ID   EME1_KLULA              Reviewed;         690 AA.
AC   Q6CNM6;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Crossover junction endonuclease EME1;
DE            EC=3.1.22.-;
GN   Name=EME1; OrderedLocusNames=KLLA0E11363g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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) (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with MUS81. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EME1/MMS4 family. {ECO:0000305}.
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DR   EMBL; CR382125; CAG99550.1; -; Genomic_DNA.
DR   RefSeq; XP_454463.1; XM_454463.1.
DR   AlphaFoldDB; Q6CNM6; -.
DR   STRING; 28985.XP_454463.1; -.
DR   EnsemblFungi; CAG99550; CAG99550; KLLA0_E11397g.
DR   GeneID; 2894598; -.
DR   KEGG; kla:KLLA0_E11397g; -.
DR   eggNOG; ENOG502RY0Q; Eukaryota.
DR   HOGENOM; CLU_023637_0_0_1; -.
DR   InParanoid; Q6CNM6; -.
DR   OMA; TICSEHE; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR006166; ERCC4_domain.
DR   Pfam; PF02732; ERCC4; 1.
DR   SMART; SM00891; ERCC4; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW   Magnesium; Meiosis; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..690
FT                   /note="Crossover junction endonuclease EME1"
FT                   /id="PRO_0000223635"
FT   REGION          181..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  79008 MW;  CFC6989BFF61A460 CRC64;
     MDEVNIIDIN DTTEQSLVGN EGTANGVVVL ISSEGEREGP PASDPIHYSL ARSLSDSVGQ
     RNVEDDDVVL LENSVSVSFS LEVEGRFQND TAIESDNEPA SQPQTQTFKR SQSRLLDEIE
     NSGLSISALS DDEEASPLVS NQRSVIHKNI ESEVKSGKYI IPLPQSSPLE KMSQVFNYQL
     ASSPTPNKSP SSRSTLPVKS PLQLSTTVAN KRSYREVQPP KFDPYLTRKL KKPQNKATAD
     VSSVALDLTK YMEDCHDLYG TLVSDTHIRQ QRSLDTKTNS YHSESNYEHD SIVIESDEDD
     DITNTRQEKP LFVQHSSQST PVSSNKLALR QPRHVEDEKI DKVKPMVNAR PFTDQEYSEM
     VKKCLGTSEM RKLYNECNKV SRTEETIYNE MILTVNNKVM ELIHSKHISF EEELKPLTII
     QNYEEFPIIR FKRKCRSIYD QTHGVFYPCD EVIANESICV LVYEALPFFH RYRTDKRGLW
     DEIRQFSKNG MKVIVVMYGL NALRKKLCNM ENRQHEDRVL EQLSGSASSQ SQSKTRRRST
     QETKMRELNI KSKNLDRIIN EVTIYANVDV FPIENLNEFS HWMKNLVWVV GKMRYDVSVK
     YKEWSHLNVK SGKSPTDVLY SFLQQVAHVN EPKAKRVVTH YKSFQSMMND MKAGYVAQSH
     DNKPLMPKSL ERALHTLYTS DDPNELIFTD