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Protein

30S ribosomal protein S3

Gene

rpsC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (By similarity).By similarity
Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.1 Publication

GO - Molecular functioni

  1. mRNA binding Source: UniProtKB-HAMAP
  2. rRNA binding Source: UniProtKB-HAMAP
  3. structural constituent of ribosome Source: GO_Central

GO - Biological processi

  1. cytoplasmic translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10902-MONOMER.
ECOL316407:JW3276-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S3
Gene namesi
Name:rpsC
Ordered Locus Names:b3314, JW3276
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10902. rpsC.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1355RRAMK → AAAMA: Decreases mRNA unwinding ability of the ribosome. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 23323230S ribosomal protein S3PRO_0000130113Add
BLAST

Proteomic databases

PaxDbiP0A7V3.
PRIDEiP0A7V3.

Expressioni

Gene expression databases

GenevestigatoriP0A7V3.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14 (By similarity). With proteins S4 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity. Some nascent polypeptide chains are able to cross-link to this protein in situ.By similarity

Protein-protein interaction databases

BioGridi852126. 1 interaction.
DIPiDIP-35807N.
IntActiP0A7V3. 188 interactions.
MINTiMINT-6478122.
STRINGi511145.b3314.

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 115Combined sources
Helixi12 – 154Combined sources
Beta strandi19 – 213Combined sources
Turni26 – 283Combined sources
Helixi29 – 4618Combined sources
Helixi47 – 493Combined sources
Beta strandi52 – 576Combined sources
Helixi60 – 623Combined sources
Beta strandi67 – 715Combined sources
Helixi73 – 775Combined sources
Helixi79 – 813Combined sources
Helixi82 – 9413Combined sources
Beta strandi95 – 973Combined sources
Beta strandi102 – 1054Combined sources
Helixi109 – 1113Combined sources
Helixi113 – 12614Combined sources
Helixi130 – 14213Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi155 – 1595Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi175 – 1773Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi182 – 1909Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi195 – 2039Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-C2-207[»]
2YKRelectron microscopy9.80C2-207[»]
4A2Ielectron microscopy16.50C2-207[»]
4ADVelectron microscopy13.50C2-233[»]
4U1UX-ray2.95AC/CC2-207[»]
4U1VX-ray3.00AC/CC2-207[»]
4U20X-ray2.90AC/CC2-207[»]
4U24X-ray2.90AC/CC2-207[»]
4U25X-ray2.90AC/CC2-207[»]
4U26X-ray2.80AC/CC2-207[»]
4U27X-ray2.80AC/CC2-207[»]
4V47electron microscopy12.30BC2-233[»]
4V48electron microscopy11.50BC2-233[»]
4V4HX-ray3.46AC/CC1-233[»]
4V4QX-ray3.46AC/CC2-233[»]
4V4Velectron microscopy15.00AC2-207[»]
4V4Welectron microscopy15.00AC2-207[»]
4V50X-ray3.22AC/CC2-233[»]
4V52X-ray3.21AC/CC2-233[»]
4V53X-ray3.54AC/CC2-233[»]
4V54X-ray3.30AC/CC2-233[»]
4V55X-ray4.00AC/CC2-233[»]
4V56X-ray3.93AC/CC2-233[»]
4V57X-ray3.50AC/CC2-233[»]
4V5BX-ray3.74BC/DC2-233[»]
4V5Helectron microscopy5.80AC2-207[»]
4V5YX-ray4.45AC/CC2-233[»]
4V64X-ray3.50AC/CC2-233[»]
4V65electron microscopy9.00AO1-233[»]
4V66electron microscopy9.00AO1-233[»]
4V69electron microscopy6.70AC2-207[»]
4V6CX-ray3.19AC/CC1-233[»]
4V6DX-ray3.81AC/CC1-233[»]
4V6EX-ray3.71AC/CC1-233[»]
4V6Kelectron microscopy8.25BG1-233[»]
4V6Lelectron microscopy13.20AG1-233[»]
4V6Melectron microscopy7.10AC2-233[»]
4V6Nelectron microscopy12.10BF2-233[»]
4V6Oelectron microscopy14.70AF2-233[»]
4V6Pelectron microscopy13.50AF2-233[»]
4V6Qelectron microscopy11.50AF2-233[»]
4V6Relectron microscopy11.50AF2-233[»]
4V6Selectron microscopy13.10BE2-233[»]
4V6Telectron microscopy8.30AC2-207[»]
4V6Velectron microscopy9.80C2-233[»]
4V6Yelectron microscopy12.00AC1-207[»]
4V6Zelectron microscopy12.00AC1-207[»]
4V70electron microscopy17.00AC1-207[»]
4V71electron microscopy20.00AC1-207[»]
4V72electron microscopy13.00AC1-207[»]
4V73electron microscopy15.00AC1-207[»]
4V74electron microscopy17.00AC1-207[»]
4V75electron microscopy12.00AC1-207[»]
4V76electron microscopy17.00AC1-207[»]
4V77electron microscopy17.00AC1-207[»]
4V78electron microscopy20.00AC1-207[»]
4V79electron microscopy15.00AC1-207[»]
4V7Aelectron microscopy9.00AC1-207[»]
4V7Belectron microscopy6.80AC1-233[»]
4V7Celectron microscopy7.60AC2-233[»]
4V7Delectron microscopy7.60BC2-233[»]
4V7Ielectron microscopy9.60BC1-233[»]
4V7SX-ray3.25AC/CC2-207[»]
4V7TX-ray3.19AC/CC2-207[»]
4V7UX-ray3.10AC/CC2-207[»]
4V7VX-ray3.29AC/CC2-207[»]
4V85X-ray3.20C1-233[»]
4V89X-ray3.70AC1-233[»]
4V9CX-ray3.30AC/CC1-233[»]
4V9DX-ray3.00AC/BC2-207[»]
4V9OX-ray2.90BC/DC/FC/HC1-233[»]
4V9PX-ray2.90BC/DC/FC/HC1-233[»]
4WF1X-ray3.09AC/CC2-207[»]
4WWWX-ray3.10QC/XC2-207[»]
ProteinModelPortaliP0A7V3.
SMRiP0A7V3. Positions 2-233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7V3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 10769KH type-2Add
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S3P family.Curated
Contains 1 KH type-2 domain.Curated

