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Protein

Selenocysteine lyase

Gene

SCLY

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

Functioni

Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium.By similarity

Catalytic activityi

L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei388 – 3881S-selanylcysteine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-HSA-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.

Names & Taxonomyi

Protein namesi
Recommended name:
Selenocysteine lyase (EC:4.4.1.16)
Short name:
hSCL
Gene namesi
Name:SCLY
Synonyms:SCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:18161. SCLY.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134979359.

Polymorphism and mutation databases

BioMutaiSCLY.
DMDMi527504087.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Selenocysteine lyasePRO_0000317012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei129 – 1291PhosphoserineCombined sources
Modified residuei259 – 2591N6-(pyridoxal phosphate)lysine

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ96I15.
MaxQBiQ96I15.
PaxDbiQ96I15.
PRIDEiQ96I15.

PTM databases

iPTMnetiQ96I15.
PhosphoSiteiQ96I15.

Expressioni

Inductioni

Up-regulated in acute glomerulonephritis. Regulated by JUN/AP-1.1 Publication

Gene expression databases

BgeeiQ96I15.
CleanExiHS_SCLY.
ExpressionAtlasiQ96I15. baseline and differential.
GenevisibleiQ96I15. HS.

Organism-specific databases

HPAiHPA020190.
HPA055760.
HPA062822.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF2IPQ9NYB02EBI-2823066,EBI-750109

Protein-protein interaction databases

BioGridi119599. 32 interactions.
IntActiQ96I15. 10 interactions.
STRINGi9606.ENSP00000254663.

Structurei

Secondary structure

1
445
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni36 – 383Combined sources
Helixi44 – 5613Combined sources
Helixi66 – 8520Combined sources
Helixi90 – 923Combined sources
Beta strandi93 – 975Combined sources
Helixi99 – 11820Combined sources
Beta strandi137 – 1415Combined sources
Helixi146 – 15712Combined sources
Beta strandi162 – 1665Combined sources
Turni170 – 1723Combined sources
Helixi177 – 1826Combined sources
Beta strandi188 – 1925Combined sources
Turni198 – 2003Combined sources
Helixi206 – 22217Combined sources
Beta strandi229 – 2335Combined sources
Turni235 – 2406Combined sources
Helixi245 – 2484Combined sources
Beta strandi251 – 2566Combined sources
Helixi257 – 2593Combined sources
Beta strandi266 – 2705Combined sources
Turni274 – 2763Combined sources
Helixi289 – 2913Combined sources
Helixi299 – 33840Combined sources
Turni340 – 3423Combined sources
Beta strandi343 – 3453Combined sources
Beta strandi358 – 3636Combined sources
Helixi370 – 3767Combined sources
Beta strandi378 – 3814Combined sources
Beta strandi383 – 3853Combined sources
Helixi387 – 3893Combined sources
Helixi398 – 4025Combined sources
Helixi407 – 4104Combined sources
Beta strandi413 – 4175Combined sources
Helixi424 – 44219Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GZCX-ray2.10A/B8-445[»]
3GZDX-ray1.80A/B/C/D8-445[»]
ProteinModelPortaliQ96I15.
SMRiQ96I15. Positions 29-444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96I15.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1549. Eukaryota.
COG1104. LUCA.
GeneTreeiENSGT00530000063513.
HOVERGENiHBG003708.
InParanoidiQ96I15.
KOiK01763.
OrthoDBiEOG7D85XM.
PhylomeDBiQ96I15.
TreeFamiTF313550.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR016454. Cysteine_dSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF005572. NifS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q96I15-1) [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
MEAAVAPGRD APAPAASQPS GCGKHNSPER KVYMDYNATT PLEPEVIQAM
60 70 80 90 100
TKAMWEAWGN PSSPYSAGRK AKDIINAARE SLAKMIGGKP QDIIFTSGGT
110 120 130 140 150
ESNNLVIHSV VKHFHANQTS KGHTGGHHSP VKGAKPHFIT SSVEHDSIRL
160 170 180 190 200
PLEHLVEEQV AAVTFVPVSK VSGQAEVDDI LAAVRPTTRL VTIMLANNET
210 220 230 240 250
GIVMPVPEIS QRIKALNQER VAAGLPPILV HTDAAQALGK QRVDVEDLGV
260 270 280 290 300
DFLTIVGHKF YGPRIGALYI RGLGEFTPLY PMLFGGGQER NFRPGTENTP
310 320 330 340 350
MIAGLGKAAE LVTQNCEAYE AHMRDVRDYL EERLEAEFGQ KRIHLNSQFP
360 370 380 390 400
GTQRLPNTCN FSIRGPRLQG HVVLAQCRVL MASVGAACHS DHGDQPSPVL
410 420 430 440
LSYGVPFDVA RNALRLSVGR STTRAEVDLV VQDLKQAVAQ LEDQA
Length:445
Mass (Da):48,149
Last modified:July 24, 2013 - v4
Checksum:iD26F3FCFB8B165D2
GO
Isoform 2 (identifier: Q96I15-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     308-445: AAELVTQNCE...QAVAQLEDQA → VSPGELEEMS

