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Protein

50S ribosomal protein L5

Gene

rplE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.3 Publications
In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.3 Publications
Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.1 Publication

GO - Molecular functioni

  • 5S rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: GO_Central
  • tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  • ribosomal large subunit assembly Source: EcoCyc
  • translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10868-MONOMER.
ECOL316407:JW3270-MONOMER.
MetaCyc:EG10868-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L5
Gene namesi
Name:rplE
Ordered Locus Names:b3308, JW3270
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10868. rplE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001249252 – 17950S ribosomal protein L5Add BLAST178

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP62399.
PaxDbiP62399.
PRIDEiP62399.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA; cross-links to the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome, contacting protein S13 and S19.7 Publications

Protein-protein interaction databases

BioGridi852112. 1 interactor.
DIPiDIP-35914N.
IntActiP62399. 71 interactors.
MINTiMINT-1238892.
STRINGi511145.b3308.

Structurei

Secondary structure

1179
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 20Combined sources18
Helixi25 – 27Combined sources3
Beta strandi31 – 37Combined sources7
Turni42 – 45Combined sources4
Helixi47 – 60Combined sources14
Beta strandi61 – 63Combined sources3
Beta strandi66 – 69Combined sources4
Beta strandi71 – 73Combined sources3
Turni75 – 78Combined sources4
Beta strandi81 – 83Combined sources3
Beta strandi84 – 87Combined sources4
Beta strandi88 – 91Combined sources4
Helixi93 – 105Combined sources13
Helixi107 – 110Combined sources4
Beta strandi111 – 113Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi128 – 133Combined sources6
Helixi135 – 137Combined sources3
Beta strandi138 – 140Combined sources3
Turni143 – 145Combined sources3
Beta strandi152 – 158Combined sources7
Helixi163 – 171Combined sources9
Turni172 – 174Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00g2-177[»]
2J28electron microscopy8.00F2-179[»]
2RDOelectron microscopy9.10F2-179[»]
3BBXelectron microscopy10.00F2-179[»]
3J5Lelectron microscopy6.60F2-178[»]
3J5Selectron microscopy7.50G2-179[»]
3J7Zelectron microscopy3.90F1-179[»]
3J8Gelectron microscopy5.00F1-179[»]
3J9Yelectron microscopy3.90F1-179[»]
3J9Zelectron microscopy3.60L72-179[»]
3JA1electron microscopy3.60LG2-179[»]
3JBUelectron microscopy3.64f1-179[»]
3JBVelectron microscopy3.32f1-179[»]
3JCDelectron microscopy3.70F1-179[»]
3JCEelectron microscopy3.20F1-179[»]
3JCJelectron microscopy3.70E1-179[»]
3JCNelectron microscopy4.60F1-179[»]
4CSUelectron microscopy5.50F2-179[»]
4U1UX-ray2.95BF/DF2-178[»]
4U1VX-ray3.00BF/DF2-178[»]
4U20X-ray2.90BF/DF2-178[»]
4U24X-ray2.90BF/DF2-178[»]
4U25X-ray2.90BF/DF2-178[»]
4U26X-ray2.80BF/DF2-178[»]
4U27X-ray2.80BF/DF2-178[»]
4UY8electron microscopy3.80F2-178[»]
4V47electron microscopy12.30AD2-179[»]
4V48electron microscopy11.50AD2-179[»]
4V4HX-ray3.46BF/DF1-179[»]
4V4QX-ray3.46BF/DF2-179[»]
4V4Velectron microscopy15.00BD3-179[»]
4V4Welectron microscopy15.00BD3-179[»]
4V50X-ray3.22BF/DF2-179[»]
4V52X-ray3.21BF/DF2-179[»]
4V53X-ray3.54BF/DF2-179[»]
4V54X-ray3.30BF/DF2-179[»]
4V55X-ray4.00BF/DF2-179[»]
4V56X-ray3.93BF/DF2-179[»]
4V57X-ray3.50BF/DF2-179[»]
4V5BX-ray3.74AF/CF2-179[»]
4V5Helectron microscopy5.80BF2-179[»]
4V5YX-ray4.45BF/DF2-179[»]
4V64X-ray3.50BF/DF2-179[»]
