ID   MUS81_DEBHA             Reviewed;         651 AA.
AC   Q6BJ48;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Crossover junction endonuclease MUS81;
DE            EC=3.1.22.-;
GN   Name=MUS81; OrderedLocusNames=DEHA2G05214g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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 EME1 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 EME1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
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DR   EMBL; CR382139; CAG90230.2; -; Genomic_DNA.
DR   RefSeq; XP_461773.2; XM_461773.1.
DR   AlphaFoldDB; Q6BJ48; -.
DR   SMR; Q6BJ48; -.
DR   STRING; 4959.XP_461773.2; -.
DR   PRIDE; Q6BJ48; -.
DR   EnsemblFungi; CAG90230; CAG90230; DEHA2G05214g.
DR   GeneID; 2904649; -.
DR   KEGG; dha:DEHA2G05214g; -.
DR   VEuPathDB; FungiDB:DEHA2G05214g; -.
DR   eggNOG; KOG2379; Eukaryota.
DR   HOGENOM; CLU_014329_1_0_1; -.
DR   InParanoid; Q6BJ48; -.
DR   OMA; WIKEWLD; -.
DR   OrthoDB; 738810at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:InterPro.
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; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.110; -; 1.
DR   Gene3D; 1.10.150.670; -; 1.
DR   InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR   InterPro; IPR042530; EME1/EME2_C.
DR   InterPro; IPR006166; ERCC4_domain.
DR   InterPro; IPR033309; Mus81.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR13451; PTHR13451; 1.
DR   Pfam; PF02732; ERCC4; 1.
DR   SMART; SM00891; ERCC4; 1.
DR   SUPFAM; SSF47802; SSF47802; 1.
DR   SUPFAM; SSF52980; SSF52980; 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..651
FT                   /note="Crossover junction endonuclease MUS81"
FT                   /id="PRO_0000223642"
FT   DOMAIN          361..458
FT                   /note="ERCC4"
FT   REGION          99..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   651 AA;  74151 MW;  ED3C32F631DAC716 CRC64;
     MEGPPGDLKH LFIEWLQEAA INATKKGTKA AILYNKALGS VRNYPLPIND PKTLKSVQFV
     GDKTCIHLSK KLEEYCKLNN FELPVAFGGL INGGVGEKRK HEVSDTSNLP DAKPKKQRKQ
     KQYIPRKRSG GYAILLALYF GDKKKTGLTK EEIIQRATPY SDKSFKSNPS ANEFYSAWSS
     IKSLQTHDLV DSSGRSSKSY FLTEEGYELA KQLKDAEGFE SSPITNHIAD LSFDNQVRVT
     PDSSYSKISQ QLDSSPLMKT KNNKDRYGLG PSRLSSTRER ILDLSSSPRL ISSPLKPKDF
     VLRESLSSHN STRPLQDRES ISKAEDGINT KTKARLVHDA SKRIYDGTNY DIWVPGEFEI
     ILIIDNREIR SQRDRDFFQT RLTSLKVECD VRPLSVGDVV WTAKHKKTGR EVILNYICER
     KRLDDLVSSI KDGRFQEQKN RLKKSGMKQF YYLVEDVVTS DMNKFGDMSD AIQTAMSMTM
     TISNFYLKRF KSIEDTIAFL ASLTQVIKDQ FAKNKTNLLV LKARSIKNQA EYSSLIAKFK
     EKFENRSTSY ECAHLFSTFQ DSMGKTGMMT VKETFILMLM GIRGVSLERA VAIQNRFKTP
     KNLIEFFFVE NNHLSELDKK QLMMDVFKNE IGNKKIGKVL SEKIYDVWGC V