Phylogenomic databases

eggNOGiCOG0092.
HOGENOMiHOG000210610.
InParanoidiP0A7V3.
KOiK02982.
OMAiMGQKTNP.
OrthoDBiEOG6K13X3.
PhylomeDBiP0A7V3.

Family and domain databases

Gene3Di3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
HAMAPiMF_01309_B. Ribosomal_S3_B.
InterProiIPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR005704. Ribosomal_S3_bac.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
[Graphical view]
PfamiPF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsiTIGR01009. rpsC_bact. 1 hit.
PROSITEiPS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7V3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQKVHPNGI RLGIVKPWNS TWFANTKEFA DNLDSDFKVR QYLTKELAKA
60 70 80 90 100
SVSRIVIERP AKSIRVTIHT ARPGIVIGKK GEDVEKLRKV VADIAGVPAQ
110 120 130 140 150
INIAEVRKPE LDAKLVADSI TSQLERRVMF RRAMKRAVQN AMRLGAKGIK
160 170 180 190 200
VEVSGRLGGA EIARTEWYRE GRVPLHTLRA DIDYNTSEAH TTYGVIGVKV
210 220 230
WIFKGEILGG MAAVEQPEKP AAQPKKQQRK GRK
Length:233
Mass (Da):25,983
Last modified:January 23, 2007 - v2
Checksum:i6D0131A285B7AAB3
GO

