SLX4_YEAS6
ID SLX4_YEAS6 Reviewed; 748 AA.
AC B5VN64;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=AWRI1631_121840;
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631;
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
CC -!- FUNCTION: Regulatory subunit that interacts with and increases the
CC activity of different structure-specific endonucleases. Has several
CC distinct roles in protecting genome stability by resolving diverse
CC forms of deleterious DNA structures. Component of the SLX1-SLX4
CC structure-specific endonuclease that resolves DNA secondary structures
CC generated during DNA repair and recombination. Has endonuclease
CC activity towards branched DNA substrates, introducing single-strand
CC cuts in duplex DNA close to junctions with ss-DNA. Has a preference for
CC simple Y, 5'-flap and replication fork-like structures. It cleaves the
CC strand bearing the 5'-non-homologous arm at the branch site junction
CC and generates ligatable, nicked products from the 5'-flap or
CC replication fork substrates. Plays a critical role in maintaining the
CC integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-
CC starting stalled replication forks. Has Holliday junction resolvase
CC activity in vitro. Interacts with the structure-specific RAD1-RAD10
CC endonuclease and promotes RAD1-RAD10-dependent 3'-non-homologous tail
CC removal (NHTR) during repair of double-strand breaks by single-strand
CC annealing. SLX4 also promotes recovery from DNA-alkylation-induced
CC replisome stalling during DNA replication by facilitating the error-
CC free mode of lesion bypass. This does not require SLX1 or RAD1-RAD10,
CC but probably RTT107. {ECO:0000255|HAMAP-Rule:MF_03110}.
CC -!- SUBUNIT: Forms a heterodimer with SLX1. Interacts with RAD1; catalytic
CC subunit of the RAD1-RAD10 endonuclease. Interacts with RTT107.
CC {ECO:0000255|HAMAP-Rule:MF_03110}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03110}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03110}.
CC -!- PTM: Phosphorylated by ATR (MEC1) and ATM (TEL1) upon DNA damage. This
CC appears to be required for the function with the RAD1-RAD10
CC endonuclease. {ECO:0000255|HAMAP-Rule:MF_03110}.
CC -!- SIMILARITY: Belongs to the SLX4 family. {ECO:0000255|HAMAP-
CC Rule:MF_03110}.
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DR EMBL; ABSV01001611; EDZ70630.1; -; Genomic_DNA.
DR AlphaFoldDB; B5VN64; -.
DR SMR; B5VN64; -.
DR Proteomes; UP000008988; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Cytoplasm; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Phosphoprotein.
FT CHAIN 1..748
FT /note="Structure-specific endonuclease subunit SLX4"
FT /id="PRO_0000388044"
FT REGION 62..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphothreonine; by ATR and ATM"
FT /evidence="ECO:0000250|UniProtKB:Q12098"
FT MOD_RES 113
FT /note="Phosphothreonine; by ATR and ATM"
FT /evidence="ECO:0000255"
FT MOD_RES 289
FT /note="Phosphoserine; by ATR and ATM"
FT /evidence="ECO:0000250|UniProtKB:Q12098"
FT MOD_RES 319
FT /note="Phosphothreonine; by ATR and ATM"
FT /evidence="ECO:0000255"
FT MOD_RES 329
FT /note="Phosphoserine; by ATR and ATM"
FT /evidence="ECO:0000250|UniProtKB:Q12098"
FT MOD_RES 355
FT /note="Phosphoserine; by ATR and ATM"
FT /evidence="ECO:0000255"
SQ SEQUENCE 748 AA; 84362 MW; 52C0FD889C8C5835 CRC64;
MELQRAQRNL KFLQNEDYVN VTDQTNLNGE SQNAYSLGME TQVPEMQFSL SSDDDSIGTQ
VKSVTAQKSP MTQETTKNDT ERNKDVDKSC NPVSTSHPDL GGSNIEENIF INTQIQSRLD
DAEEETNLKL KLEKFKYSFK SSNADDTHSN ANVTAKRRPA IRKANSKLKT KPKTKRDPKI
IKNITDFNIN NYERSRTASL LKQLSGKHKK VLDIIKTQNE GNSDKPPRAR NNKGEKATFD
TYSEQEWKDI MKLLLQKFPQ SEETDLNEVQ KFLYGSEKSS NSLDNQESSQ QRLWTASQLP
PELPDEAIQP EQEERIRDTQ SAVNFLSLSQ VMDDKSEIMK DEESIIISRG DSTSSQEYGN
GLEPQQPVGN VVGEDIELAV GTRINAFSLT DYKACKPMSV EVSRRCENST DNDYDNISIV
SDTTDETSTL FPLDQYRYVF IENDERPPLA TDTIGSTQFF TPNTSPLDGI IDLTQESFKA
VRSLISPLKV ENNKTGVTSQ ASNQVQVPAT RTPTIIPQKN LTTTLKTEEE KNNIGSSIRV
KLLQESVVKL NPKLVKHNFY RVEANDSEEE ETEFDDQFCI ADIQLVDSSK ISTKDSTQNP
TTSNDIIDTS AASSIASPEK FCEIMMSQSM KELRQSLKTV GLKPMRTKVE IIQSLQTASQ
ILSTANPDNK GEHGGVANFS KIEIFDHLTE LIEAFPDFLE RIYTFEPIPL NELIEKLFSA
EPFVSQIDEM TIREWADVQG ICLRNDKK
