EME1_SCHPO
ID EME1_SCHPO Reviewed; 735 AA.
AC Q9C103;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Crossover junction endonuclease eme1;
DE EC=3.1.21.10;
DE AltName: Full=Essential meiotic endonuclease 1;
GN Name=eme1; Synonyms=mms4, slx2; ORFNames=SPAPB1E7.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP PROTEIN SEQUENCE OF 373-387; 431-453 AND 692-706, FUNCTION, COFACTOR,
RP INTERACTION WITH MUS81, AND SUBCELLULAR LOCATION.
RX PubMed=11719193; DOI=10.1016/s0092-8674(01)00536-0;
RA Boddy M.N., Gaillard P.-H.L., McDonald W.H., Shanahan P., Yates J.R. III,
RA Russell P.;
RT "Mus81-Eme1 are essential components of a Holliday junction resolvase.";
RL Cell 107:537-548(2001).
RN [4]
RP FUNCTION, AND INTERACTION WITH MUS81.
RX PubMed=12084712; DOI=10.1074/jbc.m202120200;
RA Doe C.L., Ahn J.S., Dixon J., Whitby M.C.;
RT "Mus81-Eme1 and Rqh1 involvement in processing stalled and collapsed
RT replication forks.";
RL J. Biol. Chem. 277:32753-32759(2002).
RN [5]
RP FUNCTION.
RX PubMed=14704204; DOI=10.1093/genetics/165.4.2289;
RA Smith G.R., Boddy M.N., Shanahan P., Russell P.;
RT "Fission yeast Mus81.Eme1 Holliday junction resolvase is required for
RT meiotic crossing over but not for gene conversion.";
RL Genetics 165:2289-2293(2003).
RN [6]
RP FUNCTION.
RX PubMed=12473680; DOI=10.1074/jbc.m210006200;
RA Whitby M.C., Osman F., Dixon J.;
RT "Cleavage of model replication forks by fission yeast Mus81-Eme1 and
RT budding yeast Mus81-Mms4.";
RL J. Biol. Chem. 278:6928-6935(2003).
RN [7]
RP FUNCTION.
RX PubMed=14527419; DOI=10.1016/s1097-2765(03)00342-3;
RA Gaillard P.-H.L., Noguchi E., Shanahan P., Russell P.;
RT "The endogenous Mus81-Eme1 complex resolves Holliday junctions by a nick
RT and counternick mechanism.";
RL Mol. Cell 12:747-759(2003).
RN [8]
RP FUNCTION.
RX PubMed=14527420; DOI=10.1016/s1097-2765(03)00343-5;
RA Osman F., Dixon J., Doe C.L., Whitby M.C.;
RT "Generating crossovers by resolution of nicked Holliday junctions: a role
RT for Mus81-Eme1 in meiosis.";
RL Mol. Cell 12:761-774(2003).
RN [9]
RP FUNCTION.
RX PubMed=15486206; DOI=10.1093/nar/gkh853;
RA Doe C.L., Osman F., Dixon J., Whitby M.C.;
RT "DNA repair by a Rad22-Mus81-dependent pathway that is independent of
RT Rhp51.";
RL Nucleic Acids Res. 32:5570-5581(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-400, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Interacts with mus81 to form a DNA structure-specific
CC endonuclease with substrate preference for branched DNA structures with
CC a 5'-end at the branch nick. Typical substrates include 3'-flap
CC structures, D-loops, replication forks and nicked Holliday junctions.
CC May be required in mitosis for the processing of stalled or collapsed
CC replication fork intermediates. May be required in meiosis for the
CC repair of meiosis-specific double strand breaks subsequent to single-
CC end invasion (SEI). {ECO:0000269|PubMed:11719193,
CC ECO:0000269|PubMed:12084712, ECO:0000269|PubMed:12473680,
CC ECO:0000269|PubMed:14527419, ECO:0000269|PubMed:14527420,
CC ECO:0000269|PubMed:14704204, ECO:0000269|PubMed:15486206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage at a junction such as a reciprocal
CC single-stranded crossover between two homologous DNA duplexes
CC (Holliday junction).; EC=3.1.21.10;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11719193};
CC -!- SUBUNIT: Interacts with mus81. {ECO:0000269|PubMed:11719193,
CC ECO:0000269|PubMed:12084712}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11719193}.
