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A8QCH0

- FEN1_BRUMA

UniProt

A8QCH0 - FEN1_BRUMA

Protein

Flap endonuclease 1

Gene

FEN1

Organism
Brugia malayi (Filarial nematode worm)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 1 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.UniRule annotation

    Cofactori

    Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi34 – 341Magnesium 1UniRule annotation
    Binding sitei47 – 471DNA substrateUniRule annotation
    Binding sitei70 – 701DNA substrateUniRule annotation
    Metal bindingi86 – 861Magnesium 1UniRule annotation
    Metal bindingi158 – 1581Magnesium 1UniRule annotation
    Binding sitei158 – 1581DNA substrateUniRule annotation
    Metal bindingi160 – 1601Magnesium 1UniRule annotation
    Metal bindingi179 – 1791Magnesium 2UniRule annotation
    Metal bindingi181 – 1811Magnesium 2UniRule annotation
    Binding sitei231 – 2311DNA substrateUniRule annotation
    Metal bindingi233 – 2331Magnesium 2UniRule annotation
    Binding sitei233 – 2331DNA substrateUniRule annotation

    GO - Molecular functioni

    1. 5'-3' exonuclease activity Source: UniProtKB-HAMAP
    2. 5'-flap endonuclease activity Source: UniProtKB-HAMAP
    3. DNA binding Source: UniProtKB-HAMAP
    4. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. base-excision repair Source: UniProtKB-HAMAP
    2. DNA replication, removal of RNA primer Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Endonuclease, Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Flap endonuclease 1UniRule annotation (EC:3.1.-.-UniRule annotation)
    Short name:
    FEN-1UniRule annotation
    Alternative name(s):
    Flap structure-specific endonuclease 1UniRule annotation
    Gene namesi
    Name:FEN1UniRule annotation
    ORF Names:Bm1_49605
    OrganismiBrugia malayi (Filarial nematode worm)
    Taxonomic identifieri6279 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeBrugia
    ProteomesiUP000006672: Unassembled WGS sequence

    Subcellular locationi

    Nucleusnucleolus UniRule annotation. Nucleusnucleoplasm UniRule annotation. Mitochondrion UniRule annotation
    Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.UniRule annotation

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. nucleolus Source: UniProtKB-SubCell
    3. nucleoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 378378Flap endonuclease 1PRO_0000403511Add
    BLAST

    Post-translational modificationi

    Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.UniRule annotation

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Interacts with PCNA. Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliA8QCH0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 104104N-domainAdd
    BLAST
    Regioni122 – 253132I-domainAdd
    BLAST
    Regioni336 – 3449Interaction with PCNAUniRule annotation

    Sequence similaritiesi

    Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.UniRule annotation

    Phylogenomic databases

    KOiK04799.

    Family and domain databases

    Gene3Di3.40.50.1010. 1 hit.
    HAMAPiMF_00614. Fen.
    InterProiIPR020045. 5-3_exonuclease_C.
    IPR023426. Flap_endonuc.
    IPR008918. HhH2.
    IPR029060. PIN_domain-like.
    IPR006086. XPG-I_dom.
    IPR019974. XPG_CS.
    IPR006085. XPG_DNA_repair_N.
    [Graphical view]
    PfamiPF00867. XPG_I. 1 hit.
    PF00752. XPG_N. 1 hit.
    [Graphical view]
    SMARTiSM00279. HhH2. 1 hit.
    SM00484. XPGI. 1 hit.
    SM00485. XPGN. 1 hit.
    [Graphical view]
    SUPFAMiSSF47807. SSF47807. 1 hit.
    SSF88723. SSF88723. 1 hit.
    PROSITEiPS00841. XPG_1. 1 hit.
    PS00842. XPG_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A8QCH0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGVKDLSKVI GDHSPNSIRL KEFKGYFGRK VAVDASMCLY QFLIAVRQDG    50
    SQLQTESGET TSHLLGMFYR TIRMIDNGIK PVYVFDGKPP QMKTSELEKR 100
    TERRTEAEKQ RNDAVELGDE TSVNKFEKRL VKVTKEQSEE AKRLVTLMGI 150
    PVLDAPCEAE AQCAALAKAG KVFATVSEDM DALTFGSPIL LRQMIASEAK 200
    KLPVKEMNLN QVLKDFGMNM GQFVDLCILL GCDYVSTIRG IGPKKAFELI 250
    KKYECIENVL ETINQTKYPI PQDWQYKEAR RLFLEPDVMN CENLELVWKE 300
    PDVEGIVQFL CVEKSFNEDR VRGSLTRMQK GRQAAQQARI DSFFSVSKVV 350
    TSETTKRKNE EKNNLKKRGP SLGKKAKK 378
    Length:378
    Mass (Da):42,844
    Last modified:January 15, 2008 - v1
    Checksum:i8E9DAD594F202030
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS239429 Genomic DNA. Translation: EDP30068.1.
    RefSeqiXP_001901388.1. XM_001901353.1.

    Genome annotation databases

    EnsemblMetazoaiBm13951; Bm13951; Bm13951.
    GeneIDi6104806.
    KEGGibmy:Bm1_49605.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS239429 Genomic DNA. Translation: EDP30068.1 .
    RefSeqi XP_001901388.1. XM_001901353.1.

    3D structure databases

    ProteinModelPortali A8QCH0.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai Bm13951 ; Bm13951 ; Bm13951 .
    GeneIDi 6104806.
    KEGGi bmy:Bm1_49605.

    Organism-specific databases

    CTDi 6104806.

    Phylogenomic databases

    KOi K04799.

    Family and domain databases

    Gene3Di 3.40.50.1010. 1 hit.
    HAMAPi MF_00614. Fen.
    InterProi IPR020045. 5-3_exonuclease_C.
    IPR023426. Flap_endonuc.
    IPR008918. HhH2.
    IPR029060. PIN_domain-like.
    IPR006086. XPG-I_dom.
    IPR019974. XPG_CS.
    IPR006085. XPG_DNA_repair_N.
    [Graphical view ]
    Pfami PF00867. XPG_I. 1 hit.
    PF00752. XPG_N. 1 hit.
    [Graphical view ]
    SMARTi SM00279. HhH2. 1 hit.
    SM00484. XPGI. 1 hit.
    SM00485. XPGN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47807. SSF47807. 1 hit.
    SSF88723. SSF88723. 1 hit.
    PROSITEi PS00841. XPG_1. 1 hit.
    PS00842. XPG_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Draft genome of the filarial nematode parasite Brugia malayi."
      Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E., Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T., Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.
      , Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M., Pop M., White O., Barton G.J., Carlow C.K.S., Crawford M.J., Daub J., Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F., Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W., Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M., McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J., Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E., Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G., Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B., Blaxter M.L., Scott A.L.
      Science 317:1756-1760(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiFEN1_BRUMA
    AccessioniPrimary (citable) accession number: A8QCH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2011
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 35 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3