ID   SLX1_PICST              Reviewed;         336 AA.
AC   A3LZG5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 77.
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=PICST_90954;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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. {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; CP000501; ABN68333.2; -; Genomic_DNA.
DR   RefSeq; XP_001386362.2; XM_001386325.1.
DR   AlphaFoldDB; A3LZG5; -.
DR   SMR; A3LZG5; -.
DR   STRING; 4924.XP_001386362.2; -.
DR   PRIDE; A3LZG5; -.
DR   EnsemblFungi; ABN68333; ABN68333; PICST_90954.
DR   GeneID; 4840669; -.
DR   KEGG; pic:PICST_90954; -.
DR   eggNOG; KOG3005; Eukaryota.
DR   HOGENOM; CLU_030739_1_1_1; -.
DR   InParanoid; A3LZG5; -.
DR   OMA; INPREER; -.
DR   OrthoDB; 844266at2759; -.
DR   Proteomes; UP000002258; Chromosome 7.
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: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   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; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..336
FT                   /note="Structure-specific endonuclease subunit SLX1"
FT                   /id="PRO_0000383796"
FT   DOMAIN          21..104
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         214..290
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   REGION          37..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   336 AA;  38610 MW;  B7638633CBFE06F0 CRC64;
     MPRRPSTGTQ SDTPALHVVP SFYGVYLLQS EPKPSSFYIG STPDPPRRLR QHNGDLKAGG
     AYRTKRAGFR PWRMLLVVYD FPSKVSALQF EHSFQHCHET RHIKQEERIS KNKLSGRTLH
     HKVANVALLL RSSYFRHLPL KVLVFEEAVY NSFMNNKFVT CSHVDLLNTN FNEYFSVMEK
     DLDSTVDSWK TRHTNENEIW SMAKEAVILG SPRCALCLEP IEQVPETSSP ISKRSDLQRY
     LQSESLPLVT MCYNPQCRDV FHLSCLGHRF TNSDGFQSLI PATVNRCCSC NAKLEWRTLA
     KIATKLRYYV LKDSLQLPSQ VLENDDNYES QNVNDS