CC -!- MISCELLANEOUS: S.pombe appears to be critically dependent on the mus81-
CC eme1 endonuclease for the resolution of meiotic crossovers. This may be
CC due to the absence of an alternate pathway for crossover resolution
CC such as the MSH4-MSH5 pathway which exists in S.cerevisiae and other
CC eukaryotes.
CC -!- SIMILARITY: Belongs to the EME1/MMS4 family. {ECO:0000305}.
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DR EMBL; CU329670; CAC36923.2; -; Genomic_DNA.
DR RefSeq; NP_594132.2; NM_001019556.2.
DR AlphaFoldDB; Q9C103; -.
DR SMR; Q9C103; -.
DR BioGRID; 280084; 145.
DR IntAct; Q9C103; 1.
DR MINT; Q9C103; -.
DR STRING; 4896.SPAPB1E7.06c.1; -.
DR iPTMnet; Q9C103; -.
DR PaxDb; Q9C103; -.
DR PRIDE; Q9C103; -.
DR EnsemblFungi; SPAPB1E7.06c.1; SPAPB1E7.06c.1:pep; SPAPB1E7.06c.
DR GeneID; 2543670; -.
DR KEGG; spo:SPAPB1E7.06c; -.
DR PomBase; SPAPB1E7.06c; eme1.
DR VEuPathDB; FungiDB:SPAPB1E7.06c; -.
DR eggNOG; ENOG502R8ER; Eukaryota.
DR HOGENOM; CLU_396979_0_0_1; -.
DR InParanoid; Q9C103; -.
DR OMA; FTGRDEM; -.
DR Reactome; R-SPO-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR PRO; PR:Q9C103; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IC:PomBase.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:PomBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:PomBase.
DR GO; GO:0000709; P:meiotic joint molecule formation; TAS:PomBase.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IDA:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IDA:PomBase.
DR Gene3D; 1.10.150.670; -; 1.
DR InterPro; IPR042530; EME1/EME2_C.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR033310; Mms4/EME1/EME2.
DR PANTHER; PTHR21077; PTHR21077; 1.
DR Pfam; PF02732; ERCC4; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW Endonuclease; Hydrolase; Magnesium; Meiosis; Metal-binding; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..735
FT /note="Crossover junction endonuclease eme1"
FT /id="PRO_0000086966"
FT DOMAIN 467..691
FT /note="ERCC4"
FT REGION 245..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 400
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 735 AA; 82574 MW; 275825D6875A9838 CRC64;
MTLQSTDSAI VIDSEADVDI SSSQASPSKD NIALSEHNVI TVLDTPQRST QCDSLLKSFS
TPLVSGSEDV LPSPRDALNI TNKKSVTDNL LLSLTSSNQS TNTNLNPSSR VEIINLNSSP
PNSLSSQPKH QEFHLFHTPT IPRTTQLSSK TSSPIVIPDD NEQVASPLSK KAASLTSSPL
KDFQSSPPLS TVLQKSHSLH DILLDTNDDD HFPFTQSPLT KTKSFNDALT SSSSILKPCM
PSIASPTSNR LSHAPSTPNL FPNQDSSNTI DLINNRSKTS VENQERTFNL TSDVHLDSPT
SPSKHSSIEP NTSQEDSFQE LPSLNKLSIQ SRAFKKMRLP KISRTTDTPP ASTSNSNKKN
LDKLKKMRKL CSRSLEPYEL DSNTQRKRKR YEDSLKKSKT LDKVDSLNRK MAKELDRKNS
KELQKINKVK RTKEECLSEI ILLSPDDWAS SWYSTVRSQL DSYNCQFVVN SNQPKDSIMW
KRKVNNVFNS STNRFELSIE HEQIEPFALL RLKCRDFIKY IEEDQADTFF HEMSEKFKGC
KLILLLEGIP NYFKSLKAEL NRQYAAAVNS GTRPLLFGSL SKYQNFTKEK LESEIVRFSF
EHSILINTSN DEKETAQWIV SFTGDIALSR YKHFSKFSAR ASTTEIGHVK SADRIENSLN
FMLRQILRVT PNIANAICDQ FDSIPSLIHH LKTHGEESLT NVVIQSSISE RNLGPVLSRR
IYNTFLCKEA SSDAP
