ID   SLX4_PICGU              Reviewed;         681 AA.
AC   A5DIU9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=PGUG_03200;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Regulatory subunit of the SLX1-SLX4 structure-specific
CC       endonuclease that resolves DNA secondary structures generated during
CC       DNA repair and recombination. Has endonuclease activity towards
CC       branched DNA substrates, introducing single-strand cuts in duplex DNA
CC       close to junctions with ss-DNA. {ECO:0000255|HAMAP-Rule:MF_03110}.
CC   -!- SUBUNIT: Forms a heterodimer with SLX1. {ECO:0000255|HAMAP-
CC       Rule:MF_03110}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03110}.
CC   -!- PTM: Phosphorylated in response to DNA damage. {ECO:0000255|HAMAP-
CC       Rule:MF_03110}.
CC   -!- SIMILARITY: Belongs to the SLX4 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03110}.
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DR   EMBL; CH408157; EDK39102.2; -; Genomic_DNA.
DR   RefSeq; XP_001485471.1; XM_001485421.1.
DR   AlphaFoldDB; A5DIU9; -.
DR   SMR; A5DIU9; -.
DR   EnsemblFungi; EDK39102; EDK39102; PGUG_03200.
DR   GeneID; 5127109; -.
DR   KEGG; pgu:PGUG_03200; -.
DR   VEuPathDB; FungiDB:PGUG_03200; -.
DR   eggNOG; ENOG502RS18; Eukaryota.
DR   HOGENOM; CLU_429039_0_0_1; -.
DR   InParanoid; A5DIU9; -.
DR   OMA; CKEPAND; -.
DR   OrthoDB; 1409030at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0033557; C:Slx1-Slx4 complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR   HAMAP; MF_03110; Endonuc_su_Slx4; 1.
DR   InterPro; IPR027784; Slx4_ascomycetes.
DR   InterPro; IPR018574; Structure-sp_endonuc_su_Slx4.
DR   Pfam; PF09494; Slx4; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..681
FT                   /note="Structure-specific endonuclease subunit SLX4"
FT                   /id="PRO_0000388041"
FT   REGION          239..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..282
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  76784 MW;  24A8C2FFE5B2F04D CRC64;
     MSNDVYFESI HMQSNYEEFE TQAQERENIS KISTSLSKFR KMSPKSTRSF KVKSAPLTNR
     KARNRIKSIN AHVSAQYKVS NGQQNDDILD FFLKRKHNIS SILEGVEDLE NRNIVSNDTP
     QPSDNTGNYS SQLFTQEEWF QILRRIKLRF PKLSARTRKS LKYVTTKLEH LKNINSDDDS
     PQLWTQAASL PEEGLVNEDM KWLYELDDEQ MDIGSSFCNV DEDSDQKLFV LTLSQAMGER
     EKSEPDVEII SDSSPEPTQL LNDGIIEEEH EVDEEEEDNE NEEKSEKQLA SSPTQISSDD
     TQEQLTNRAE ISSYEASSLF PNTLETQKQP VKSTIQKQAS VVVPDYPKIS NVKDEEIILS
     SSPTRDNEIF QTPRKYSVES VRSSPSSRSG RLGRLMVSPL KLLSPDRLDA SQSVYSTARS
     SPTKQKRVRG REVNEKIVRK RFKTSRVEVA GNFHLKASDD LKIVSTVDKV NGSEVEDSED
     DDHSVSIIEI THEVNDEELK AVDEEVTGEA EDGPSIIQVP SSPGNENLQE DLTSMQTSIA
     SVTQEVPSNY TATQMRQALR SLDFPPERSK EGMASSLTRA ASIAGTSVSS LLTPDAPYEE
     VKNQIYSAIS ESVKKDQLWH ERVLSYEPIV LEEFKQWLGE LDKDLKFDVT FLQQYCDHMG
     ITTTIGTTTG TTAGTNTTTT D