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Protein

40S ribosomal protein S0-A

Gene

RPS0A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.2 PublicationsUniRule annotation

GO - Molecular functioni

  1. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  3. endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  4. ribosomal small subunit assembly Source: SGD
  5. rRNA export from nucleus Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-30896-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_248935. Ribosomal scanning and start codon recognition.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257608. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_257951. Peptide chain elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S0-AUniRule annotation
Alternative name(s):
Nucleic acid-binding protein NAB1A
Gene namesi
Name:RPS0AUniRule annotation
Synonyms:NAB1, NAB1A, YST1
Ordered Locus Names:YGR214W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

SGDiS000003446. RPS0A.

Subcellular locationi

Cytoplasm 2 PublicationsUniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Reduction in growth rate, a decrease in free 40S subunits, an increase in the amount of free 60S subunits and a decrease in polysome size.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 PublicationsUniRule annotation
Chaini2 – 25225140S ribosomal protein S0-APRO_0000134370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 PublicationsUniRule annotation

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32905.
PeptideAtlasiP32905.

2D gel databases

SWISS-2DPAGEP32905.

Expressioni

Gene expression databases

GenevestigatoriP32905.

Interactioni

Subunit structurei

Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S).2 Publications

Protein-protein interaction databases

BioGridi33467. 102 interactions.
DIPiDIP-5553N.
IntActiP32905. 155 interactions.
MINTiMINT-562708.
STRINGi4932.YGR214W.

Structurei

Secondary structure

1
252
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Helixi11 – 2010Combined sources
Turni21 – 233Combined sources
Helixi31 – 366Combined sources
Beta strandi37 – 415Combined sources
Turni42 – 443Combined sources
Beta strandi45 – 484Combined sources
Helixi50 – 6415Combined sources
Beta strandi67 – 693Combined sources
Helixi70 – 723Combined sources
Beta strandi73 – 775Combined sources
Helixi80 – 9213Combined sources
Beta strandi96 – 1005Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi119 – 1246Combined sources
Turni126 – 1294Combined sources
Helixi130 – 1378Combined sources
Turni138 – 1403Combined sources
Beta strandi143 – 1475Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi164 – 1663Combined sources
Helixi169 – 18214Combined sources
Beta strandi183 – 1875Combined sources
Beta strandi190 – 1923Combined sources
Helixi199 – 2013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-B14-198[»]
3J6Xelectron microscopy6.10S01-252[»]
3J6Yelectron microscopy6.10S01-252[»]
3J77electron microscopy6.20S01-252[»]
3J78electron microscopy6.30S01-252[»]
3V88X-ray3.00A1-252[»]
4U3MX-ray3.00S0/s02-252[»]
4U3NX-ray3.20S0/s02-252[»]
4U3UX-ray2.90S0/s02-252[»]
4U4NX-ray3.10S0/s02-252[»]
4U4OX-ray3.60S0/s02-252[»]
4U4QX-ray3.00S0/s02-252[»]
4U4RX-ray2.80S0/s02-252[»]
4U4UX-ray3.00S0/s02-252[»]
4U4YX-ray3.20S0/s02-252[»]
4U4ZX-ray3.10S0/s02-252[»]
4U50X-ray3.20S0/s02-252[»]
4U51X-ray3.20S0/s02-252[»]
4U52X-ray3.00S0/s02-252[»]
4U53X-ray3.30S0/s02-252[»]
4U55X-ray3.20S0/s02-252[»]
4U56X-ray3.45S0/s02-252[»]
4U6FX-ray3.10S0/s02-252[»]
4V4Belectron microscopy11.70AB14-198[»]
4V6Ielectron microscopy8.80AA1-252[»]
4V7RX-ray4.00AA/CA1-252[»]
4V88X-ray3.00AA/CA1-252[»]
4V8Yelectron microscopy4.30AA1-252[»]
4V8Zelectron microscopy6.60AA1-252[»]
4V92electron microscopy3.70A2-207[»]
ProteinModelPortaliP32905.
SMRiP32905. Positions 2-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32905.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S2P family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000015036.
HOGENOMiHOG000232073.
InParanoidiP32905.
KOiK02998.
OMAiTTHIGST.
OrthoDBiEOG741ZD0.

Family and domain databases

HAMAPiMF_03015. Ribosomal_S2_euk.
InterProiIPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. Sa_S2_E_A. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P32905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLPATFDLT PEDAQLLLAA NTHLGARNVQ VHQEPYVFNA RPDGVHVINV
60 70 80 90 100
GKTWEKLVLA ARIIAAIPNP EDVVAISSRT FGQRAVLKFA AHTGATPIAG
110 120 130 140 150
RFTPGSFTNY ITRSFKEPRL VIVTDPRSDA QAIKEASYVN IPVIALTDLD
160 170 180 190 200
SPSEFVDVAI PCNNRGKHSI GLIWYLLARE VLRLRGALVD RTQPWSIMPD
210 220 230 240 250
LYFYRDPEEV EQQVAEEATT EEAGEEEAKE EVTEEQAEAT EWAEENADNV

EW
Length:252
Mass (Da):28,024
Last modified:January 23, 2007 - v3
Checksum:iD6F263456282C771
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88277 Genomic DNA. Translation: AAB05643.1.
Z72999 Genomic DNA. Translation: CAA97241.1.
BK006941 Genomic DNA. Translation: DAA08308.1.
PIRiS42143.
RefSeqiNP_011730.1. NM_001181343.1.

