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

Elongation factor-like GTPase 1

Gene

EFL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with SBDS, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Has low intrinsic GTPase activity. GTPase activity is increased by contact with 60S ribosome subunits.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 338GTPBy similarity
Nucleotide bindingi92 – 965GTPBy similarity
Nucleotide bindingi146 – 1494GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • ribosome binding Source: UniProtKB

GO - Biological processi

  • mature ribosome assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis, Ribosome biogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor-like GTPase 1
Alternative name(s):
Elongation factor Tu GTP-binding domain-containing protein 1
Elongation factor-like 1
Protein FAM42A
Gene namesi
Name:EFL1Imported
Synonyms:EFTUD1, FAM42A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:25789. EFL1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331T → A: Loss of GTPase activity. Abolishes dissociation of EIF6 from 60S pre-ribosome subunits. 1 Publication
Mutagenesisi96 – 961H → A: Loss of GTPase activity. Abolishes dissociation of EIF6 from 60S pre-ribosome subunits. 1 Publication

Organism-specific databases

PharmGKBiPA134902221.

Polymorphism and mutation databases

BioMutaiEFTUD1.
DMDMi166232397.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11201120Elongation factor-like GTPase 1PRO_0000313805Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei528 – 5281N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ7Z2Z2.
MaxQBiQ7Z2Z2.
PaxDbiQ7Z2Z2.
PRIDEiQ7Z2Z2.

PTM databases

iPTMnetiQ7Z2Z2.
PhosphoSiteiQ7Z2Z2.

Miscellaneous databases

PMAP-CutDBQ7Z2Z2.

Expressioni

Gene expression databases

BgeeiQ7Z2Z2.
CleanExiHS_EFTUD1.
ExpressionAtlasiQ7Z2Z2. baseline and differential.
GenevisibleiQ7Z2Z2. HS.

Organism-specific databases

HPAiHPA039654.
HPA047110.
HPA052345.

Interactioni

Subunit structurei

Associates with the 60S ribosomal subunit.1 Publication

Protein-protein interaction databases

BioGridi122761. 32 interactions.
IntActiQ7Z2Z2. 11 interactions.
STRINGi9606.ENSP00000268206.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5ANBelectron microscopy4.10K1-1120[»]
5ANCelectron microscopy4.20K1-1120[»]
ProteinModelPortaliQ7Z2Z2.
SMRiQ7Z2Z2. Positions 5-424, 464-1100.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 272256tr-type GPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0467. Eukaryota.
COG0480. LUCA.
GeneTreeiENSGT00550000074806.
HOGENOMiHOG000231586.
HOVERGENiHBG101597.
InParanoidiQ7Z2Z2.
KOiK14536.
OMAiVPSCPPF.
OrthoDBiEOG7TTQ6X.
PhylomeDBiQ7Z2Z2.
TreeFamiTF105909.

