ID   SLX4_CHAGB              Reviewed;         958 AA.
AC   Q2HCM6;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=CHGG_02028;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAQ93793.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH408029; EAQ93793.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001221249.1; XM_001221248.1.
DR   AlphaFoldDB; Q2HCM6; -.
DR   SMR; Q2HCM6; -.
DR   PRIDE; Q2HCM6; -.
DR   EnsemblFungi; EAQ93793; EAQ93793; CHGG_02028.
DR   GeneID; 4388104; -.
DR   eggNOG; ENOG502SEB3; Eukaryota.
DR   HOGENOM; CLU_005957_0_0_1; -.
DR   InParanoid; Q2HCM6; -.
DR   OrthoDB; 231792at2759; -.
DR   Proteomes; UP000001056; 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:0003677; F:DNA binding; 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; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR027784; Slx4_ascomycetes.
DR   InterPro; IPR018574; Structure-sp_endonuc_su_Slx4.
DR   Pfam; PF02178; AT_hook; 3.
DR   Pfam; PF09494; Slx4; 1.
DR   PRINTS; PR00929; ATHOOK.
DR   SMART; SM00384; AT_hook; 3.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..958
FT                   /note="Structure-specific endonuclease subunit SLX4"
FT                   /id="PRO_0000388025"
FT   REGION          89..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..672
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..774
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   958 AA;  102188 MW;  7229153B993FE9A7 CRC64;
     MAHHDSVLVI SSSPDFPSIC DLLPKATRQP SLRSGSNAAP VSNDAPAAFT SAANIWQSSR
     ARHLEGAEIS NIGPSQSATT AADLATVPAE SPIKSGVEGP TLPLGGDKKK PRTAGARKKK
     GKTETIEPPL ALDMAVADGP VAVAPPKKSG RKPRAKKDAT LAQTTLPKGK VTKTAAREIT
     KAQKKAETVS RHFTPHTSAP PELVAGPIDD SPSVFEPAMA RRMDWTPPRE SASVHCLADS
     SMEKEVSSSA LSLQDHVFKN LQDTYGRTME ASGYIGAALP LTSMDVLGKR KLVEMVSCVG
     HRQEIPQASP TKPKVVKKKP RTITELATAA YRRPEEAERS TLSRQQDTHI PSGNLELPSE
     QLTAASKSAS AKPKAAKKAP KPRATKKKQS PPEPILLSPT SAMRQVSNQD FVFGTASQLA
     TEDDPVLLRA LHEAMKVSNQ ADSDPFATPS PGNSNLAIRR RSGAGLWAAG ARYGDGDLLD
     AEVLDLTRSS PLTLAQFAQN PPPPCPEAVL ADKPPVESAY IEIEMSDDTL DLTISPPVGS
     PKTLPPCPPR PGGQAVRHKD SNLAVSGRPQ TPPQEADFDP PPSNQEQHQL LLSQSNTPQQ
     PQPAPPPPPS FELYTDARLA KEVASYGFKV VKKRTAMIAL LNRCWESRNK TALGSTAAQA
     AMSTSAPNQA ASPSRPRGRP RKDSLTATTE VVQAPSPAKK GRKKAGVVSG AGSEVPQPEK
     WPRGRPRKDS AASVSSITAP AATNPRRRSA AISDVDSDEP QVEKRSRGRP KKDATTSPAT
     RATRAKAPPS PKRAKSPCTT QPAPTTPRRR KAPAKQIFEI PDSGSDDPFA SSAPSSPDQH
     SDLFSSPPAV DLSVTEDTEA SLIASPTTQD VSLFGYITRA VASAPPTKDP ANPSWHEKML
     MYDPIILEDL TAWLNAGRLD QVGFDGEVAP GDVKKWCESK SVCCLWRVNL RGKERKRF