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Protein

50S ribosomal protein L1

Gene

rpl1

Organism
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probably involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.By similarity
Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciSACI330779:GH9J-1433-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L1UniRule annotation
Gene namesi
Name:rpl1UniRule annotation
Ordered Locus Names:Saci_1458
OrganismiSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Taxonomic identifieri330779 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001018 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22122150S ribosomal protein L1PRO_0000125812Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi330779.Saci_1458.

Structurei

Secondary structure

1
221
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 1912Combined sources
Turni21 – 233Combined sources
Beta strandi32 – 4110Combined sources
Helixi44 – 463Combined sources
Turni47 – 493Combined sources
Beta strandi52 – 565Combined sources
Beta strandi67 – 704Combined sources
Helixi73 – 819Combined sources
Beta strandi85 – 873Combined sources
Helixi90 – 967Combined sources
Helixi100 – 1089Combined sources
Beta strandi111 – 1155Combined sources
Helixi117 – 1193Combined sources
Helixi120 – 1267Combined sources
Helixi128 – 1314Combined sources
Helixi132 – 1343Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi143 – 1453Combined sources
Helixi148 – 1558Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi163 – 17412Combined sources
Helixi179 – 19618Combined sources
Turni200 – 2023Combined sources
Beta strandi203 – 2108Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MZPX-ray2.65A5-220[»]
4V49X-ray8.7055-220[»]
4V4AX-ray9.5055-220[»]
4V4GX-ray11.5075-220[»]
ProteinModelPortaliP35024.
SMRiP35024. Positions 4-220.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35024.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L1P family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04289. Archaea.
COG0081. LUCA.
HOGENOMiHOG000207016.
KOiK02863.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_A. Ribosomal_L1_A.
InterProiIPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023669. Ribosomal_L1_arc.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVLADKES LIEALKLALS TEYNVKRNFT QSVEIILTFK GIDMKKGDLK
60 70 80 90 100
LREIVPLPKQ PSKAKRVLVV PSFEQLEYAK KASPNVVITR EELQKLQGQK
110 120 130 140 150
RPVKKLARQN EWFLINQESM ALAGRILGPA LGPRGKFPTP LPNTADISEY
160 170 180 190 200
INRFKRSVLV KTKDQPQVQV FIGTEDMKPE DLAENAIAVL NAIENKAKVE
210 220
TNLRNIYVKT TMGKAVKVKR A
Length:221
Mass (Da):24,935
Last modified:August 30, 2005 - v2
Checksum:i47A26B9251F89F2F
GO

Sequence cautioni

The sequence AAY80779.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731F → S in CAA41763 (PubMed:7966335).Curated
Sequence conflicti73 – 731F → S (PubMed:2497941).Curated
Sequence conflicti85 – 851N → K in CAA41763 (PubMed:7966335).Curated
Sequence conflicti85 – 851N → K (PubMed:2497941).Curated
Sequence conflicti108 – 1081R → I in CAA41763 (PubMed:7966335).Curated
Sequence conflicti108 – 1081R → I (PubMed:2497941).Curated
Sequence conflicti159 – 1591L → I in CAA41763 (PubMed:7966335).Curated
Sequence conflicti159 – 1591L → I (PubMed:2497941).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59038 Genomic DNA. Translation: CAA41763.1.
CP000077 Genomic DNA. Translation: AAY80779.1. Different initiation.
PIRiS53649.

Genome annotation databases

EnsemblBacteriaiAAY80779; AAY80779; Saci_1458.
KEGGisai:Saci_1458.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59038 Genomic DNA. Translation: CAA41763.1.
CP000077 Genomic DNA. Translation: AAY80779.1. Different initiation.
PIRiS53649.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MZPX-ray2.65A5-220[»]
4V49X-ray8.7055-220[»]
4V4AX-ray9.5055-220[»]
4V4GX-ray11.5075-220[»]
ProteinModelPortaliP35024.
SMRiP35024. Positions 4-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi330779.Saci_1458.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAY80779; AAY80779; Saci_1458.
KEGGisai:Saci_1458.

Phylogenomic databases

eggNOGiarCOG04289. Archaea.
COG0081. LUCA.
HOGENOMiHOG000207016.
KOiK02863.

Enzyme and pathway databases

BioCyciSACI330779:GH9J-1433-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP35024.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_A. Ribosomal_L1_A.
InterProiIPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023669. Ribosomal_L1_arc.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and transcription of the L11-L1-L10-L12 ribosomal protein gene operon from the extreme thermophilic archaeon Sulfolobus acidocaldarius."
    Ramirez C., Shimmin L.C., Leggatt P., Matheson A.T.
    J. Mol. Biol. 244:242-249(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structure and evolution of the L11, L1, L10, and L12 equivalent ribosomal proteins in eubacteria, archaebacteria, and eucaryotes."
    Ramirez C., Shimmin L.C., Newton C.H., Matheson A.T., Dennis P.P.
    Can. J. Microbiol. 35:234-244(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Erratum
    Ramirez C., Shimmin L.C., Newton C.H., Matheson A.T., Dennis P.P.
    Can. J. Microbiol. 35:975-975(1989)
  4. "The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
    Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
    J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 5-220 IN COMPLEX WITH A T.THERMOPHILUS RRNA FRAGMENT.

Entry informationi

Entry nameiRL1_SULAC
AccessioniPrimary (citable) accession number: P35024
Secondary accession number(s): Q4J8V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 30, 2005
Last modified: December 9, 2015
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius.1 Publication

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

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.