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Protein

Respiratory burst oxidase homolog protein F

Gene

RBOHF

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

Functioni

Calcium-dependent NADPH oxidase that generates superoxide. Generates reactive oxygen species (ROS) during incompatible interactions with pathogens and is important in the regulation of the hypersensitive response (HR). Involved in abscisic acid-induced stomatal closing and in UV-B and abscisic acid ROS-dependent signaling.5 Publications

Enzyme regulationi

Inhibited by diphenylene iodonium (DPI).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi277 – 2771CalciumBy similarity
Metal bindingi279 – 2791CalciumBy similarity
Metal bindingi281 – 2811CalciumBy similarity
Metal bindingi283 – 2831Calcium; via carbonyl oxygenBy similarity
Metal bindingi288 – 2881CalciumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi277 – 288121Add
BLAST
Calcium bindingi321 – 332122Add
BLAST

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • NAD(P)H oxidase activity Source: TAIR
  • peroxidase activity Source: UniProtKB-KW

GO - Biological processi

  • abscisic acid-activated signaling pathway Source: TAIR
  • carbohydrate homeostasis Source: TAIR
  • defense response by callose deposition Source: TAIR
  • ethylene-activated signaling pathway Source: TAIR
  • hydrogen peroxide biosynthetic process Source: TAIR
  • negative regulation of programmed cell death Source: TAIR
  • osmosensory signaling pathway Source: TAIR
  • regulation of stomatal movement Source: TAIR
  • respiratory burst involved in defense response Source: TAIR
  • response to ethylene Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Ligandi

Calcium, FAD, Flavoprotein, Metal-binding, NADP

Enzyme and pathway databases

BioCyciARA:AT1G64060-MONOMER.
ReactomeiR-ATH-209968. Thyroxine biosynthesis.
R-ATH-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Respiratory burst oxidase homolog protein F (EC:1.11.1.-, EC:1.6.3.-)
Alternative name(s):
Cytochrome b245 beta chain homolog RbohAp108
NADPH oxidase RBOHF
Short name:
AtRBOHF
Gene namesi
Name:RBOHF
Synonyms:RBOHAP108
Ordered Locus Names:At1g64060
ORF Names:F22C12.18
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G64060.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 387386CytoplasmicSequence analysisAdd
BLAST
Transmembranei388 – 40821Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini409 – 47567ExtracellularSequence analysisAdd
BLAST
Transmembranei476 – 49217Helical; Name=2By similarityAdd
BLAST
Topological domaini493 – 52735CytoplasmicSequence analysisAdd
BLAST
Transmembranei528 – 54821Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini549 – 57022ExtracellularSequence analysisAdd
BLAST
Transmembranei571 – 59121Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini592 – 5998CytoplasmicSequence analysis
Transmembranei600 – 61718Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini618 – 744127ExtracellularSequence analysisAdd
BLAST
Transmembranei745 – 76521Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini766 – 944179CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: GOC
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 944943Respiratory burst oxidase homolog protein FPRO_0000313758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei354 – 3541PhosphoserineBy similarity
Modified residuei358 – 3581PhosphoserineBy similarity

Post-translational modificationi

Not glycosylated. Phosphorylated by CIPK26.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO48538.
PRIDEiO48538.

PTM databases

iPTMnetiO48538.

Expressioni

Tissue specificityi

Expressed in roots, stems, seedlings, inflorescences, leaves and guard cells.3 Publications

Inductioni

Up-regulated by abscisic acid.1 Publication

Gene expression databases

GenevisibleiO48538. AT.

Interactioni

Subunit structurei

Monomer and homodimer (By similarity). Interacts (via N-terminus) with CIPK26 (PubMed:23335733). Interacts (via N-terminus) with SRC2 (PubMed:23872431).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SRK2EQ940H64EBI-7197253,EBI-782514

Protein-protein interaction databases

BioGridi27931. 3 interactions.
IntActiO48538. 1 interaction.
MINTiMINT-7260067.
STRINGi3702.AT1G64060.1.

