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O27670 (FEN_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:fen
Ordered Locus Names:MTH_1633
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter ›

Protein attributes

Sequence length328 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. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA By similarity. HAMAP-Rule MF_00614

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. PCNA stimulates the nuclease activity without altering cleavage specificity By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328Flap endonuclease 1 HAMAP-Rule MF_00614
PRO_0000154056

Regions

Region1 – 9898N-domain HAMAP-Rule MF_00614
Region116 – 247132I-domain HAMAP-Rule MF_00614
Region320 – 3289Interaction with PCNA By similarity

Sites

Metal binding271Magnesium 1 By similarity
Metal binding801Magnesium 1 By similarity
Metal binding1521Magnesium 1 By similarity
Metal binding1541Magnesium 1 By similarity
Metal binding1731Magnesium 2 By similarity
Metal binding1751Magnesium 2 By similarity
Metal binding2261Magnesium 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O27670 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: CAC1C6046561FDE4

FASTA32837,170
        10         20         30         40         50         60 
MGVKLRDVVS PRRIRLEDLR GRTVAVDAAN TLYQFLSSIR QRDGTPLMDS RGRVTSHLSG 

        70         80         90        100        110        120 
ILYRTAAVME REIRVIYVFD GRSHHLKGET VSRRADIRKK SEVEWKRALE EGDIDRAKKY 

       130        140        150        160        170        180 
AVRSSRMSSE ILESSKRLLE LLGIPYVQAP GEGEAQASYM VKMGDAWAVA SQDYDCLLFG 

       190        200        210        220        230        240 
APRVVRNLTL SGKLEDPEII ELESTLRELS ISHTQLVDMA LLVGTDFNEG VKGIGARRGL 

       250        260        270        280        290        300 
KLIREKGDIF KVIRDLEADI GGDPQVLRRI FLEPEVSEDY EIRWRKPDVE GVIEFLCTEH 

       310        320 
GFSEDRVRAA LKKFEGASST QKSLEDWF

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000666 Genomic DNA. Translation: AAB86106.1.
PIRC69085.
RefSeqNP_276745.1. NC_000916.1.

3D structure databases

ProteinModelPortalO27670.
ModBaseSearch...

Protein-protein interaction databases

STRING187420.MTH1633.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB86106; AAB86106; MTH_1633.
GeneID1470718.
KEGGmth:MTH1633.

Phylogenomic databases

eggNOGCOG0258.
KOK04799.
OMADYDSLLF.
ProtClustDBPRK03980.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-1635-MONOMER.

Family and domain databases

HAMAPMF_00614. Fen.
InterProIPR020045. 5-3_exonuclease_C.
IPR023426. Flap_endonuc.
IPR019973. Flap_structure-sp_endonuc_arc.
IPR008918. HhH2.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PANTHERPTHR11081. PTHR11081. 1 hit.
PfamPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSPR00853. XPGRADSUPER.
SMARTSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMSSF47807. 5_3_exo_C. 1 hit.
TIGRFAMsTIGR03674. fen_arch. 1 hit.
PROSITEPS00841. XPG_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFEN_METTH
AccessionPrimary (citable) accession number: O27670
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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