Mass spectrometryi

Molecular mass is 25851.9 Da from positions 2 - 233. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26466.1.
U18997 Genomic DNA. Translation: AAA58111.1.
U00096 Genomic DNA. Translation: AAC76339.1.
AP009048 Genomic DNA. Translation: BAE77977.1.
PIRiH23129. R3EC3.
RefSeqiNP_417773.1. NC_000913.3.
YP_492118.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76339; AAC76339; b3314.
BAE77977; BAE77977; BAE77977.
GeneIDi12932292.
947814.
KEGGiecj:Y75_p3862.
eco:b3314.
PATRICi32122060. VBIEscCol129921_3407.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26466.1.
U18997 Genomic DNA. Translation: AAA58111.1.
U00096 Genomic DNA. Translation: AAC76339.1.
AP009048 Genomic DNA. Translation: BAE77977.1.
PIRiH23129. R3EC3.
RefSeqiNP_417773.1. NC_000913.3.
YP_492118.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-C2-207[»]
2YKRelectron microscopy9.80C2-207[»]
4A2Ielectron microscopy16.50C2-207[»]
4ADVelectron microscopy13.50C2-233[»]
4U1UX-ray2.95AC/CC2-207[»]
4U1VX-ray3.00AC/CC2-207[»]
4U20X-ray2.90AC/CC2-207[»]
4U24X-ray2.90AC/CC2-207[»]
4U25X-ray2.90AC/CC2-207[»]
4U26X-ray2.80AC/CC2-207[»]
4U27X-ray2.80AC/CC2-207[»]
4V47electron microscopy12.30BC2-233[»]
4V48electron microscopy11.50BC2-233[»]
4V4HX-ray3.46AC/CC1-233[»]
4V4QX-ray3.46AC/CC2-233[»]
4V4Velectron microscopy15.00AC2-207[»]
4V4Welectron microscopy15.00AC2-207[»]
4V50X-ray3.22AC/CC2-233[»]
4V52X-ray3.21AC/CC2-233[»]
4V53X-ray3.54AC/CC2-233[»]
4V54X-ray3.30AC/CC2-233[»]
4V55X-ray4.00AC/CC2-233[»]
4V56X-ray3.93AC/CC2-233[»]
4V57X-ray3.50AC/CC2-233[»]
4V5BX-ray3.74BC/DC2-233[»]
4V5Helectron microscopy5.80AC2-207[»]
4V5YX-ray4.45AC/CC2-233[»]
4V64X-ray3.50AC/CC2-233[»]
4V65electron microscopy9.00AO1-233[»]
4V66electron microscopy9.00AO1-233[»]
4V69electron microscopy6.70AC2-207[»]
4V6CX-ray3.19AC/CC1-233[»]
4V6DX-ray3.81AC/CC1-233[»]
4V6EX-ray3.71AC/CC1-233[»]
4V6Kelectron microscopy8.25BG1-233[»]
4V6Lelectron microscopy13.20AG1-233[»]
4V6Melectron microscopy7.10AC2-233[»]
4V6Nelectron microscopy12.10BF2-233[»]
4V6Oelectron microscopy14.70AF2-233[»]
4V6Pelectron microscopy13.50AF2-233[»]
4V6Qelectron microscopy11.50AF2-233[»]
4V6Relectron microscopy11.50AF2-233[»]
4V6Selectron microscopy13.10BE2-233[»]
4V6Telectron microscopy8.30AC2-207[»]
4V6Velectron microscopy9.80C2-233[»]
4V6Yelectron microscopy12.00AC1-207[»]
4V6Zelectron microscopy12.00AC1-207[»]
4V70electron microscopy17.00AC1-207[»]
4V71electron microscopy20.00AC1-207[»]
4V72electron microscopy13.00AC1-207[»]
4V73electron microscopy15.00AC1-207[»]
4V74electron microscopy17.00AC1-207[»]
4V75electron microscopy12.00AC1-207[»]
4V76electron microscopy17.00AC1-207[»]
4V77electron microscopy17.00AC1-207[»]
4V78electron microscopy20.00AC1-207[»]
4V79electron microscopy15.00AC1-207[»]
4V7Aelectron microscopy9.00AC1-207[»]
4V7Belectron microscopy6.80AC1-233[»]
4V7Celectron microscopy7.60AC2-233[»]
4V7Delectron microscopy7.60BC2-233[»]
4V7Ielectron microscopy9.60BC1-233[»]
4V7SX-ray3.25AC/CC2-207[»]
4V7TX-ray3.19AC/CC2-207[»]
4V7UX-ray3.10AC/CC2-207[»]
4V7VX-ray3.29AC/CC2-207[»]
4V85X-ray3.20C1-233[»]
4V89X-ray3.70AC1-233[»]
4V9CX-ray3.30AC/CC1-233[»]
4V9DX-ray3.00AC/BC2-207[»]
4V9OX-ray2.90BC/DC/FC/HC1-233[»]
4V9PX-ray2.90BC/DC/FC/HC1-233[»]
4WF1X-ray3.09AC/CC2-207[»]
4WWWX-ray3.10QC/XC2-207[»]
ProteinModelPortaliP0A7V3.
SMRiP0A7V3. Positions 2-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852126. 1 interaction.
DIPiDIP-35807N.
IntActiP0A7V3. 188 interactions.
MINTiMINT-6478122.
STRINGi511145.b3314.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00759. Tetracycline.

