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Protein

Thiosulfate sulfurtransferase

Gene

TST

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

Functioni

Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity (By similarity). Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA.By similarity2 Publications

Catalytic activityi

Thiosulfate + cyanide = sulfite + thiocyanate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871SubstrateBy similarity
Active sitei248 – 2481Cysteine persulfide intermediatePROSITE-ProRule annotation
Binding sitei250 – 2501SubstrateBy similarity

GO - Molecular functioni

  1. 5S rRNA binding Source: UniProtKB
  2. thiosulfate sulfurtransferase activity Source: ProtInc

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. cyanate catabolic process Source: ProtInc
  3. epithelial cell differentiation Source: UniProtKB
  4. rRNA import into mitochondrion Source: UniProtKB
  5. rRNA transport Source: UniProtKB
  6. small molecule metabolic process Source: Reactome
  7. sulfide oxidation, using sulfide:quinone oxidoreductase Source: Reactome
  8. sulfur amino acid catabolic process Source: Reactome
  9. sulfur amino acid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_116010. Sulfide oxidation to sulfate.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase (EC:2.8.1.1)
Alternative name(s):
Rhodanese
Gene namesi
Name:TST
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:12388. TST.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrial inner membrane Source: Ensembl
  4. mitochondrial matrix Source: ProtInc
  5. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37055.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 297296Thiosulfate sulfurtransferasePRO_0000139395Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141N6-acetyllysine; alternate1 Publication
Modified residuei14 – 141N6-succinyllysine; alternateBy similarity
Glycosylationi35 – 351O-linked (GlcNAc)By similarity
Modified residuei136 – 1361N6-acetyllysine; alternateBy similarity
Modified residuei136 – 1361N6-succinyllysine; alternateBy similarity
Modified residuei163 – 1631N6-acetyllysineBy similarity
Modified residuei175 – 1751N6-acetyllysine; alternateBy similarity
Modified residuei175 – 1751N6-succinyllysine; alternateBy similarity
Modified residuei224 – 2241N6-acetyllysine; alternateBy similarity
Modified residuei224 – 2241N6-succinyllysine; alternateBy similarity
Modified residuei236 – 2361N6-acetyllysineBy similarity
Modified residuei237 – 2371N6-acetyllysine; alternateBy similarity
Modified residuei237 – 2371N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiQ16762.
PaxDbiQ16762.
PeptideAtlasiQ16762.
PRIDEiQ16762.

2D gel databases

REPRODUCTION-2DPAGEIPI00216293.

PTM databases

PhosphoSiteiQ16762.

Expressioni

Gene expression databases

BgeeiQ16762.
CleanExiHS_TST.
ExpressionAtlasiQ16762. baseline and differential.
GenevestigatoriQ16762.

Organism-specific databases

HPAiCAB009546.
HPA003044.
HPA003643.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi113114. 13 interactions.
IntActiQ16762. 2 interactions.
STRINGi9606.ENSP00000249042.

Structurei

3D structure databases

ProteinModelPortaliQ16762.
SMRiQ16762. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 143119Rhodanese 1PROSITE-ProRule annotationAdd
BLAST
Domaini173 – 288116Rhodanese 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 15916HingeAdd
BLAST

Domaini

Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).By similarity

Sequence similaritiesi

Contains 2 rhodanese domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2897.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiQ16762.
KOiK01011.
OMAiSRAQGRY.
OrthoDBiEOG72ZCGB.
PhylomeDBiQ16762.
TreeFamiTF315133.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q16762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE
60 70 80 90 100
RHVPGASFFD IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD
110 120 130 140 150
GEHLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP
160 170 180 190 200
AVFKATLDRS LLKTYEQVLE NLESKRFQLV DSRSQGRFLG TEPEPDAVGL
210 220 230 240 250
DSGHIRGAVN MPFMDFLTED GFEKGPEELR ALFQTKKVDL SQPLIATCRK
260 270 280 290
GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPESRVS QGKSEKA
Length:297
Mass (Da):33,429
Last modified:January 23, 2007 - v4
Checksum:iBDAE6EE4E47A5650
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti102 – 1021E → D.1 Publication
Corresponds to variant rs35156365 [ dbSNP | Ensembl ].
VAR_051799
Natural varianti228 – 2281E → G.
Corresponds to variant rs1049270 [ dbSNP | Ensembl ].
VAR_051800

