UniProtKB - P46946 (COM1_YEAST)
DNA endonuclease SAE2
SAE2
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 PublicationsMiscellaneous
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 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 function | DNA-binding, Endonuclease, Hydrolase, Nuclease |
Biological process | DNA damage, DNA repair, Meiosis |
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 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000003143, SAE2 |
VEuPathDBi | FungiDB:YGL175C |
Subcellular locationi
Nucleus
- Mre11 complex Source: SGD
- nucleoplasm Source: Reactome
- nucleus Source: SGD
Other locations
- cytoplasm Source: SGD
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 72 | S → A: Reduces DNA damage-induced phosphorylation; when associated with A-73, A-75, A-76 and A-90. 1 Publication | 1 | |
Mutagenesisi | 73 | S → 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 Publications | 1 | |
Mutagenesisi | 75 | T → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-75, A-76 and A-90. 1 Publication | 1 | |
Mutagenesisi | 76 | S → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-73, A-75 and A-90. 1 Publication | 1 | |
Mutagenesisi | 90 | T → 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 Publications | 1 | |
Mutagenesisi | 223 | R → A: Leads to camptothecin hypersensitivity and loss of function; when associated with A-225. 1 Publication | 1 | |
Mutagenesisi | 225 | L → A: Leads to camptothecin hypersensitivity and loss of function; when associated with A-223. 1 Publication | 1 | |
Mutagenesisi | 249 | S → 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 Publications | 1 | |
Mutagenesisi | 267 | S → A: Leads to camptothecin hypersensitivity and loss of function. 2 Publications | 1 | |
Mutagenesisi | 267 | S → E: Leads to constitutive activation of the DNA repair function. 2 Publications | 1 | |
Mutagenesisi | 270 | G → D: Abolishes DNA-binding and endonuclease activity. 1 Publication | 1 | |
Mutagenesisi | 278 | S → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-279, and A-289. 1 Publication | 1 | |
Mutagenesisi | 279 | T → 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 Publications | 1 | |
Mutagenesisi | 289 | S → 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 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000097565 | 1 – 345 | DNA endonuclease SAE2Add BLAST | 345 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 143 | PhosphoserineCombined sources | 1 | |
Modified residuei | 267 | Phosphoserine; by CDC282 Publications | 1 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinProteomic databases
MaxQBi | P46946 |
PaxDbi | P46946 |
PRIDEi | P46946 |
PTM databases
iPTMneti | P46946 |
Interactioni
Subunit structurei
Dimer or multimer.
Interacts with MRE11.
1 PublicationBinary interactionsi
P46946
With | #Exp. | IntAct |
---|---|---|
MRE11 [P32829] | 2 | EBI-16440,EBI-11255 |
itself | 3 | EBI-16440,EBI-16440 |
XRS2 [P33301] | 3 | EBI-16440,EBI-20599 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 33078, 178 interactors |
DIPi | DIP-1603N |
IntActi | P46946, 8 interactors |
MINTi | P46946 |
STRINGi | 4932.YGL175C |
Miscellaneous databases
RNActi | P46946, protein |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 21 – 172 | DNA-bindingAdd BLAST | 152 | |
Regioni | 265 – 290 | DisorderedSequence analysisAdd BLAST | 26 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | ENOG502S084, Eukaryota |
HOGENOMi | CLU_064983_0_0_1 |
InParanoidi | P46946 |
OMAi | PPYEREY |
i Sequence
Sequence statusi: Complete.
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
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 |
PIRi | S59236 |
RefSeqi | NP_011340.1, NM_001181040.1 |
Genome annotation databases
EnsemblFungii | YGL175C_mRNA; YGL175C; YGL175C |
GeneIDi | 852700 |
KEGGi | sce:YGL175C |
Similar proteinsi
Cross-referencesi
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 |
PIRi | S59236 |
RefSeqi | NP_011340.1, NM_001181040.1 |
3D structure databases
AlphaFoldDBi | P46946 |
SMRi | P46946 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 33078, 178 interactors |
DIPi | DIP-1603N |
IntActi | P46946, 8 interactors |
MINTi | P46946 |
STRINGi | 4932.YGL175C |
PTM databases
iPTMneti | P46946 |
Proteomic databases
MaxQBi | P46946 |
PaxDbi | P46946 |
PRIDEi | P46946 |
Genome annotation databases
EnsemblFungii | YGL175C_mRNA; YGL175C; YGL175C |
GeneIDi | 852700 |
KEGGi | sce:YGL175C |
Organism-specific databases
SGDi | S000003143, SAE2 |
VEuPathDBi | FungiDB:YGL175C |
Phylogenomic databases
eggNOGi | ENOG502S084, Eukaryota |
HOGENOMi | CLU_064983_0_0_1 |
InParanoidi | P46946 |
OMAi | PPYEREY |
Miscellaneous databases
PROi | PR:P46946 |
RNActi | P46946, protein |
Family and domain databases
MobiDBi | Search... |
Entry informationi
Entry namei | COM1_YEAST | |
Accessioni | P46946Primary (citable) accession number: P46946 Secondary accession number(s): D6VTX7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 1, 1995 | |
Last modified: | May 25, 2022 | |
This is version 156 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome VII
Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names - SIMILARITY comments
Index of protein domains and families