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Protein

CDGSH iron-sulfur domain-containing protein 1

Gene

CISD1

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

Functioni

Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in Fe-S cluster shuttling and/or in redox reactions.By similarity2 Publications

Cofactori

[2Fe-2S] cluster5 PublicationsNote: Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster is redox-active and pH labile and is significantly less stable at pH 4.5 as compared with pH 7.0.5 Publications

Redox potential

E is 0 +/- 10 mV for 2Fe-2S at pH 7.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi72 – 721Iron-sulfur (2Fe-2S)
Metal bindingi74 – 741Iron-sulfur (2Fe-2S)
Metal bindingi83 – 831Iron-sulfur (2Fe-2S)
Metal bindingi87 – 871Iron-sulfur (2Fe-2S); via pros nitrogen

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
CDGSH iron-sulfur domain-containing protein 1
Alternative name(s):
MitoNEET
Gene namesi
Name:CISD1
Synonyms:C10orf70, ZCD1
ORF Names:MDS029
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:30880. CISD1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei14 – 3118Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini32 – 10877CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 721C → S: Abolishes absorption in the 300-500 nm range. 1 Publication
Mutagenesisi74 – 741C → S: Abolishes absorption in the 300-500 nm range. 1 Publication
Mutagenesisi83 – 831C → S: Abolishes absorption in the 300-500 nm range. 1 Publication
Mutagenesisi84 – 841D → N: Does not affect absorption in the 300-500 nm range. 1 Publication
Mutagenesisi87 – 871H → C: Affects absorption in the 300-500 nm range but it is not reduced. Increased stability of the 2Fe-2S cluster at low pH. 1 Publication
Mutagenesisi87 – 871H → Q: Abolishes absorption in the 300-500 nm range. 1 Publication

Organism-specific databases

PharmGKBiPA162382289.

Polymorphism and mutation databases

BioMutaiCISD1.
DMDMi25453105.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 108107CDGSH iron-sulfur domain-containing protein 1PRO_0000089803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Cross-linki42 – 42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei55 – 551N6-acetyllysineBy similarity
Cross-linki55 – 55Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei68 – 681N6-acetyllysineBy similarity
Cross-linki68 – 68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki78 – 78Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki79 – 79Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki89 – 89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei104 – 1041N6-acetyllysineBy similarity
Cross-linki104 – 104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki105 – 105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki106 – 106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9NZ45.
PaxDbiQ9NZ45.
PeptideAtlasiQ9NZ45.
PRIDEiQ9NZ45.

PTM databases

PhosphoSiteiQ9NZ45.

Expressioni

Tissue specificityi

Expression is reduced in cells derived from cystic fibrosis patients.1 Publication

Inductioni

Expression is down-regulated by glibenclamide and 5-[(4-carboxyphenyl)methylene]-2-thioxo-3-(3-trifluoromethyl)phenyl-4-thiazolidinone (CFTR(inh)172), and up-regulated by cAMP/isoproterenol/IBMX, components that inhibit and stimulate chloride transport activity respectively.1 Publication

Gene expression databases

BgeeiQ9NZ45.
CleanExiHS_CISD1.
ExpressionAtlasiQ9NZ45. baseline and differential.
GenevisibleiQ9NZ45. HS.

Organism-specific databases

HPAiCAB045965.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi120949. 6 interactions.
DIPiDIP-46446N.
IntActiQ9NZ45. 2 interactions.
STRINGi9606.ENSP00000363041.

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi47 – 493Combined sources
Beta strandi53 – 6614Combined sources
Beta strandi68 – 714Combined sources
Beta strandi73 – 753Combined sources
Turni78 – 814Combined sources
Helixi86 – 949Combined sources
Beta strandi98 – 1047Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QD0X-ray1.81A/B32-108[»]
2QH7X-ray1.50A/B33-108[»]
2R13X-ray1.80A33-108[»]
3EW0X-ray1.40A/B33-108[»]
3LPQX-ray1.70A/B33-107[»]
3REEX-ray1.76A32-108[»]
4EZFX-ray1.19A/B33-108[»]
4F1EX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R33-108[»]
4F28X-ray1.55A/B33-108[»]
4F2CX-ray1.35A/B33-108[»]
ProteinModelPortaliQ9NZ45.
SMRiQ9NZ45. Positions 33-107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZ45.

