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Protein

GON-4-like protein

Gene

Gon4l

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has transcriptional repressor activity, probably as part of a complex with YY1, SIN3A AND HDAC1 (PubMed:21454521). Required for B cell lymphopoiesis (PubMed:20530203).2 Publications

GO - Molecular functioni

  • DNA binding Source: InterPro
  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

  • B cell differentiation Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
GON-4-like protein
Alternative name(s):
GON-4 homolog
Gene namesi
Name:Gon4l
Synonyms:Gon4, Kiaa1606
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1917579. Gon4l.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22602260GON-4-like proteinPRO_0000197110Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei347 – 3471PhosphoserineBy similarity
Cross-linki536 – 536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei784 – 7841PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9DB00.
MaxQBiQ9DB00.
PaxDbiQ9DB00.
PRIDEiQ9DB00.

PTM databases

PhosphoSiteiQ9DB00.

Expressioni

Tissue specificityi

Expressed in thymus. Specifically expressed in B cells and their precursors (at protein level). Also detected in brain, heart, spleen and bone marrow.1 Publication

Gene expression databases

BgeeiQ9DB00.

Interactioni

Subunit structurei

Found in a complex with YY1, SIN3A and HDAC1.1 Publication

Protein-protein interaction databases

BioGridi217912. 3 interactions.
STRINGi10090.ENSMUSP00000080397.

