| Tag | Content |
|---|
| CPLM ID | CPLM-031804 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Flap endonuclease 1 |
Protein Synonyms/Alias | FEN-1; Flap structure-specific endonuclease 1 |
Gene Name | FEN1 |
Gene Synonyms/Alias | TGME49_051620; TGVEG_000730 |
Created Date | July 27, 2013 |
Organism | Toxoplasma gondii |
NCBI Taxa ID | 5811 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 8 | MGIKGLGKFVGDFAP | acetylation | [1] |
|
Reference | [1] Lysine acetylation is widespread on proteins of diverse function and localization in the protozoan parasite Toxoplasma gondii. Jeffers V, Sullivan WJ Jr. Eukaryot Cell. 2012 Jun;11(6):735-42. [ PMID: 22544907] |
Functional Description | 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). |
Sequence Annotation | REGION 1 106 N-domain (By similarity).
REGION 124 263 I-domain (By similarity).
REGION 344 352 Interaction with PCNA (By similarity).
METAL 34 34 Magnesium 1 (By similarity).
METAL 88 88 Magnesium 1 (By similarity).
METAL 160 160 Magnesium 1 (By similarity).
METAL 162 162 Magnesium 1 (By similarity).
METAL 181 181 Magnesium 2 (By similarity).
METAL 183 183 Magnesium 2 (By similarity).
METAL 243 243 Magnesium 2 (By similarity).
BINDING 47 47 DNA substrate (By similarity).
BINDING 72 72 DNA substrate (By similarity).
BINDING 160 160 DNA substrate (By similarity).
BINDING 241 241 DNA substrate (By similarity).
BINDING 243 243 DNA substrate (By similarity). |
Keyword | Complete proteome; DNA damage; DNA repair; DNA replication; Endonuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding; Mitochondrion; Nuclease; Nucleus; Phosphoprotein; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 552 AA |
Protein Sequence | MGIKGLGKFV GDFAPRAIKR QEPGSFTGRV IAIDASMSLY QFMVAIRDGN SFGNFTNDAG 60
DCTSHIAGML NRAIRLLEQG VRPVYVFDGK PPELKSGELA KRRELRESAQ EAAEKAREEG 120
NVEELRKQIV RSVRVSKQHN EDVKRLLRLM GLPVVEAPCE AEAQCAELTK NRKVWATATE 180
DADALTFGAT RLIRNLTFGE RASGSGASAT ASGILVIDLP TLLEELQFSQ EQFIDFCILC 240
GCDYCGTLKG VGAKTAYSLV KEHGSIEKIL EVVDPEKVPD GFCFQEAREF FRHPEVTPAD 300
RVHVAWGEVD VDGLKAFLVQ ENQFNEQRVE NYITRLKKAR GKTAQTRLES FFGATVTKSS 360
SLMHKQLAEK QKELEKKKNR SVRGFAALKG KTAGARPAGA TAPKRAKTPE EEPAQKKAKR 420
SGPQAEGAEE AGAEAERESK KECERERLEK TETANAAKGE EKDAKGEPTA EKAEKVEVKE 480
EATEATADAA QDSGGQEKNS EGDEKTTSTD KGKRMSLLFS ENASVPSPRG ETNLFAEGEG 540
EENVAPSGTR AF 552 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. GO:0008409; F:5'-3' exonuclease activity; IEA:HAMAP. GO:0017108; F:5'-flap endonuclease activity; IEA:HAMAP. GO:0003677; F:DNA binding; IEA:HAMAP. GO:0000287; F:magnesium ion binding; IEA:HAMAP. GO:0006284; P:base-excision repair; IEA:HAMAP. GO:0043137; P:DNA replication, removal of RNA primer; IEA:HAMAP. GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC. |
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Pfam | |
SMART | |
PROSITE | |
PRINTS | |