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Protein

50S ribosomal protein L20

Gene

rplT

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity).By similarity

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

BioCyciTTHE300852:GH8R-578-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L20
Gene namesi
Name:rplT
Ordered Locus Names:TTHA0553
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 11811750S ribosomal protein L20PRO_0000177250Add
BLAST

Proteomic databases

PRIDEiP60491.

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA0553.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 2012Combined sources
Turni21 – 233Combined sources
Helixi27 – 304Combined sources
Helixi34 – 7037Combined sources
Helixi76 – 8510Combined sources
Helixi93 – 953Combined sources
Turni96 – 1005Combined sources
Helixi103 – 11513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RU/YU1-118[»]
1VY4X-ray2.60BU/DU1-118[»]
1VY5X-ray2.55BU/DU1-118[»]
1VY6X-ray2.90BU/DU1-118[»]
1VY7X-ray2.80BU/DU1-118[»]
4L47X-ray3.22RU/YU1-118[»]
4L71X-ray3.90RU/YU1-118[»]
4LELX-ray3.90RU/YU1-118[»]
4LFZX-ray3.92RU/YU1-118[»]
4LNTX-ray2.94RU/YU1-118[»]
4LSKX-ray3.48RU/YU1-118[»]
4LT8X-ray3.14RU/YU1-118[»]
4P6FX-ray3.60RU/YU1-118[»]
4P70X-ray3.68RU/YU1-118[»]
4TUAX-ray3.60RU/YU1-118[»]
4TUBX-ray3.60RU/YU1-118[»]
4TUCX-ray3.60RU/YU1-118[»]
4TUDX-ray3.60RU/YU1-118[»]
4TUEX-ray3.50RU/YU1-118[»]
4V4PX-ray5.5011-116[»]
4V4XX-ray5.00BT1-118[»]
4V4YX-ray5.50BT1-118[»]
4V4ZX-ray4.51BT1-118[»]
4V51X-ray2.80BU/DU2-118[»]
4V5AX-ray3.50BU/DU2-118[»]
4V5CX-ray3.30BU/DU1-118[»]
4V5DX-ray3.50BU/DU1-118[»]
4V5EX-ray3.45BU/DU1-118[»]
4V5FX-ray3.60BU/DU1-118[»]
4V5GX-ray3.60BU/DU1-118[»]
4V5JX-ray3.10BU/DU1-118[»]
4V5KX-ray3.20BU/DU1-118[»]
4V5LX-ray3.10BU1-118[»]
4V5Melectron microscopy7.80BU1-118[»]
4V5Nelectron microscopy7.60BU1-118[»]
4V5PX-ray3.10BU/DU1-118[»]
4V5QX-ray3.10BU/DU1-118[»]
4V5RX-ray3.10BU/DU1-118[»]
4V5SX-ray3.10BU/DU1-118[»]
4V68electron microscopy6.40BU2-118[»]
4V6AX-ray3.10BU/DU1-118[»]
4V6FX-ray3.10A1/D11-118[»]
4V6GX-ray3.50B1/D11-118[»]
4V7JX-ray3.30AU/BU1-118[»]
4V7KX-ray3.60AU/BU1-118[»]
4V7LX-ray3.00BU/DU1-118[»]
4V7MX-ray3.45BU/DU1-118[»]
4V7WX-ray3.00BU/DU1-118[»]
4V7XX-ray3.00BU/DU1-118[»]
4V7YX-ray3.00BU/DU1-118[»]
4V7ZX-ray3.10BU/DU1-118[»]
4V87X-ray3.10A1/D12-118[»]
4V8AX-ray3.20AU/BU1-118[»]
4V8BX-ray3.00B1/D11-118[»]
4V8CX-ray3.30A1/B11-118[»]
4V8DX-ray3.00B1/D11-118[»]
4V8EX-ray3.30A1/C11-118[»]
4V8FX-ray3.30A1/D11-118[»]
4V8GX-ray3.00BU/DU1-118[»]
4V8HX-ray3.10BU/DU1-118[»]
4V8IX-ray2.70BU/DU1-118[»]
4V8JX-ray3.90BU/DU1-118[»]
4V8NX-ray3.10BU/DU1-118[»]
4V8OX-ray3.80BU1-118[»]
4V8QX-ray3.10AU1-118[»]
4V8UX-ray3.70BU/DU1-118[»]
4V8XX-ray3.35BU/DU1-118[»]
4V90X-ray2.95BU2-118[»]
4V95X-ray3.20BU/DU1-118[»]
4V97X-ray3.52BU/DU1-118[»]
4V9AX-ray3.30B1/D11-118[»]
4V9BX-ray3.10B1/D11-118[»]
4V9HX-ray2.86BU1-118[»]
4V9IX-ray3.30BU/DU2-118[»]
4V9RX-ray3.00BU/DU1-118[»]
4V9SX-ray3.10BU/DU1-118[»]
4W2EX-ray2.90U1-118[»]
4W2FX-ray2.40BU/DU1-118[»]
4W2GX-ray2.55BU/DU1-118[»]
4W2HX-ray2.70BU/DU1-118[»]
4W2IX-ray2.70BU/DU1-118[»]
4W4GX-ray3.30RU/YU1-118[»]
4WPOX-ray2.80AU/CU1-118[»]
4WQ1X-ray3.1085/C82-118[»]
4WQFX-ray2.80AU/CU1-118[»]
4WQRX-ray3.1585/C81-118[»]
4WQUX-ray2.80AU/CU1-118[»]
4WQYX-ray2.80AU/CU1-118[»]
4WR6X-ray3.0585/C81-118[»]
4WRAX-ray3.0585/C81-118[»]
4WROX-ray3.05C81-118[»]
4WSDX-ray2.9585/C81-118[»]
4WSMX-ray3.3085/C81-118[»]
4WT1X-ray3.0585/C81-118[»]
4WT8X-ray3.40CT/DT2-118[»]
4WU1X-ray3.2085/C81-118[»]
4WZDX-ray3.1085/C81-118[»]
4WZOX-ray3.3085/C81-118[»]
4Y4OX-ray2.301U/2U1-118[»]
4Y4PX-ray2.501U/2U1-118[»]
4YPBX-ray3.40RU/YU1-118[»]
4YZVX-ray3.10RU/YU1-118[»]
4Z3SX-ray2.651U/2U1-118[»]
4Z8CX-ray2.901U/2U1-118[»]
4ZERX-ray3.101U/2U2-117[»]
5A9Zelectron microscopy4.70AR2-118[»]
5AA0electron microscopy5.00AR2-118[»]
5D8BX-ray3.63KB/O1-118[»]
5DOXX-ray3.101U/2U1-118[»]
5DOYX-ray2.601U/2U1-118[»]
5E7KX-ray3.2085/C81-118[»]
5E81X-ray2.9585/C81-118[»]
5EL4X-ray3.1585/C81-118[»]
5EL5X-ray3.1585/C81-118[»]
5EL6X-ray3.1085/C81-118[»]
5EL7X-ray3.1585/C81-118[»]
5F8KX-ray2.801U/2U2-117[»]
5FDUX-ray2.901U/2U2-117[»]
5FDVX-ray2.801U/2U2-117[»]
5HAUX-ray3.001S/2S1-118[»]
5HCPX-ray2.891U/2U1-118[»]
5HCQX-ray2.801U/2U1-118[»]
5HCRX-ray2.801U/2U1-118[»]
5HD1X-ray2.701U/2U1-118[»]
5IB7X-ray2.9985/C81-118[»]
5IB8X-ray3.1385/C81-118[»]
5IBBX-ray2.9685/C81-118[»]
5IMQelectron microscopy3.80m1-118[»]
5IMRelectron microscopy-m1-118[»]
5J4BX-ray2.601U/2U1-118[»]
5J4CX-ray2.801U/2U1-118[»]
5J8BX-ray2.60U1-118[»]
ProteinModelPortaliP60491.
SMRiP60491. Positions 2-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60491.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L20P family.Curated