Structurei

3D structure databases

ProteinModelPortaliO48538.
SMRiO48538. Positions 172-339, 730-944.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini264 – 29936EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini308 – 34336EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini426 – 583158Ferric oxidoreductaseAdd
BLAST
Domaini622 – 742121FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni207 – 2159EF-hand-like 1By similarity
Regioni241 – 25212EF-hand-like 2By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili102 – 12625Sequence analysisAdd
BLAST
Coiled coili157 – 18428Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi239 – 2424Poly-Arg

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 ferric oxidoreductase domain.Curated

Keywords - Domaini

Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
HOGENOMiHOG000216670.
InParanoidiO48538.
KOiK13447.
OMAiFYQYKQK.
PhylomeDBiO48538.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR000778. Cyt_b245_heavy_chain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR013623. NADPH_Ox.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
PF08414. NADPH_Ox. 1 hit.
[Graphical view]
PRINTSiPR00466. GP91PHOX.
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O48538-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPFSKNDRR RWSFDSVSAG KTAVGSASTS PGTEYSINGD QEFVEVTIDL
60 70 80 90 100
QDDDTIVLRS VEPATAINVI GDISDDNTGI MTPVSISRSP TMKRTSSNRF
110 120 130 140 150
RQFSQELKAE AVAKAKQLSQ ELKRFSWSRS FSGNLTTTST AANQSGGAGG
160 170 180 190 200
GLVNSALEAR ALRKQRAQLD RTRSSAQRAL RGLRFISNKQ KNVDGWNDVQ
210 220 230 240 250
SNFEKFEKNG YIYRSDFAQC IGMKDSKEFA LELFDALSRR RRLKVEKINH
260 270 280 290 300
DELYEYWSQI NDESFDSRLQ IFFDIVDKNE DGRITEEEVK EIIMLSASAN
310 320 330 340 350
KLSRLKEQAE EYAALIMEEL DPERLGYIEL WQLETLLLQK DTYLNYSQAL
360 370 380 390 400
SYTSQALSQN LQGLRGKSRI HRMSSDFVYI MQENWKRIWV LSLWIMIMIG
410 420 430 440 450
LFLWKFFQYK QKDAFHVMGY CLLTAKGAAE TLKFNMALIL FPVCRNTITW
460 470 480 490 500
LRSTRLSYFV PFDDNINFHK TIAGAIVVAV ILHIGDHLAC DFPRIVRATE
510 520 530 540 550
YDYNRYLFHY FQTKQPTYFD LVKGPEGITG ILMVILMIIS FTLATRWFRR
560 570 580 590 600
NLVKLPKPFD RLTGFNAFWY SHHLFVIVYI LLILHGIFLY FAKPWYVRTT
610 620 630 640 650
WMYLAVPVLL YGGERTLRYF RSGSYSVRLL KVAIYPGNVL TLQMSKPTQF
660 670 680 690 700
RYKSGQYMFV QCPAVSPFEW HPFSITSAPE DDYISIHIRQ LGDWTQELKR
710 720 730 740 750
VFSEVCEPPV GGKSGLLRAD ETTKKSLPKL LIDGPYGAPA QDYRKYDVLL
760 770 780 790 800
LVGLGIGATP FISILKDLLN NIVKMEEHAD SISDFSRSSE YSTGSNGDTP
810 820 830 840 850
RRKRILKTTN AYFYWVTREQ GSFDWFKGVM NEVAELDQRG VIEMHNYLTS
860 870 880 890 900
VYEEGDARSA LITMVQALNH AKNGVDIVSG TRVRTHFARP NWKKVLTKLS
910 920 930 940
SKHCNARIGV FYCGVPVLGK ELSKLCNTFN QKGSTKFEFH KEHF
Length:944
Mass (Da):108,418
Last modified:June 1, 1998 - v1
Checksum:i1ABAEC316AE80F9B
GO

Sequence cautioni

The sequence AAF24574.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAF00352.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti908 – 9081I → T in BAA28953 (PubMed:9628030).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008111 mRNA. Translation: BAA28953.1.
AF015301 mRNA. Translation: AAB87789.1.
AC007764 Genomic DNA. Translation: AAF24574.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE34186.1.
AK228418 mRNA. Translation: BAF00352.1. Sequence problems.
PIRiT03826.
RefSeqiNP_564821.1. NM_105079.2.
UniGeneiAt.235.

Genome annotation databases

EnsemblPlantsiAT1G64060.1; AT1G64060.1; AT1G64060.
GeneIDi842710.
GrameneiAT1G64060.1; AT1G64060.1; AT1G64060.
KEGGiath:AT1G64060.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008111 mRNA. Translation: BAA28953.1.
AF015301 mRNA. Translation: AAB87789.1.
AC007764 Genomic DNA. Translation: AAF24574.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE34186.1.
AK228418 mRNA. Translation: BAF00352.1. Sequence problems.
PIRiT03826.
RefSeqiNP_564821.1. NM_105079.2.
UniGeneiAt.235.

