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Protein

Phospholipid-transporting ATPase DNF2

Gene

DNF2

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

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids. Required for protein transport from Golgi to vacuoles.1 Publication

Catalytic activityi

ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei712 – 71214-aspartylphosphate intermediateCurated

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • magnesium ion binding Source: InterPro
  • phospholipid-translocating ATPase activity Source: SGD

GO - Biological processi

  • endocytosis Source: SGD
  • establishment or maintenance of cell polarity Source: SGD
  • intracellular protein transport Source: SGD
  • phospholipid translocation Source: SGD
  • response to pheromone involved in conjugation with cellular fusion Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid transport, Protein transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29698-MONOMER.
ReactomeiR-SCE-936837. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.8.5. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid-transporting ATPase DNF2 (EC:3.6.3.1)
Alternative name(s):
Flippase DNF2
Gene namesi
Name:DNF2
Ordered Locus Names:YDR093W
ORF Names:YD8557.01
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR093W.
SGDiS000002500. DNF2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 252252CytoplasmicSequence analysisAdd
BLAST
Transmembranei253 – 27321HelicalSequence analysisAdd
BLAST
Topological domaini274 – 2774ExtracellularSequence analysis
Transmembranei278 – 29821HelicalSequence analysisAdd
BLAST
Topological domaini299 – 598300CytoplasmicSequence analysisAdd
BLAST
Transmembranei599 – 61921HelicalSequence analysisAdd
BLAST
Topological domaini620 – 63920ExtracellularSequence analysisAdd
BLAST
Transmembranei640 – 66021HelicalSequence analysisAdd
BLAST
Topological domaini661 – 1231571CytoplasmicSequence analysisAdd
BLAST
Transmembranei1232 – 125221HelicalSequence analysisAdd
BLAST
Topological domaini1253 – 126210ExtracellularSequence analysis
Transmembranei1263 – 128321HelicalSequence analysisAdd
BLAST
Topological domaini1284 – 131330CytoplasmicSequence analysisAdd
BLAST
Transmembranei1314 – 133421HelicalSequence analysisAdd
BLAST
Topological domaini1335 – 135016ExtracellularSequence analysisAdd
BLAST
Transmembranei1351 – 137121HelicalSequence analysisAdd
BLAST
Topological domaini1372 – 13776CytoplasmicSequence analysis
Transmembranei1378 – 139821HelicalSequence analysisAdd
BLAST
Topological domaini1399 – 141820ExtracellularSequence analysisAdd
BLAST
Transmembranei1419 – 143921HelicalSequence analysisAdd
BLAST
Topological domaini1440 – 1612173CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: GOC
  • mating projection tip membrane Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16121612Phospholipid-transporting ATPase DNF2PRO_0000046234Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701PhosphothreonineCombined sources
Modified residuei85 – 851PhosphoserineCombined sources
Modified residuei389 – 3891PhosphoserineCombined sources
Modified residuei392 – 3921PhosphoserineCombined sources
Modified residuei396 – 3961PhosphoserineCombined sources
Modified residuei403 – 4031PhosphoserineCombined sources
Modified residuei406 – 4061PhosphotyrosineCombined sources
Modified residuei782 – 7821PhosphothreonineCombined sources
Cross-linki938 – 938Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei1542 – 15421PhosphoserineCombined sources
Modified residuei1592 – 15921PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by FPK1 and KIN82.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ12675.

PTM databases

iPTMnetiQ12675.

Interactioni

Protein-protein interaction databases

BioGridi32150. 38 interactions.
DIPiDIP-8055N.
IntActiQ12675. 4 interactions.
MINTiMINT-4480759.

Structurei

3D structure databases

ProteinModelPortaliQ12675.
SMRiQ12675. Positions 1152-1208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00770000120474.
HOGENOMiHOG000202528.
InParanoidiQ12675.
KOiK01530.
OMAiTEIHEHE.
OrthoDBiEOG7FR7QR.

