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Protein

50S ribosomal protein L3

Gene

rplC

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

Functioni

One of two assembly initiator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.2 Publications

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: CAFA

GO - Biological processi

  • ribosomal large subunit assembly Source: CAFA
  • translation Source: InterPro

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10866-MONOMER.
MetaCyc:EG10866-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L3
Alternative name(s):
Large ribosomal subunit protein uL31 Publication
Gene namesi
Name:rplC
Ordered Locus Names:b3320, JW3282
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10866. rplC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: CAFA

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000770981 – 20950S ribosomal protein L3Add BLAST209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38N6-succinyllysine1 Publication1
Modified residuei150N5-methylglutamine1 Publication1

Post-translational modificationi

Methylated by PrmB.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

EPDiP60438.
PaxDbiP60438.
PRIDEiP60438.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit (PubMed:365579, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Forms a cluster with proteins L14 and L19.9 Publications

Protein-protein interaction databases

DIPiDIP-10744N.
IntActiP60438. 144 interactors.
MINTiMINT-1302843.
STRINGi511145.b3320.

Structurei

Secondary structure

1209
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 15Combined sources12
Beta strandi21 – 28Combined sources8
Beta strandi32 – 38Combined sources7
Turni40 – 42Combined sources3
Beta strandi43 – 45Combined sources3
Beta strandi47 – 51Combined sources5
Turni57 – 59Combined sources3
Helixi62 – 71Combined sources10
Beta strandi80 – 83Combined sources4
Helixi98 – 101Combined sources4
Beta strandi105 – 112Combined sources8
Beta strandi117 – 119Combined sources3
Helixi121 – 125Combined sources5
Beta strandi132 – 135Combined sources4
Beta strandi140 – 142Combined sources3
Beta strandi163 – 166Combined sources4
Beta strandi168 – 181Combined sources14
Turni182 – 185Combined sources4
Beta strandi186 – 191Combined sources6
Beta strandi200 – 205Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00e2-209[»]
2J28electron microscopy8.00D1-209[»]
2RDOelectron microscopy9.10D1-209[»]
3BBXelectron microscopy10.00D1-209[»]
3J5Lelectron microscopy6.60D1-209[»]
3J7Zelectron microscopy3.90D1-209[»]
3J8Gelectron microscopy5.00D1-209[»]
3J9Yelectron microscopy3.90D1-209[»]
3J9Zelectron microscopy3.60LX1-209[»]
3JA1electron microscopy3.60LE1-209[»]
3JBUelectron microscopy3.64d1-209[»]
3JBVelectron microscopy3.32d1-209[»]
3JCDelectron microscopy3.70D1-209[»]
3JCEelectron microscopy3.20D1-209[»]
3JCJelectron microscopy3.70C1-209[»]
3JCNelectron microscopy4.60D1-209[»]
4CSUelectron microscopy5.50D1-209[»]
4U1UX-ray2.95BD/DD1-209[»]
4U1VX-ray3.00BD/DD1-209[»]
4U20X-ray2.90BD/DD1-209[»]
4U24X-ray2.90BD/DD1-209[»]
4U25X-ray2.90BD/DD1-209[»]
4U26X-ray2.80BD/DD1-209[»]
4U27X-ray2.80BD/DD1-209[»]
4UY8electron microscopy3.80D1-209[»]
4V47electron microscopy12.30AB1-209[»]
4V48electron microscopy11.50AB1-209[»]
4V4HX-ray3.46BD/DD1-209[»]
4V4QX-ray3.46BD/DD1-209[»]
4V4Velectron microscopy15.00BB1-209[»]
4V4Welectron microscopy15.00BB1-209[»]
4V50X-ray3.22BD/DD1-209[»]
4V52X-ray3.21BD/DD1-209[»]
4V53X-ray3.54BD/DD1-209[»]
