COM1_YEAST
ID COM1_YEAST Reviewed; 345 AA.
AC P46946; D6VTX7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=DNA endonuclease SAE2;
DE EC=3.1.-.-;
DE AltName: Full=Completion of meiotic recombination protein 1;
DE AltName: Full=Sporulation in the absence of SPO11 protein 2;
GN Name=SAE2; Synonyms=COM1; OrderedLocusNames=YGL175C; ORFNames=G1639;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9215888; DOI=10.1093/genetics/146.3.797;
RA McKee A.H.Z., Kleckner N.;
RT "A general method for identifying recessive diploid-specific mutations in
RT Saccharomyces cerevisiae, its application to the isolation of mutants
RT blocked at intermediate stages of meiotic prophase and characterization of
RT a new gene SAE2.";
RL Genetics 146:797-816(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8619317; DOI=10.1002/yea.320111209;
RA Bertani I., Coglievina M., Zaccaria P., Klima R., Bruschi C.V.;
RT "The sequence of an 11.1 kb fragment on the left arm of Saccharomyces
RT cerevisiae chromosome VII reveals six open reading frames including NSP49,
RT KEM1 and four putative new genes.";
RL Yeast 11:1187-1194(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=9215887; DOI=10.1093/genetics/146.3.781;
RA Prinz S., Amon A., Klein F.;
RT "Isolation of COM1, a new gene required to complete meiotic double-strand
RT break-induced recombination in Saccharomyces cerevisiae.";
RL Genetics 146:781-795(1997).
RN [6]
RP FUNCTION.
RX PubMed=11052944; DOI=10.1126/science.290.5492.806;
RA Borde V., Goldman A.S., Lichten M.;
RT "Direct coupling between meiotic DNA replication and recombination
RT initiation.";
RL Science 290:806-809(2000).
RN [7]
RP FUNCTION.
RX PubMed=11333222; DOI=10.1093/genetics/158.1.109;
RA Rattray A.J., McGill C.B., Shafer B.K., Strathern J.N.;
RT "Fidelity of mitotic double-strand-break repair in Saccharomyces
RT cerevisiae: a role for SAE2/COM1.";
RL Genetics 158:109-122(2001).
RN [8]
RP FUNCTION.
RX PubMed=11983174; DOI=10.1016/s1097-2765(02)00498-7;
RA Neale M.J., Ramachandran M., Trelles-Sticken E., Scherthan H.,
RA Goldman A.S.;
RT "Wild-type levels of Spo11-induced DSBs are required for normal single-
RT strand resection during meiosis.";
RL Mol. Cell 9:835-846(2002).
RN [9]
RP FUNCTION.
RX PubMed=11832209; DOI=10.1016/s0092-8674(02)00614-1;
RA Lobachev K.S., Gordenin D.A., Resnick M.A.;
RT "The Mre11 complex is required for repair of hairpin-capped double-strand
RT breaks and prevention of chromosome rearrangements.";
RL Cell 108:183-193(2002).
RN [10]
RP FUNCTION.
RX PubMed=12839620; DOI=10.1046/j.1365-2443.2003.00659.x;
RA Fukuda T., Nogami S., Ohya Y.;
RT "VDE-initiated intein homing in Saccharomyces cerevisiae proceeds in a
RT meiotic recombination-like manner.";
RL Genes Cells 8:587-602(2003).
RN [11]
RP FUNCTION.
RX PubMed=12925751; DOI=10.1091/mbc.e02-11-0719;
RA Viscardi V., Baroni E., Romano M., Lucchini G., Longhese M.P.;
RT "Sudden telomere lengthening triggers a Rad53-dependent checkpoint in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:3126-3143(2003).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [13]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15369670; DOI=10.1016/j.cell.2004.08.015;
RA Lisby M., Barlow J.H., Burgess R.C., Rothstein R.;
RT "Choreography of the DNA damage response: spatiotemporal relationships
RT among checkpoint and repair proteins.";
RL Cell 118:699-713(2004).
RN [15]
RP FUNCTION.
RX PubMed=14729978; DOI=10.1128/mcb.24.3.1351-1364.2004;
RA Yu J., Marshall K., Yamaguchi M., Haber J.E., Weil C.F.;
RT "Microhomology-dependent end joining and repair of transposon-induced DNA
RT hairpins by host factors in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 24:1351-1364(2004).
RN [16]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-72; SER-73; THR-75;
RP SER-76; THR-90; SER-249; SER-278; THR-279 AND SER-289.