Family and domain databases

Gene3Di2.70.150.10. 3 hits.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
IPR026871. PLip_transp_ATPase.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 2 hits.
PTHR24092:SF87. PTHR24092:SF87. 2 hits.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12675-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPSKPTSP FVDDIEHESG SASNGLSSMS PFDDSFQFEK PSSAHGNIEV
60 70 80 90 100
AKTGGSVLKR QSKPMKDIST PDLSKVTFDG IDDYSNDNDI NDDDELNGKK
110 120 130 140 150
TEIHEHENEV DDDLHSFQAT PMPNTGGFED VELDNNEGSN NDSQADHKLK
160 170 180 190 200
RVRFGTRRNK SGRIDINRSK TLKWAKKNFH NAIDEFSTKE DSLENSALQN
210 220 230 240 250
RSDELRTVYY NLPLPEDMLD EDGLPLAVYP RNKIRTTKYT PLTFFPKNIL
260 270 280 290 300
FQFHNFANIY FLILLILGAF QIFGVTNPGF ASVPLIVIVI ITAIKDGIED
310 320 330 340 350
SRRTVLDLEV NNTRTHILSG VKNENVAVDN VSLWRRFKKA NTRALIKIFE
360 370 380 390 400
YFSENLTAAG REKKLQKKRE ELRRKRNSRS FGPRGSLDSI GSYRMSADFG
410 420 430 440 450
RPSLDYENLN QTMSQANRYN DGENLVDRTL QPNPECRFAK DYWKNVKVGD
460 470 480 490 500
IVRVHNNDEI PADMILLSTS DVDGACYVET KNLDGETNLK VRQSLKCSKI
510 520 530 540 550
IKSSRDITRT KFWVESEGPH ANLYSYQGNF KWQDTQNGNI RNEPVNINNL
560 570 580 590 600
LLRGCTLRNT KWAMGMVIFT GDDTKIMINA GVTPTKKSRI SRELNFSVIL
610 620 630 640 650
NFVLLFILCF TAGIVNGVYY KQKPRSRDYF EFGTIGGSAS TNGFVSFWVA
660 670 680 690 700
VILYQSLVPI SLYISVEIIK TAQAIFIYTD VLLYNAKLDY PCTPKSWNIS
710 720 730 740 750
DDLGQIEYIF SDKTGTLTQN VMEFKKCTIN GVSYGRAYTE ALAGLRKRQG
760 770 780 790 800
VDVESEGRRE KEEIAKDRET MIDELRSMSD NTQFCPEDLT FVSKEIVEDL
810 820 830 840 850
KGSSGDHQQK CCEHFLLALA LCHSVLVEPN KDDPKKLDIK AQSPDESALV
860 870 880 890 900
STARQLGYSF VGSSKSGLIV EIQGVQKEFQ VLNVLEFNSS RKRMSCIIKI
910 920 930 940 950
PGSTPKDEPK ALLICKGADS VIYSRLDRTQ NDATLLEKTA LHLEEYATEG
960 970 980 990 1000
LRTLCLAQRE LTWSEYERWV KTYDVAAASV TNREEELDKV TDVIERELIL
1010 1020 1030 1040 1050
LGGTAIEDRL QDGVPDSIAL LAEAGIKLWV LTGDKVETAI NIGFSCNVLN
1060 1070 1080 1090 1100
NDMELLVVKA SGEDVEEFGS DPIQVVNNLV TKYLREKFGM SGSEEELKEA
1110 1120 1130 1140 1150
KREHGLPQGN FAVIIDGDAL KVALNGEEMR RKFLLLCKNC KAVLCCRVSP
1160 1170 1180 1190 1200
AQKAAVVKLV KKTLDVMTLA IGDGSNDVAM IQSADVGVGI AGEEGRQAVM
1210 1220 1230 1240 1250
CSDYAIGQFR YVTRLVLVHG KWCYKRLAEM IPQFFYKNVI FTLSLFWYGI
1260 1270 1280 1290 1300
YNNFDGSYLF EYTYLTFYNL AFTSVPVILL AVLDQDVSDT VSMLVPQLYR
1310 1320 1330 1340 1350
VGILRKEWNQ TKFLWYMLDG VYQSVICFFF PYLAYHKNMV VTENGLGLDH
1360 1370 1380 1390 1400
RYFVGVFVTA IAVTSCNFYV FMEQYRWDWF CGLFICLSLA VFYGWTGIWT
1410 1420 1430 1440 1450
SSSSSNEFYK GAARVFAQPA YWAVLFVGVL FCLLPRFTID CIRKIFYPKD
1460 1470 1480 1490 1500
IEIVREMWLR GDFDLYPQGY DPTDPSRPRI NEIRPLTDFK EPISLDTHFD
1510 1520 1530 1540 1550
GVSHSQETIV TEEIPMSILN GEQGSRKGYR VSTTLERRDQ LSPVTTTNNL
1560 1570 1580 1590 1600
PRRSMASARG NKLRTSLDRT REEMLANHQL DTRYSVERAR ASLDLPGINH
1610
AETLLSQRSR DR
Length:1,612
Mass (Da):182,619
Last modified:November 1, 1997 - v1
Checksum:i09719DF264256BEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47746 Genomic DNA. Translation: CAA87668.1.
BK006938 Genomic DNA. Translation: DAA11940.1.
PIRiS51243.
RefSeqiNP_010378.1. NM_001180401.1.

