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MUS81_DICDI
ID   MUS81_DICDI             Reviewed;         920 AA.
AC   Q551H0; Q8T856;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Probable crossover junction endonuclease mus81;
DE            EC=3.1.22.-;
GN   Name=mus81; ORFNames=DDB_G0276519;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Component of a DNA structure-specific endonuclease with
CC       substrate preference for branched DNA structures with a 5'-end at the
CC       branch nick. May be required in mitosis for the processing of stalled
CC       or collapsed replication fork intermediates. May be required in meiosis
CC       for the repair of meiosis-specific double strand breaks subsequent to
CC       single-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; AAFI02000015; EAL69213.1; -; Genomic_DNA.
DR   RefSeq; XP_643164.1; XM_638072.1.
DR   AlphaFoldDB; Q551H0; -.
DR   SMR; Q551H0; -.
DR   STRING; 44689.DDB0304698; -.
DR   PaxDb; Q551H0; -.
DR   EnsemblProtists; EAL69213; EAL69213; DDB_G0276519.
DR   GeneID; 8620572; -.
DR   KEGG; ddi:DDB_G0276519; -.
DR   dictyBase; DDB_G0276519; mus81.
DR   eggNOG; KOG2379; Eukaryota.
DR   HOGENOM; CLU_316989_0_0_1; -.
DR   InParanoid; Q551H0; -.
DR   OMA; CIVDNRE; -.
DR   PRO; PR:Q551H0; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048257; F:3'-flap endonuclease activity; IBA:GO_Central.
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:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
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   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; Manganese; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..920
FT                   /note="Probable crossover junction endonuclease mus81"
FT                   /id="PRO_0000367256"
FT   DOMAIN          635..731
FT                   /note="ERCC4"
FT   REGION          90..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..557
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   920 AA;  104294 MW;  968A2AFA57B9FFEE CRC64;
     MSTNKNHNNN TNNNDNNICI NPHIVEFLNK QITNIKNRPG ADIKTTSIYK KAIRSLNLYP
     LPVFSGKECE VLNGFGPSLT KKINDYLKTT SHPLYPKGPP TPLKSIYNRN NNNNDNNNNN
     NNNNNNNNNN NNNNNNNNNN NSPKKKIRKS KNNNTTSTIS NTQSNLIGTE SPSKNQNKQL
     ERELKSKKKK QQSAILEQIV EEEDINFEIP TNENYYDYGS GSCFDNNDDN DDGYISSGIN
     TTPDDLNKSF NFDFGSFDNG IPNYNNNNDN GGDNENNINS DIDSNKIKTT TSINDNHKEK
     YQKNNENYIH ENEDNGDDVI VLISPIKTYK YGDMLNKSPS KFKSPSKLRS HNTTNTFNNS
     NFSNSDNDNN NNIRITTPLK NQNFNKFNDS IIFSPSISSP SPSKLSNYHK YLNNNNNNIK
     NTPISTSKKR KCNFSSPLLF SPFKYGVTSP FSPSKMKLKS PFKKRFKNDK SPSSSISKNK
     NSKSNDIVNN DFEDDDEVVN IQSESEINNN NNQFTSHNDN YNYSYNYNNN SNNINNNNNN
     DDDDDFDLTE TEDEKDDYDK DDRTFSNLSV RLSFTEEDLA GVNIGESIIN NSKLPKVIPS
     QIPPPTQSTQ STSTSTSTSK SKSKSTIKIK FKNIKCIIDN REVKSVTERD YICNKLNERG
     INAQVKKLEL GDFVWVAIDE HDNEWLLNYI IERKRVDDLS SSIIDGRYKE QKFRLSKSGC
     DNIIYLIEGI VSNTINSSSQ SQKKTWGTVN FSLSPDALAT ALVTTSICEG IIIKETKTID
     NTIDYIVNIT EYFKEKLLKN NNSGGGGGDE IIKFLFANKN TQCTLENFNQ LNSKSKGLKL
     IEFFATQLIQ IPGCSAEKAH SITQVYPTPM SLYLALKAIK DKESGESHFK DFTFGKNKRR
     FGQDVSEVIY NLYTNKKYLN
 
 
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