RX PubMed=15121837; DOI=10.1128/mcb.24.10.4151-4165.2004;
RA Baroni E., Viscardi V., Cartagena-Lirola H., Lucchini G., Longhese M.P.;
RT "The functions of budding yeast Sae2 in the DNA damage response require
RT Mec1- and Tel1-dependent phosphorylation.";
RL Mol. Cell. Biol. 24:4151-4165(2004).
RN [17]
RP FUNCTION.
RX PubMed=15655113; DOI=10.1101/gad.321105;
RA Prieler S., Penkner A., Borde V., Klein F.;
RT "The control of Spo11's interaction with meiotic recombination hotspots.";
RL Genes Dev. 19:255-269(2005).
RN [18]
RP FUNCTION.
RX PubMed=15937224; DOI=10.1101/gad.1315805;
RA Rattray A.J., Shafer B.K., Neelam B., Strathern J.N.;
RT "A mechanism of palindromic gene amplification in Saccharomyces
RT cerevisiae.";
RL Genes Dev. 19:1390-1399(2005).
RN [19]
RP FUNCTION.
RX PubMed=15834151; DOI=10.1534/genetics.104.028795;
RA Deng C., Brown J.A., You D., Brown J.M.;
RT "Multiple endonucleases function to repair covalent topoisomerase I
RT complexes in Saccharomyces cerevisiae.";
RL Genetics 170:591-600(2005).
RN [20]
RP FUNCTION.
RX PubMed=16162495; DOI=10.1074/jbc.m508339200;
RA Clerici M., Mantiero D., Lucchini G., Longhese M.P.;
RT "The Saccharomyces cerevisiae Sae2 protein promotes resection and bridging
RT of double strand break ends.";
RL J. Biol. Chem. 280:38631-38638(2005).
RN [21]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-73; THR-90; SER-249;
RP THR-279 AND SER-289.
RX PubMed=16861895; DOI=10.4161/cc.5.14.2916;
RA Cartagena-Lirola H., Guerini I., Viscardi V., Lucchini G., Longhese M.P.;
RT "Budding yeast Sae2 is an in vivo target of the Mec1 and Tel1 checkpoint
RT kinases during meiosis.";
RL Cell Cycle 5:1549-1559(2006).
RN [22]
RP FUNCTION.
RX PubMed=16374511; DOI=10.1038/sj.embor.7400593;
RA Clerici M., Mantiero D., Lucchini G., Longhese M.P.;
RT "The Saccharomyces cerevisiae Sae2 protein negatively regulates DNA damage
RT checkpoint signalling.";
RL EMBO Rep. 7:212-218(2006).
RN [23]
RP FUNCTION.
RX PubMed=17565964; DOI=10.1534/genetics.107.076539;
RA Lee K., Lee S.E.;
RT "Saccharomyces cerevisiae Sae2- and Tel1-dependent single-strand DNA
RT formation at DNA break promotes microhomology-mediated end joining.";
RL Genetics 176:2003-2014(2007).
RN [24]
RP SUBUNIT, AND INTERACTION WITH MRE11.
RX PubMed=17989249; DOI=10.1101/gr.6667007;
RA Suter B., Fetchko M.J., Imhof R., Graham C.I., Stoffel-Studer I.,
RA Zbinden C., Raghavan M., Lopez L., Beneti L., Hort J., Fillingham J.,
RA Greenblatt J.F., Giaever G., Nislow C., Stagljar I.;
RT "Examining protein protein interactions using endogenously tagged yeast
RT arrays: the cross-and-capture system.";
RL Genome Res. 17:1774-1782(2007).
RN [25]
RP FUNCTION, DNA-BINDING, DOMAIN, AND MUTAGENESIS OF GLY-270.
RX PubMed=18042458; DOI=10.1016/j.molcel.2007.11.001;
RA Lengsfeld B.M., Rattray A.J., Bhaskara V., Ghirlando R., Paull T.T.;
RT "Sae2 is an endonuclease that processes hairpin DNA cooperatively with the
RT Mre11/Rad50/Xrs2 complex.";
RL Mol. Cell 28:638-651(2007).
RN [26]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-73;
RP THR-90; SER-249; THR-279 AND SER-289.
RX PubMed=18670132; DOI=10.1266/ggs.83.209;
RA Terasawa M., Ogawa T., Tsukamoto Y., Ogawa H.;
RT "Sae2p phosphorylation is crucial for cooperation with Mre11p for resection
RT of DNA double-strand break ends during meiotic recombination in
RT Saccharomyces cerevisiae.";
RL Genes Genet. Syst. 83:209-217(2008).
RN [27]
RP FUNCTION, MUTAGENESIS OF ARG-223; LEU-225 AND SER-267, AND PHOSPHORYLATION
RP AT SER-267.
