX-ray2.80G1-348[»]
3CMEX-ray2.95G1-348[»]
3CPWX-ray2.70G1-348[»]
3CXCX-ray3.00G1-348[»]
3G4SX-ray3.20G1-348[»]
3G6EX-ray2.70G1-348[»]
3G71X-ray2.85G1-348[»]
3I55X-ray3.11G1-348[»]
3I56X-ray2.90G1-348[»]
3OW2X-ray2.70G12-73[»]
4V9FX-ray2.40G6-211[»]
ProteinModelPortaliP15825.
SMRiP15825. Positions 7-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15825.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L10P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0244.
HOGENOMiHOG000229909.
KOiK02864.
OMAiVMDARNL.

Family and domain databases

Gene3Di1.10.10.380. 2 hits.
HAMAPiMF_00280. Ribosomal_L10_arch.
InterProiIPR022909. 50S_L10_arch.
IPR013522. Ribosomal_L10_N_arc.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15825-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAESERKTE TIPEWKQEEV DAIVEMIESY ESVGVVNIAG IPSRQLQDMR
60 70 80 90 100
RDLHGTAELR VSRNTLLERA LDDVDDGLED LNGYITGQVG LIGTDDNPFS
110 120 130 140 150
LFQELEASKT PAPIGAGEVA PNDIVIPEGD TGVDPGPFVG ELQSVGADAR
160 170 180 190 200
IQEGSIQVLS DSTVLDTGEE VSQELSNVLN ELGIEPKEVG LDLRAVFADG
210 220 230 240 250
VLFEPEELEL DIDEYRSDIQ AAAGRAFNLS VNADYPTATT APTMLQSARG
260 270 280 290 300
NAKSLALQAA IEDPEVVPDL VSKADAQVRA LASQIDDEEA LPEELQGVEA
310 320 330 340
DVATEEPTDD QDDDTASEDD ADADDAAEEA DDDDDDDEDA GDALGAMF
Length:348
Mass (Da):37,150
Last modified:January 4, 2005 - v2
Checksum:i4063B1C9D2FCB164
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481A → D in CAA35795 (PubMed:2320419).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51430 Genomic DNA. Translation: CAA35795.1.
AY596297 Genomic DNA. Translation: AAV46344.1.
PIRiS08422. R5HS10.
RefSeqiWP_011223609.1. NC_006396.1.
YP_136050.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46344; AAV46344; rrnAC1417.
GeneIDi3128417.
KEGGihma:rrnAC1417.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51430 Genomic DNA. Translation: CAA35795.1.
AY596297 Genomic DNA. Translation: AAV46344.1.
PIRiS08422. R5HS10.
RefSeqiWP_011223609.1. NC_006396.1.
YP_136050.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JJ2X-ray2.40G1-348[»]
1K73X-ray3.01I1-348[»]
1K8AX-ray3.00I1-348[»]
1K9MX-ray3.00I1-348[»]
1KC8X-ray3.01I1-348[»]
1KD1X-ray3.00I1-348[»]
1KQSX-ray3.10G1-348[»]
1M1KX-ray3.20I1-348[»]
1M90X-ray2.80I1-348[»]
1N8RX-ray3.00I1-348[»]
1NJIX-ray3.00I1-348[»]
1Q7YX-ray3.20I1-348[»]
1Q81X-ray2.95I1-348[»]
1Q82X-ray2.98I1-348[»]
1Q86X-ray3.00I1-348[»]
1QVFX-ray3.10G1-348[»]
1QVGX-ray2.90G1-348[»]
1S72X-ray2.40G1-348[»]
1VQ4X-ray2.70G1-348[»]
1VQ5X-ray2.60G1-348[»]
1VQ6X-ray2.70G1-348[»]
1VQ7X-ray2.50G1-348[»]
1VQ8X-ray2.20G1-348[»]
1VQ9X-ray2.40G1-348[»]
1VQKX-ray2.30G1-348[»]
1VQLX-ray2.30G1-348[»]
1VQMX-ray2.30G1-348[»]
1VQNX-ray2.40G1-348[»]
1VQOX-ray2.20G1-348[»]
1VQPX-ray2.25G1-348[»]
1W2BX-ray3.50G1-348[»]
1YHQX-ray2.40G1-348[»]
1YI2X-ray2.65G1-348[»]
1YIJX-ray2.60G1-348[»]
1YITX-ray2.80G1-348[»]
1YJ9X-ray2.90G1-348[»]
1YJNX-ray3.00G1-348[»]
1YJWX-ray2.90G1-348[»]
1ZB4model-A1-130[»]
2OTJX-ray2.90G1-348[»]
2OTLX-ray2.70G1-348[»]
2QA4X-ray3.00G1-348[»]
2QEXX-ray2.90G1-348[»]
3CC2X-ray2.40G1-348[»]
3CC4X-ray2.70G1-348[»]
3CC7X-ray2.70G1-348[»]
3CCEX-ray2.75G1-348[»]
3CCJX-ray2.70G1-348[»]
3CCLX-ray2.90G1-348[»]
3CCMX-ray2.55G1-348[»]
3CCQX-ray2.90G1-348[»]
3CCRX-ray3.00G1-348[»]
3CCSX-ray2.95G1-348[»]
3CCUX-ray2.80G1-348[»]
3CCVX-ray2.90G1-348[»]
3CD6X-ray2.75G1-348[»]
3CMAX-ray2.80G1-348[»]
3CMEX-ray2.95G1-348[»]
3CPWX-ray2.70G1-348[»]
3CXCX-ray3.00G1-348[»]
3G4SX-ray3.20G1-348[»]
3G6EX-ray2.70G1-348[»]
3G71X-ray2.85G1-348[»]
3I55X-ray3.11G1-348[»]
3I56X-ray2.90G1-348[»]
3OW2X-ray2.70G12-73[»]
4V9FX-ray2.40G6-211[»]
ProteinModelPortaliP15825.
SMRiP15825. Positions 7-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC1417.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV46344; AAV46344; rrnAC1417.
GeneIDi3128417.
KEGGihma:rrnAC1417.

