Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Eye-specific diacylglycerol kinase

Gene

rdgA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Required for the maintenance of phospholipid turnover within the photoreceptor.1 Publication

Catalytic activityi

ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri591 – 64151Phorbol-ester/DAG-type 1Add
BLAST
Zinc fingeri661 – 72464Phorbol-ester/DAG-type 2Add
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • diacylglycerol kinase activity Source: FlyBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • actin filament organization Source: FlyBase
  • deactivation of rhodopsin mediated signaling Source: FlyBase
  • intracellular signal transduction Source: InterPro
  • lipid phosphorylation Source: FlyBase
  • phosphatidic acid biosynthetic process Source: FlyBase
  • phosphatidylinositol biosynthetic process Source: FlyBase
  • phosphorylation Source: FlyBase
  • photoreceptor cell maintenance Source: FlyBase
  • phototransduction Source: FlyBase
  • protein kinase C-activating G-protein coupled receptor signaling pathway Source: InterPro
  • rhodopsin mediated signaling pathway Source: FlyBase
  • sensory perception of smell Source: FlyBase
  • sensory perception of sound Source: FlyBase
  • thermotaxis Source: FlyBase
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_309807. Effects of PIP2 hydrolysis.
SABIO-RKQ09103.
SignaLinkiQ09103.

Names & Taxonomyi

Protein namesi
Recommended name:
Eye-specific diacylglycerol kinase (EC:2.7.1.107)
Short name:
DAG kinase 2
Short name:
DGK 2
Short name:
Diglyceride kinase 2
Alternative name(s):
Retinal degeneration A protein
Gene namesi
Name:rdgA
Synonyms:DGK2
ORF Names:CG34344
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0261549. rdgA.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB-SubCell
  • microtubule associated complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Flies exhibit photoreceptor cells that degenerate within a week after eclosion.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14571457Eye-specific diacylglycerol kinasePRO_0000218474Add
BLAST

Proteomic databases

PaxDbiQ09103.

Expressioni

Tissue specificityi

Expressed specifically in adult eye.1 Publication

Gene expression databases

BgeeiQ09103.

Interactioni

Protein-protein interaction databases

BioGridi58282. 12 interactions.
IntActiQ09103. 4 interactions.
STRINGi7227.FBpp0305778.

Structurei

3D structure databases

ProteinModelPortaliQ09103.
SMRiQ09103. Positions 1275-1443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini808 – 944137DAGKcPROSITE-ProRule annotationAdd
BLAST
Repeati1320 – 134930ANK 1Add
BLAST
Repeati1353 – 138230ANK 2Add
BLAST
Repeati1389 – 141830ANK 3Add
BLAST
Repeati1422 – 145130ANK 4Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 65Poly-Gln
Compositional biasi24 – 3916Thr-richAdd
BLAST
Compositional biasi110 – 1156Poly-Ser
Compositional biasi227 – 2315Poly-Glu
Compositional biasi763 – 77816Gly-richAdd
BLAST