RX PubMed=18716619; DOI=10.1038/nature07215;
RA Huertas P., Cortes-Ledesma F., Sartori A.A., Aguilera A., Jackson S.P.;
RT "CDK targets Sae2 to control DNA-end resection and homologous
RT recombination.";
RL Nature 455:689-692(2008).
RN [28]
RP FUNCTION.
RX PubMed=18806779; DOI=10.1038/nature07312;
RA Mimitou E.P., Symington L.S.;
RT "Sae2, Exo1 and Sgs1 collaborate in DNA double-strand break processing.";
RL Nature 455:770-774(2008).
RN [29]
RP FUNCTION.
RX PubMed=19361851; DOI=10.1016/j.cell.2009.02.016;
RA Doksani Y., Bermejo R., Fiorani S., Haber J.E., Foiani M.;
RT "Replicon dynamics, dormant origin firing, and terminal fork integrity
RT after double-strand break formation.";
RL Cell 137:247-258(2009).
RN [30]
RP FUNCTION.
RX PubMed=19124276; DOI=10.1016/j.dnarep.2008.11.017;
RA Lisnic B., Svetec I.K., Stafa A., Zgaga Z.;
RT "Size-dependent palindrome-induced intrachromosomal recombination in
RT yeast.";
RL DNA Repair 8:383-389(2009).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [32]
RP FUNCTION, MUTAGENESIS OF SER-267, AND PHOSPHORYLATION AT SER-267.
RX PubMed=20150422; DOI=10.1074/jbc.m110.104083;
RA Manfrini N., Guerini I., Citterio A., Lucchini G., Longhese M.P.;
RT "Processing of meiotic DNA double strand breaks requires cyclin-dependent
RT kinase and multiple nucleases.";
RL J. Biol. Chem. 285:11628-11637(2010).
RN [33]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=20061370; DOI=10.1093/nar/gkp1222;
RA Janke R., Herzberg K., Rolfsmeier M., Mar J., Bashkirov V.I.,
RA Haghnazari E., Cantin G., Yates J.R. III, Heyer W.D.;
RT "A truncated DNA-damage-signaling response is activated after DSB formation
RT in the G1 phase of Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 38:2302-2313(2010).
CC -!- FUNCTION: Endonuclease that cooperates with the MRX complex in
CC processing meiotic and mitotic double-strand breaks by allowing the
CC endonucleolytic removal of SPO11 from the break sites and ensuring both
CC resection and intrachromosomal association of the broken ends. Required
CC for proper recovery from checkpoint-mediated cell cycle arrest after
CC DNA damage. MRX complex and SAE2 remove a small oligonucleotide(s) from
CC the DNA ends to form an early intermediate which is rapidly processed
CC by EXO1 and/or SGS1 to generate extensive tracts of single-stranded DNA
CC that serve as substrate for RAD51. Plays a transitional role in the
CC dissociation of MRE11 from, and the recruitment of RAD52 to, repair
CC foci. Ensures that both ends of a DSB participate in a recombination
CC event and impairs the formation of palindromic structures in the
CC genome. With TEL1, promotes microhomology-mediated end joining (MMEJ)
CC but inhibits non-homologous end joining (NHEJ), likely by regulating
CC MRE11-dependent ssDNA accumulation at DNA break. SAE2 and MRX are
CC particularly important for removal of hairpins, bulky adducts and other
CC irregular end structures. Facilitates telomere length reequilibration
CC and subsequent checkpoint switch off. Involved in homing efficiency of
CC VMA1 intein VDE and in repair of transposon excision sites.
CC {ECO:0000269|PubMed:11052944, ECO:0000269|PubMed:11333222,
CC ECO:0000269|PubMed:11832209, ECO:0000269|PubMed:11983174,
CC ECO:0000269|PubMed:12839620, ECO:0000269|PubMed:12925751,
CC ECO:0000269|PubMed:14729978, ECO:0000269|PubMed:15121837,
CC ECO:0000269|PubMed:15369670, ECO:0000269|PubMed:15655113,
CC ECO:0000269|PubMed:15834151, ECO:0000269|PubMed:15937224,
CC ECO:0000269|PubMed:16162495, ECO:0000269|PubMed:16374511,
CC ECO:0000269|PubMed:16861895, ECO:0000269|PubMed:17565964,
CC ECO:0000269|PubMed:18042458, ECO:0000269|PubMed:18670132,
CC ECO:0000269|PubMed:18716619, ECO:0000269|PubMed:18806779,
CC ECO:0000269|PubMed:19124276, ECO:0000269|PubMed:19361851,
CC ECO:0000269|PubMed:20061370, ECO:0000269|PubMed:20150422,
CC ECO:0000269|PubMed:9215887}.