Family and domain databases

Gene3Di3.30.230.10. 2 hits.
3.30.70.240. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF54211. SSF54211. 3 hits.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7Z2Z2-1) [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
MVLNSLDKMI QLQKNTANIR NICVLAHVDH GKTTLADCLI SSNGIISSRL
60 70 80 90 100
AGKLRYMDSR EDEQIRGITM KSSAISLHYA TGNEEYLINL IDSPGHVDFS
110 120 130 140 150
SEVSTAVRIC DGCIIVVDAV EGVCPQTQAV LRQAWLENIR PVLVINKIDR
160 170 180 190 200
LIVELKFTPQ EAYSHLKNIL EQINALTGTL FTSKVLEERA ERETESQVNP
210 220 230 240 250
NSEQGEQVYD WSTGLEDTDD SHLYFSPEQG NVVFTSAIDG WGFGIEHFAR
260 270 280 290 300
IYSQKIGIKK EVLMKTLWGD YYINMKAKKI MKGDQAKGKK PLFVQLILEN
310 320 330 340 350
IWSLYDAVLK KDKDKIDKIV TSLGLKIGAR EARHSDPKVQ INAICSQWLP
360 370 380 390 400
ISHAVLAMVC QKLPSPLDIT AERVERLMCT GSQTFDSFPP ETQALKAAFM
410 420 430 440 450
KCGSEDTAPV IIFVSKMFAV DAKALPQNKP RPLTQEEIAQ RRERARQRHA
460 470 480 490 500
EKLAAAQGQA PLEPTQDGSA IETCPKGEEP RGDEQQVESM TPKPVLQEEN
510 520 530 540 550
NQESFIAFAR VFSGVARRGK KIFVLGPKYS PLEFLRRVPL GFSAPPDGLP
560 570 580 590 600
QVPHMAYCAL ENLYLLMGRE LEYLEEVPPG NVLGIGGLQD FVLKSATLCS
610 620 630 640 650
LPSCPPFIPL NFEATPIVRV AVEPKHPSEM PQLVKGMKLL NQADPCVQIL
660 670 680 690 700
IQETGEHVLV TAGEVHLQRC LDDLKERFAK IHISVSEPII PFRETITKPP
710 720 730 740 750
KVDMVNEEIG KQQKVAVIHQ MKEDQSKIPE GIQVDSDGLI TITTPNKLAT
760 770 780 790 800
LSVRAMPLPE EVTQILEENS DLIRSMEQLT SSLNEGENTH MIHQKTQEKI
810 820 830 840 850
WEFKGKLEQH LTGRRWRNIV DQIWSFGPRK CGPNILVNKS EDFQNSVWTG
860 870 880 890 900
PADKASKEAS RYRDLGNSIV SGFQLATLSG PMCEEPLMGV CFVLEKWDLS
910 920 930 940 950
KFEEQGASDL AKEGQEENET CSGGNENQEL QDGCSEAFEK RTSQKGESPL
960 970 980 990 1000
TDCYGPFSGQ LIATMKEACR YALQVKPQRL MAAMYTCDIM ATGDVLGRVY
1010 1020 1030 1040 1050
AVLSKREGRV LQEEMKEGTD MFIIKAVLPV AESFGFADEI RKRTSGLASP
1060 1070 1080 1090 1100
QLVFSHWEII PSDPFWVPTT EEEYLHFGEK ADSENQARKY MNAVRKRKGL
1110 1120
YVEEKIVEHA EKQRTLSKNK
Length:1,120
Mass (Da):125,430
Last modified:January 15, 2008 - v2
Checksum:iCCD765953015F109
GO
Isoform 2 (identifier: Q7Z2Z2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     32-82: Missing.

Show »
Length:1,069
Mass (Da):119,887
Checksum:i2E9AFF5FA9B27625
GO

Sequence cautioni

The sequence BAB14450.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti456 – 4561A → V in CAD98101 (PubMed:17974005).Curated
Sequence conflicti632 – 6321Q → R in BAB14450 (PubMed:14702039).Curated
Sequence conflicti696 – 6961I → T in CAD98101 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti478 – 4781E → D.2 Publications
Corresponds to variant rs2292189 [ dbSNP | Ensembl ].
VAR_037746
Natural varianti617 – 6171I → V.
Corresponds to variant rs1128431 [ dbSNP | Ensembl ].
VAR_037747
Natural varianti711 – 7111K → R.
Corresponds to variant rs2292071 [ dbSNP | Ensembl ].
VAR_037748

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei32 – 8251Missing in isoform 2. 1 PublicationVSP_030152Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023181 mRNA. Translation: BAB14450.1. Different initiation.
AK300348 mRNA. Translation: BAH13266.1.
BX538332 mRNA. Translation: CAD98101.1.
AC026624 Genomic DNA. No translation available.
AC026956 Genomic DNA. No translation available.
CCDSiCCDS42070.1. [Q7Z2Z2-2]
CCDS42071.1. [Q7Z2Z2-1]
RefSeqiNP_001035700.1. NM_001040610.2. [Q7Z2Z2-2]
NP_078856.4. NM_024580.5. [Q7Z2Z2-1]
XP_011520300.1. XM_011521998.1. [Q7Z2Z2-1]
UniGeneiHs.459114.

