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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene

DLST

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

Functioni

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activityi

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei424 – 4241Sequence Analysis
Active sitei428 – 4281Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. generation of precursor metabolites and energy Source: ProtInc
  4. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  5. lysine catabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
  7. tricarboxylic acid cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciMetaCyc:HS04324-MONOMER.
ReactomeiREACT_1298. Lysine catabolism.
REACT_1785. Citric acid cycle (TCA cycle).
UniPathwayiUPA00868; UER00840.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC:2.3.1.61)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name:
OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
E2K
Gene namesi
Name:DLST
Synonyms:DLTS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:2911. DLST.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. membrane Source: UniProtKB
  3. mitochondrial matrix Source: Reactome
  4. nucleus Source: UniProtKB
  5. oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27367.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6767Mitochondrion1 PublicationAdd
BLAST
Chaini68 – 453386Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101N6-lipoyllysinePROSITE-ProRule annotation
Modified residuei154 – 1541N6-acetyllysineBy similarity
Modified residuei267 – 2671N6-acetyllysineBy similarity
Modified residuei272 – 2721N6-acetyllysineBy similarity
Modified residuei273 – 2731N6-acetyllysineBy similarity
Modified residuei277 – 2771N6-acetyllysineBy similarity
Modified residuei307 – 3071N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP36957.
PaxDbiP36957.
PRIDEiP36957.

2D gel databases

OGPiP36957.
UCD-2DPAGEP36957.

PTM databases

PhosphoSiteiP36957.

Expressioni

Gene expression databases

BgeeiP36957.
CleanExiHS_DLST.
ExpressionAtlasiP36957. baseline and differential.
GenevestigatoriP36957.

Organism-specific databases

HPAiHPA003010.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

BioGridi108087. 27 interactions.
IntActiP36957. 21 interactions.
MINTiMINT-3014449.
STRINGi9606.ENSP00000335304.

Structurei

3D structure databases

ProteinModelPortaliP36957.
SMRiP36957. Positions 73-140, 220-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 14475Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
GeneTreeiENSGT00760000119373.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiP36957.
KOiK00658.
OMAiFEKKHAV.
PhylomeDBiP36957.
TreeFamiTF314164.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P36957-1) [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
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPNSRKVVI
60 70 80 90 100
NNSVFSVRFF RTTAVCKDDL VTVKTPAFAE SVTEGDVRWE KAVGDTVAED
110 120 130 140 150
EVVCEIETDK TSVQVPSPAN GVIEALLVPD GGKVEGGTPL FTLRKTGAAP
160 170 180 190 200
AKAKPAEAPA AAAPKAEPTA AAVPPPAAPI PTQMPPVPSP SQPPSGKPVS
210 220 230 240 250
AVKPTVAPPL AEPGAGKGLR SEHREKMNRM RQRIAQRLKE AQNTCAMLTT
260 270 280 290 300
FNEIDMSNIQ EMRARHKEAF LKKHNLKLGF MSAFVKASAF ALQEQPVVNA
310 320 330 340 350
VIDDTTKEVV YRDYIDISVA VATPRGLVVP VIRNVEAMNF ADIERTITEL
360 370 380 390 400
GEKARKNELA IEDMDGGTFT ISNGGVFGSL FGTPIINPPQ SAILGMHGIF
410 420 430 440 450
DRPVAIGGKV EVRPMMYVAL TYDHRLIDGR EAVTFLRKIK AAVEDPRVLL

LDL
Length:453
Mass (Da):48,755
Last modified:January 11, 2011 - v4
Checksum:iA30E8CC959106B8F
GO
Isoform 2 (identifier: P36957-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MLSRSRCVSRAFSRSLSAFQKGN → MTWLQSKPQRLQNLSQREMSGGR
     24-109: Missing.

Note: No experimental confirmation available.

Show »
Length:367
Mass (Da):39,553
Checksum:i3EEF7F48175530EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152RS → AP in BAA03871. (PubMed:8268217)Curated
Sequence conflicti14 – 152RS → AP in BAA05536. (PubMed:8076640)Curated
Sequence conflicti14 – 152RS → AP in AAB59629. 1 PublicationCurated
Sequence conflicti132 – 1321G → T in BAA03871. (PubMed:8268217)Curated
Sequence conflicti212 – 2121E → D in BAA03871. (PubMed:8268217)Curated
Sequence conflicti212 – 2121E → D in BAA05536. (PubMed:8076640)Curated
Sequence conflicti312 – 3121R → T in BAA05536. (PubMed:8076640)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti213 – 2131P → A.2 Publications
Corresponds to variant rs2853769 [ dbSNP | Ensembl ].
VAR_004976
Natural varianti384 – 3841P → T.
VAR_004977