Structurei

Secondary structure

1
2260
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2173 – 21753Combined sources
Helixi2177 – 218913Combined sources
Turni2194 – 21963Combined sources
Helixi2197 – 22048Combined sources
Helixi2209 – 222517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UG2NMR-A2148-2228[»]
ProteinModelPortaliQ9DB00.
SMRiQ9DB00. Positions 2140-2229.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DB00.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1648 – 172073PAH 1PROSITE-ProRule annotationAdd
BLAST
Domaini1730 – 180172PAH 2PROSITE-ProRule annotationAdd
BLAST
Domaini2167 – 222054Myb-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni610 – 1364755Required for interaction with YY1, SIN3A AND HDAC1, and transcriptional repression activity1 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi242 – 2487Poly-Lys
Compositional biasi380 – 3856Poly-Glu
Compositional biasi450 – 4567Poly-Pro
Compositional biasi519 – 57860Asp-richAdd
BLAST
Compositional biasi622 – 6254Poly-Glu
Compositional biasi1476 – 157095Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 Myb-like domain.PROSITE-ProRule annotation
Contains 2 PAH (paired amphipathic helix) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IHDM. Eukaryota.
ENOG410XS4M. LUCA.
HOGENOMiHOG000082442.
HOVERGENiHBG081563.
InParanoidiQ9DB00.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.20.1160.11. 1 hit.
InterProiIPR033277. GON-4-like.
IPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR003822. PAH.
[Graphical view]
PANTHERiPTHR16088:SF11. PTHR16088:SF11. 3 hits.
PfamiPF02671. PAH. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF47762. SSF47762. 2 hits.
PROSITEiPS50090. MYB_LIKE. 1 hit.
PS51477. PAH. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DB00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPCKKRRLS VTESSQQQDD QEGDDLDLEA AVKPDTDQLP DSASESLSWG
60 70 80 90 100
QSQDSAVCPE GLSMQDGDDQ LRAEGLSLNS KMLAQHVNLA VLEAVDVAVS
110 120 130 140 150
QEIPLPSLES SHSLPVHVDK GRLQVSASKK GKRVVFTPGQ VTREDRGDHP
160 170 180 190 200
VPEEPPSGEP AEEAKTEGGE LELRSDGEVP LLSSSSQSAK PGAQPRKSVQ
210 220 230 240 250
PDGSAFPQDK PLGPLVRQAE EEMEDGGLFI PTEEQDSEES DKKKKTKKGT
260 270 280 290 300
KRKRDGKGPE QGTMVYDPKL DDMLDRTLED GAKQHNLTAV NVRNILHEVI
310 320 330 340 350
TNEHVVAMMK AAISETEDMP LFEPKMTRSK LKEVVEKGVV IPTWNISPIK
360 370 380 390 400
KASEIKQPPQ FVDIHLEEDD SSDEEYSPDE EEEDETAEES LLESDVESTA
410 420 430 440 450
SSPRGVKRSR LRLSSEVAET DEESGMLSEV EKAATPALRH ISAEVVPMGP
460 470 480 490 500
PPPPKPKQSR DSVFMEKLDA VDEELASSPV CMDSFQPMED SLIAFRTRSK
510 520 530 540 550
MPLKDVPLGQ LEAELQAPDI TPDMYDPNTA DDEDWKQWLG GLINDDVENE
560 570 580 590 600
DEADDDDDPE YNFLEDLDEP DTEDFRTDRA VRITKKEVNG LMEELFETVQ
610 620 630 640 650
SVVPSKFQDE MGFSNMEDDG PEEEERATES RPSFNTPQAL RFEEPLANLL
660 670 680 690 700
NERHRTVKEL LEQLKMKKPS VRQQPEVEKL KPQEEAAHQT LVLDPAQRSR
710 720 730 740 750
LQQQMQQHVQ LLTQIYLLTT SNPNLSSEAS TTRIFLKELG TFAENSIALH
760 770 780 790 800
QQFNPRFQTL FQPCNWMGAM RLIEDFTQVS IDCSPHKTAK KTASEFPCLP
810 820 830 840 850
KQVAWILATN KVFMYPELLP ICSLKANNPR DKTIFTKAED NLLALGLKHF
860 870 880 890 900
EGTEFPKPLI SKYLVTCKTA HQLTVRIKNL NLNRAPNNVI KFYKKTKQLP
910 920 930 940 950
VLVRCCEEIQ PHQWKPPFEK EEHRLPFWLK ASLQSIQDEL RNISEGATEG
960 970 980 990 1000
GSVTTATESS TDQHLQKASP ALGDEPQYPL LLPKGVVLKL KPGSKRFSRK
1010 1020 1030 1040 1050
AWRQKRPLVQ KPLLIQPSPS VQPVFNPGKM ATWPTQSEVP PSNTVVQIPH
1060 1070 1080 1090 1100
LIQPAAVLQT LPGFPSVGVR GEDGFESPTA LPAMPCGSEA RTTFPLSETQ
1110 1120 1130 1140 1150
SAPPSCSAPK LMLPSLAPSK FRKPYVRRKP TRRKGAKVSP CVKPAPIIHP
1160 1170 1180 1190 1200
TPVIFTVPAT TVKVVSIGGG CNMIQPVSAA VAPSPQTIPI TTLLVNPTTF
1210 1220 1230 1240 1250
PCSLNQPLVA SSISPLIVSS NPLTLPVTSI PEDKAQVKLD VAEGKNAPQN
1260 1270 1280 1290 1300
PESKLKPQEL TPLCTTVFSK EEPKSWHSSA DTGSQEAFSE SSACSWAVVK
1310 1320 1330 1340 1350
TESQEGSSEK SACGWTVVKT EDGGHAVEPL PQNLQDSLSS SSKDLLNMVK
1360 1370 1380 1390 1400
MEAQDCMVEI SSNFPKQDIG EEVKEECSME LDSESPQEKP SSASEMSKQT
1410 1420 1430 1440 1450
VLQREDMQAA KSPSVPQDAA AEGRTSSHAS RGLPKSTLSS MGQGGGLSGP
1460 1470 1480 1490 1500
PGKLEDSANA DGQSVGTPAG PDTGGEKDGP EEEEEEDFDD LTQDEEDELS
1510 1520 1530 1540 1550
SASEESVLSV PELQETMEKL TWLASERRMS QEGESEEENS QEENSEPEEE
1560 1570 1580 1590 1600
EEEEAEGMET LQKEDEVNDE AVGDAAKKPP STLASPQTAP EIETSIAPAG
1610 1620 1630 1640 1650
ESIKAAGKGR SSHRARNKRG SRARASKDTS KLLLLYDEDI LDRDPLREQK
1660 1670 1680 1690 1700
DLAFAQAYLT RVREALQHTP GKYEDFLQII YEFESSTQMH SAVDLFKSLQ
1710 1720 1730 1740 1750
TLLQDWPQLL KDFAAFLLPE QALSCGLFEE QQAFEKSRKF LRQLEICFAE
1760 1770 1780 1790 1800
NPSHHQKIIK VLQGCADCLP QDIAELKTQM WQLLRGHDHL QDEFSIFFDH
1810 1820 1830 1840 1850
LRPAASRMGD FEEINWTEEK EYEFDGFEEV ILPDVEEDEE PAKVSTASKS
1860 1870 1880 1890 1900
KRRKEIGVQH QDKDTEWPEA AKDCSCSCHE GGPESKLKKS KRRNCHCSSK
1910 1920 1930 1940 1950
VCDSKPYKSK EPPELVGSGP LHEASTVPGS KEAGQGKDML EEEILEEQEN
1960 1970 1980 1990 2000
MEVTQSKTAR TTRKGEAPAP GSTIGSTLLC PAEVTPMELL LEGPALCSAE
2010 2020 2030 2040 2050
TPRLPPQTGA VVCSVRRNQA GPEVVSCLST SSLPPEEGED QRAAANSETI
2060 2070 2080 2090 2100
APHREASETE RLPETVEHSA PLPSPVSTRT RDTGRRHICG KAGSQSWLIE
2110 2120 2130 2140 2150
SRAEAEAAHV AAPICEKSSG ARASEAAPKT AREVLAEDSG TQGMGPEGAL
2160 2170 2180 2190 2200
PKASEATVCA NNSKVSSTGE KVVLWTREAD RVILTMCQEQ GAQPHTFSVI
2210 2220 2230 2240 2250
SQQLGNKTPV EVSHRFRELM QLFHTACEAS SEDEDDATST SNADQLSDHG
2260
DLLSEEELDE
Length:2,260
Mass (Da):248,742
Last modified:July 27, 2011 - v3
Checksum:iBB0F605666D642C6
GO

