ID   SLX4_AJECN              Reviewed;         834 AA.
AC   A6R4H9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=HCAG_04537;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(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; CH476658; EDN08027.1; -; Genomic_DNA.
DR   RefSeq; XP_001540697.1; XM_001540647.1.
DR   AlphaFoldDB; A6R4H9; -.
DR   SMR; A6R4H9; -.
DR   EnsemblFungi; EDN08027; EDN08027; HCAG_04537.
DR   GeneID; 5447106; -.
DR   KEGG; aje:HCAG_04537; -.
DR   VEuPathDB; FungiDB:HCAG_04537; -.
DR   HOGENOM; CLU_016773_0_0_1; -.
DR   OMA; TWHEKIL; -.
DR   OrthoDB; 231792at2759; -.
DR   Proteomes; UP000009297; 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..834
FT                   /note="Structure-specific endonuclease subunit SLX4"
FT                   /id="PRO_0000388008"
FT   REGION          80..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   834 AA;  91204 MW;  DC9D9C30BD6681CC CRC64;
     MDNTAITSQS SSTPLVCSVT PIIVGSPPSP ANVIELSSPS TPPTPLTLLA SLSETPSRKT
     TNPDTNGENT ICHGVRQVRR VPRNNPVTGP SKEHKQRTRS PKTTTRREIK IVEGDRLIVG
     HDKREKKGET TKRMKKRDGV ADKKLYARVS KVKSSENLDL DAKIPSSKVC NNTLPLVGDD
     MDNGSSELKL EQAIKRRHDW TPTREVTTPV VDVAELHSSP CGKAVTRMHG VGTLLSDYGF
     SGVVETSLGT KSESFRNAPT TKRPMELQKF STVPAIPTPT ESSTTEDVQG SSSKQQRVKA
     KKPQKGKLTT ITSHATAKYC VADQTVDLDY IQNVAPKSPR RKNISNRPSG TKHSNSGRGK
     SSTLKNDNGR PVFRVVPPLE AFKSFEGQEL LFGTSSQLER GYPEYPCDET QDTQNSPSNS
     AAVSELAVPY RISSEGKDLG SSLFGLSGSK NLWSASARDL TGAVFEGDEI DFQGASMGLS
     VLATKSRCHP GNRGPPRRNL VDVDNVPDKK LDIDTTEGEN GNHSSVADNI VDRENLNPKI
     SANTSETNLE CAPQNKPAFS RFTTSELAKK VAAYGFKPIK SRDNMISLLE KCWETQSKTL
     ILESKPNQGT DDARKNGFRK ENHSDVRVRP DSATLANRRS PKKQQAKALS KFQEPNNFLP
     IENSTTTASM LPIISSHTIL INDDQLSDSV GETVSFLPSL DHNGNGTTIQ ENMLEIKSPA
     TPNARRSRQG SSSASFSIEP PSLASQITKA IKSQPRTRAF NGLKQPTWYE KILMYDPIQL
     EDLAAWLNTD GFGRIGEDRE VGPGVVREWC ESKGVCCVWK KQVSGRSHYL PMVS