ID   SLX4_UNCRE              Reviewed;         818 AA.
AC   C4JJE8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=UREG_01755;
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704;
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; CH476615; EEP76906.1; -; Genomic_DNA.
DR   RefSeq; XP_002542239.1; XM_002542193.1.
DR   AlphaFoldDB; C4JJE8; -.
DR   SMR; C4JJE8; -.
DR   EnsemblFungi; EEP76906; EEP76906; UREG_01755.
DR   GeneID; 8443808; -.
DR   KEGG; ure:UREG_01755; -.
DR   VEuPathDB; FungiDB:UREG_01755; -.
DR   eggNOG; ENOG502SEB3; Eukaryota.
DR   HOGENOM; CLU_016773_0_0_1; -.
DR   InParanoid; C4JJE8; -.
DR   OrthoDB; 231792at2759; -.
DR   Proteomes; UP000002058; 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..818
FT                   /note="Structure-specific endonuclease subunit SLX4"
FT                   /id="PRO_0000388049"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..712
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   818 AA;  89414 MW;  FBF7E95B45C9F424 CRC64;
     MSFLNSSRRR TRSPSPGQIF APSATPIVID SSPSVPSASS ILDSLLGEFS EARDPYTVEA
     GPTGRSSDHL FSSPGVLTQS PGRENVPPRP SERTKDAHGK DRFLVSTERN GRSPFRGNPY
     RSAEIHSPKG RLKAPTKEGG TRKTKKFSSS NRTLTGRSTK FLAKTASKPT QSSKVPSEIP
     AAKLDSLQWE DGELRLELAT TRRGSWTPIK DTSIDIVDPT RNLSPSNVSA AGSQKFSSML
     SDYGFTKGST LTMENELRRE VPTTKRRLEL LQGTANDIFS EGDFSRPPEK SVVNPNGTHS
     RRSRKTTSTT ITSLSTAQYG HQDSRQMSNL ADFFPSGEAV ERPSGAIKKL KTSKSGTKKK
     GVKKAKEAPL FKVASIEDAL KSLEDQVCLF GTSSQLERVS SDEEPQMANF NLNAQFPRKN
     SRPQKTRSPC SNPKTSKSLW YASSRGYDDI EFVDMIDSSN PKTLESVEAS TFVTPIDSSP
     MHSQVASQMV FENPCDVSHV LTKIPQTGPK DPIENPVCPE IQIRHSGNVK TQSTSGQSIP
     SFRGLTTAQL AQKVASFGFK PLRSREKMIS LLEKCWESQQ QTHIPAMLPA SHTALPDSVT
     RAEQMSKRDT IKSRDIRASK SRSNSNHIPG LVSSTSQNTG YAAKSPDCIR GSSKSNDIGT
     TQGSPLLTTQ SVIVIPDSDD SDNDNNPTGG AYSYPSLASN TPSSSTRTMA SESLLSVRTR
     YEANVGEEQG SNDINQQITK AIRAQPRLVA INGVKRPTWL EKILMYDPIV LDDLTVWLNT
     EGLDQIGEDS EVSGTTVREW CESKGICCTW KKKRHVAP