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Protein

DNA cross-link repair 1A protein

Gene

DCLRE1A

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

Functioni

May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons.1 Publication

GO - Molecular functioni

  • 5'-3' exodeoxyribonuclease activity Source: CACAO
  • damaged DNA binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA cross-link repair 1A protein
Alternative name(s):
SNM1 homolog A
Short name:
hSNM1
Short name:
hSNM1A
Gene namesi
Name:DCLRE1A
Synonyms:KIAA0086, SNM1, SNM1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:17660. DCLRE1A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi838 – 8381D → N: Impaired nuclear focus formation, reduced interaction with PIAS and increased sensitivity to cisplatin. 1 Publication
Mutagenesisi994 – 9941H → A: Impaired nuclear focus formation, reduced interaction with PIAS and increased sensitivity to cisplatin. 1 Publication

Organism-specific databases

PharmGKBiPA27174.

Polymorphism and mutation databases

DMDMi311033461.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10401040DNA cross-link repair 1A proteinPRO_0000209116Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki488 – 488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei590 – 5901PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6PJP8.
MaxQBiQ6PJP8.
PaxDbiQ6PJP8.
PRIDEiQ6PJP8.

PTM databases

iPTMnetiQ6PJP8.
PhosphoSiteiQ6PJP8.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, liver, pancreas, placenta and skeletal muscle.1 Publication

Inductioni

During mitosis. The mRNA encoding this protein contains an internal ribosome entry site (IRES) in its 5'-UTR. This 5'-UTR generally suppresses translation while specifically promoting expression during mitosis, when cap-dependent translation may be impaired.1 Publication

Gene expression databases

BgeeiQ6PJP8.
CleanExiHS_DCLRE1A.
GenevisibleiQ6PJP8. HS.

Organism-specific databases

HPAiHPA036907.

Interactioni

Subunit structurei

Binds constitutively to TP53BP1. Binds CDC27, which is itself a component of the anaphase promoting complex (APC). Binds PIAS1.

Protein-protein interaction databases

BioGridi115263. 6 interactions.
IntActiQ6PJP8. 1 interaction.
STRINGi9606.ENSP00000355185.

