ID   SLX4_NEUCR              Reviewed;        1013 AA.
AC   Q7SFJ3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Structure-specific endonuclease subunit slx4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=slx4; ORFNames=NCU08628;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002236; EAA35600.1; -; Genomic_DNA.
DR   RefSeq; XP_964836.1; XM_959743.2.
DR   AlphaFoldDB; Q7SFJ3; -.
DR   SMR; Q7SFJ3; -.
DR   STRING; 5141.EFNCRP00000008653; -.
DR   PRIDE; Q7SFJ3; -.
DR   EnsemblFungi; EAA35600; EAA35600; NCU08628.
DR   GeneID; 3880996; -.
DR   KEGG; ncr:NCU08628; -.
DR   VEuPathDB; FungiDB:NCU08628; -.
DR   HOGENOM; CLU_005957_0_0_1; -.
DR   InParanoid; Q7SFJ3; -.
DR   OMA; TWHEKIL; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..1013
FT                   /note="Structure-specific endonuclease subunit slx4"
FT                   /id="PRO_0000388034"
FT   REGION          63..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          755..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..211
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..842
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1013 AA;  109921 MW;  3A657D707A10E02C CRC64;
     MAHNDTIDII SSSPEFPDIS VLVAKAASKK SALRTGSNAT PIPSDAVGLG TFTSAASIWH
     LSQVMDEEKP TKNSSSRPAK ETPAIATSVS TVAVEVSATT TTAVSEEKPG KKPRKPRKKK
     DETTAAVDEN APPKPPARRG RPPKQKDVEG QPALPKSKAT KPAAKPRASR KKAETVSKHF
     AASAHASTAD PPEEPSKNPA ASKPPKPIPV QNIDEPVDLE PAARRRLDWT PPPDDRPPPA
     AGNSSVVKEL PSSTTAHTEP PVAFGKLLDT YGCEPETIQP SEGTKGNVLG KRKLIEMVAT
     TTTTNTATDK LTSPETSPTK PKAPKKKPRT ITDLATAAYR IQDPVDDSIS TVAPKQDTLL
     GYIDVEDEDA AVKPGGAKTK AVSKKPAKAR VSKKKPEPRK QLLLSPHSAL RQVSGQNFVF
     GTSSQLVTED TDLLRALHES MKTAGNAQES DPFMSSPVKF SNIASRSKMG NNKLWRVGAR
     DEDGDLLDLE IFDLTEAVEV PEDVVQQADK PAVDVPEREA SPRKQVEREA ERAIGIFSSD
     PVATERLTIT GPETLISTLS IKGKESVRRT TKSPPPNPVA PPRERTPQRA RPPSRDSLSS
     RLRSPQTETS PRPTTPPRVS AVLDLDYDFD DYEPPPSNQE HYQLLEQSQK TSPSKTQQRK
     QQQQQQQQQQ QQQKKRDPPP RPKYEVFTDA QLSREIASYG FKPIKKRAAM IRLLEQCWES
     KTGAATGKST GLGDNTLQEG TGSLEPAHRS INSVAVSPDR GRGQTIQGAH MQEARAGIKM
     AASATKRPRK KAAVASASAP RTSTMENPPK AATAASTSTT TAPLPALSAS TSKRQRRTSL
     SSIRPRPPIL EIPDSDIDIS DSDPFASSPP VSSPDASPPA SQLFSTPEKH HQDHKHDLAA
     EMSLITDCEE SLLDMTSRTP SEADLFKHIT EAITTAPRTT NPSEPSWHEK ILMYDPIILE
     ELTAWLNTAG KGLDRVGWEG CEAGTEEVRR WCESKGVGWV WREGNRGQVR KRF