Genome annotation databases

EnsemblFungiiYGR214W; YGR214W; YGR214W.
GeneIDi853128.
KEGGisce:YGR214W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88277 Genomic DNA. Translation: AAB05643.1.
Z72999 Genomic DNA. Translation: CAA97241.1.
BK006941 Genomic DNA. Translation: DAA08308.1.
PIRiS42143.
RefSeqiNP_011730.1. NM_001181343.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-B14-198[»]
3J6Xelectron microscopy6.10S01-252[»]
3J6Yelectron microscopy6.10S01-252[»]
3J77electron microscopy6.20S01-252[»]
3J78electron microscopy6.30S01-252[»]
3V88X-ray3.00A1-252[»]
4U3MX-ray3.00S0/s02-252[»]
4U3NX-ray3.20S0/s02-252[»]
4U3UX-ray2.90S0/s02-252[»]
4U4NX-ray3.10S0/s02-252[»]
4U4OX-ray3.60S0/s02-252[»]
4U4QX-ray3.00S0/s02-252[»]
4U4RX-ray2.80S0/s02-252[»]
4U4UX-ray3.00S0/s02-252[»]
4U4YX-ray3.20S0/s02-252[»]
4U4ZX-ray3.10S0/s02-252[»]
4U50X-ray3.20S0/s02-252[»]
4U51X-ray3.20S0/s02-252[»]
4U52X-ray3.00S0/s02-252[»]
4U53X-ray3.30S0/s02-252[»]
4U55X-ray3.20S0/s02-252[»]
4U56X-ray3.45S0/s02-252[»]
4U6FX-ray3.10S0/s02-252[»]
4V4Belectron microscopy11.70AB14-198[»]
4V6Ielectron microscopy8.80AA1-252[»]
4V7RX-ray4.00AA/CA1-252[»]
4V88X-ray3.00AA/CA1-252[»]
4V8Yelectron microscopy4.30AA1-252[»]
4V8Zelectron microscopy6.60AA1-252[»]
4V92electron microscopy3.70A2-207[»]
ProteinModelPortaliP32905.
SMRiP32905. Positions 2-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33467. 102 interactions.
DIPiDIP-5553N.
IntActiP32905. 155 interactions.
MINTiMINT-562708.
STRINGi4932.YGR214W.

2D gel databases

SWISS-2DPAGEP32905.

Proteomic databases

MaxQBiP32905.
PeptideAtlasiP32905.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR214W; YGR214W; YGR214W.
GeneIDi853128.
KEGGisce:YGR214W.

Organism-specific databases

SGDiS000003446. RPS0A.

Phylogenomic databases

GeneTreeiENSGT00390000015036.
HOGENOMiHOG000232073.
InParanoidiP32905.
KOiK02998.
OMAiTTHIGST.
OrthoDBiEOG741ZD0.

Enzyme and pathway databases

BioCyciYEAST:G3O-30896-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_248935. Ribosomal scanning and start codon recognition.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257608. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_257951. Peptide chain elongation.

Miscellaneous databases

EvolutionaryTraceiP32905.
NextBioi973178.

Gene expression databases

GenevestigatoriP32905.

Family and domain databases

HAMAPiMF_03015. Ribosomal_S2_euk.
InterProiIPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. Sa_S2_E_A. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast proteins related to the p40/laminin receptor precursor are essential components of the 40 S ribosomal subunit."
    Demianova M.A., Formosa T.G., Ellis S.R.
    J. Biol. Chem. 271:11383-11391(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: PROTEIN SEQUENCE OF 118-133 AND 231-248.
    Strain: ATCC 204508 / S288c.
  6. "Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway."
    Norbeck J., Blomberg A.
    J. Biol. Chem. 272:5544-5554(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-36 AND 135-146.
    Strain: ATCC 44827 / SKQ2N.
  7. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
    Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
    Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT SER-2.
  8. "The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution."
    Ardini E., Pesole G., Tagliabue E., Magnifico A., Castronovo V., Sobel M.E., Colnaghi M.I., Menard S.
    Mol. Biol. Evol. 15:1017-1025(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE EVOLUTION.
  9. "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
    Planta R.J., Mager W.H.
    Yeast 14:471-477(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE, SUBUNIT.
  10. "Yeast proteins related to the p40/laminin receptor precursor are required for 20S ribosomal RNA processing and the maturation of 40S ribosomal subunits."
    Ford C.L., Randal-Whitis L., Ellis S.R.
    Cancer Res. 59:704-710(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  11. "The action of N-terminal acetyltransferases on yeast ribosomal proteins."
    Arnold R.J., Polevoda B., Reilly J.P., Sherman F.
    J. Biol. Chem. 274:37035-37040(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2 BY NATA.
  12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. "Ribosomal proteins Rps0 and Rps21 of Saccharomyces cerevisiae have overlapping functions in the maturation of the 3' end of 18S rRNA."
    Tabb-Massey A., Caffrey J.M., Logsden P., Taylor S., Trent J.O., Ellis S.R.
    Nucleic Acids Res. 31:6798-6805(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  15. "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions."
    Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J.
    Cell 107:373-386(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 14-198, ELECTRON MICROSCOPY.
  16. "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
    Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
    EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 14-198, ELECTRON MICROSCOPY.

Entry informationi

Entry nameiRSSA1_YEAST
AccessioniPrimary (citable) accession number: P32905
Secondary accession number(s): D6VUZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 93700 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for S0 in yeast.
This protein appears to have acquired a second function as a laminin receptor specifically in the vertebrate lineage. This protein does not bind laminin.

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
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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.