4V65electron microscopy9.00B22-179[»]
4V66electron microscopy9.00B22-179[»]
4V69electron microscopy6.70BF2-179[»]
4V6CX-ray3.19BF/DF1-179[»]
4V6DX-ray3.81BF/DF1-179[»]
4V6EX-ray3.71BF/DF1-179[»]
4V6Kelectron microscopy8.25AG1-179[»]
4V6Lelectron microscopy13.20BG1-179[»]
4V6Melectron microscopy7.10BF2-179[»]
4V6Nelectron microscopy12.10AG2-179[»]
4V6Oelectron microscopy14.70BG2-179[»]
4V6Pelectron microscopy13.50BG2-179[»]
4V6Qelectron microscopy11.50BG2-179[»]
4V6Relectron microscopy11.50BG2-179[»]
4V6Selectron microscopy13.10AG2-179[»]
4V6Telectron microscopy8.30BF2-178[»]
4V6Velectron microscopy9.80BG2-179[»]
4V6Yelectron microscopy12.00BF1-179[»]
4V6Zelectron microscopy12.00BF1-179[»]
4V70electron microscopy17.00BF1-179[»]
4V71electron microscopy20.00BF1-179[»]
4V72electron microscopy13.00BF1-179[»]
4V73electron microscopy15.00BF1-179[»]
4V74electron microscopy17.00BF1-179[»]
4V75electron microscopy12.00BF1-179[»]
4V76electron microscopy17.00BF1-179[»]
4V77electron microscopy17.00BF1-179[»]
4V78electron microscopy20.00BF1-179[»]
4V79electron microscopy15.00BF1-179[»]
4V7Aelectron microscopy9.00BF1-179[»]
4V7Belectron microscopy6.80BF1-179[»]
4V7Celectron microscopy7.60BG2-179[»]
4V7Delectron microscopy7.60AG2-179[»]
4V7Ielectron microscopy9.60AF1-179[»]
4V7SX-ray3.25BF2-178[»]
DF2-179[»]
4V7TX-ray3.19BF2-178[»]
DF2-179[»]
4V7UX-ray3.10BF/DF2-179[»]
4V7VX-ray3.29BF2-178[»]
DF2-179[»]
4V85X-ray3.20F1-179[»]
4V89X-ray3.70BF1-179[»]
4V9CX-ray3.30BF/DF1-179[»]
4V9DX-ray3.00CF/DF2-178[»]
4V9OX-ray2.90AF/CF/EF/GF1-179[»]
4V9PX-ray2.90AF/CF/EF/GF1-179[»]
4WF1X-ray3.09BF/DF2-178[»]
4WOIX-ray3.00BF/CF1-179[»]
4WWWX-ray3.10RF/YF2-179[»]
4YBBX-ray2.10CF/DF2-178[»]
5ADYelectron microscopy4.50F1-179[»]
5AFIelectron microscopy2.90F1-179[»]
5AKAelectron microscopy5.70F2-179[»]
5GADelectron microscopy3.70F1-179[»]
5GAEelectron microscopy3.33F1-179[»]
5GAFelectron microscopy4.30F2-178[»]
5GAGelectron microscopy3.80F1-179[»]
5GAHelectron microscopy3.80F1-179[»]
5IQRelectron microscopy3.00E1-179[»]
5IT8X-ray3.12CF/DF2-178[»]
5J5BX-ray2.80CF/DF2-178[»]
5J7LX-ray3.00CF/DF2-178[»]
5J88X-ray3.32CF/DF2-179[»]
5J8AX-ray3.10CF/DF2-179[»]
5J91X-ray2.96CF/DF2-179[»]
5JC9X-ray3.03CF/DF2-178[»]
5JTEelectron microscopy3.60BF1-179[»]
5JU8electron microscopy3.60BF1-179[»]
5KCRelectron microscopy3.601G1-179[»]
5KCSelectron microscopy3.901G1-179[»]
5KPSelectron microscopy3.90E1-179[»]
5KPVelectron microscopy4.10D1-179[»]
5KPWelectron microscopy3.90D1-179[»]
5KPXelectron microscopy3.90D1-179[»]
5L3Pelectron microscopy3.70G1-179[»]
ProteinModelPortaliP62399.
SMRiP62399.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62399.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L5P family.Curated

Phylogenomic databases

eggNOGiENOG4105CW6. Bacteria.
COG0094. LUCA.
HOGENOMiHOG000231311.
InParanoidiP62399.
KOiK02931.
OMAiEQVMFHE.
PhylomeDBiP62399.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
HAMAPiMF_01333_B. Ribosomal_L5_B. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
[Graphical view]
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62399-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKLHDYYKD EVVKKLMTEF NYNSVMQVPR VEKITLNMGV GEAIADKKLL
60 70 80 90 100
DNAAADLAAI SGQKPLITKA RKSVAGFKIR QGYPIGCKVT LRGERMWEFF
110 120 130 140 150
ERLITIAVPR IRDFRGLSAK SFDGRGNYSM GVREQIIFPE IDYDKVDRVR
160 170
GLDITITTTA KSDEEGRALL AAFDFPFRK
Length:179
Mass (Da):20,302
Last modified:January 23, 2007 - v2
Checksum:iB2E95A8BE4B8D2A7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti94E → Q AA sequence (PubMed:791672).Curated1
Sequence conflicti127N → D AA sequence (PubMed:791672).Curated1

