ID   SLX4_TALMQ              Reviewed;         792 AA.
AC   B6QL24;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Structure-specific endonuclease subunit slx4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=slx4; ORFNames=PMAA_055930;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(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; DS995903; EEA21801.1; -; Genomic_DNA.
DR   RefSeq; XP_002150410.1; XM_002150374.1.
DR   AlphaFoldDB; B6QL24; -.
DR   SMR; B6QL24; -.
DR   STRING; 441960.B6QL24; -.
DR   EnsemblFungi; EEA21801; EEA21801; PMAA_055930.
DR   GeneID; 7027915; -.
DR   KEGG; tmf:PMAA_055930; -.
DR   VEuPathDB; FungiDB:PMAA_055930; -.
DR   HOGENOM; CLU_016773_0_0_1; -.
DR   OrthoDB; 231792at2759; -.
DR   PhylomeDB; B6QL24; -.
DR   Proteomes; UP000001294; 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..792
FT                   /note="Structure-specific endonuclease subunit slx4"
FT                   /id="PRO_0000388039"
FT   REGION          59..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..637
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   792 AA;  86858 MW;  8011E95A874EEB6E CRC64;
     MASKFDNTIV IPASSPEQNW ARSVSPCTPS RLFGLSPLSP SPPSLLSPSK LFDEVRLKMQ
     NDQPSPKSPL GKVSKKATAP ITTAGTPIVS EHFTQTARSG SSKAKTIRNR KSSKSQEGQN
     KILTGRVAKA TATSKAKDTT GSKLNAGTKK TKTTSNSQDD KPTKEAETKK VVDSEGLNLE
     EALKRRSDWT PPKASVPAII SLDEDSPSGN CGAKTSFGYS LRDYHYSRDN SVSEAILPRK
     EGNPTKRRRL ELVESEILQE RKPLQQRQTK DAEKTRKTKA KPKKHPKTIT ARMTALYEPI
     DETEGLFVFD EELEAGEDFK KPAKPKKKTS TKQKEPDCVI LSPAAATKSL NDQNFLFGTC
     SQLERDDSPT FFEETQKAIR LSENLTLENP ALSTISTVPS TTSIVIKYTS KKSHWSEAAR
     DFHGAVVQPE IIDMTDSPTI DTALSQLSEM NREAPKMASL VSAKPTSGIK PLTEKEIIPS
     CRPTADIQST SSKPKSNKIG PDIVGKKAEP STKKPTNQLP EMPNFNGYTD VELRKKVKSY
     GLKAIGRRKR LIALLDKCWQ SKHGNVATSA DDVETSSLAA INGTASVSTA RISDTQVSEE
     LPVRKKSDGE SKAASRAGKR KVVEKPAARK DETAAKKAAS PIRTSSYMVD EIEDSEEEII
     PSPTRIRVQR QSSTRQTTPA IGCLPLGSKS KRPSTKNKAS TFDECTLIEL QSSIARAIRL
     QTRPKNLLTN GSCPPQLTWH EKILLYEPII LEDFATWLNT EGFALVSEDR EVGVALVRTW
     CESQGICCTF RA