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Protein

DNA repair protein RAD5

Gene

RAD5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable helicase, member of the UBC2/RAD6 epistasis group. Functions with the DNA repair protein RAD18 in error-free postreplication DNA repair. Involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. Seems to be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs. Recruits the UBC13-MMS2 dimer to chromatin for DNA repair.8 Publications

Cofactori

Kineticsi

  1. KM=525 µM for ATP

    pH dependencei

    Optimum pH is 7.0. for ATPase activity.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi532 – 5398ATPPROSITE-ProRule annotation
    Zinc fingeri914 – 96148RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • DNA-dependent ATPase activity Source: SGD
    • four-way junction DNA binding Source: SGD
    • four-way junction helicase activity Source: SGD
    • Y-form DNA binding Source: SGD
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • DNA duplex unwinding Source: GOC
    • double-strand break repair Source: SGD
    • error-prone translesion synthesis Source: SGD
    • free ubiquitin chain polymerization Source: SGD
    • postreplication repair Source: SGD
    • protein polyubiquitination Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32191-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein RAD5 (EC:3.6.4.-)
    Alternative name(s):
    Radiation sensitivity protein 5
    Revertibility protein 2
    Gene namesi
    Name:RAD5
    Synonyms:REV2, SNM2
    Ordered Locus Names:YLR032W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome XII

    Organism-specific databases

    CYGDiYLR032w.
    EuPathDBiFungiDB:YLR032W.
    SGDiS000004022. RAD5.

    Subcellular locationi

    GO - Cellular componenti

    • chromosome, telomeric region Source: SGD
    • cytoplasm Source: UniProtKB-SubCell
    • nuclear chromatin Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi538 – 5392KT → AA: Increased sensitivity toward ionizing radiation. 1 Publication
    Mutagenesisi914 – 9141C → S: Abolishes interaction with UBC13. 2 Publications
    Mutagenesisi916 – 9161I → A: Abolishes interaction with UBC13. 1 Publication
    Mutagenesisi944 – 9441Y → A: Abolishes interaction with UBC13. 1 Publication
    Mutagenesisi959 – 9591N → A: Abolishes interaction with UBC13. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 11691168DNA repair protein RAD5PRO_0000056130Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei20 – 201Phosphoserine1 Publication
    Modified residuei23 – 231Phosphoserine1 Publication
    Modified residuei129 – 1291Phosphoserine1 Publication
    Modified residuei130 – 1301Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP32849.
    PaxDbiP32849.
    PeptideAtlasiP32849.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with POL30, RAD18, UBC9 and UBC13.4 Publications

    Protein-protein interaction databases

    BioGridi31306. 162 interactions.
    DIPiDIP-5830N.
    IntActiP32849. 3 interactions.
    MINTiMINT-2784640.
    STRINGi4932.YLR032W.

