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Protein

40S ribosomal protein S18

Gene

RPS18A

more
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA.By similarity

GO - Molecular functioni

GO - Biological processi

  • ribosome biogenesis Source: GO_Central
  • translation Source: GO_Central
  • translational initiation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiR-ATH-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-ATH-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-ATH-72689. Formation of a pool of free 40S subunits.
R-ATH-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-ATH-72702. Ribosomal scanning and start codon recognition.
R-ATH-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-ATH-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-ATH-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S18
Gene namesi
Name:RPS18A
Synonyms:PFL
Ordered Locus Names:At1g22780
ORF Names:T22J18.5
AND
Name:RPS18B
Ordered Locus Names:At1g34030
ORF Names:F12G12.15, T15K4.9
AND
Name:RPS18C
Ordered Locus Names:At4g09800
ORF Names:F17A8.150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componentsi: Chromosome 1, Chromosome 4

Organism-specific databases

TAIRiAT1G22780.
AT1G34030.
AT4G09800.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
  • cytosol Source: TAIR
  • cytosolic ribosome Source: TAIR
  • cytosolic small ribosomal subunit Source: TAIR
  • membrane Source: TAIR
  • nucleolus Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • ribosome Source: TAIR
  • small ribosomal subunit Source: GO_Central
  • vacuolar membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 15215140S ribosomal protein S18PRO_0000132224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP34788.
PRIDEiP34788.

Expressioni

Gene expression databases

ExpressionAtlasiP34788. baseline and differential.
GenevisibleiP34788. AT.

Interactioni

Protein-protein interaction databases

BioGridi11868. 3 interactions.
24123. 2 interactions.
25532. 1 interaction.
IntActiP34788. 3 interactions.
STRINGi3702.AT4G09800.1.

Structurei

3D structure databases

ProteinModelPortaliP34788.
SMRiP34788. Positions 7-142.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S13P family.Curated

Phylogenomic databases

eggNOGiKOG3311. Eukaryota.
COG0099. LUCA.
HOGENOMiHOG000039877.
InParanoidiP34788.
KOiK02964.
OMAiRIMNTDL.
PhylomeDBiP34788.

Family and domain databases

Gene3Di4.10.910.10. 1 hit.
HAMAPiMF_01315. Ribosomal_S13_S18.
InterProiIPR027437. 30s_Rbsml_prot_S13_C.
IPR001892. Ribosomal_S13.
IPR010979. Ribosomal_S13-like_H2TH.
IPR018269. Ribosomal_S13_CS.
[Graphical view]
PfamiPF00416. Ribosomal_S13. 1 hit.
[Graphical view]
PIRSFiPIRSF002134. Ribosomal_S13. 1 hit.
SUPFAMiSSF46946. SSF46946. 1 hit.
PROSITEiPS00646. RIBOSOMAL_S13_1. 1 hit.
PS50159. RIBOSOMAL_S13_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P34788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLVANEEFQ HILRVLNTNV DGKQKIMFAL TSIKGIGRRL ANIVCKKADV
60 70 80 90 100
DMNKRAGELS AAEIDNLMTI VANPRQFKIP DWFLNRQKDY KDGKYSQVVS
110 120 130 140 150
NALDMKLRDD LERLKKIRNH RGLRHYWGLR VRGQHTKTTG RRGKTVGVSK

KR
Length:152
Mass (Da):17,545
Last modified:February 1, 1994 - v1
Checksum:i4D060D6614A85092
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481A → T in AAK43840 (PubMed:14593172).Curated
Sequence conflicti48 – 481A → T in AAL47385 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23165 Genomic DNA. Translation: CAA80684.1.
Z28701 mRNA. Translation: CAA82273.1.
Z28702 mRNA. Translation: CAA82274.1.
Z28962 Genomic DNA. Translation: CAA82275.1.
Y12227 Genomic DNA. Translation: CAA72909.1.
AC003979 Genomic DNA. Translation: AAC25506.1.
AC015446 Genomic DNA. Translation: AAG12534.1.
AC079286 Genomic DNA. Translation: AAG12853.1.
AL049482 Genomic DNA. Translation: CAB39647.1.
AL161515 Genomic DNA. Translation: CAB78103.1.
CP002684 Genomic DNA. Translation: AEE30287.1.
CP002684 Genomic DNA. Translation: AEE31659.1.
CP002687 Genomic DNA. Translation: AEE82800.1.
AF411781 mRNA. Translation: AAL06471.1.
AF386941 mRNA. Translation: AAK62386.1.
AF370463 mRNA. Translation: AAK43840.1.
AY034965 mRNA. Translation: AAK59471.1.
AY064680 mRNA. Translation: AAL47385.1.
AY070029 mRNA. Translation: AAL47500.1.
AY086334 mRNA. Translation: AAM64403.1.
AY086800 mRNA. Translation: AAM63849.1.
BT006539 mRNA. Translation: AAP21347.1.
AY087428 mRNA. Translation: AAM64976.1.
PIRiS46223. S37496.
RefSeqiNP_173692.1. NM_102125.3.
NP_192718.1. NM_117048.3.
NP_564434.1. NM_103125.4.
UniGeneiAt.179.
At.180.
At.20392.
At.33672.