Mass spectrometryi

Molecular mass is 20169.8 Da from positions 2 - 179. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25717.1.
U18997 Genomic DNA. Translation: AAA58105.1.
U00096 Genomic DNA. Translation: AAC76333.1.
AP009048 Genomic DNA. Translation: BAE77983.1.
M10195 Genomic DNA. Translation: AAA24051.1.
PIRiG65123. R5EC5.
RefSeqiNP_417767.1. NC_000913.3.
WP_001096200.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76333; AAC76333; b3308.
BAE77983; BAE77983; BAE77983.
GeneIDi24910142.
947800.
KEGGiecj:JW3270.
eco:b3308.
PATRICi32122048. VBIEscCol129921_3401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25717.1.
U18997 Genomic DNA. Translation: AAA58105.1.
U00096 Genomic DNA. Translation: AAC76333.1.
AP009048 Genomic DNA. Translation: BAE77983.1.
M10195 Genomic DNA. Translation: AAA24051.1.
PIRiG65123. R5EC5.
RefSeqiNP_417767.1. NC_000913.3.
WP_001096200.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00g2-177[»]
2J28electron microscopy8.00F2-179[»]
2RDOelectron microscopy9.10F2-179[»]
3BBXelectron microscopy10.00F2-179[»]
3J5Lelectron microscopy6.60F2-178[»]
3J5Selectron microscopy7.50G2-179[»]
3J7Zelectron microscopy3.90F1-179[»]
3J8Gelectron microscopy5.00F1-179[»]
3J9Yelectron microscopy3.90F1-179[»]
3J9Zelectron microscopy3.60L72-179[»]
3JA1electron microscopy3.60LG2-179[»]
3JBUelectron microscopy3.64f1-179[»]
3JBVelectron microscopy3.32f1-179[»]
3JCDelectron microscopy3.70F1-179[»]
3JCEelectron microscopy3.20F1-179[»]
3JCJelectron microscopy3.70E1-179[»]
3JCNelectron microscopy4.60F1-179[»]
4CSUelectron microscopy5.50F2-179[»]
4U1UX-ray2.95BF/DF2-178[»]
4U1VX-ray3.00BF/DF2-178[»]
4U20X-ray2.90BF/DF2-178[»]
4U24X-ray2.90BF/DF2-178[»]
4U25X-ray2.90BF/DF2-178[»]
4U26X-ray2.80BF/DF2-178[»]
4U27X-ray2.80BF/DF2-178[»]
4UY8electron microscopy3.80F2-178[»]
4V47electron microscopy12.30AD2-179[»]
4V48electron microscopy11.50AD2-179[»]
4V4HX-ray3.46BF/DF1-179[»]
4V4QX-ray3.46BF/DF2-179[»]
4V4Velectron microscopy15.00BD3-179[»]
4V4Welectron microscopy15.00BD3-179[»]
4V50X-ray3.22BF/DF2-179[»]
4V52X-ray3.21BF/DF2-179[»]
4V53X-ray3.54BF/DF2-179[»]
4V54X-ray3.30BF/DF2-179[»]
4V55X-ray4.00BF/DF2-179[»]
4V56X-ray3.93BF/DF2-179[»]
4V57X-ray3.50BF/DF2-179[»]
4V5BX-ray3.74AF/CF2-179[»]
4V5Helectron microscopy5.80BF2-179[»]
4V5YX-ray4.45BF/DF2-179[»]
4V64X-ray3.50BF/DF2-179[»]
4V65electron microscopy9.00B22-179[»]
4V66electron microscopy9.00B22-179[»]
4V69electron microscopy6.70BF2-179[»]
4V6CX-ray3.19BF/DF1-179[»]
4V6DX-ray3.81BF/DF1-179[»]
4V6EX-ray3.71BF/DF1-179[»]
4V6Kelectron microscopy8.25AG1-179[»]
4V6Lelectron microscopy13.20BG1-179[»]
4V6Melectron microscopy7.10BF2-179[»]
4V6Nelectron microscopy12.10AG2-179[»]
4V6Oelectron microscopy14.70BG2-179[»]
4V6Pelectron microscopy13.50BG2-179[»]
4V6Qelectron microscopy11.50BG2-179[»]
4V6Relectron microscopy11.50BG2-179[»]
4V6Selectron microscopy13.10AG2-179[»]
4V6Telectron microscopy8.30BF2-178[»]
4V6Velectron microscopy9.80BG2-179[»]
4V6Yelectron microscopy12.00BF1-179[»]
4V6Zelectron microscopy12.00BF1-179[»]
4V70electron microscopy17.00BF1-179[»]
4V71electron microscopy20.00BF1-179[»]