    Structurei

    3D structure databases

    ProteinModelPortaliP32849.
    SMRiP32849. Positions 527-900, 909-1142.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini519 – 730212Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini995 – 1165171Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi681 – 6844DEGH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi42 – 6019Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi303 – 31513Arg/Lys-rich (basic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the SNF2/RAD54 helicase family.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri914 – 96148RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0553.
    GeneTreeiENSGT00790000123060.
    HOGENOMiHOG000040492.
    InParanoidiP32849.
    KOiK15505.
    OMAiKHGLSWM.
    OrthoDBiEOG7PCJR9.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    3.40.50.300. 4 hits.
    InterProiIPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR014905. HIRAN.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF08797. HIRAN. 1 hit.
    PF00176. SNF2_N. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00910. HIRAN. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P32849-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSHIEQEERK RFFNDDLDTS ETSLNFKSEN KESFLFANSH NDDDDDVVVS
    60 70 80 90 100
    VSDTTEGEGD RSIVPVRREI EEEGQNQFIT ELLRIIPEMP KDLVMELNEK
    110 120 130 140 150
    FGSQEEGLSL ALSHYFDHNS GTSISKIPSS PNQLNTLSDT SNSTLSPSSF
    160 170 180 190 200
    HPKRRRIYGF RNQTRLEDKV TWKRFIGALQ VTGMATRPTV RPLKYGSQMK
    210 220 230 240 250
    LKRSSEEISA TKVYDSRGRK KASMASLVRI FDIQYDREIG RVSEDIAQIL
    260 270 280 290 300
    YPLLSSHEIS FEVTLIFCDN KRLSIGDSFI LQLDCFLTSL IFEERNDGES
    310 320 330 340 350
    LMKRRRTEGG NKREKDNGNF GRTLTETDEE LESRSKRLAL LKLFDKLRLK
    360 370 380 390 400
    PILDEQKALE KHKIELNSDP EIIDLDNDEI CSNQVTEVHN NLRDTQHEEE
    410 420 430 440 450
    TMNLNQLKTF YKAAQSSESL KSLPETEPSR DVFKLELRNY QKQGLTWMLR
    460 470 480 490 500
    REQEFAKAAS DGEASETGAN MINPLWKQFK WPNDMSWAAQ NLQQDHVNVE
    510 520 530 540 550
    DGIFFYANLH SGEFSLAKPI LKTMIKGGIL SDEMGLGKTV AAYSLVLSCP
    560 570 580 590 600
    HDSDVVDKKL FDIENTAVSD NLPSTWQDNK KPYASKTTLI VVPMSLLTQW
    610 620 630 640 650
    SNEFTKANNS PDMYHEVYYG GNVSSLKTLL TKTKTPPTVV LTTYGIVQNE
    660 670 680 690 700
    WTKHSKGRMT DEDVNISSGL FSVNFYRIII DEGHNIRNRT TVTSKAVMAL
    710 720 730 740 750
    QGKCKWVLTG TPIINRLDDL YSLVKFLELD PWRQINYWKT FVSTPFESKN
    760 770 780 790 800
    YKQAFDVVNA ILEPVLLRRT KQMKDKDGKP LVELPPKEVV IKRLPFSKSQ
    810 820 830 840 850
    DLLYKFLLDK AEVSVKSGIA RGDLLKKYST ILVHILRLRQ VCCHPGLIGS
    860 870 880 890 900
    QDENDEDLSK NNKLVTEQTV ELDSLMRVVS ERFDNSFSKE ELDAMIQRLK
    910 920 930 940 950
    VKYPDNKSFQ SLECSICTTE PMDLDKALFT ECGHSFCEKC LFEYIEFQNS
    960 970 980 990 1000
    KNLGLKCPNC RNQIDACRLL ALVQTNSNSK NLEFKPYSPA SKSSKITALL
    1010 1020 1030 1040 1050
    KELQLLQDSS AGEQVVIFSQ FSTYLDILEK ELTHTFSKDV AKIYKFDGRL
    1060 1070 1080 1090 1100
    SLKERTSVLA DFAVKDYSRQ KILLLSLKAG GVGLNLTCAS HAYMMDPWWS
    1110 1120 1130 1140 1150
    PSMEDQAIDR LHRIGQTNSV KVMRFIIQDS IEEKMLRIQE KKRTIGEAMD
    1160
    TDEDERRKRR IEEIQMLFE
    Length:1,169
    Mass (Da):134,002
    Last modified:October 1, 1993 - v1
    Checksum:i226B720097433EE2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti478 – 4781Q → R in AAB23590 (PubMed:1394508).Curated
    Sequence conflicti635 – 6351T → N in AAB23590 (PubMed:1394508).Curated
    Sequence conflicti846 – 8461G → S in AAB23590 (PubMed:1394508).Curated
    Sequence conflicti898 – 8981R → S in AAB23590 (PubMed:1394508).Curated
    Sequence conflicti973 – 9731V → A in AAB23590 (PubMed:1394508).Curated
    Sequence conflicti1063 – 10631A → R in AAB23590 (PubMed:1394508).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M96644 Genomic DNA. Translation: AAA34951.1.
    Z73204 Genomic DNA. Translation: CAA97556.1.
    S46103 Genomic DNA. Translation: AAB23590.1.
    BK006945 Genomic DNA. Translation: DAA09350.1.
    PIRiS64859.
    RefSeqiNP_013132.1. NM_001181919.1.

