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A8QCH0 (FEN1_BRUMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Flap endonuclease 1

Short name=FEN-1
EC=3.1.-.-
Alternative name(s):
Flap structure-specific endonuclease 1
Gene names
Name:FEN1
ORF Names:Bm1_49605
OrganismBrugia malayi (Filarial nematode worm) [Complete proteome]
Taxonomic identifier6279 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeBrugia

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_03140

Cofactor

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.

Subunit structure

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.

Subcellular location

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. HAMAP-Rule MF_03140

Post-translational modification

Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma By similarity. HAMAP-Rule MF_03140

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Flap endonuclease 1 HAMAP-Rule MF_03140
PRO_0000403511

Regions

Region1 – 104104N-domain HAMAP-Rule MF_03140
Region122 – 253132I-domain HAMAP-Rule MF_03140
Region336 – 3449Interaction with PCNA By similarity

Sites

Metal binding341Magnesium 1 By similarity
Metal binding861Magnesium 1 By similarity
Metal binding1581Magnesium 1 By similarity
Metal binding1601Magnesium 1 By similarity
Metal binding1791Magnesium 2 By similarity
Metal binding1811Magnesium 2 By similarity
Metal binding2331Magnesium 2 By similarity
Binding site471DNA substrate By similarity
Binding site701DNA substrate By similarity
Binding site1581DNA substrate By similarity
Binding site2311DNA substrate By similarity
Binding site2331DNA substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A8QCH0 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 8E9DAD594F202030

FASTA37842,844
        10         20         30         40         50         60 
MGVKDLSKVI GDHSPNSIRL KEFKGYFGRK VAVDASMCLY QFLIAVRQDG SQLQTESGET 

        70         80         90        100        110        120 
TSHLLGMFYR TIRMIDNGIK PVYVFDGKPP QMKTSELEKR TERRTEAEKQ RNDAVELGDE 

       130        140        150        160        170        180 
TSVNKFEKRL VKVTKEQSEE AKRLVTLMGI PVLDAPCEAE AQCAALAKAG KVFATVSEDM 

       190        200        210        220        230        240 
DALTFGSPIL LRQMIASEAK KLPVKEMNLN QVLKDFGMNM GQFVDLCILL GCDYVSTIRG 

       250        260        270        280        290        300 
IGPKKAFELI KKYECIENVL ETINQTKYPI PQDWQYKEAR RLFLEPDVMN CENLELVWKE 

       310        320        330        340        350        360 
PDVEGIVQFL CVEKSFNEDR VRGSLTRMQK GRQAAQQARI DSFFSVSKVV TSETTKRKNE 

       370 
EKNNLKKRGP SLGKKAKK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS239429 Genomic DNA. Translation: EDP30068.1.
RefSeqXP_001901388.1. XM_001901353.1.

3D structure databases

ProteinModelPortalA8QCH0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaBm13951; Bm13951; Bm13951.
GeneID6104806.
KEGGbmy:Bm1_49605.

Organism-specific databases

CTD6104806.

Phylogenomic databases

KOK04799.

Family and domain databases

Gene3D3.40.50.1010. 1 hit.
HAMAPMF_00614. Fen.
InterProIPR020045. 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]
PfamPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
SMARTSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMSSF47807. SSF47807. 1 hit.
SSF88723. SSF88723. 1 hit.
PROSITEPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFEN1_BRUMA
AccessionPrimary (citable) accession number: A8QCH0
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families