Genome annotation databases

EnsembliENST00000268206; ENSP00000268206; ENSG00000140598. [Q7Z2Z2-1]
ENST00000359445; ENSP00000352418; ENSG00000140598. [Q7Z2Z2-2]
GeneIDi79631.
KEGGihsa:79631.
UCSCiuc002bgt.2. human. [Q7Z2Z2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023181 mRNA. Translation: BAB14450.1. Different initiation.
AK300348 mRNA. Translation: BAH13266.1.
BX538332 mRNA. Translation: CAD98101.1.
AC026624 Genomic DNA. No translation available.
AC026956 Genomic DNA. No translation available.
CCDSiCCDS42070.1. [Q7Z2Z2-2]
CCDS42071.1. [Q7Z2Z2-1]
RefSeqiNP_001035700.1. NM_001040610.2. [Q7Z2Z2-2]
NP_078856.4. NM_024580.5. [Q7Z2Z2-1]
XP_011520300.1. XM_011521998.1. [Q7Z2Z2-1]
UniGeneiHs.459114.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5ANBelectron microscopy4.10K1-1120[»]
5ANCelectron microscopy4.20K1-1120[»]
ProteinModelPortaliQ7Z2Z2.
SMRiQ7Z2Z2. Positions 5-424, 464-1100.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122761. 32 interactions.
IntActiQ7Z2Z2. 11 interactions.
STRINGi9606.ENSP00000268206.

PTM databases

iPTMnetiQ7Z2Z2.
PhosphoSiteiQ7Z2Z2.

Polymorphism and mutation databases

BioMutaiEFTUD1.
DMDMi166232397.

Proteomic databases

EPDiQ7Z2Z2.
MaxQBiQ7Z2Z2.
PaxDbiQ7Z2Z2.
PRIDEiQ7Z2Z2.

Protocols and materials databases

DNASUi79631.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268206; ENSP00000268206; ENSG00000140598. [Q7Z2Z2-1]
ENST00000359445; ENSP00000352418; ENSG00000140598. [Q7Z2Z2-2]
GeneIDi79631.
KEGGihsa:79631.
UCSCiuc002bgt.2. human. [Q7Z2Z2-1]

Organism-specific databases

CTDi79631.
GeneCardsiEFTUD1.
H-InvDBHIX0038366.
HGNCiHGNC:25789. EFL1.
HPAiHPA039654.
HPA047110.
HPA052345.
neXtProtiNX_Q7Z2Z2.
PharmGKBiPA134902221.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0467. Eukaryota.
COG0480. LUCA.
GeneTreeiENSGT00550000074806.
HOGENOMiHOG000231586.
HOVERGENiHBG101597.
InParanoidiQ7Z2Z2.
KOiK14536.
OMAiVPSCPPF.
OrthoDBiEOG7TTQ6X.
PhylomeDBiQ7Z2Z2.
TreeFamiTF105909.

Miscellaneous databases

GenomeRNAii79631.
NextBioi68729.
PMAP-CutDBQ7Z2Z2.
PROiQ7Z2Z2.

Gene expression databases

BgeeiQ7Z2Z2.
CleanExiHS_EFTUD1.
ExpressionAtlasiQ7Z2Z2. baseline and differential.
GenevisibleiQ7Z2Z2. HS.

Family and domain databases

Gene3Di3.30.230.10. 2 hits.
3.30.70.240. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF54211. SSF54211. 3 hits.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-478.
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ASP-478.
    Tissue: Fetal brain.
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF THR-33 AND HIS-96.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEFL1_HUMAN
AccessioniPrimary (citable) accession number: Q7Z2Z2
Secondary accession number(s): A6NKY5, B7Z6I0, Q9H8Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: April 13, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.