ID   SLX4_SCLS1              Reviewed;         922 AA.
AC   A7F2D1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Structure-specific endonuclease subunit slx4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=slx4; ORFNames=SS1G_12078;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476639; EDN95873.1; -; Genomic_DNA.
DR   RefSeq; XP_001587049.1; XM_001586999.1.
DR   AlphaFoldDB; A7F2D1; -.
DR   SMR; A7F2D1; -.
DR   STRING; 665079.A7F2D1; -.
DR   PRIDE; A7F2D1; -.
DR   EnsemblFungi; EDN95873; EDN95873; SS1G_12078.
DR   GeneID; 5483213; -.
DR   KEGG; ssl:SS1G_12078; -.
DR   VEuPathDB; FungiDB:sscle_05g040650; -.
DR   eggNOG; ENOG502S832; Eukaryota.
DR   HOGENOM; CLU_005957_1_0_1; -.
DR   InParanoid; A7F2D1; -.
DR   OMA; TWHEKIL; -.
DR   Proteomes; UP000001312; 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..922
FT                   /note="Structure-specific endonuclease subunit slx4"
FT                   /id="PRO_0000388047"
FT   REGION          86..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          717..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..656
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   922 AA;  101156 MW;  A211527EB23BC539 CRC64;
     MATTDVFIIS SSPPRRLVSH IASSPPLPSL DKMVNGKKAS NLRQGSSVAP IPTGATIFAS
     ASTLLRESSS GSLQGFDNAR SFVTSAVQDE NDLKKSAKPK APRKTAPKKE DGTVEKVAKA
     SRKTVKKKDK DVSGDFVDEL VGEAAEIIAE KKPRKPRAKK GDNAEGKSGS VAEATVEKKP
     RKSRAKKAVD ATGEDLKEKV PRKSRAKKTD VEAGIETVPK EKAVRKPRAK NSDLDSNLQS
     KMVKGRVTKS AVNASNTHKV ETSKADTGNK HFAPNPIVED IVADEGFGLV EAIRRRTNWT
     PPKSTKVPID LEDSPEAQES DTSKGFAELL GSFGYSSYQA DSIEKRISSG VSNGAAATRK
     RKLIEMVTTN IPREPGSKTT KEKAVKKKAR TLTDLATSAY ATAEDDDNLL DAPTPLLQYF
     PHAAPEGSTN NGFKIPPKPR SKSPMKRVQK SKTGSAEEPI LLSPESAMKQ VSNQDFVFGT
     SSQLAREDSP SLLRDLHDAM QASNELDDYD DPFVSPPTKI AERGKAVVAA KRNLWSIAAR
     DNHGDLMDVE TIDLAHTPVA KPDRIMLSQK PSSLVTPGKD DWFDIDEIED NRPPSTQVPL
     RETGPIERSI NFQLLDSPTQ PKNTSKDSSK VFPQKKGTKS LVDKSTTPKK VDASKMPDYE
     SFTTPQLTRE IQKYKFKQIK SRKRMIDLLI QCYESQNRPA LGVLQGNIPI ITQNSLEKSK
     DVADSSTQVK PTIPSPRRGR AKKVTTSTAS LPKSKAKSKM TDTVAFLEMD SDTPLSKIRT
     PQKSRKGKQP LEDIFDSDHP ITPSPPRRSD SQIRKISKAL ELSPDNNQDD EAQQAQLFTH
     IYTAITKAPP SQDPFNPSWH EKILLYDPII LEDLASWLNT GALSKVGWDE EVAPLEVKKW
     CESKSICCLW KENQGGGARS RY