ID   SLX4_AJECG              Reviewed;         843 AA.
AC   C0NBH5;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=HCBG_00471;
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEH11016.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; GG663363; EEH11016.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C0NBH5; -.
DR   SMR; C0NBH5; -.
DR   PRIDE; C0NBH5; -.
DR   EnsemblFungi; EEH11016; EEH11016; HCBG_00471.
DR   HOGENOM; CLU_016773_0_0_1; -.
DR   InParanoid; C0NBH5; -.
DR   OrthoDB; 231792at2759; -.
DR   Proteomes; UP000001631; 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..843
FT                   /note="Structure-specific endonuclease subunit SLX4"
FT                   /id="PRO_0000388007"
FT   REGION          26..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   843 AA;  92634 MW;  61C803D9BECA5B74 CRC64;
     MDNSAITSQS NPTPLVCSVT PIIVGSPPSP ANVIELSSPS TPPTPLTLLA SFSKTPSRKT
     TSPDSNGENT ICHGVRQVRR VPRNNPGREK KSITGPSKEH KQRTRSPKTT TRREIKIVEG
     DRLIVGHDKR EKKGATTKRM KKRDGVADKK LYARVSKVKS SENLDLDAKI PSSKVCNNTL
     PLVGDDMDNE SSELQLEQAI KRRHDWTPAR EVTTPVVDVA ELHSSPCGKA VTRMHGVGTL
     LSDYGFSGVV ETSLGTKSES FRNAPTTKRP MELQKFSTVP AIPTPTESST TEDIQGSSSK
     QQRVKAKKPQ KGKLTTITSH ATAKYCVADQ TVDLDYIQNV APKSPGRKNI SNRPSGMKHS
     NSGRGKSSTL KNDNGPPVFR VVPPLEAFKS FEGQELLFGT SSQLERGHPE YRCDETQDIQ
     NSPSNSAAVS ELAVPYRISS EGKNLGSSLF RLSGSKNLWS ASARDLTGAV FEVDEIDFQE
     PSMGLSVLAT KSRCHPGNRG PPRRNLVDVD NVPDKKLDID TTEGENGNHS SVADNIVDRE
     NLNPKISANT SETNLECAPR NKPAFSRFTT SELAKKVAAY GFKPIKSRDN MISLLERCWE
     TQSKTFMPES KPNQGTDDAR KNGFRKENHS DVRVRPDSAT LANRRSPKKR QAKALSKFQE
     PNNFLPIENS TTTASMLPIE HVISSHTILI NDDQLSDSVG ETVSFLPTLD HNGNGTTLQE
     NMLEIKSPAT PNARHSRQRS SSTSFSIEPP SLASQITKAI KSQPRIRAFN GLKQPTWYEK
     ILMYDPIQLE DLAAWLNTDG FGRIGEDREV GPGVVREWCE SKGVCCVWKK QVSGRSHCLP
     MVS