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323MLSRS…FQKGN → MTWLQSKPQRLQNLSQREMS GGR in isoform 2. 1 PublicationVSP_056439Add
BLAST
Alternative sequencei24 – 10986Missing in isoform 2. 1 PublicationVSP_056440Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16373 mRNA. Translation: BAA03871.1.
D26535 Genomic DNA. Translation: BAA05536.1.
L37418 mRNA. Translation: AAB59629.1.
AK289414 mRNA. Translation: BAF82103.1.
AK299505 mRNA. Translation: BAH13054.1.
AC006530 Genomic DNA. Translation: AAD30181.1.
CH471061 Genomic DNA. Translation: EAW81199.1.
BC000302 mRNA. Translation: AAH00302.1.
BC001922 mRNA. Translation: AAH01922.1.
CCDSiCCDS9833.1. [P36957-1]
PIRiS39786. PN0673.
RefSeqiNP_001924.2. NM_001933.4. [P36957-1]
UniGeneiHs.525459.

Genome annotation databases

EnsembliENST00000334220; ENSP00000335304; ENSG00000119689. [P36957-1]
GeneIDi1743.
KEGGihsa:1743.
UCSCiuc001xqs.3. human. [P36957-1]

Polymorphism databases

DMDMi317373578.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16373 mRNA. Translation: BAA03871.1.
D26535 Genomic DNA. Translation: BAA05536.1.
L37418 mRNA. Translation: AAB59629.1.
AK289414 mRNA. Translation: BAF82103.1.
AK299505 mRNA. Translation: BAH13054.1.
AC006530 Genomic DNA. Translation: AAD30181.1.
CH471061 Genomic DNA. Translation: EAW81199.1.
BC000302 mRNA. Translation: AAH00302.1.
BC001922 mRNA. Translation: AAH01922.1.
CCDSiCCDS9833.1. [P36957-1]
PIRiS39786. PN0673.
RefSeqiNP_001924.2. NM_001933.4. [P36957-1]
UniGeneiHs.525459.

3D structure databases

ProteinModelPortaliP36957.
SMRiP36957. Positions 73-140, 220-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108087. 27 interactions.
IntActiP36957. 21 interactions.
MINTiMINT-3014449.
STRINGi9606.ENSP00000335304.

PTM databases

PhosphoSiteiP36957.

Polymorphism databases

DMDMi317373578.

2D gel databases

OGPiP36957.
UCD-2DPAGEP36957.

Proteomic databases

MaxQBiP36957.
PaxDbiP36957.
PRIDEiP36957.

Protocols and materials databases

DNASUi1743.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334220; ENSP00000335304; ENSG00000119689. [P36957-1]
GeneIDi1743.
KEGGihsa:1743.
UCSCiuc001xqs.3. human. [P36957-1]

Organism-specific databases

CTDi1743.
GeneCardsiGC14P075348.
H-InvDBHIX0131240.
HGNCiHGNC:2911. DLST.
HPAiHPA003010.
MIMi126063. gene.
neXtProtiNX_P36957.
PharmGKBiPA27367.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0508.
GeneTreeiENSGT00760000119373.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiP36957.
KOiK00658.
OMAiFEKKHAV.
PhylomeDBiP36957.
TreeFamiTF314164.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.
BioCyciMetaCyc:HS04324-MONOMER.
ReactomeiREACT_1298. Lysine catabolism.
REACT_1785. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiDLST. human.
GeneWikiiDLST.
GenomeRNAii1743.
NextBioi35479821.
PROiP36957.
SOURCEiSearch...

Gene expression databases

BgeeiP36957.
CleanExiHS_DLST.
ExpressionAtlasiP36957. baseline and differential.
GenevestigatoriP36957.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3."
    Nakano K., Matsuda S., Sakamoto T., Takase C., Nakagawa S., Ohta S., Ariyama T., Inazawa J., Abe T., Miyata T.
    Biochim. Biophys. Acta 1216:360-368(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-213.
  2. "Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex."
    Nakano K., Takase C., Sakamoto T., Nakagawa S., Inazawa J., Ohta S., Matuda S.
    Eur. J. Biochem. 224:179-189(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-213.
    Tissue: Peripheral blood.
  3. "Physical mapping and nucleotide sequence analysis of the human dihydrolipoamide succinyltransferase gene."
    Keryanov S., Liang Y., Rogaev E.I., Sherrington R., Tsuda T., Rogaeva E., Chi H., Crapper-Mclachlan D., Chumakov Y., Rommens J.M., St George-Hyslop P.H.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  8. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
    Xu G., Shin S.B., Jaffrey S.R.
    Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 68-89.
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiODO2_HUMAN
AccessioniPrimary (citable) accession number: P36957
Secondary accession number(s): B7Z5W8
, E7ESY5, Q7LDY7, Q9BQ32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 11, 2011
Last modified: January 7, 2015
This is version 164 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 14
    Human chromosome 14: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.