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Protein

DNA endonuclease SAE2

Gene

SAE2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endonuclease that cooperates with the MRX complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of SPO11 from the break sites and ensuring both resection and intrachromosomal association of the broken ends. Required for proper recovery from checkpoint-mediated cell cycle arrest after DNA damage. MRX complex and SAE2 remove a small oligonucleotide(s) from the DNA ends to form an early intermediate which is rapidly processed by EXO1 and/or SGS1 to generate extensive tracts of single-stranded DNA that serve as substrate for RAD51. Plays a transitional role in the dissociation of MRE11 from, and the recruitment of RAD52 to, repair foci. Ensures that both ends of a DSB participate in a recombination event and impairs the formation of palindromic structures in the genome. With TEL1, promotes microhomology-mediated end joining (MMEJ) but inhibits non-homologous end joining (NHEJ), likely by regulating MRE11-dependent ssDNA accumulation at DNA break. SAE2 and MRX are particularly important for removal of hairpins, bulky adducts and other irregular end structures. Facilitates telomere length reequilibration and subsequent checkpoint switch off. Involved in homing efficiency of VMA1 intein VDE and in repair of transposon excision sites.25 Publications

Miscellaneous

Present with 1030 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • double-stranded DNA binding Source: SGD
  • endodeoxyribonuclease activity Source: Reactome
  • identical protein binding Source: IntAct
  • single-stranded DNA endodeoxyribonuclease activity Source: SGD

GO - Biological processi

  • DNA catabolic process, endonucleolytic Source: SGD
  • DNA double-strand break processing Source: SGD
  • DNA double-strand break processing involved in repair via synthesis-dependent strand annealing Source: SGD
  • gene conversion at mating-type locus, DNA double-strand break processing Source: SGD
  • meiotic DNA double-strand break formation Source: SGD
  • meiotic DNA double-strand break processing Source: SGD
  • positive regulation of dephosphorylation Source: SGD
  • positive regulation of exonuclease activity Source: SGD
  • telomere maintenance Source: SGD
  • telomeric 3' overhang formation Source: SGD

Keywordsi

Molecular functionDNA-binding, Endonuclease, Hydrolase, Nuclease
Biological processDNA damage, DNA repair, Meiosis

Enzyme and pathway databases

BioCyciYEAST:G3O-30663-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA endonuclease SAE2 (EC:3.1.-.-)
Alternative name(s):
Completion of meiotic recombination protein 1
Sporulation in the absence of SPO11 protein 2
Gene namesi
Name:SAE2
Synonyms:COM1
Ordered Locus Names:YGL175C
ORF Names:G1639
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL175C.
SGDiS000003143. SAE2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi72S → A: Reduces DNA damage-induced phosphorylation; when associated with A-73, A-75, A-76 and A-90. 1 Publication1
Mutagenesisi73S → A: Reduces DNA damage-induced phosphorylation; when associated with A-73, A-75, A-76 and A-90. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-90, A-249, A-279 and A-289. 3 Publications1
Mutagenesisi75T → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-75, A-76 and A-90. 1 Publication1
Mutagenesisi76S → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-73, A-75 and A-90. 1 Publication1
Mutagenesisi90T → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-73, A-75 and A-76. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-249, A-279 and A-289. 3 Publications1
Mutagenesisi223R → A: Leads to camptothecin hypersensitivity and loss of function; when associated with A-225. 1 Publication1
Mutagenesisi225L → A: Leads to camptothecin hypersensitivity and loss of function; when associated with A-223. 1 Publication1
Mutagenesisi249S → A: Reduces DNA damage-induced phosphorylation; when associated with A-278, A-279, and A-289. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-90, A-279 and A-289. 3 Publications1
Mutagenesisi267S → A: Leads to camptothecin hypersensitivity and loss of function. 2 Publications1
Mutagenesisi267S → E: Leads to constitutive activation of the DNA repair function. 2 Publications1
Mutagenesisi270G → D: Abolishes DNA-binding and endonuclease activity. 1 Publication1
Mutagenesisi278S → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-279, and A-289. 1 Publication1
Mutagenesisi279T → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-278, and A-289. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-90, A-249 and A-289. 3 Publications1
Mutagenesisi289S → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-278, and A-279. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-90, A-249 and A-279. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000975651 – 345DNA endonuclease SAE2Add BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei143PhosphoserineCombined sources1
Modified residuei267Phosphoserine; by CDC282 Publications1

Post-translational modificationi

Phosphorylated forms accumulate periodically during the unperturbed cell cycle and in response to DNA damage in G2. Phosphorylated by MEC1 and TEL1. Mutagenesis experiments showed that several of the 5 residues located in canonical (S/T)Q motifs, which are favored for phosphorylation by ATM/ATR kinases (Ser-73, Thr-90, Ser-249, Thr-279 and Ser-289) may be phosphorylated. Phosphorylated at Ser-267 by CDC28 which is required to initiate meiotic DSB resection by allowing SPO11 removal from DSB ends.6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46946.
PRIDEiP46946.

PTM databases

iPTMnetiP46946.

Interactioni

Subunit structurei

Dimer or multimer. Interacts with MRE11.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi33078. 138 interactors.
DIPiDIP-1603N.
IntActiP46946. 8 interactors.
MINTiMINT-391468.
STRINGi4932.YGL175C.

Structurei

3D structure databases

ProteinModelPortaliP46946.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 172DNA-bindingAdd BLAST152

Sequence similaritiesi

Belongs to the COM1/SAE2/CtIP family.Curated

Phylogenomic databases

InParanoidiP46946.
OMAiWTHENED.
OrthoDBiEOG092C34HO.

Sequencei

Sequence statusi: Complete.

P46946-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTGEENVYL KSSLSILKEL SLDELLNVQY DVTTLIAKRV QALQNRNKCV
60 70 80 90 100
LEEPNSKLAE ILCHEKNAPQ QSSQTSAGPG EQDSEDFILT QFDEDIKKES
110 120 130 140 150
AEVHYRNENK HTVQLPLVTM PPNRHKRKIS EFSSPLNGLN NLSDLEDCSD
160 170 180 190 200
TVIHEKDNDK ENKTRKLLGI ELENPESTSP NLYKNVKDNF LFDFNTNPLT
210 220 230 240 250
KRAWILEDFR PNEDIAPVKR GRRKLERFYA QVGKPEDSKH RSLSVVIESQ
260 270 280 290 300
NSDYEFAFDN LRNRSKSPPG FGRLDFPSTQ EGNEDKKKSQ EIIRRKTKYR
310 320 330 340
FLMASNNKIP PYEREYVFKR EQLNQIVDDG CFFWSDKLLQ IYARC
Length:345
Mass (Da):40,097
Last modified:November 1, 1995 - v1
Checksum:i284D57A3C11DD92B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49447 Genomic DNA. Translation: AAB96338.1.
X84705 Genomic DNA. Translation: CAA59178.1.
Z72697 Genomic DNA. Translation: CAA96887.1.
BK006941 Genomic DNA. Translation: DAA07938.1.
PIRiS59236.
RefSeqiNP_011340.1. NM_001181040.1.

Genome annotation databases

EnsemblFungiiYGL175C; YGL175C; YGL175C.
GeneIDi852700.
KEGGisce:YGL175C.

Similar proteinsi

Entry informationi

Entry nameiCOM1_YEAST
AccessioniPrimary (citable) accession number: P46946
Secondary accession number(s): D6VTX7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 22, 2017
This is version 131 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names