Proteomic databases

PaxDbiP0A7V3.
PRIDEiP0A7V3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76339; AAC76339; b3314.
BAE77977; BAE77977; BAE77977.
GeneIDi12932292.
947814.
KEGGiecj:Y75_p3862.
eco:b3314.
PATRICi32122060. VBIEscCol129921_3407.

Organism-specific databases

EchoBASEiEB0895.
EcoGeneiEG10902. rpsC.

Phylogenomic databases

eggNOGiCOG0092.
HOGENOMiHOG000210610.
InParanoidiP0A7V3.
KOiK02982.
OMAiMGQKTNP.
OrthoDBiEOG6K13X3.
PhylomeDBiP0A7V3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10902-MONOMER.
ECOL316407:JW3276-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7V3.
PROiP0A7V3.

Gene expression databases

GenevestigatoriP0A7V3.

Family and domain databases

Gene3Di3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
HAMAPiMF_01309_B. Ribosomal_S3_B.
InterProiIPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR005704. Ribosomal_S3_bac.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
[Graphical view]
PfamiPF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsiTIGR01009. rpsC_bact. 1 hit.
PROSITEiPS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the Escherichia coli S10 ribosomal protein operon."
    Zurawski G., Zurawski S.M.
    Nucleic Acids Res. 13:4521-4526(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The primary structure of protein S3 from the small ribosomal subunit of Escherichia coli."
    Brauer D., Roming R.
    FEBS Lett. 106:352-357(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-233.
    Strain: K.
  5. "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
    Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
    EMBO J. 14:4578-4588(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 39-49 AND 87-108, CROSS-LINKING TO RRNA.
    Strain: MRE-600.
  6. "Flexibility of the nascent polypeptide chain within the ribosome --contacts from the peptide N-terminus to a specific region of the 30S subunit."
    Choi K.M., Atkins J.F., Gesteland R.F., Brimacombe R.
    Eur. J. Biochem. 255:409-413(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
  7. "mRNA helicase activity of the ribosome."
    Takyar S., Hickerson R.P., Noller H.F.
    Cell 120:49-58(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN MRNA HELICASE ACTIVITY, MUTAGENESIS.
    Strain: MRE-600.
  8. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  9. "All-atom homology model of the Escherichia coli 30S ribosomal subunit."
    Tung C.-S., Joseph S., Sanbonmatsu K.Y.
    Nat. Struct. Biol. 9:750-755(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  10. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS3_ECOLI
AccessioniPrimary (citable) accession number: P0A7V3
Secondary accession number(s): P02352, Q2M6X9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 109 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

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.