Show »
Length:317
Mass (Da):33,957
Checksum:iA831471CE76E5B11
GO

Sequence cautioni

The sequence BAA91659.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → MPGSSGAGM in EAW71139 (Ref. 3) Curated
Sequence conflicti42 – 421L → V in AAF36816 (PubMed:10692412).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521K → E.
Corresponds to variant rs7597367 [ dbSNP | Ensembl ].
VAR_038464
Natural varianti175 – 1751A → T.1 Publication
Corresponds to variant rs3210400 [ dbSNP | Ensembl ].
VAR_038465
Natural varianti276 – 2761F → S.
Corresponds to variant rs35637307 [ dbSNP | Ensembl ].
VAR_038466

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei308 – 445138AAELV…LEDQA → VSPGELEEMS in isoform 2. 1 PublicationVSP_030854Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF175767 mRNA. Translation: AAF36816.1.
AC016757 Genomic DNA. Translation: AAY24333.1.
AC016776 Genomic DNA. Translation: AAY24221.1.
CH471063 Genomic DNA. Translation: EAW71139.1.
BC000586 mRNA. Translation: AAH00586.2.
BC007891 mRNA. Translation: AAH07891.1.
AK001377 mRNA. Translation: BAA91659.1. Different initiation.
RefSeqiNP_057594.4. NM_016510.5.
UniGeneiHs.731909.

Genome annotation databases

EnsembliENST00000409736; ENSP00000387162; ENSG00000132330. [Q96I15-2]
GeneIDi51540.
KEGGihsa:51540.
UCSCiuc061uct.1. human. [Q96I15-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF175767 mRNA. Translation: AAF36816.1.
AC016757 Genomic DNA. Translation: AAY24333.1.
AC016776 Genomic DNA. Translation: AAY24221.1.
CH471063 Genomic DNA. Translation: EAW71139.1.
BC000586 mRNA. Translation: AAH00586.2.
BC007891 mRNA. Translation: AAH07891.1.
AK001377 mRNA. Translation: BAA91659.1. Different initiation.
RefSeqiNP_057594.4. NM_016510.5.
UniGeneiHs.731909.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GZCX-ray2.10A/B8-445[»]
3GZDX-ray1.80A/B/C/D8-445[»]
ProteinModelPortaliQ96I15.
SMRiQ96I15. Positions 29-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119599. 32 interactions.
IntActiQ96I15. 10 interactions.
STRINGi9606.ENSP00000254663.

PTM databases

iPTMnetiQ96I15.
PhosphoSiteiQ96I15.

Polymorphism and mutation databases

BioMutaiSCLY.
DMDMi527504087.

Proteomic databases

EPDiQ96I15.
MaxQBiQ96I15.
PaxDbiQ96I15.
PRIDEiQ96I15.

Protocols and materials databases

DNASUi51540.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000409736; ENSP00000387162; ENSG00000132330. [Q96I15-2]
GeneIDi51540.
KEGGihsa:51540.
UCSCiuc061uct.1. human. [Q96I15-1]

Organism-specific databases

CTDi51540.
GeneCardsiSCLY.
H-InvDBHIX0114427.
HGNCiHGNC:18161. SCLY.
HPAiHPA020190.
HPA055760.
HPA062822.
MIMi611056. gene.
neXtProtiNX_Q96I15.
PharmGKBiPA134979359.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1549. Eukaryota.
COG1104. LUCA.
GeneTreeiENSGT00530000063513.
HOVERGENiHBG003708.
InParanoidiQ96I15.
KOiK01763.
OrthoDBiEOG7D85XM.
PhylomeDBiQ96I15.
TreeFamiTF313550.

Enzyme and pathway databases

ReactomeiR-HSA-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.

Miscellaneous databases

ChiTaRSiSCLY. human.
EvolutionaryTraceiQ96I15.
GenomeRNAii51540.
NextBioi35534783.
PROiQ96I15.
SOURCEiSearch...

Gene expression databases

BgeeiQ96I15.
CleanExiHS_SCLY.
ExpressionAtlasiQ96I15. baseline and differential.
GenevisibleiQ96I15. HS.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR016454. Cysteine_dSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF005572. NifS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis."
    Mihara H., Kurihara T., Watanabe T., Yoshimura T., Esaki N.
    J. Biol. Chem. 275:6195-6200(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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), VARIANT THR-175.
    Tissue: Brain.
  5. "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] OF 189-445.
    Tissue: Teratocarcinoma.
  6. "Enhanced expression of selenocysteine lyase in acute glomerulonephritis and its regulation by AP-1."
    Jafari C., Panzer U., Steinmetz O.M., Zahner G., Stahl R.A., Harendza S.
    Cell. Mol. Biol. Lett. 11:424-437(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY JUN.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [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. "Structure of human selenocysteine lyase."
    Structural genomics consortium (SGC)
    Submitted (JUL-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-445 IN COMPLEX WITH PYRIDOXAL PHOSPHATE.

Entry informationi

Entry nameiSCLY_HUMAN
AccessioniPrimary (citable) accession number: Q96I15
Secondary accession number(s): B9A068
, J3KN06, Q53SN1, Q53SN8, Q7L670, Q9NVT7, Q9NZR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 24, 2013
Last modified: April 13, 2016
This is version 126 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.