Phylogenomic databases

eggNOGiENOG4108YZX. Bacteria.
COG0292. LUCA.
HOGENOMiHOG000035046.
KOiK02887.
OMAiRKAKEQM.
PhylomeDBiP60491.

Family and domain databases

CDDicd07026. Ribosomal_L20. 1 hit.
HAMAPiMF_00382. Ribosomal_L20. 1 hit.
InterProiIPR005813. Ribosomal_L20.
[Graphical view]
PANTHERiPTHR10986. PTHR10986. 1 hit.
PfamiPF00453. Ribosomal_L20. 1 hit.
[Graphical view]
PRINTSiPR00062. RIBOSOMALL20.
TIGRFAMsiTIGR01032. rplT_bact. 1 hit.
PROSITEiPS00937. RIBOSOMAL_L20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P60491-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRAKTGVVR RRKHKKILKL AKGYWGLRSK SFRKARETLF AAGNYAYAHR
60 70 80 90 100
KRRKRDFRRL WIVRINAACR QHGLNYSTFI HGLKKAGIEV DRKNLADLAV
110
REPQVFAELV ERAKAAQG
Length:118
Mass (Da):13,743
Last modified:January 23, 2007 - v3
Checksum:iA5A8B028B15145F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251W → WV AA sequence (PubMed:11154066).Curated