Structurei

Secondary structure

1
1040
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi703 – 7053Combined sources
Beta strandi710 – 7156Combined sources
Beta strandi718 – 7214Combined sources
Beta strandi727 – 7293Combined sources
Helixi735 – 7384Combined sources
Beta strandi749 – 7513Combined sources
Helixi753 – 76210Combined sources
Helixi767 – 7693Combined sources
Beta strandi770 – 7723Combined sources
Beta strandi779 – 7813Combined sources
Beta strandi784 – 7907Combined sources
Beta strandi792 – 7943Combined sources
Beta strandi798 – 8036Combined sources
Beta strandi809 – 8124Combined sources
Helixi820 – 8245Combined sources
Helixi826 – 8283Combined sources
Beta strandi834 – 8374Combined sources
Helixi851 – 86818Combined sources
Beta strandi872 – 88110Combined sources
Helixi884 – 89310Combined sources
Helixi902 – 9098Combined sources
Helixi916 – 9194Combined sources
Beta strandi920 – 9223Combined sources
Helixi924 – 9263Combined sources
Beta strandi928 – 9336Combined sources
Helixi934 – 9363Combined sources
Helixi939 – 9479Combined sources
Helixi949 – 9513Combined sources
Beta strandi955 – 9617Combined sources
Beta strandi979 – 9813Combined sources
Beta strandi984 – 9896Combined sources
Helixi997 – 100711Combined sources
Beta strandi1010 – 10145Combined sources
Helixi1021 – 103818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B87X-ray2.16A676-1040[»]
5AHRX-ray2.19A700-1040[»]
ProteinModelPortaliQ6PJP8.
SMRiQ6PJP8. Positions 696-1040.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Nuclear localization regionAdd
BLAST
Regioni396 – 614219Nuclear focus formationAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1361. Eukaryota.
COG1236. LUCA.
GeneTreeiENSGT00530000063183.
HOGENOMiHOG000168450.
HOVERGENiHBG081418.
InParanoidiQ6PJP8.
KOiK15340.
OMAiPDGLLCT.
OrthoDBiEOG71VSSC.
PhylomeDBiQ6PJP8.
TreeFamiTF314510.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR011084. DRMBL.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF07522. DRMBL. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6PJP8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEDISEEDI WEYKSKRKPK RVDPNNGSKN ILKSVEKATD GKYQSKRSRN
60 70 80 90 100
RKRAAEAKEV KDHEVPLGNA GCQTSVASSQ NSSCGDGIQQ TQDKETTPGK
110 120 130 140 150
LCRTQKSQHV SPKIRPVYDG YCPNCQMPFS SLIGQTPRWH VFECLDSPPR
160 170 180 190 200
SETECPDGLL CTSTIPFHYK RYTHFLLAQS RAGDHPFSSP SPASGGSFSE
210 220 230 240 250
TKSGVLCSLE ERWSSYQNQT DNSVSNDPLL MTQYFKKSPS LTEASEKIST
260 270 280 290 300
HIQTSQQALQ FTDFVENDKL VGVALRLANN SEHINLPLPE NDFSDCEISY
310 320 330 340 350
SPLQSDEDTH DIDEKPDDSQ EQLFFTESSK DGSLEEDDDS CGFFKKRHGP
360 370 380 390 400
LLKDQDESCP KVNSFLTRDK YDEGLYRFNS LNDLSQPISQ NNESTLPYDL
410 420 430 440 450
ACTGGDFVLF PPALAGKLAA SVHQATKAKP DEPEFHSAQS NKQKQVIEES
460 470 480 490 500
SVYNQVSLPL VKSLMLKPFE SQVEGYLSSQ PTQNTIRKLS SENLNAKNNT
510 520 530 540 550
NSACFCRKAL EGVPVGKATI LNTENLSSTP APKYLKILPS GLKYNARHPS
560 570 580 590 600
TKVMKQMDIG VYFGLPPKRK EEKLLGESAL EGINLNPVPS PNQKRSSQCK
610 620 630 640 650
RKAEKSLSDL EFDASTLHES QLSVELSSER SQRQKKRCRK SNSLQEGACQ
660 670 680 690 700
KRSDHLINTE SEAVNLSKVK VFTKSAHGGL QRGNKKIPES SNVGGSRKKT
710 720 730 740 750
CPFYKKIPGT GFTVDAFQYG VVEGCTAYFL THFHSDHYAG LSKHFTFPVY
760 770 780 790 800
CSEITGNLLK NKLHVQEQYI HPLPLDTECI VNGVKVVLLD ANHCPGAVMI
810 820 830 840 850
LFYLPNGTVI LHTGDFRADP SMERSLLADQ KVHMLYLDTT YCSPEYTFPS
860 870 880 890 900
QQEVIRFAIN TAFEAVTLNP HALVVCGTYS IGKEKVFLAI ADVLGSKVGM
910 920 930 940 950
SQEKYKTLQC LNIPEINSLI TTDMCSSLVH LLPMMQINFK GLQSHLKKCG
960 970 980 990 1000
GKYNQILAFR PTGWTHSNKF TRIADVIPQT KGNISIYGIP YSEHSSYLEM
1010 1020 1030 1040
KRFVQWLKPQ KIIPTVNVGT WKSRSTMEKY FREWKLEAGY
Length:1,040
Mass (Da):116,400
Last modified:November 2, 2010 - v3
Checksum:i708FFA1F75451803
GO

Sequence cautioni

The sequence BAA07646.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581K → E.1 Publication
Corresponds to variant rs17235066 [ dbSNP | Ensembl ].
VAR_023286
Natural varianti59 – 591E → D.1 Publication
Corresponds to variant rs17228665 [ dbSNP | Ensembl ].
VAR_023287
Natural varianti71 – 711G → D.1 Publication
Corresponds to variant rs17228672 [ dbSNP | Ensembl ].
VAR_023288
Natural varianti287 – 2871P → L.1 Publication
Corresponds to variant rs17235094 [ dbSNP | Ensembl ].
VAR_023289
Natural varianti317 – 3171D → H.3 Publications
Corresponds to variant rs3750898 [ dbSNP | Ensembl ].
VAR_023290
Natural varianti582 – 5821G → W.1 Publication
Corresponds to variant rs17855759 [ dbSNP | Ensembl ].
VAR_030574
Natural varianti859 – 8591I → F.1 Publication
Corresponds to variant rs11196530 [ dbSNP | Ensembl ].
VAR_023291

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D42045 mRNA. Translation: BAA07646.2. Different initiation.
AY607842 Genomic DNA. Translation: AAT09762.1.
AL592546 Genomic DNA. Translation: CAI12637.1.
CH471066 Genomic DNA. Translation: EAW49489.1.
CH471066 Genomic DNA. Translation: EAW49490.1.
BC013124 mRNA. Translation: AAH13124.1.
BC062582 mRNA. Translation: AAH62582.1.
CCDSiCCDS7584.1.
RefSeqiNP_001258745.1. NM_001271816.1.
NP_055696.3. NM_014881.4.
XP_006718153.1. XM_006718090.1.
XP_011538731.1. XM_011540429.1.
UniGeneiHs.1560.
Hs.703616.