4V54X-ray3.30BD/DD1-209[»]
4V55X-ray4.00BD/DD1-209[»]
4V56X-ray3.93BD/DD1-209[»]
4V57X-ray3.50BD/DD1-209[»]
4V5BX-ray3.74AD/CD1-209[»]
4V5Helectron microscopy5.80BD1-209[»]
4V5YX-ray4.45BD/DD1-209[»]
4V64X-ray3.50BD/DD1-209[»]
4V65electron microscopy9.00BY1-209[»]
4V66electron microscopy9.00BY1-209[»]
4V69electron microscopy6.70BD1-209[»]
4V6CX-ray3.19BD/DD1-209[»]
4V6DX-ray3.81BD/DD1-209[»]
4V6EX-ray3.71BD/DD1-209[»]
4V6Kelectron microscopy8.25AE1-209[»]
4V6Lelectron microscopy13.20BE1-209[»]
4V6Melectron microscopy7.10BD1-209[»]
4V6Nelectron microscopy12.10AE1-209[»]
4V6Oelectron microscopy14.70BE1-209[»]
4V6Pelectron microscopy13.50BE1-209[»]
4V6Qelectron microscopy11.50BE1-209[»]
4V6Relectron microscopy11.50BE1-209[»]
4V6Selectron microscopy13.10AE1-209[»]
4V6Telectron microscopy8.30BD1-209[»]
4V6Velectron microscopy9.80BE1-209[»]
4V6Yelectron microscopy12.00BD1-209[»]
4V6Zelectron microscopy12.00BD1-209[»]
4V70electron microscopy17.00BD1-209[»]
4V71electron microscopy20.00BD1-209[»]
4V72electron microscopy13.00BD1-209[»]
4V73electron microscopy15.00BD1-209[»]
4V74electron microscopy17.00BD1-209[»]
4V75electron microscopy12.00BD1-209[»]
4V76electron microscopy17.00BD1-209[»]
4V77electron microscopy17.00BD1-209[»]
4V78electron microscopy20.00BD1-209[»]
4V79electron microscopy15.00BD1-209[»]
4V7Aelectron microscopy9.00BD1-209[»]
4V7Belectron microscopy6.80BD1-209[»]
4V7Celectron microscopy7.60BE1-209[»]
4V7Delectron microscopy7.60AE1-209[»]
4V7Ielectron microscopy9.60AD1-209[»]
4V7SX-ray3.25BD/DD1-209[»]
4V7TX-ray3.19BD/DD1-209[»]
4V7UX-ray3.10BD/DD1-209[»]
4V7VX-ray3.29BD/DD1-209[»]
4V85X-ray3.20D1-209[»]
4V89X-ray3.70BD1-209[»]
4V9CX-ray3.30BD/DD1-209[»]
4V9DX-ray3.00CD/DD1-209[»]
4V9OX-ray2.90AD/CD/ED/GD1-209[»]
4V9PX-ray2.90AD/CD/ED/GD1-209[»]
4WF1X-ray3.09BD/DD1-209[»]
4WOIX-ray3.00BD/CD1-209[»]
4WWWX-ray3.10RD/YD1-209[»]
4YBBX-ray2.10CD/DD1-209[»]
5ADYelectron microscopy4.50D1-209[»]
5AFIelectron microscopy2.90D1-209[»]
5AKAelectron microscopy5.70D1-209[»]
5GADelectron microscopy3.70D1-209[»]
5GAEelectron microscopy3.33D1-209[»]
5GAFelectron microscopy4.30D1-209[»]
5GAGelectron microscopy3.80D1-209[»]
5GAHelectron microscopy3.80D1-209[»]
5H5Uelectron microscopy3.00D1-209[»]
5IQRelectron microscopy3.00C1-209[»]
5IT8X-ray3.12CD/DD1-209[»]
5J5BX-ray2.80CD/DD1-209[»]
5J7LX-ray3.00CD/DD1-209[»]
5J88X-ray3.32CD/DD1-209[»]
5J8AX-ray3.10CD/DD1-209[»]
5J91X-ray2.96CD/DD1-209[»]
5JC9X-ray3.03CD/DD1-209[»]
5JTEelectron microscopy3.60BD1-209[»]
5JU8electron microscopy3.60BD1-209[»]
5KCRelectron microscopy3.601E1-209[»]
5KCSelectron microscopy3.901E1-209[»]
5KPSelectron microscopy3.90C1-209[»]
5KPVelectron microscopy4.10B1-209[»]
5KPWelectron microscopy3.90B1-209[»]
5KPXelectron microscopy3.90B1-209[»]
5L3Pelectron microscopy3.70E1-209[»]
5LZAelectron microscopy3.60D1-209[»]
5LZBelectron microscopy5.30D1-209[»]
5LZCelectron microscopy4.80D1-209[»]
5LZDelectron microscopy3.40D1-209[»]
5LZEelectron microscopy3.50D1-209[»]
5LZFelectron microscopy4.60D1-209[»]
5MDVelectron microscopy2.97C1-209[»]
5MDWelectron microscopy3.06C1-209[»]
5MDYelectron microscopy3.35C1-209[»]
5MDZelectron microscopy3.10C1-209[»]
5MGPelectron microscopy3.10D1-209[»]
5U4Ielectron microscopy3.50D1-209[»]
ProteinModelPortaliP60438.
SMRiP60438.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60438.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105EEE. Bacteria.
COG0087. LUCA.
HOGENOMiHOG000100368.
InParanoidiP60438.
KOiK02906.
OMAiKRMAGRY.
PhylomeDBiP60438.