Mass spectrometryi

Molecular mass is 13612 Da from positions 2 - 118. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70376.1.
RefSeqiWP_011172639.1. NC_006461.1.
YP_143819.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70376; BAD70376; BAD70376.
GeneIDi3169980.
KEGGittj:TTHA0553.
PATRICi23956083. VBITheThe93045_0552.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70376.1.
RefSeqiWP_011172639.1. NC_006461.1.
YP_143819.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RU/YU1-118[»]
1VY4X-ray2.60BU/DU1-118[»]
1VY5X-ray2.55BU/DU1-118[»]
1VY6X-ray2.90BU/DU1-118[»]
1VY7X-ray2.80BU/DU1-118[»]
4L47X-ray3.22RU/YU1-118[»]
4L71X-ray3.90RU/YU1-118[»]
4LELX-ray3.90RU/YU1-118[»]
4LFZX-ray3.92RU/YU1-118[»]
4LNTX-ray2.94RU/YU1-118[»]
4LSKX-ray3.48RU/YU1-118[»]
4LT8X-ray3.14RU/YU1-118[»]
4P6FX-ray3.60RU/YU1-118[»]
4P70X-ray3.68RU/YU1-118[»]
4TUAX-ray3.60RU/YU1-118[»]
4TUBX-ray3.60RU/YU1-118[»]
4TUCX-ray3.60RU/YU1-118[»]
4TUDX-ray3.60RU/YU1-118[»]
4TUEX-ray3.50RU/YU1-118[»]
4V4PX-ray5.5011-116[»]
4V4XX-ray5.00BT1-118[»]
4V4YX-ray5.50BT1-118[»]
4V4ZX-ray4.51BT1-118[»]
4V51X-ray2.80BU/DU2-118[»]
4V5AX-ray3.50BU/DU2-118[»]
4V5CX-ray3.30BU/DU1-118[»]
4V5DX-ray3.50BU/DU1-118[»]
4V5EX-ray3.45BU/DU1-118[»]
4V5FX-ray3.60BU/DU1-118[»]
4V5GX-ray3.60BU/DU1-118[»]
4V5JX-ray3.10BU/DU1-118[»]
4V5KX-ray3.20BU/DU1-118[»]
4V5LX-ray3.10BU1-118[»]
4V5Melectron microscopy7.80BU1-118[»]
4V5Nelectron microscopy7.60BU1-118[»]
4V5PX-ray3.10BU/DU1-118[»]
4V5QX-ray3.10BU/DU1-118[»]
4V5RX-ray3.10BU/DU1-118[»]
4V5SX-ray3.10BU/DU1-118[»]
4V68electron microscopy6.40BU2-118[»]
4V6AX-ray3.10BU/DU1-118[»]
4V6FX-ray3.10A1/D11-118[»]
4V6GX-ray3.50B1/D11-118[»]
4V7JX-ray3.30AU/BU1-118[»]
4V7KX-ray3.60AU/BU1-118[»]
4V7LX-ray3.00BU/DU1-118[»]
4V7MX-ray3.45BU/DU1-118[»]
4V7WX-ray3.00BU/DU1-118[»]
4V7XX-ray3.00BU/DU1-118[»]
4V7YX-ray3.00BU/DU1-118[»]
4V7ZX-ray3.10BU/DU1-118[»]
4V87X-ray3.10A1/D12-118[»]
4V8AX-ray3.20AU/BU1-118[»]
4V8BX-ray3.00B1/D11-118[»]
4V8CX-ray3.30A1/B11-118[»]
4V8DX-ray3.00B1/D11-118[»]
4V8EX-ray3.30A1/C11-118[»]
4V8FX-ray3.30A1/D11-118[»]
4V8GX-ray3.00BU/DU1-118[»]
4V8HX-ray3.10BU/DU1-118[»]
4V8IX-ray2.70BU/DU1-118[»]
4V8JX-ray3.90BU/DU1-118[»]
4V8NX-ray3.10BU/DU1-118[»]
4V8OX-ray3.80BU1-118[»]
4V8QX-ray3.10AU1-118[»]
4V8UX-ray3.70BU/DU1-118[»]
4V8XX-ray3.35BU/DU1-118[»]
4V90X-ray2.95BU2-118[»]
4V95X-ray3.20BU/DU1-118[»]
4V97X-ray3.52BU/DU1-118[»]
4V9AX-ray3.30B1/D11-118[»]
4V9BX-ray3.10B1/D11-118[»]
4V9HX-ray2.86BU1-118[»]
4V9IX-ray3.30BU/DU2-118[»]
4V9RX-ray3.00BU/DU1-118[»]
4V9SX-ray3.10BU/DU1-118[»]
4W2EX-ray2.90U1-118[»]
4W2FX-ray2.40BU/DU1-118[»]
4W2GX-ray2.55BU/DU1-118[»]
4W2HX-ray2.70BU/DU1-118[»]
