Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A8QCH0

- FEN1_BRUMA

UniProt

A8QCH0 - FEN1_BRUMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Flap endonuclease 1

Gene

FEN1

Organism
Brugia malayi (Filarial nematode worm)
Status
Reviewed - Annotation score: 3 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.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: 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
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 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-HAMAP
  2. nucleus Source: UniProtKB-HAMAP
Complete GO annotation...

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

InParanoidiA8QCH0.
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

        10         20         30         40         50
MGVKDLSKVI GDHSPNSIRL KEFKGYFGRK VAVDASMCLY QFLIAVRQDG
60 70 80 90 100
SQLQTESGET TSHLLGMFYR TIRMIDNGIK PVYVFDGKPP QMKTSELEKR
110 120 130 140 150
TERRTEAEKQ RNDAVELGDE TSVNKFEKRL VKVTKEQSEE AKRLVTLMGI
160 170 180 190 200
PVLDAPCEAE AQCAALAKAG KVFATVSEDM DALTFGSPIL LRQMIASEAK
210 220 230 240 250
KLPVKEMNLN QVLKDFGMNM GQFVDLCILL GCDYVSTIRG IGPKKAFELI
260 270 280 290 300
KKYECIENVL ETINQTKYPI PQDWQYKEAR RLFLEPDVMN CENLELVWKE
310 320 330 340 350
PDVEGIVQFL CVEKSFNEDR VRGSLTRMQK GRQAAQQARI DSFFSVSKVV
360 370
TSETTKRKNE EKNNLKKRGP SLGKKAKK
Length:378
Mass (Da):42,844
Last modified:January 15, 2008 - v1
Checksum:i8E9DAD594F202030
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

InParanoidi A8QCH0.
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: November 26, 2014
This is version 37 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