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87292 mRNA. Translation: BAA13327.1.
CR456598 mRNA. Translation: CAG30484.1.
CR456998 mRNA. Translation: CAG33279.1.
AK091874 mRNA. Translation: BAG52433.1.
Z73420 Genomic DNA. Translation: CAA97762.1.
CH471095 Genomic DNA. Translation: EAW60132.1.
BC010148 mRNA. Translation: AAH10148.1.
CCDSiCCDS13938.1.
PIRiJC5286.
RefSeqiNP_001257412.1. NM_001270483.1.
NP_003303.2. NM_003312.5.
UniGeneiHs.474783.

Genome annotation databases

EnsembliENST00000249042; ENSP00000249042; ENSG00000128311.
ENST00000403892; ENSP00000385828; ENSG00000128311.
ENST00000622841; ENSP00000478739; ENSG00000128311.
GeneIDi7263.
KEGGihsa:7263.
UCSCiuc003aqg.4. human.

Polymorphism databases

DMDMi3122965.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87292 mRNA. Translation: BAA13327.1.
CR456598 mRNA. Translation: CAG30484.1.
CR456998 mRNA. Translation: CAG33279.1.
AK091874 mRNA. Translation: BAG52433.1.
Z73420 Genomic DNA. Translation: CAA97762.1.
CH471095 Genomic DNA. Translation: EAW60132.1.
BC010148 mRNA. Translation: AAH10148.1.
CCDSiCCDS13938.1.
PIRiJC5286.
RefSeqiNP_001257412.1. NM_001270483.1.
NP_003303.2. NM_003312.5.
UniGeneiHs.474783.

3D structure databases

ProteinModelPortaliQ16762.
SMRiQ16762. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113114. 13 interactions.
IntActiQ16762. 2 interactions.
STRINGi9606.ENSP00000249042.

PTM databases

PhosphoSiteiQ16762.

Polymorphism databases

DMDMi3122965.

2D gel databases

REPRODUCTION-2DPAGEIPI00216293.

Proteomic databases

MaxQBiQ16762.
PaxDbiQ16762.
PeptideAtlasiQ16762.
PRIDEiQ16762.

Protocols and materials databases

DNASUi7263.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249042; ENSP00000249042; ENSG00000128311.
ENST00000403892; ENSP00000385828; ENSG00000128311.
ENST00000622841; ENSP00000478739; ENSG00000128311.
GeneIDi7263.
KEGGihsa:7263.
UCSCiuc003aqg.4. human.

Organism-specific databases

CTDi7263.
GeneCardsiGC22M037408.
HGNCiHGNC:12388. TST.
HPAiCAB009546.
HPA003044.
HPA003643.
MIMi180370. gene.
neXtProtiNX_Q16762.
PharmGKBiPA37055.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2897.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiQ16762.
KOiK01011.
OMAiSRAQGRY.
OrthoDBiEOG72ZCGB.
PhylomeDBiQ16762.
TreeFamiTF315133.

Enzyme and pathway databases

ReactomeiREACT_116010. Sulfide oxidation to sulfate.

Miscellaneous databases

GeneWikiiTST_(gene).
GenomeRNAii7263.
NextBioi28395.
PROiQ16762.
SOURCEiSearch...

Gene expression databases

BgeeiQ16762.
CleanExiHS_TST.
ExpressionAtlasiQ16762. baseline and differential.
GenevestigatoriQ16762.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-102.
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8.
    Tissue: Platelet.
  9. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Mitochondrial enzyme rhodanese is essential for 5 S ribosomal RNA import into human mitochondria."
    Smirnov A., Comte C., Mager-Heckel A.M., Addis V., Krasheninnikov I.A., Martin R.P., Entelis N., Tarassov I.
    J. Biol. Chem. 285:30792-30803(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18."
    Smirnov A., Entelis N., Martin R.P., Tarassov I.
    Genes Dev. 25:1289-1305(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  13. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTHTR_HUMAN
AccessioniPrimary (citable) accession number: Q16762
Secondary accession number(s): B3KRM1, Q6IB06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 133 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.