ID   SLX4_BLAGS              Reviewed;         856 AA.
AC   C5JR12; A0A179URQ6;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=BDBG_04672;
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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; GG657456; OAT09112.1; -; Genomic_DNA.
DR   RefSeq; XP_002624808.1; XM_002624762.1.
DR   AlphaFoldDB; C5JR12; -.
DR   SMR; C5JR12; -.
DR   PRIDE; C5JR12; -.
DR   EnsemblFungi; OAT09112; OAT09112; BDBG_04672.
DR   GeneID; 8504567; -.
DR   KEGG; bgh:BDBG_04672; -.
DR   VEuPathDB; FungiDB:BDBG_04672; -.
DR   HOGENOM; CLU_016773_0_0_1; -.
DR   Proteomes; UP000002038; 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..856
FT                   /note="Structure-specific endonuclease subunit SLX4"
FT                   /id="PRO_0000388010"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          38..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..736
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   856 AA;  93074 MW;  EACF1D26738BCB57 CRC64;
     MDNAAIASQS NTPPSNGRSS ARFVTPISVH SSPISAEVIE PSSPFSPPSP STLLTSLSKS
     PSHKISNLQM DGAKTTCLEV IQNSSLVVDS PKRQDKSITG SKAKPASTMR HGQRTASHKM
     ATQTEIQTVD GDRLIVSPKT RKKKAATAKR TRKQDGVAER RLHGHVSKVK SPGDLKLDAK
     IPPSKPCDNK APSVGDNTDN ELERQTGGLQ LEKATKRRLD WTPTKEGPIP MVDLAEVHSS
     SCGKSVIRTH SAGTLLSNYG FSGVVNTSLA PMPETCDNGP TTKRLMELQN FYSASGIQTP
     TESRPATNDS QSISSKQQRV KVKKPQKAKL TTLTSYVTAK YSVVDQTADL DRIETVNSGK
     NKKMGVTKRT SGTERANAAR GKSDTLKNGN GPPVFKVVPP LEAFKSFDGQ ELLFGTSSQL
     EHGHSEDQDE EIQHTADSIN KSNVVPRPAV SKGLGSSLFR LSSSKNLWSA SSRDLTGAVL
     QVDEIDLSER SIEVSTPAAK YKRKTGIRDL SGQNVIDVEK DTRTLAANID TRELDNMNEP
     SLAEDDLVYR ENLESTNAKL NSQTPANISE AMLERPPPDK PIFGGFTTSE LAKQVAAYGF
     KPIKSRDKMI SLLEKCWENQ SKSSKLEPKP NQRNHKSQGD DLAERQLLGL KPRSDSISFV
     ITRSPKKRLA KTSVKSQEPK SFSLSNEGPR ITSKLPMKRF VSPCAILIDD DQSSDSVGEA
     LPLSPSHSSN GNGTLHHPQD CDEIHAPTTQ MAIRSAKSSI SVSSTTNLPS LSSQITKAVQ
     SQPRIRAFKG LKQPTWYEKI LMYDPIQLED LAAWLNTGGF GLIGEDREVG AGVVREWCES
     KGICCVWKKQ ASAKSH