Phylogenomic databases

eggNOGiCOG0244.
HOGENOMiHOG000229909.
KOiK02864.
OMAiVMDARNL.

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1279-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP15825.

Family and domain databases

Gene3Di1.10.10.380. 2 hits.
HAMAPiMF_00280. Ribosomal_L10_arch.
InterProiIPR022909. 50S_L10_arch.
IPR013522. Ribosomal_L10_N_arc.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the genes encoding the L11, L1, L10 and L12 equivalent ribosomal proteins from the archaebacterium Halobacterium marismortui."
    Arndt E., Weigel C.
    Nucleic Acids Res. 18:1285-1285(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  3. "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.
  4. "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.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  6. "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.
  7. "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.
  8. "Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation."
    Diaconu M., Kothe U., Schlunzen F., Fischer N., Harms J.M., Tonevitsky A.G., Stark H., Rodnina M.V., Wahl M.C.
    Cell 121:991-1004(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MODEL, PROBABLE INTERACTION WITH L11 (RPL11) AND L12 (RPL12).
  9. "Structure of the base of the L7/L12 stalk of the Haloarcula marismortui large ribosomal subunit: analysis of L11 movements."
    Kavran J.M., Steitz T.A.
    J. Mol. Biol. 371:1047-1059(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), RRNA-BINDING, INTERACTION WITH L11.
  10. "Revisiting the Haloarcula marismortui 50S ribosomal subunit model."
    Gabdulkhakov A., Nikonov S., Garber M.
    Acta Crystallogr. D 69:997-1004(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 6-211 OF THE 50S SUBUNIT.

Entry informationi

Entry nameiRL10_HALMA
AccessioniPrimary (citable) accession number: P15825
Secondary accession number(s): Q5V2A8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 4, 2005
Last modified: July 22, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Has been called L10e and L10E in this organism; in this case "e/E" is for E.coli-like, not eukaryotic-type protein.

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

External Data

Dasty 3

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 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.