Genome annotation databases

EnsemblFungiiYDR093W; YDR093W; YDR093W.
GeneIDi851667.
KEGGisce:YDR093W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47746 Genomic DNA. Translation: CAA87668.1.
BK006938 Genomic DNA. Translation: DAA11940.1.
PIRiS51243.
RefSeqiNP_010378.1. NM_001180401.1.

3D structure databases

ProteinModelPortaliQ12675.
SMRiQ12675. Positions 1152-1208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32150. 38 interactions.
DIPiDIP-8055N.
IntActiQ12675. 4 interactions.
MINTiMINT-4480759.

Protein family/group databases

TCDBi3.A.3.8.5. the p-type atpase (p-atpase) superfamily.

PTM databases

iPTMnetiQ12675.

Proteomic databases

MaxQBiQ12675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR093W; YDR093W; YDR093W.
GeneIDi851667.
KEGGisce:YDR093W.

Organism-specific databases

EuPathDBiFungiDB:YDR093W.
SGDiS000002500. DNF2.

Phylogenomic databases

GeneTreeiENSGT00770000120474.
HOGENOMiHOG000202528.
InParanoidiQ12675.
KOiK01530.
OMAiTEIHEHE.
OrthoDBiEOG7FR7QR.

Enzyme and pathway databases

BioCyciYEAST:G3O-29698-MONOMER.
ReactomeiR-SCE-936837. Ion transport by P-type ATPases.

Miscellaneous databases

PROiQ12675.

Family and domain databases

Gene3Di2.70.150.10. 3 hits.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
IPR026871. PLip_transp_ATPase.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 2 hits.
PTHR24092:SF87. PTHR24092:SF87. 2 hits.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "An essential subfamily of Drs2p-related P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system."
    Hua Z., Fatheddin P., Graham T.R.
    Mol. Biol. Cell 13:3162-3177(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  5. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70; SER-389; SER-392 AND SER-1542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry."
    Nakano K., Yamamoto T., Kishimoto T., Noji T., Tanaka K.
    Mol. Biol. Cell 19:1783-1797(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY FPK1 AND KIN82.
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1542 AND SER-1592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-396; SER-403; TYR-406; THR-782; SER-1542 AND SER-1592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-938, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATC4_YEAST
AccessioniPrimary (citable) accession number: Q12675
Secondary accession number(s): D6VS80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.