    Genome annotation databases

    EnsemblFungiiYLR032W; YLR032W; YLR032W.
    GeneIDi850719.
    KEGGisce:YLR032W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M96644 Genomic DNA. Translation: AAA34951.1.
    Z73204 Genomic DNA. Translation: CAA97556.1.
    S46103 Genomic DNA. Translation: AAB23590.1.
    BK006945 Genomic DNA. Translation: DAA09350.1.
    PIRiS64859.
    RefSeqiNP_013132.1. NM_001181919.1.

    3D structure databases

    ProteinModelPortaliP32849.
    SMRiP32849. Positions 527-900, 909-1142.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31306. 162 interactions.
    DIPiDIP-5830N.
    IntActiP32849. 3 interactions.
    MINTiMINT-2784640.
    STRINGi4932.YLR032W.

    Proteomic databases

    MaxQBiP32849.
    PaxDbiP32849.
    PeptideAtlasiP32849.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYLR032W; YLR032W; YLR032W.
    GeneIDi850719.
    KEGGisce:YLR032W.

    Organism-specific databases

    CYGDiYLR032w.
    EuPathDBiFungiDB:YLR032W.
    SGDiS000004022. RAD5.

    Phylogenomic databases

    eggNOGiCOG0553.
    GeneTreeiENSGT00790000123060.
    HOGENOMiHOG000040492.
    InParanoidiP32849.
    KOiK15505.
    OMAiKHGLSWM.
    OrthoDBiEOG7PCJR9.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32191-MONOMER.

    Miscellaneous databases

    NextBioi966793.
    PROiP32849.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    3.40.50.300. 4 hits.
    InterProiIPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR014905. HIRAN.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF08797. HIRAN. 1 hit.
    PF00176. SNF2_N. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00910. HIRAN. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Saccharomyces cerevisiae RAD5-encoded DNA repair protein contains DNA helicase and zinc-binding sequence motifs and affects the stability of simple repetitive sequences in the genome."
      Johnson R.E., Henderson S.T., Petes T.D., Prakash S., Bankmann M., Prakash L.
      Mol. Cell. Biol. 12:3807-3818(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "The REV2 gene of Saccharomyces cerevisiae: cloning and DNA sequence."
      Ahne F., Baur M., Eckardt-Schupp F.
      Curr. Genet. 22:277-282(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-1063.
    5. "Yeast DNA repair protein RAD5 that promotes instability of simple repetitive sequences is a DNA-dependent ATPase."
      Johnson R.E., Prakash S., Prakash L.
      J. Biol. Chem. 269:28259-28262(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "The RAD5 gene product is involved in the avoidance of non-homologous end-joining of DNA double strand breaks in the yeast Saccharomyces cerevisiae."
      Ahne F., Ja B., Eckardt-Schupp F.
      Nucleic Acids Res. 25:743-749(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair."
      Ulrich H.D., Jentsch S.
      EMBO J. 19:3388-3397(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-914, SUBUNIT, INTERACTION WITH RAD18 AND UBC13.
    8. "The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and two error-free postreplication repair pathways."
      Xiao W., Chow B.L., Broomfield S., Hanna M.
      Genetics 155:1633-1641(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae."
      Torres-Ramos C.A., Prakash S., Prakash L.
      Mol. Cell. Biol. 22:2419-2426(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO."
      Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.
      Nature 419:135-141(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH POL30 AND UBC9.
    11. "Protein-protein interactions within an E2-RING finger complex. Implications for ubiquitin-dependent DNA damage repair."
      Ulrich H.D.
      J. Biol. Chem. 278:7051-7058(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH UBC13, MUTAGENESIS OF CYS-914; ILE-916; TYR-944 AND ASN-959.
    12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. "The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes to DNA double-strand break repair in a ubiquitin-independent manner."
      Chen S., Davies A.A., Sagan D., Ulrich H.D.
      Nucleic Acids Res. 33:5878-5886(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH POL30; RAD18 AND UBC13, MUTAGENESIS OF 538-LYS-THR-539.
    15. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-129 AND SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRAD5_YEAST
    AccessioniPrimary (citable) accession number: P32849
    Secondary accession number(s): D6VY34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: June 24, 2015
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1520 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    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.