Family & Domainsi

Sequence similaritiesi

Belongs to the CISD protein family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG236423.
GeneTreeiENSGT00390000001233.
HOGENOMiHOG000242301.
HOVERGENiHBG052444.
InParanoidiQ9NZ45.
OMAiKDHRNKS.
OrthoDBiEOG7GQXZ6.
PhylomeDBiQ9NZ45.
TreeFamiTF324661.

Family and domain databases

InterProiIPR018967. FeS-contain_CDGSH-typ.
IPR006622. FeS-contain_CDGSH-typ_subfam.
IPR019610. FeS-contain_mitoNEET_N.
[Graphical view]
PfamiPF10660. MitoNEET_N. 1 hit.
PF09360. zf-CDGSH. 1 hit.
[Graphical view]
SMARTiSM00704. ZnF_CDGSH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9NZ45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLTSSSSVR VEWIAAVTIA AGTAAIGYLA YKRFYVKDHR NKAMINLHIQ
60 70 80 90 100
KDNPKIVHAF DMEDLGDKAV YCRCWRSKKF PFCDGAHTKH NEETGDNVGP

LIIKKKET
Length:108
Mass (Da):12,199
Last modified:October 1, 2000 - v1
Checksum:i2E47000F0635CBB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY960578 mRNA. Translation: AAY32336.1.
AF220049 mRNA. Translation: AAF67642.1.
AK312017 mRNA. Translation: BAG34955.1.
CH471083 Genomic DNA. Translation: EAW54163.1.
BC005962 mRNA. Translation: AAH05962.1.
BC007043 mRNA. Translation: AAH07043.1.
BC008474 mRNA. Translation: AAH08474.1.
BC059168 mRNA. Translation: AAH59168.1.
CCDSiCCDS7251.1.
RefSeqiNP_060934.1. NM_018464.4.
UniGeneiHs.370102.

Genome annotation databases

EnsembliENST00000333926; ENSP00000363041; ENSG00000122873.
GeneIDi55847.
KEGGihsa:55847.
UCSCiuc001jkc.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY960578 mRNA. Translation: AAY32336.1.
AF220049 mRNA. Translation: AAF67642.1.
AK312017 mRNA. Translation: BAG34955.1.
CH471083 Genomic DNA. Translation: EAW54163.1.
BC005962 mRNA. Translation: AAH05962.1.
BC007043 mRNA. Translation: AAH07043.1.
BC008474 mRNA. Translation: AAH08474.1.
BC059168 mRNA. Translation: AAH59168.1.
CCDSiCCDS7251.1.
RefSeqiNP_060934.1. NM_018464.4.
UniGeneiHs.370102.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QD0X-ray1.81A/B32-108[»]
2QH7X-ray1.50A/B33-108[»]
2R13X-ray1.80A33-108[»]
3EW0X-ray1.40A/B33-108[»]
3LPQX-ray1.70A/B33-107[»]
3REEX-ray1.76A32-108[»]
4EZFX-ray1.19A/B33-108[»]
4F1EX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R33-108[»]
4F28X-ray1.55A/B33-108[»]
4F2CX-ray1.35A/B33-108[»]
ProteinModelPortaliQ9NZ45.
SMRiQ9NZ45. Positions 33-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120949. 6 interactions.
DIPiDIP-46446N.
IntActiQ9NZ45. 2 interactions.
STRINGi9606.ENSP00000363041.

Chemistry

BindingDBiQ9NZ45.
ChEMBLiCHEMBL1795168.

PTM databases

PhosphoSiteiQ9NZ45.

Polymorphism and mutation databases

BioMutaiCISD1.
DMDMi25453105.