Family and domain databases

HAMAPiMF_01325_B. Ribosomal_L3_B. 1 hit.
InterProiView protein in InterPro
IPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
PANTHERiPTHR11229. PTHR11229. 1 hit.
PfamiView protein in Pfam
PF00297. Ribosomal_L3. 1 hit.
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03625. L3_bact. 1 hit.
PROSITEiView protein in PROSITE
PS00474. RIBOSOMAL_L3. 1 hit.

Sequencei

Sequence statusi: Complete.

P60438-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIGLVGKKVG MTRIFTEDGV SIPVTVIEVE ANRVTQVKDL ANDGYRAIQV
60 70 80 90 100
TTGAKKANRV TKPEAGHFAK AGVEAGRGLW EFRLAEGEEF TVGQSISVEL
110 120 130 140 150
FADVKKVDVT GTSKGKGFAG TVKRWNFRTQ DATHGNSLSH RVPGSIGQNQ
160 170 180 190 200
TPGKVFKGKK MAGQMGNERV TVQSLDVVRV DAERNLLLVK GAVPGATGSD

LIVKPAVKA
Length:209
Mass (Da):22,244
Last modified:July 21, 1986 - v1
Checksum:iEA8E10EDD2C0A8FD
GO

Mass spectrometryi

Molecular mass is 22257.2 Da from positions 1 - 209. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26460.1.
U18997 Genomic DNA. Translation: AAA58117.1.
U00096 Genomic DNA. Translation: AAC76345.1.
AP009048 Genomic DNA. Translation: BAE77971.1.
V00344 Genomic DNA. Translation: CAA23634.1.
PIRiA02757. R5EC3.
RefSeqiNP_417779.1. NC_000913.3.
WP_000579833.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76345; AAC76345; b3320.
BAE77971; BAE77971; BAE77971.
GeneIDi947817.
KEGGiecj:JW3282.
eco:b3320.
PATRICi32122072. VBIEscCol129921_3413.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26460.1.
U18997 Genomic DNA. Translation: AAA58117.1.
U00096 Genomic DNA. Translation: AAC76345.1.
AP009048 Genomic DNA. Translation: BAE77971.1.
V00344 Genomic DNA. Translation: CAA23634.1.
PIRiA02757. R5EC3.
RefSeqiNP_417779.1. NC_000913.3.
WP_000579833.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00e2-209[»]
2J28electron microscopy8.00D1-209[»]
2RDOelectron microscopy9.10D1-209[»]
3BBXelectron microscopy10.00D1-209[»]
3J5Lelectron microscopy6.60D1-209[»]
3J7Zelectron microscopy3.90D1-209[»]
3J8Gelectron microscopy5.00D1-209[»]
3J9Yelectron microscopy3.90D1-209[»]
3J9Zelectron microscopy3.60LX1-209[»]
3JA1electron microscopy3.60LE1-209[»]
3JBUelectron microscopy3.64d1-209[»]
3JBVelectron microscopy3.32d1-209[»]
3JCDelectron microscopy3.70D1-209[»]
3JCEelectron microscopy3.20D1-209[»]
3JCJelectron microscopy3.70C1-209[»]
3JCNelectron microscopy4.60D1-209[»]
4CSUelectron microscopy5.50D1-209[»]
4U1UX-ray2.95BD/DD1-209[»]
4U1VX-ray3.00BD/DD1-209[»]
4U20X-ray2.90BD/DD1-209[»]
4U24X-ray2.90BD/DD1-209[»]
4U25X-ray2.90BD/DD1-209[»]
4U26X-ray2.80BD/DD1-209[»]
4U27X-ray2.80BD/DD1-209[»]
4UY8electron microscopy3.80D1-209[»]
4V47electron microscopy12.30AB1-209[»]
4V48electron microscopy11.50AB1-209[»]
4V4HX-ray3.46BD/DD1-209[»]
4V4QX-ray3.46BD/DD1-209[»]
4V4Velectron microscopy15.00BB1-209[»]
4V4Welectron microscopy15.00BB1-209[»]
4V50X-ray3.22BD/DD1-209[»]
4V52X-ray3.21BD/DD1-209[»]
4V53X-ray3.54BD/DD1-209[»]
4V54X-ray3.30BD/DD1-209[»]
4V55X-ray4.00BD/DD1-209[»]
4V56X-ray3.93BD/DD1-209[»]
4V57X-ray3.50BD/DD1-209[»]
4V5BX-ray3.74AD/CD1-209[»]
4V5Helectron microscopy5.80BD1-209[»]
4V5YX-ray4.45BD/DD1-209[»]
4V64X-ray3.50BD/DD1-209[»]
