ID   SLX1_YEAS6              Reviewed;         304 AA.
AC   B5VEH8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Structure-specific endonuclease subunit SLX1 {ECO:0000255|HAMAP-Rule:MF_03100};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
GN   Name=SLX1 {ECO:0000255|HAMAP-Rule:MF_03100}; ORFNames=AWRI1631_23050;
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: Catalytic 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. Has a preference for simple Y, 5'-flap
CC       and replication fork-like structures. It cleaves the strand bearing the
CC       5'-non-homologous arm at the branch site junction and generates
CC       ligatable, nicked products from the 5'-flap or replication fork
CC       substrates. Plays a critical role in maintaining the integrity of the
CC       ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled
CC       replication forks. Has Holliday junction resolvase activity in vitro.
CC       {ECO:0000255|HAMAP-Rule:MF_03100}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03100};
CC   -!- SUBUNIT: Forms a heterodimer with SLX4. {ECO:0000255|HAMAP-
CC       Rule:MF_03100}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100}.
CC   -!- SIMILARITY: Belongs to the SLX1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03100}.
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DR   EMBL; ABSV01000169; EDZ73665.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VEH8; -.
DR   SMR; B5VEH8; -.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
DR   GO; GO:0033557; C:Slx1-Slx4 complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.1440.10; -; 1.
DR   HAMAP; MF_03100; Endonuc_su_Slx1; 1.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR   InterPro; IPR027520; Slx1.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF01541; GIY-YIG; 1.
DR   SMART; SM00465; GIYc; 1.
DR   SUPFAM; SSF82771; SSF82771; 1.
DR   PROSITE; PS50164; GIY_YIG; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW   Metal-binding; Nuclease; Nucleus; Zinc; Zinc-finger.
FT   CHAIN           1..304
FT                   /note="Structure-specific endonuclease subunit SLX1"
FT                   /id="PRO_0000383805"
FT   DOMAIN          12..95
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         218..282
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
SQ   SEQUENCE   304 AA;  35778 MW;  09E5B56C9240B9C3 CRC64;
     MSQKIQQHQF PDFYCCYLLQ SINKRQSFYV GSTPNPVRRL RQHNGKLAVG GAYRTKRDGS
     RPWEMIMIVR GFPSKIAALQ FEHAWQHGYQ THYIAEKDRV VKHKAGGRTL HHKVALMKLL
     LKHEFFQRMN LIVDVFNIKA WEVWKQDKFF IERDRFPINI QINENALEEP KEKTVDVLMD
     HSDENLKVVE AVYTKVIENE RNIFETFEKK LTTGVVRCEI CEKEIDYTSE EQNLKPFVAL
     CNNKDCGSVN HLKCLHRYFL DDEQLIVGRR NLIPRGGKCP KCDTFCDWTT LVKFSTRMKL
     AHGK