Sequence cautioni

The sequence AAH16616.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB23992.1 differs from that shown.Chimeric cDNA.Curated
The sequence BAC65813.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591P → L in BAC65813 (PubMed:12693553).Curated
Sequence conflicti734 – 7341I → V in BAC65813 (PubMed:12693553).Curated
Sequence conflicti1080 – 10801A → S in BAC65813 (PubMed:12693553).Curated
Sequence conflicti1341 – 13411S → P in BAC65813 (PubMed:12693553).Curated
Sequence conflicti1354 – 13541Q → E in BAC65813 (PubMed:12693553).Curated
Sequence conflicti1364 – 13641F → L in BAC65813 (PubMed:12693553).Curated
Sequence conflicti1392 – 13921S → R in BAC65813 (PubMed:12693553).Curated
Sequence conflicti1407 – 14071M → T in BAC65813 (PubMed:12693553).Curated
Sequence conflicti1438 – 14381L → P in BAC65813 (PubMed:12693553).Curated
Sequence conflicti1458 – 14581A → V in BAC65813 (PubMed:12693553).Curated
Sequence conflicti2069 – 20691S → P in BAC65813 (PubMed:12693553).Curated
Sequence conflicti2069 – 20691S → P in AAH16616 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC127377 Genomic DNA. No translation available.
AK005385 mRNA. Translation: BAB23992.1. Different termination.
AK122531 mRNA. Translation: BAC65813.1. Different initiation.
BC016616 mRNA. Translation: AAH16616.1. Different initiation.
RefSeqiXP_011238572.1. XM_011240270.1.
UniGeneiMm.126870.
Mm.482358.

Genome annotation databases

GeneIDi76022.
UCSCiuc008pxb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC127377 Genomic DNA. No translation available.
AK005385 mRNA. Translation: BAB23992.1. Different termination.
AK122531 mRNA. Translation: BAC65813.1. Different initiation.
BC016616 mRNA. Translation: AAH16616.1. Different initiation.
RefSeqiXP_011238572.1. XM_011240270.1.
UniGeneiMm.126870.
Mm.482358.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UG2NMR-A2148-2228[»]
ProteinModelPortaliQ9DB00.
SMRiQ9DB00. Positions 2140-2229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217912. 3 interactions.
STRINGi10090.ENSMUSP00000080397.

PTM databases

PhosphoSiteiQ9DB00.

Proteomic databases

EPDiQ9DB00.
MaxQBiQ9DB00.
PaxDbiQ9DB00.
PRIDEiQ9DB00.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi76022.
UCSCiuc008pxb.1. mouse.

Organism-specific databases

CTDi54856.
MGIiMGI:1917579. Gon4l.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IHDM. Eukaryota.
ENOG410XS4M. LUCA.
HOGENOMiHOG000082442.
HOVERGENiHBG081563.
InParanoidiQ9DB00.

Miscellaneous databases

ChiTaRSiGon4l. mouse.
EvolutionaryTraceiQ9DB00.
PROiQ9DB00.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DB00.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.20.1160.11. 1 hit.
InterProiIPR033277. GON-4-like.
IPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR003822. PAH.
[Graphical view]
PANTHERiPTHR16088:SF11. PTHR16088:SF11. 3 hits.
PfamiPF02671. PAH. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF47762. SSF47762. 2 hits.
PROSITEiPS50090. MYB_LIKE. 1 hit.
PS51477. PAH. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-168.
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-2260.
    Tissue: Brain.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1531-2260.
    Strain: FVB/N.
    Tissue: Mammary gland.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  6. Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. "The developmental regulator protein Gon4l associates with protein YY1, co-repressor Sin3a, and histone deacetylase 1 and mediates transcriptional repression."
    Lu P., Hankel I.L., Hostager B.S., Swartzendruber J.A., Friedman A.D., Brenton J.L., Rothman P.B., Colgan J.D.
    J. Biol. Chem. 286:18311-18319(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH YY1; SIN3A AND HDAC1, SUBCELLULAR LOCATION.
  8. "Solution structure of mouse hypothetical gene (2610100B20Rik) product homologous to Myb DNA-binding domain."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 2148-2230.

Entry informationi

Entry nameiGON4L_MOUSE
AccessioniPrimary (citable) accession number: Q9DB00
Secondary accession number(s): E9Q5N3, Q80TB4, Q91YI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.