Genome annotation databases

EnsemblPlantsiAT1G22780.1; AT1G22780.1; AT1G22780.
AT1G34030.1; AT1G34030.1; AT1G34030.
AT4G09800.1; AT4G09800.1; AT4G09800.
GeneIDi826569.
838884.
840300.
GrameneiAT1G22780.1; AT1G22780.1; AT1G22780.
AT1G34030.1; AT1G34030.1; AT1G34030.
AT4G09800.1; AT4G09800.1; AT4G09800.
KEGGiath:AT1G22780.
ath:AT1G34030.
ath:AT4G09800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23165 Genomic DNA. Translation: CAA80684.1.
Z28701 mRNA. Translation: CAA82273.1.
Z28702 mRNA. Translation: CAA82274.1.
Z28962 Genomic DNA. Translation: CAA82275.1.
Y12227 Genomic DNA. Translation: CAA72909.1.
AC003979 Genomic DNA. Translation: AAC25506.1.
AC015446 Genomic DNA. Translation: AAG12534.1.
AC079286 Genomic DNA. Translation: AAG12853.1.
AL049482 Genomic DNA. Translation: CAB39647.1.
AL161515 Genomic DNA. Translation: CAB78103.1.
CP002684 Genomic DNA. Translation: AEE30287.1.
CP002684 Genomic DNA. Translation: AEE31659.1.
CP002687 Genomic DNA. Translation: AEE82800.1.
AF411781 mRNA. Translation: AAL06471.1.
AF386941 mRNA. Translation: AAK62386.1.
AF370463 mRNA. Translation: AAK43840.1.
AY034965 mRNA. Translation: AAK59471.1.
AY064680 mRNA. Translation: AAL47385.1.
AY070029 mRNA. Translation: AAL47500.1.
AY086334 mRNA. Translation: AAM64403.1.
AY086800 mRNA. Translation: AAM63849.1.
BT006539 mRNA. Translation: AAP21347.1.
AY087428 mRNA. Translation: AAM64976.1.
PIRiS46223. S37496.
RefSeqiNP_173692.1. NM_102125.3.
NP_192718.1. NM_117048.3.
NP_564434.1. NM_103125.4.
UniGeneiAt.179.
At.180.
At.20392.
At.33672.

3D structure databases

ProteinModelPortaliP34788.
SMRiP34788. Positions 7-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi11868. 3 interactions.
24123. 2 interactions.
25532. 1 interaction.
IntActiP34788. 3 interactions.
STRINGi3702.AT4G09800.1.

Proteomic databases

PaxDbiP34788.
PRIDEiP34788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G22780.1; AT1G22780.1; AT1G22780.
AT1G34030.1; AT1G34030.1; AT1G34030.
AT4G09800.1; AT4G09800.1; AT4G09800.
GeneIDi826569.
838884.
840300.
GrameneiAT1G22780.1; AT1G22780.1; AT1G22780.
AT1G34030.1; AT1G34030.1; AT1G34030.
AT4G09800.1; AT4G09800.1; AT4G09800.
KEGGiath:AT1G22780.
ath:AT1G34030.
ath:AT4G09800.

Organism-specific databases

TAIRiAT1G22780.
AT1G34030.
AT4G09800.

Phylogenomic databases

eggNOGiKOG3311. Eukaryota.
COG0099. LUCA.
HOGENOMiHOG000039877.
InParanoidiP34788.
KOiK02964.
OMAiRIMNTDL.
PhylomeDBiP34788.

Enzyme and pathway databases

ReactomeiR-ATH-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-ATH-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-ATH-72689. Formation of a pool of free 40S subunits.
R-ATH-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-ATH-72702. Ribosomal scanning and start codon recognition.
R-ATH-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-ATH-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-ATH-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiP34788.

Gene expression databases

ExpressionAtlasiP34788. baseline and differential.
GenevisibleiP34788. AT.

Family and domain databases

Gene3Di4.10.910.10. 1 hit.
HAMAPiMF_01315. Ribosomal_S13_S18.
InterProiIPR027437. 30s_Rbsml_prot_S13_C.
IPR001892. Ribosomal_S13.
IPR010979. Ribosomal_S13-like_H2TH.
IPR018269. Ribosomal_S13_CS.
[Graphical view]
PfamiPF00416. Ribosomal_S13. 1 hit.
[Graphical view]
PIRSFiPIRSF002134. Ribosomal_S13. 1 hit.
SUPFAMiSSF46946. SSF46946. 1 hit.
PROSITEiPS00646. RIBOSOMAL_S13_1. 1 hit.
PS50159. RIBOSOMAL_S13_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An S18 ribosomal protein gene copy at the Arabidopsis PFL locus affects plant development by its specific expression in meristems."
    van Lijsebettens M., Vanderhaeghen R., de Block M., Bauw G., Villarroel R., Lister C., Dean C., van Montagu M.
    EMBO J. 13:3378-3388(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 56-64 AND 95-106 (RPS18A AND RPS18B).
    Strain: cv. C24 and cv. Columbia.
  2. "Sequence analysis of a 24-kb contiguous genomic region at the Arabidopsis thaliana PFL locus on chromosome 1."
    Terryn N., Neyt P., de Clercq R., de Keyser A., van den Daele H., Ardiles W., Dehais P., Rouze P., Gielen J., Villarroel R., van Montagu M.
    FEBS Lett. 416:156-160(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (RPS18A).
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (RPS18A AND RPS18B).
    Strain: cv. Columbia.
  4. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (RPS18C).
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (RPS18A; RPS18B AND RPS18C).
    Strain: cv. Columbia.
  7. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (RPS18A).
  8. "The organization of cytoplasmic ribosomal protein genes in the Arabidopsis genome."
    Barakat A., Szick-Miranda K., Chang I.-F., Guyot R., Blanc G., Cooke R., Delseny M., Bailey-Serres J.
    Plant Physiol. 127:398-415(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRS18_ARATH
AccessioniPrimary (citable) accession number: P34788
Secondary accession number(s): Q94K22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 6, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.