ID   SLX1_PHANO              Reviewed;         366 AA.
AC   Q0UAL6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 3.
DT   25-MAY-2022, entry version 66.
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=SNOG_11198;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT81697.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445342; EAT81697.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001801442.1; XM_001801390.1.
DR   AlphaFoldDB; Q0UAL6; -.
DR   SMR; Q0UAL6; -.
DR   STRING; 321614.Q0UAL6; -.
DR   PRIDE; Q0UAL6; -.
DR   GeneID; 5978350; -.
DR   KEGG; pno:SNOG_11198; -.
DR   InParanoid; Q0UAL6; -.
DR   OrthoDB; 844266at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0033557; C:Slx1-Slx4 complex; IBA:GO_Central.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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..366
FT                   /note="Structure-specific endonuclease subunit SLX1"
FT                   /id="PRO_0000383794"
FT   DOMAIN          14..95
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         234..289
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   REGION          31..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..354
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  41673 MW;  604D1326BFA1054C CRC64;
     MSEALKIESR PIPAFYCCYL LRSKNRKSYY IGSTPNPARR LGQHNGSSKG GAKRTSMQGK
     RPWEMTCIVT GFPSKFAALQ FEWAWQNTHA TRHIDKDVRD ARAEELQKGK KKATSPGRRR
     KRPPMSLEAR LKNLHHLLSV DSFCRWPLNL RFFAPDVFVQ WERHTTKMTT TLRKSITIQL
     TPAEIPKLAS DVSTELQTHF IPEVIRAIPV AYEDCKQYIE KSRRVLEDDQ RLGCGVCKNP
     ADMSSSLILV CPIEACQTVS HLSCLSNKFL TEGGELETLV PLEGTCPGCR SCIKWATMIK
     ELSLRTNGEE ELKLLFKPKR KRKSDNPAES DAADGQALEQ EDEELDETWM EDMSQDEEPS
     PVKKSR