CC -!- SUBUNIT: Dimer or multimer. Interacts with MRE11.
CC {ECO:0000269|PubMed:17989249}.
CC -!- INTERACTION:
CC P46946; P32829: MRE11; NbExp=2; IntAct=EBI-16440, EBI-11255;
CC P46946; P46946: SAE2; NbExp=3; IntAct=EBI-16440, EBI-16440;
CC P46946; P33301: XRS2; NbExp=3; IntAct=EBI-16440, EBI-20599;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:15369670, ECO:0000269|PubMed:18670132}.
CC Note=Accumulates in foci at the precise time when MRE11 foci
CC disassemble and RAD52 foci assemble (PubMed:18670132). Remains
CC associated with DSBs along with MRE11 in nuclease-deficient cells
CC (PubMed:18670132).
CC -!- PTM: Phosphorylated forms accumulate periodically during the
CC unperturbed cell cycle and in response to DNA damage in G2.
CC Phosphorylated by MEC1 and TEL1. Mutagenesis experiments showed that
CC several of the 5 residues located in canonical (S/T)Q motifs, which are
CC favored for phosphorylation by ATM/ATR kinases (Ser-73, Thr-90, Ser-
CC 249, Thr-279 and Ser-289) may be phosphorylated. Phosphorylated at Ser-
CC 267 by CDC28 which is required to initiate meiotic DSB resection by
CC allowing SPO11 removal from DSB ends. {ECO:0000269|PubMed:15121837,
CC ECO:0000269|PubMed:16861895, ECO:0000269|PubMed:18670132,
CC ECO:0000269|PubMed:18716619, ECO:0000269|PubMed:20061370,
CC ECO:0000269|PubMed:20150422}.
CC -!- MISCELLANEOUS: Present with 1030 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the COM1/SAE2/CtIP family. {ECO:0000305}.
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DR EMBL; U49447; AAB96338.1; -; Genomic_DNA.
DR EMBL; X84705; CAA59178.1; -; Genomic_DNA.
DR EMBL; Z72697; CAA96887.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07938.1; -; Genomic_DNA.
DR PIR; S59236; S59236.
DR RefSeq; NP_011340.1; NM_001181040.1.
DR AlphaFoldDB; P46946; -.
DR SMR; P46946; -.
DR BioGRID; 33078; 179.
DR DIP; DIP-1603N; -.
DR IntAct; P46946; 8.
DR MINT; P46946; -.
DR STRING; 4932.YGL175C; -.
DR iPTMnet; P46946; -.
DR MaxQB; P46946; -.
DR PaxDb; P46946; -.
DR PRIDE; P46946; -.
DR EnsemblFungi; YGL175C_mRNA; YGL175C; YGL175C.
DR GeneID; 852700; -.
DR KEGG; sce:YGL175C; -.
DR SGD; S000003143; SAE2.
DR VEuPathDB; FungiDB:YGL175C; -.
DR eggNOG; ENOG502S084; Eukaryota.
DR HOGENOM; CLU_064983_0_0_1; -.
DR InParanoid; P46946; -.
DR OMA; PPYEREY; -.
DR BioCyc; YEAST:G3O-30663-MON; -.
DR PRO; PR:P46946; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P46946; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0030870; C:Mre11 complex; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; EXP:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:SGD.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:SGD.
DR GO; GO:0010791; P:DNA double-strand break processing involved in repair via synthesis-dependent strand annealing; IMP:SGD.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IMP:SGD.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IGI:SGD.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IMP:SGD.
DR GO; GO:0035306; P:positive regulation of dephosphorylation; IMP:SGD.
DR GO; GO:1905779; P:positive regulation of exonuclease activity; IDA:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR GO; GO:0031860; P:telomeric 3' overhang formation; IMP:SGD.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; DNA-binding; Endonuclease; Hydrolase;
KW Meiosis; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..345
FT /note="DNA endonuclease SAE2"
FT /id="PRO_0000097565"
FT REGION 21..172
FT /note="DNA-binding"
FT REGION 265..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 267
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:18716619,
FT ECO:0000269|PubMed:20150422"
FT MUTAGEN 72
FT /note="S->A: Reduces DNA damage-induced phosphorylation;
FT when associated with A-73, A-75, A-76 and A-90."
FT /evidence="ECO:0000269|PubMed:15121837"
FT MUTAGEN 73
FT /note="S->A: Reduces DNA damage-induced phosphorylation;
FT when associated with A-73, A-75, A-76 and A-90. Abolishes
FT DNA damage-induced phosphorylation and function in DNA
FT repair; when associated with A-90, A-249, A-279 and A-289."