4W2IX-ray2.70BU/DU1-118[»]
4W4GX-ray3.30RU/YU1-118[»]
4WPOX-ray2.80AU/CU1-118[»]
4WQ1X-ray3.1085/C82-118[»]
4WQFX-ray2.80AU/CU1-118[»]
4WQRX-ray3.1585/C81-118[»]
4WQUX-ray2.80AU/CU1-118[»]
4WQYX-ray2.80AU/CU1-118[»]
4WR6X-ray3.0585/C81-118[»]
4WRAX-ray3.0585/C81-118[»]
4WROX-ray3.05C81-118[»]
4WSDX-ray2.9585/C81-118[»]
4WSMX-ray3.3085/C81-118[»]
4WT1X-ray3.0585/C81-118[»]
4WT8X-ray3.40CT/DT2-118[»]
4WU1X-ray3.2085/C81-118[»]
4WZDX-ray3.1085/C81-118[»]
4WZOX-ray3.3085/C81-118[»]
4Y4OX-ray2.301U/2U1-118[»]
4Y4PX-ray2.501U/2U1-118[»]
4YPBX-ray3.40RU/YU1-118[»]
4YZVX-ray3.10RU/YU1-118[»]
4Z3SX-ray2.651U/2U1-118[»]
4Z8CX-ray2.901U/2U1-118[»]
4ZERX-ray3.101U/2U2-117[»]
5A9Zelectron microscopy4.70AR2-118[»]
5AA0electron microscopy5.00AR2-118[»]
5D8BX-ray3.63KB/O1-118[»]
5DOXX-ray3.101U/2U1-118[»]
5DOYX-ray2.601U/2U1-118[»]
5E7KX-ray3.2085/C81-118[»]
5E81X-ray2.9585/C81-118[»]
5EL4X-ray3.1585/C81-118[»]
5EL5X-ray3.1585/C81-118[»]
5EL6X-ray3.1085/C81-118[»]
5EL7X-ray3.1585/C81-118[»]
5F8KX-ray2.801U/2U2-117[»]
5FDUX-ray2.901U/2U2-117[»]
5FDVX-ray2.801U/2U2-117[»]
5HAUX-ray3.001S/2S1-118[»]
5HCPX-ray2.891U/2U1-118[»]
5HCQX-ray2.801U/2U1-118[»]
5HCRX-ray2.801U/2U1-118[»]
5HD1X-ray2.701U/2U1-118[»]
5IB7X-ray2.9985/C81-118[»]
5IB8X-ray3.1385/C81-118[»]
5IBBX-ray2.9685/C81-118[»]
5IMQelectron microscopy3.80m1-118[»]
5IMRelectron microscopy-m1-118[»]
5J4BX-ray2.601U/2U1-118[»]
5J4CX-ray2.801U/2U1-118[»]
5J8BX-ray2.60U1-118[»]
ProteinModelPortaliP60491.
SMRiP60491. Positions 2-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0553.

Proteomic databases

PRIDEiP60491.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70376; BAD70376; BAD70376.
GeneIDi3169980.
KEGGittj:TTHA0553.
PATRICi23956083. VBITheThe93045_0552.

Phylogenomic databases

eggNOGiENOG4108YZX. Bacteria.
COG0292. LUCA.
HOGENOMiHOG000035046.
KOiK02887.
OMAiRKAKEQM.
PhylomeDBiP60491.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-578-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60491.

Family and domain databases

CDDicd07026. Ribosomal_L20. 1 hit.
HAMAPiMF_00382. Ribosomal_L20. 1 hit.
InterProiIPR005813. Ribosomal_L20.
[Graphical view]
PANTHERiPTHR10986. PTHR10986. 1 hit.
PfamiPF00453. Ribosomal_L20. 1 hit.
[Graphical view]
PRINTSiPR00062. RIBOSOMALL20.
TIGRFAMsiTIGR01032. rplT_bact. 1 hit.
PROSITEiPS00937. RIBOSOMAL_L20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL20_THET8
AccessioniPrimary (citable) accession number: P60491
Secondary accession number(s): Q5SKU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 106 of the entry and version 3 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.