Sequence similaritiesi

Contains 4 ANK repeats.PROSITE-ProRule annotation
Contains 1 DAGKc domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri591 – 64151Phorbol-ester/DAG-type 1Add
BLAST
Zinc fingeri661 – 72464Phorbol-ester/DAG-type 2Add
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000119050.
InParanoidiQ09103.
OMAiINGKHMW.
OrthoDBiEOG76HQ0Q.
PhylomeDBiQ09103.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR016064. NAD/diacylglycerol_kinase.
IPR002219. PE/DAG-bd.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF00130. C1_1. 2 hits.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 4 hits.
SM00109. C1. 1 hit.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 1 hit.
SSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50146. DAGK. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q09103-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQQQQQPSID QLPEPTASTS NSATTKPTIA TATTSTTTTS GNNFHQQLQA
60 70 80 90 100
TTAATMQRLR TTFTRSRTPT GAEMKMQNSL EVPKQVRSAS FDEMQLESQR
110 120 130 140 150
ASSSLLKQQS SSSASADERS SEAGFLQVPL AAHQQRSHSF DSATASAGSD
160 170 180 190 200
DSGTFLEVPR RLKARRSSST KTPPPCIHCH YLEEYERRMT AEQRYFIDHR
210 220 230 240 250
ELTALSYSNT SSEASEDEDE VEGHNAEEEE EGSAAIEDAE EETTEAATEE
260 270 280 290 300
ADEDPRTEVE SEHDHDPDDD AALEMDIRIG NMSQGSSIEE SRARLPRQMR
310 320 330 340 350
RHTIGSSSVT SASEDEGLEG SDNGSPHFGN TLLPPQPTTP CGITFTLSPT
360 370 380 390 400
NGDYPSPPHL PLDPGSPPIS PCSSNSGRLP ALAPIISTPC SSADADDAGA
410 420 430 440 450
AMGLPVRARR RSISRQEAIF VEPTGNSLEN VSHEEVDNSN TKSSVDTADS
460 470 480 490 500
LDEASTMATC GSPGAAGGSG ASSSHHNAFV VRDIYLMVPD LKRDRAASVD
510 520 530 540 550
SCFSKLSSNA KTEELQPSAD GCFLTVPNIN ATRSRSVDIV LPTDEQARYK
560 570 580 590 600
ALSMTGSTVT YADGRTASAS NSRRPIRIVP DWTENAVQGE HYWKPTSASG
610 620 630 640 650
DLCCLNEECI KSGQRMKCSA CQLVAHHNCI PFVNEKSTLA CKPTYRDVGI
660 670 680 690 700
RQYREQTTTH HHWVHRKLEK GKCKQCGKFF PMKQAVQSKL FGSKEIVALA
710 720 730 740 750
CAWCHEIYHN KEACFNQAKI GEECRLGNYA PIIVPPSWIV KLPTKGNFKS
760 770 780 790 800
SIRVSNKNNA ASGSGGGGAG GGAGGGGGKS KKQTQRRQKG KEEKKEPRAF
810 820 830 840 850
IVKPIPSPEV IPVIVFINPK SGGNQGHKLL GKFQHLLNPR QVFDLTQGGP
860 870 880 890 900
KMGLDMFRKA PNLRVLACGG DGTVGWVLSV LDQIQPPLQP APAVGVLPLG
910 920 930 940 950
TGNDLARALG WGGGYTDEPI GKILREIGMS QCVLMDRWRV KVTPNDDVTD
960 970 980 990 1000
DHVDRSKPNV PLNVINNYFS FGVDAHIALE FHEAREAHPE RFNSRLRNKM
1010 1020 1030 1040 1050
YYGQMGGKDL ILRQYRNLSQ WVTLECDGQD FTGKLRDAGC HAVLFLNIPS
1060 1070 1080 1090 1100
YGGGTHPWND SFGASKPSID DGLMEVVGLT TYQLPMLQAG MHGTCICQCR
1110 1120 1130 1140 1150
KARIITKRTI PMQVDGEACR VKPSVIEIEL LNKALMLSKR KHGRGDVQVN
1160 1170 1180 1190 1200
PLEKMQLHIL RVTMQQYEQY HYDKEMLRKL ANKLGQIEIE SQCDLEHVRN
1210 1220 1230 1240 1250
MLNTKFEESI SYPKVSQDWC FIDSCTAEHY FRIDRAQEHL HYICDIAIDE
1260 1270 1280 1290 1300
LYILDHEAAT MPQTPDQERS FAAFSQRQAQ NERRQMDQAQ GRGPGSTDED
1310 1320 1330 1340 1350
LQIGSKPIKV MKWKSPILEQ TSDAILLAAQ SGDLNMLRAL HEQGYSLQSV
1360 1370 1380 1390 1400
NKNGQTALHF ACKYNHRDIV KYIIASATRR LINMADKELG QTALHIAAEQ
1410 1420 1430 1440 1450
NRRDICVMLV AAGAHLDTLD SGGNTPMMVA FNKNANEIAT YLESKQGTQP

VDGWLDD
Length:1,457
Mass (Da):160,142
Last modified:June 21, 2005 - v2
Checksum:i8F4E33E9C1B665D1
GO
Isoform B (identifier: Q09103-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-116: MQQQQQPSID...KQQSSSSASA → MPERSISQRD...EDIEMLDYDT
     117-564: Missing.
     1315-1315: S → SNKDRLFSFNEDVFGCGFS
     1445-1457: KQGTQPVDGWLDD → QERFMHLEKQTRI

Note: No experimental confirmation available.
Show »
Length:1,027
Mass (Da):115,579
Checksum:i70B26B9A087A84F9
GO
Isoform C (identifier: Q09103-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-132: MQQQQQPSID...AGFLQVPLAA → MERLLHAVRE...SLGAWRRKRR
     133-565: Missing.

Note: No experimental confirmation available.
Show »
Length:1,024
Mass (Da):113,748
Checksum:iD8119DAF5644BDC4
GO