4V65electron microscopy9.00BY1-209[»]
4V66electron microscopy9.00BY1-209[»]
4V69electron microscopy6.70BD1-209[»]
4V6CX-ray3.19BD/DD1-209[»]
4V6DX-ray3.81BD/DD1-209[»]
4V6EX-ray3.71BD/DD1-209[»]
4V6Kelectron microscopy8.25AE1-209[»]
4V6Lelectron microscopy13.20BE1-209[»]
4V6Melectron microscopy7.10BD1-209[»]
4V6Nelectron microscopy12.10AE1-209[»]
4V6Oelectron microscopy14.70BE1-209[»]
4V6Pelectron microscopy13.50BE1-209[»]
4V6Qelectron microscopy11.50BE1-209[»]
4V6Relectron microscopy11.50BE1-209[»]
4V6Selectron microscopy13.10AE1-209[»]
4V6Telectron microscopy8.30BD1-209[»]
4V6Velectron microscopy9.80BE1-209[»]
4V6Yelectron microscopy12.00BD1-209[»]
4V6Zelectron microscopy12.00BD1-209[»]
4V70electron microscopy17.00BD1-209[»]
4V71electron microscopy20.00BD1-209[»]
4V72electron microscopy13.00BD1-209[»]
4V73electron microscopy15.00BD1-209[»]
4V74electron microscopy17.00BD1-209[»]
4V75electron microscopy12.00BD1-209[»]
4V76electron microscopy17.00BD1-209[»]
4V77electron microscopy17.00BD1-209[»]
4V78electron microscopy20.00BD1-209[»]
4V79electron microscopy15.00BD1-209[»]
4V7Aelectron microscopy9.00BD1-209[»]
4V7Belectron microscopy6.80BD1-209[»]
4V7Celectron microscopy7.60BE1-209[»]
4V7Delectron microscopy7.60AE1-209[»]
4V7Ielectron microscopy9.60AD1-209[»]
4V7SX-ray3.25BD/DD1-209[»]
4V7TX-ray3.19BD/DD1-209[»]
4V7UX-ray3.10BD/DD1-209[»]
4V7VX-ray3.29BD/DD1-209[»]
4V85X-ray3.20D1-209[»]
4V89X-ray3.70BD1-209[»]
4V9CX-ray3.30BD/DD1-209[»]
4V9DX-ray3.00CD/DD1-209[»]
4V9OX-ray2.90AD/CD/ED/GD1-209[»]
4V9PX-ray2.90AD/CD/ED/GD1-209[»]
4WF1X-ray3.09BD/DD1-209[»]
4WOIX-ray3.00BD/CD1-209[»]
4WWWX-ray3.10RD/YD1-209[»]
4YBBX-ray2.10CD/DD1-209[»]
5ADYelectron microscopy4.50D1-209[»]
5AFIelectron microscopy2.90D1-209[»]
5AKAelectron microscopy5.70D1-209[»]
5GADelectron microscopy3.70D1-209[»]
5GAEelectron microscopy3.33D1-209[»]
5GAFelectron microscopy4.30D1-209[»]
5GAGelectron microscopy3.80D1-209[»]
5GAHelectron microscopy3.80D1-209[»]
5H5Uelectron microscopy3.00D1-209[»]
5IQRelectron microscopy3.00C1-209[»]
5IT8X-ray3.12CD/DD1-209[»]
5J5BX-ray2.80CD/DD1-209[»]
5J7LX-ray3.00CD/DD1-209[»]
5J88X-ray3.32CD/DD1-209[»]
5J8AX-ray3.10CD/DD1-209[»]
5J91X-ray2.96CD/DD1-209[»]
5JC9X-ray3.03CD/DD1-209[»]
5JTEelectron microscopy3.60BD1-209[»]
5JU8electron microscopy3.60BD1-209[»]
5KCRelectron microscopy3.601E1-209[»]
5KCSelectron microscopy3.901E1-209[»]
5KPSelectron microscopy3.90C1-209[»]
5KPVelectron microscopy4.10B1-209[»]
5KPWelectron microscopy3.90B1-209[»]
5KPXelectron microscopy3.90B1-209[»]
5L3Pelectron microscopy3.70E1-209[»]
5LZAelectron microscopy3.60D1-209[»]
5LZBelectron microscopy5.30D1-209[»]
5LZCelectron microscopy4.80D1-209[»]
5LZDelectron microscopy3.40D1-209[»]
5LZEelectron microscopy3.50D1-209[»]
5LZFelectron microscopy4.60D1-209[»]
5MDVelectron microscopy2.97C1-209[»]
5MDWelectron microscopy3.06C1-209[»]
5MDYelectron microscopy3.35C1-209[»]
5MDZelectron microscopy3.10C1-209[»]
5MGPelectron microscopy3.10D1-209[»]
5U4Ielectron microscopy3.50D1-209[»]
ProteinModelPortaliP60438.
SMRiP60438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10744N.
IntActiP60438. 144 interactors.
MINTiMINT-1302843.
STRINGi511145.b3320.

