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A8QCH0

- FEN1_BRUMA

UniProt

A8QCH0 - FEN1_BRUMA

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Protein
Flap endonuclease 1
Gene
FEN1, Bm1_49605
Organism
Brugia malayi (Filarial nematode worm)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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 By similarity.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 By similarity.

Sites

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

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

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 1 (EC:3.1.-.-)
Short name:
FEN-1
Alternative name(s):
Flap structure-specific endonuclease 1
Gene namesi
Name:FEN1
ORF Names:Bm1_49605
OrganismiBrugia malayi (Filarial nematode worm)
Taxonomic identifieri6279 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeBrugia
ProteomesiUP000006672: Unassembled WGS sequence

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

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

Post-translational modificationi

Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma By similarity.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 By similarity.

Structurei

3D structure databases

ProteinModelPortaliA8QCH0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 104104N-domainUniRule annotation
Add
BLAST
Regioni122 – 253132I-domainUniRule annotation
Add
BLAST
Regioni336 – 3449Interaction with PCNA By similarity

Sequence similaritiesi

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

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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: June 11, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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