FT /evidence="ECO:0000269|PubMed:15121837,
FT ECO:0000269|PubMed:16861895, ECO:0000269|PubMed:18670132"
FT MUTAGEN 75
FT /note="T->A: Reduces DNA damage-induced phosphorylation;
FT when associated with A-72, A-75, A-76 and A-90."
FT /evidence="ECO:0000269|PubMed:15121837"
FT MUTAGEN 76
FT /note="S->A: Reduces DNA damage-induced phosphorylation;
FT when associated with A-72, A-73, A-75 and A-90."
FT /evidence="ECO:0000269|PubMed:15121837"
FT MUTAGEN 90
FT /note="T->A: Reduces DNA damage-induced phosphorylation;
FT when associated with A-72, A-73, A-75 and A-76. Abolishes
FT DNA damage-induced phosphorylation and function in DNA
FT repair; when associated with A-73, A-249, A-279 and A-289."
FT /evidence="ECO:0000269|PubMed:15121837,
FT ECO:0000269|PubMed:16861895, ECO:0000269|PubMed:18670132"
FT MUTAGEN 223
FT /note="R->A: Leads to camptothecin hypersensitivity and
FT loss of function; when associated with A-225."
FT /evidence="ECO:0000269|PubMed:18716619"
FT MUTAGEN 225
FT /note="L->A: Leads to camptothecin hypersensitivity and
FT loss of function; when associated with A-223."
FT /evidence="ECO:0000269|PubMed:18716619"
FT MUTAGEN 249
FT /note="S->A: Reduces DNA damage-induced phosphorylation;
FT when associated with A-278, A-279, and A-289. Abolishes DNA
FT damage-induced phosphorylation and function in DNA repair;
FT when associated with A-73, A-90, A-279 and A-289."
FT /evidence="ECO:0000269|PubMed:15121837,
FT ECO:0000269|PubMed:16861895, ECO:0000269|PubMed:18670132"
FT MUTAGEN 267
FT /note="S->A: Leads to camptothecin hypersensitivity and
FT loss of function."
FT /evidence="ECO:0000269|PubMed:18716619,
FT ECO:0000269|PubMed:20150422"
FT MUTAGEN 267
FT /note="S->E: Leads to constitutive activation of the DNA
FT repair function."
FT /evidence="ECO:0000269|PubMed:18716619,
FT ECO:0000269|PubMed:20150422"
FT MUTAGEN 270
FT /note="G->D: Abolishes DNA-binding and endonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:18042458"
FT MUTAGEN 278
FT /note="S->A: Reduces DNA damage-induced phosphorylation;
FT when associated with A-249, A-279, and A-289."
FT /evidence="ECO:0000269|PubMed:15121837"
FT MUTAGEN 279
FT /note="T->A: Reduces DNA damage-induced phosphorylation;
FT when associated with A-249, A-278, and A-289. Abolishes DNA
FT damage-induced phosphorylation and function in DNA repair;
FT when associated with A-73, A-90, A-249 and A-289."
FT /evidence="ECO:0000269|PubMed:15121837,
FT ECO:0000269|PubMed:16861895, ECO:0000269|PubMed:18670132"
FT MUTAGEN 289
FT /note="S->A: Reduces DNA damage-induced phosphorylation;
FT when associated with A-249, A-278, and A-279. Abolishes DNA
FT damage-induced phosphorylation and function in DNA repair;
FT when associated with A-73, A-90, A-249 and A-279."
FT /evidence="ECO:0000269|PubMed:15121837,
FT ECO:0000269|PubMed:16861895, ECO:0000269|PubMed:18670132"
SQ SEQUENCE 345 AA; 40097 MW; 284D57A3C11DD92B CRC64;
MVTGEENVYL KSSLSILKEL SLDELLNVQY DVTTLIAKRV QALQNRNKCV LEEPNSKLAE
ILCHEKNAPQ QSSQTSAGPG EQDSEDFILT QFDEDIKKES AEVHYRNENK HTVQLPLVTM
PPNRHKRKIS EFSSPLNGLN NLSDLEDCSD TVIHEKDNDK ENKTRKLLGI ELENPESTSP
NLYKNVKDNF LFDFNTNPLT KRAWILEDFR PNEDIAPVKR GRRKLERFYA QVGKPEDSKH
RSLSVVIESQ NSDYEFAFDN LRNRSKSPPG FGRLDFPSTQ EGNEDKKKSQ EIIRRKTKYR
FLMASNNKIP PYEREYVFKR EQLNQIVDDG CFFWSDKLLQ IYARC