3D structure databases

ProteinModelPortaliO48538.
SMRiO48538. Positions 172-339, 730-944.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27931. 3 interactions.
IntActiO48538. 1 interaction.
MINTiMINT-7260067.
STRINGi3702.AT1G64060.1.

PTM databases

iPTMnetiO48538.

Proteomic databases

PaxDbiO48538.
PRIDEiO48538.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G64060.1; AT1G64060.1; AT1G64060.
GeneIDi842710.
GrameneiAT1G64060.1; AT1G64060.1; AT1G64060.
KEGGiath:AT1G64060.

Organism-specific databases

TAIRiAT1G64060.

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
HOGENOMiHOG000216670.
InParanoidiO48538.
KOiK13447.
OMAiFYQYKQK.
PhylomeDBiO48538.

Enzyme and pathway databases

BioCyciARA:AT1G64060-MONOMER.
ReactomeiR-ATH-209968. Thyroxine biosynthesis.
R-ATH-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

PROiO48538.

Gene expression databases

GenevisibleiO48538. AT.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR000778. Cyt_b245_heavy_chain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR013623. NADPH_Ox.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
PF08414. NADPH_Ox. 1 hit.
[Graphical view]
PRINTSiPR00466. GP91PHOX.
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91phox)."
    Torres M.A., Onouchi H., Hamada S., Machida C., Hammond-Kosack K.E., Jones J.D.G.
    Plant J. 14:365-370(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: cv. Landsberg erecta.
  2. "A plant homolog of the neutrophil NADPH oxidase gp91phox subunit gene encodes a plasma membrane protein with Ca2+ binding motifs."
    Keller T., Damude H.G., Werner D., Doerner P., Dixon R.A., Lamb C.
    Plant Cell 10:255-266(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-3, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CALCIUM-BINDING DATA, LACK OF GLYCOSYLATION.
    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].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for accumulation of reactive oxygen intermediates in the plant defense response."
    Torres M.A., Dangl J.L., Jones J.D.G.
    Proc. Natl. Acad. Sci. U.S.A. 99:517-522(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA signaling in Arabidopsis."
    Kwak J.M., Mori I.C., Pei Z.-M., Leonhardt N., Torres M.A., Dangl J.L., Bloom R.E., Bodde S., Jones J.D.G., Schroeder J.I.
    EMBO J. 22:2623-2633(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY ABSCISIC ACID, TISSUE SPECIFICITY.
  8. "Ethylene-induced stomatal closure in Arabidopsis occurs via AtrbohF-mediated hydrogen peroxide synthesis."
    Desikan R., Last K., Harrett-Williams R., Tagliavia C., Harter K., Hooley R., Hancock J.T., Neill S.J.
    Plant J. 47:907-916(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  9. "The role of NADPH oxidase and MAP kinase phosphatase in UV-B-dependent gene expression in Arabidopsis."
    Kalbina I., Strid A.
    Plant Cell Environ. 29:1783-1793(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Extracellular ATP induces the accumulation of superoxide via NADPH oxidases in Arabidopsis."
    Song C.J., Steinebrunner I., Wang X., Stout S.C., Roux S.J.
    Plant Physiol. 140:1222-1232(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Production of reactive oxygen species by plant NADPH oxidases."
    Sagi M., Fluhr R.
    Plant Physiol. 141:336-340(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  12. "A low temperature-inducible protein AtSRC2 enhances the ROS-producing activity of NADPH oxidase AtRbohF."
    Kawarazaki T., Kimura S., Iizuka A., Hanamata S., Nibori H., Michikawa M., Imai A., Abe M., Kaya H., Kuchitsu K.
    Biochim. Biophys. Acta 1833:2775-2780(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRC2.
  13. "The Calcineurin B-like calcium sensors CBL1 and CBL9 together with their interacting protein kinase CIPK26 regulate the Arabidopsis NADPH oxidase RBOHF."
    Drerup M.M., Schluecking K., Hashimoto K., Manishankar P., Steinhorst L., Kuchitsu K., Kudla J.
    Mol. Plant 6:559-569(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIPK26, PHOSPHORYLATION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRBOHF_ARATH
AccessioniPrimary (citable) accession number: O48538
Secondary accession number(s): O80342, Q0WR97, Q9SH56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

Was originally called RBOHA.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.