P39750

PR
Gene name
rad2
Protein name
Flap endonuclease 1
Names
FEN-1, DNA repair protein rad2, Flap structure-specific endonuclease 1
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPAC3G6.06c
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

69-145 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P39750

Entry ID Method Resolution Chain Position Source
AF-P39750-F1 Predicted AlphaFoldDB

3 variants for P39750

Variant ID(s) Position Change Description Diseaes Association Provenance
I_5390469_T_C 115 T>A No Jeffares_SNPs
I_5390160_C_T 218 D>N No Jeffares_SNPs
I_5389937_C_A 292 G>V No Jeffares_SNPs

No associated diseases with P39750

5 regional properties for P39750

Type Name Position InterPro Accession
domain XPG, N-terminal 1 - 108 IPR006085
domain XPG-I domain 147 - 234 IPR006086
conserved_site Helix-hairpin-helix motif, class 2 221 - 254 IPR008918
conserved_site XPG conserved site 80 - 94 IPR019974-1
conserved_site XPG conserved site 150 - 164 IPR019974-2

Functions

Description
EC Number
Subcellular Localization
  • Nucleus, nucleolus
  • Nucleus, nucleoplasm
  • Mitochondrion
  • Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
site of double-strand break A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.

7 GO annotations of molecular function

Name Definition
5'-3' exodeoxyribonuclease activity Catalysis of the sequential cleavage of mononucleotides from a free 5' terminus of a DNA molecule.
5'-3' exonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 5' end.
5'-flap endonuclease activity Catalysis of the cleavage of a 5' flap structure in DNA, but not other DNA structures; processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
double-stranded DNA 5'-3' exodeoxyribonuclease activity Catalysis of the sequential cleavage of mononucleotides from a free 5' terminus of a double-stranded DNA molecule.
magnesium ion binding Binding to a magnesium (Mg) ion.
single-stranded DNA 5'-3' exodeoxyribonuclease activity Catalysis of the sequential cleavage of nucleotides (such as mononucleotides or dinucleotides) from a free 5' terminus of a single-stranded DNA molecule.

3 GO annotations of biological process

Name Definition
base-excision repair In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.
DNA replication, removal of RNA primer Removal of the Okazaki RNA primer from the lagging strand of replicating DNA, by a combination of the actions of DNA polymerase, DNA helicase and an endonuclease.
UV-damage excision repair A DNA repair process that is initiated by an endonuclease that introduces a single-strand incision immediately 5' of a UV-induced damage site. UV-damage excision repair acts on both cyclobutane pyrimidine dimers (CPDs) and pyrimidine-pyrimidone 6-4 photoproducts (6-4PPs).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGIKGLAQVL SEHAPASVKH NDIKNYFGRK VAIDASMSLY QFLIQVRSQD GQQLMNEQGE
70 80 90 100 110 120
TTSHLMGMFY RTLRIVDNGI KPCFVFDGKP PTLKSGELAK RVARHQKARE DQEETKEVGT
130 140 150 160 170 180
AEMVDRFAKR TVKVTRQHND EAKRLLELMG IPFVNAPCEA EAQCAALARS GKVYAAASED
190 200 210 220 230 240
MDTLCFQAPV LLRHLTFSEQ RKEPISEYNI EKALNGLDMS VEQFVDLCIL LGCDYCEPIR
250 260 270 280 290 300
GVGPARAVEL IRQYGTLDRF VKEADRSKYP IPEDWPYEDA RRLFLDAEVL PGEEIELKWK
310 320 330 340 350 360
SPDADGIIQF LVKEKGFNED RVKLGINRLE KASKTIPQGR LDSFFKPVPS SPKKPVDTKS
370
KGSAKRKRDS NKGGESKKKR