4V72electron microscopy13.00BF1-179[»]
4V73electron microscopy15.00BF1-179[»]
4V74electron microscopy17.00BF1-179[»]
4V75electron microscopy12.00BF1-179[»]
4V76electron microscopy17.00BF1-179[»]
4V77electron microscopy17.00BF1-179[»]
4V78electron microscopy20.00BF1-179[»]
4V79electron microscopy15.00BF1-179[»]
4V7Aelectron microscopy9.00BF1-179[»]
4V7Belectron microscopy6.80BF1-179[»]
4V7Celectron microscopy7.60BG2-179[»]
4V7Delectron microscopy7.60AG2-179[»]
4V7Ielectron microscopy9.60AF1-179[»]
4V7SX-ray3.25BF2-178[»]
DF2-179[»]
4V7TX-ray3.19BF2-178[»]
DF2-179[»]
4V7UX-ray3.10BF/DF2-179[»]
4V7VX-ray3.29BF2-178[»]
DF2-179[»]
4V85X-ray3.20F1-179[»]
4V89X-ray3.70BF1-179[»]
4V9CX-ray3.30BF/DF1-179[»]
4V9DX-ray3.00CF/DF2-178[»]
4V9OX-ray2.90AF/CF/EF/GF1-179[»]
4V9PX-ray2.90AF/CF/EF/GF1-179[»]
4WF1X-ray3.09BF/DF2-178[»]
4WOIX-ray3.00BF/CF1-179[»]
4WWWX-ray3.10RF/YF2-179[»]
4YBBX-ray2.10CF/DF2-178[»]
5ADYelectron microscopy4.50F1-179[»]
5AFIelectron microscopy2.90F1-179[»]
5AKAelectron microscopy5.70F2-179[»]
5GADelectron microscopy3.70F1-179[»]
5GAEelectron microscopy3.33F1-179[»]
5GAFelectron microscopy4.30F2-178[»]
5GAGelectron microscopy3.80F1-179[»]
5GAHelectron microscopy3.80F1-179[»]
5IQRelectron microscopy3.00E1-179[»]
5IT8X-ray3.12CF/DF2-178[»]
5J5BX-ray2.80CF/DF2-178[»]
5J7LX-ray3.00CF/DF2-178[»]
5J88X-ray3.32CF/DF2-179[»]
5J8AX-ray3.10CF/DF2-179[»]
5J91X-ray2.96CF/DF2-179[»]
5JC9X-ray3.03CF/DF2-178[»]
5JTEelectron microscopy3.60BF1-179[»]
5JU8electron microscopy3.60BF1-179[»]
5KCRelectron microscopy3.601G1-179[»]
5KCSelectron microscopy3.901G1-179[»]
5KPSelectron microscopy3.90E1-179[»]
5KPVelectron microscopy4.10D1-179[»]
5KPWelectron microscopy3.90D1-179[»]
5KPXelectron microscopy3.90D1-179[»]
5L3Pelectron microscopy3.70G1-179[»]
ProteinModelPortaliP62399.
SMRiP62399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852112. 1 interactor.
DIPiDIP-35914N.
IntActiP62399. 71 interactors.
MINTiMINT-1238892.
STRINGi511145.b3308.

Proteomic databases

EPDiP62399.
PaxDbiP62399.
PRIDEiP62399.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76333; AAC76333; b3308.
BAE77983; BAE77983; BAE77983.
GeneIDi24910142.
947800.
KEGGiecj:JW3270.
eco:b3308.
PATRICi32122048. VBIEscCol129921_3401.

Organism-specific databases

EchoBASEiEB0861.
EcoGeneiEG10868. rplE.

Phylogenomic databases

eggNOGiENOG4105CW6. Bacteria.
COG0094. LUCA.
HOGENOMiHOG000231311.
InParanoidiP62399.
KOiK02931.
OMAiEQVMFHE.
PhylomeDBiP62399.

Enzyme and pathway databases

BioCyciEcoCyc:EG10868-MONOMER.
ECOL316407:JW3270-MONOMER.
MetaCyc:EG10868-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP62399.
PROiP62399.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
HAMAPiMF_01333_B. Ribosomal_L5_B. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
[Graphical view]
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL5_ECOLI
AccessioniPrimary (citable) accession number: P62399
Secondary accession number(s): P02389, Q2M6X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 133 of the entry and version 2 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. 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.