Sequence cautioni

The sequence AAQ22428.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321A → V in BAA04135 (PubMed:8248222).Curated
Sequence conflicti208 – 2081S → T in BAA04135 (PubMed:8248222).Curated
Sequence conflicti438 – 4381N → K in BAA04135 (PubMed:8248222).Curated
Sequence conflicti565 – 5651R → RR in BAA04135 (PubMed:8248222).Curated
Sequence conflicti667 – 6671K → N in BAA04135 (PubMed:8248222).Curated
Sequence conflicti679 – 6846Missing in BAA04135 (PubMed:8248222).Curated
Sequence conflicti778 – 7781G → GGG in BAA04135 (PubMed:8248222).Curated
Sequence conflicti924 – 9241L → M in AAQ22428 (Ref. 5) Curated
Sequence conflicti983 – 9831E → G in AAQ22428 (Ref. 5) Curated
Sequence conflicti1128 – 11281I → N in AAQ22428 (Ref. 5) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 132132MQQQQ…VPLAA → MERLLHAVREEFQTEDEYET EVDDEGNVLHRSSISSCSSS SSSSNTSSSSDGSNSTASQP LSPSLPQPRRRLQRSDSFGS VGGGVAGGVAGSGATGAGGV RRFRRSSIGMQRKSAFRQRK LDSLGAWRRKRR in isoform C. CuratedVSP_030265Add
BLAST
Alternative sequencei1 – 116116MQQQQ…SSASA → MPERSISQRDLDEIEIESDE EEEELEQGVGLSTRSRRNRR GASDSPAASRARNATNGIQN RGRERERERERERSRERFGG TNAADEARFYDDEEQRMEDD GEEDSDEDIEMLDYDT in isoform B. 1 PublicationVSP_030264Add
BLAST
Alternative sequencei117 – 564448Missing in isoform B. 1 PublicationVSP_030266Add
BLAST
Alternative sequencei133 – 565433Missing in isoform C. CuratedVSP_030267Add
BLAST
Alternative sequencei1315 – 13151S → SNKDRLFSFNEDVFGCGFS in isoform B. 1 PublicationVSP_028732
Alternative sequencei1445 – 145713KQGTQ…GWLDD → QERFMHLEKQTRI in isoform B. 1 PublicationVSP_028733Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17315 mRNA. Translation: BAA04135.1.
AE014298 Genomic DNA. Translation: AAF46430.2.
AE014298 Genomic DNA. Translation: ABW09364.1.
AE014298 Genomic DNA. Translation: ABW09365.1.
AY075349 mRNA. Translation: AAL68208.1.
BT009959 mRNA. Translation: AAQ22428.1. Sequence problems.
PIRiT13709.
RefSeqiNP_001096916.1. NM_001103446.2. [Q09103-3]
NP_001096917.1. NM_001103447.4. [Q09103-2]
NP_511092.2. NM_078537.3. [Q09103-1]
UniGeneiDm.5516.

Genome annotation databases

EnsemblMetazoaiFBtr0302660; FBpp0291800; FBgn0261549. [Q09103-1]
GeneIDi31826.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17315 mRNA. Translation: BAA04135.1.
AE014298 Genomic DNA. Translation: AAF46430.2.
AE014298 Genomic DNA. Translation: ABW09364.1.
AE014298 Genomic DNA. Translation: ABW09365.1.
AY075349 mRNA. Translation: AAL68208.1.
BT009959 mRNA. Translation: AAQ22428.1. Sequence problems.
PIRiT13709.
RefSeqiNP_001096916.1. NM_001103446.2. [Q09103-3]
NP_001096917.1. NM_001103447.4. [Q09103-2]
NP_511092.2. NM_078537.3. [Q09103-1]
UniGeneiDm.5516.

3D structure databases

ProteinModelPortaliQ09103.
SMRiQ09103. Positions 1275-1443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58282. 12 interactions.
IntActiQ09103. 4 interactions.
STRINGi7227.FBpp0305778.

Proteomic databases

PaxDbiQ09103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0302660; FBpp0291800; FBgn0261549. [Q09103-1]
GeneIDi31826.

Organism-specific databases

CTDi31826.
FlyBaseiFBgn0261549. rdgA.

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000119050.
InParanoidiQ09103.
OMAiINGKHMW.
OrthoDBiEOG76HQ0Q.
PhylomeDBiQ09103.

Enzyme and pathway databases

ReactomeiREACT_309807. Effects of PIP2 hydrolysis.
SABIO-RKQ09103.
SignaLinkiQ09103.

Miscellaneous databases

ChiTaRSirdgA. fly.
GenomeRNAii31826.
NextBioi775516.
PROiQ09103.

Gene expression databases

BgeeiQ09103.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR016064. NAD/diacylglycerol_kinase.
IPR002219. PE/DAG-bd.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF00130. C1_1. 2 hits.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 4 hits.
SM00109. C1. 1 hit.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 1 hit.
SSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50146. DAGK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila retinal degeneration A gene encodes an eye-specific diacylglycerol kinase with cysteine-rich zinc-finger motifs and ankyrin repeats."
    Masai I., Okazaki A., Hosoya T., Hotta Y.
    Proc. Natl. Acad. Sci. U.S.A. 90:11157-11161(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    Strain: Canton-S.
    Tissue: Head.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Head.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiDGK2_DROME
AccessioniPrimary (citable) accession number: Q09103
Secondary accession number(s): A8JV38
, A8JV40, Q0KHU7, Q7YU71, Q8SY47, Q9W3A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 21, 2005
Last modified: July 22, 2015
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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.