Proteomic databases

EPDiP60438.
PaxDbiP60438.
PRIDEiP60438.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76345; AAC76345; b3320.
BAE77971; BAE77971; BAE77971.
GeneIDi947817.
KEGGiecj:JW3282.
eco:b3320.
PATRICi32122072. VBIEscCol129921_3413.

Organism-specific databases

EchoBASEiEB0859.
EcoGeneiEG10866. rplC.

Phylogenomic databases

eggNOGiENOG4105EEE. Bacteria.
COG0087. LUCA.
HOGENOMiHOG000100368.
InParanoidiP60438.
KOiK02906.
OMAiKRMAGRY.
PhylomeDBiP60438.

Enzyme and pathway databases

BioCyciEcoCyc:EG10866-MONOMER.
MetaCyc:EG10866-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60438.
PROiPR:P60438.

Family and domain databases

HAMAPiMF_01325_B. Ribosomal_L3_B. 1 hit.
InterProiView protein in InterPro
IPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
PANTHERiPTHR11229. PTHR11229. 1 hit.
PfamiView protein in Pfam
PF00297. Ribosomal_L3. 1 hit.
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03625. L3_bact. 1 hit.
PROSITEiView protein in PROSITE
PS00474. RIBOSOMAL_L3. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL3_ECOLI
AccessioniPrimary (citable) accession number: P60438
Secondary accession number(s): P02386, Q2M6Y5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 10, 2017
This is version 138 of the entry and version 1 of the sequence. See 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.