Genome annotation databases

EnsembliENST00000361384; ENSP00000355185; ENSG00000198924.
ENST00000369305; ENSP00000358311; ENSG00000198924.
GeneIDi9937.
KEGGihsa:9937.
UCSCiuc001law.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D42045 mRNA. Translation: BAA07646.2. Different initiation.
AY607842 Genomic DNA. Translation: AAT09762.1.
AL592546 Genomic DNA. Translation: CAI12637.1.
CH471066 Genomic DNA. Translation: EAW49489.1.
CH471066 Genomic DNA. Translation: EAW49490.1.
BC013124 mRNA. Translation: AAH13124.1.
BC062582 mRNA. Translation: AAH62582.1.
CCDSiCCDS7584.1.
RefSeqiNP_001258745.1. NM_001271816.1.
NP_055696.3. NM_014881.4.
XP_006718153.1. XM_006718090.1.
XP_011538731.1. XM_011540429.1.
UniGeneiHs.1560.
Hs.703616.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B87X-ray2.16A676-1040[»]
5AHRX-ray2.19A700-1040[»]
ProteinModelPortaliQ6PJP8.
SMRiQ6PJP8. Positions 696-1040.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115263. 6 interactions.
IntActiQ6PJP8. 1 interaction.
STRINGi9606.ENSP00000355185.

PTM databases

iPTMnetiQ6PJP8.
PhosphoSiteiQ6PJP8.

Polymorphism and mutation databases

DMDMi311033461.

Proteomic databases

EPDiQ6PJP8.
MaxQBiQ6PJP8.
PaxDbiQ6PJP8.
PRIDEiQ6PJP8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361384; ENSP00000355185; ENSG00000198924.
ENST00000369305; ENSP00000358311; ENSG00000198924.
GeneIDi9937.
KEGGihsa:9937.
UCSCiuc001law.4. human.

Organism-specific databases

CTDi9937.
GeneCardsiDCLRE1A.
HGNCiHGNC:17660. DCLRE1A.
HPAiHPA036907.
MIMi609682. gene.
neXtProtiNX_Q6PJP8.
PharmGKBiPA27174.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1361. Eukaryota.
COG1236. LUCA.
GeneTreeiENSGT00530000063183.
HOGENOMiHOG000168450.
HOVERGENiHBG081418.
InParanoidiQ6PJP8.
KOiK15340.
OMAiPDGLLCT.
OrthoDBiEOG71VSSC.
PhylomeDBiQ6PJP8.
TreeFamiTF314510.

Enzyme and pathway databases

ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.

Miscellaneous databases

ChiTaRSiDCLRE1A. human.
GeneWikiiDCLRE1A.
GenomeRNAii9937.
NextBioi37488.
PROiQ6PJP8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PJP8.
CleanExiHS_DCLRE1A.
GenevisibleiQ6PJP8. HS.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR011084. DRMBL.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF07522. DRMBL. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. NIEHS SNPs program
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-58; ASP-59; ASP-71; LEU-287; HIS-317 AND PHE-859.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-317.
  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], VARIANTS HIS-317 AND TRP-582.
    Tissue: Cervix and Lung.
  6. "Disruption of mouse SNM1 causes increased sensitivity to the DNA interstrand cross-linking agent mitomycin C."
    Dronkert M.L.G., de Wit J., Boeve M., Vasconcelos M.L., van Steeg H., Tan T.L.R., Hoeijmakers J.H.J., Kanaar R.
    Mol. Cell. Biol. 20:4553-4561(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Translation of hSNM1 is mediated by an internal ribosome entry site that upregulates expression during mitosis."
    Zhang X., Richie C., Legerski R.J.
    DNA Repair 1:379-390(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "hSnm1 colocalizes and physically associates with 53BP1 before and after DNA damage."
    Richie C.T., Peterson C., Lu T., Hittelman W.N., Carpenter P.B., Legerski R.J.
    Mol. Cell. Biol. 22:8635-8647(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TP53BP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Deficiency in SNM1 abolishes an early mitotic checkpoint induced by spindle stress."
    Akhter S., Richie C.T., Deng J.M., Brey E., Zhang X., Patrick C. Jr., Behringer R.R., Legerski R.J.
    Mol. Cell. Biol. 24:10448-10455(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC27.
  10. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PIAS1, MUTAGENESIS OF ASP-838 AND HIS-994.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDCR1A_HUMAN
AccessioniPrimary (citable) accession number: Q6PJP8
Secondary accession number(s): D3DRC1
, Q14701, Q6P5Y3, Q6PKL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 2, 2010
Last modified: May 11, 2016
This is version 115 of the entry and version 3 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 10
    Human chromosome 10: 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.