Proteomic databases

MaxQBiQ9NZ45.
PaxDbiQ9NZ45.
PeptideAtlasiQ9NZ45.
PRIDEiQ9NZ45.

Protocols and materials databases

DNASUi55847.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333926; ENSP00000363041; ENSG00000122873.
GeneIDi55847.
KEGGihsa:55847.
UCSCiuc001jkc.5. human.

Organism-specific databases

CTDi55847.
GeneCardsiGC10P060028.
H-InvDBHIX0201471.
HGNCiHGNC:30880. CISD1.
HPAiCAB045965.
MIMi611932. gene.
neXtProtiNX_Q9NZ45.
PharmGKBiPA162382289.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG236423.
GeneTreeiENSGT00390000001233.
HOGENOMiHOG000242301.
HOVERGENiHBG052444.
InParanoidiQ9NZ45.
OMAiKDHRNKS.
OrthoDBiEOG7GQXZ6.
PhylomeDBiQ9NZ45.
TreeFamiTF324661.

Miscellaneous databases

ChiTaRSiCISD1. human.
EvolutionaryTraceiQ9NZ45.
GenomeRNAii55847.
NextBioi61099.
PROiQ9NZ45.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NZ45.
CleanExiHS_CISD1.
ExpressionAtlasiQ9NZ45. baseline and differential.
GenevisibleiQ9NZ45. HS.

Family and domain databases

InterProiIPR018967. FeS-contain_CDGSH-typ.
IPR006622. FeS-contain_CDGSH-typ_subfam.
IPR019610. FeS-contain_mitoNEET_N.
[Graphical view]
PfamiPF10660. MitoNEET_N. 1 hit.
PF09360. zf-CDGSH. 1 hit.
[Graphical view]
SMARTiSM00704. ZnF_CDGSH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  2. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
    Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hematopoietic stem cell.
  3. "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].
    Tissue: Spleen.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Bone marrow, Brain and Lung.
  6. "The outer mitochondrial membrane protein mitoNEET contains a novel redox-active 2Fe-2S cluster."
    Wiley S.E., Paddock M.L., Abresch E.C., Gross L., van der Geer P., Nechushtai R., Murphy A.N., Jennings P.A., Dixon J.E.
    J. Biol. Chem. 282:23745-23749(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, MUTAGENESIS OF CYS-72; CYS-74; CYS-83; ASP-84 AND HIS-87.
  7. "MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity."
    Wiley S.E., Murphy A.N., Ross S.A., van der Geer P., Dixon J.E.
    Proc. Natl. Acad. Sci. U.S.A. 104:5318-5323(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, COFACTOR.
  8. "Crystal structure of Miner1: The redox-active 2Fe-2S protein causative in Wolfram Syndrome 2."
    Conlan A.R., Axelrod H.L., Cohen A.E., Abresch E.C., Zuris J., Yee D., Nechushtai R., Jennings P.A., Paddock M.L.
    J. Mol. Biol. 392:143-153(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria."
    Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M., Kirkpatrick D.S., Bingol B., Corn J.E.
    Nat. Cell Biol. 17:160-169(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-42; LYS-55; LYS-68; LYS-78; LYS-79; LYS-89; LYS-104; LYS-105 AND LYS-106.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 33-108, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
  14. "MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone."
    Paddock M.L., Wiley S.E., Axelrod H.L., Cohen A.E., Roy M., Abresch E.C., Capraro D., Murphy A.N., Nechushtai R., Dixon J.E., Jennings P.A.
    Proc. Natl. Acad. Sci. U.S.A. 104:14342-14347(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 33-108, FUNCTION, COFACTOR, SUBUNIT.
  15. "Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins."
    Lin J., Zhou T., Ye K., Wang J.
    Proc. Natl. Acad. Sci. U.S.A. 104:14640-14645(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 32-108, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCISD1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZ45
Secondary accession number(s): Q1X902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 127 of the entry and version 1 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

Miscellaneous

Binds pioglitazone, an anti-diabetes drug. Binding increases the stability of the 2Fe-2S cluster.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.