ID   SLX1_DROSE              Reviewed;         298 AA.
AC   B4I3R2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Structure-specific endonuclease subunit SLX1 homolog {ECO:0000255|HAMAP-Rule:MF_03100};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
GN   Name=slx1; ORFNames=GM10768;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Catalytic subunit of a heterodimeric 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 mus312/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=EDW54855.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH480821; EDW54855.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002038318.1; XM_002038282.1.
DR   AlphaFoldDB; B4I3R2; -.
DR   SMR; B4I3R2; -.
DR   STRING; 7238.B4I3R2; -.
DR   PRIDE; B4I3R2; -.
DR   EnsemblMetazoa; FBtr0193753; FBpp0192245; FBgn0165714.
DR   GeneID; 6613849; -.
DR   KEGG; dse:6613849; -.
DR   Proteomes; UP000001292; 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: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; IPR026850; FANCL_C.
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; PF11793; FANCL_C; 1.
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; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..298
FT                   /note="Structure-specific endonuclease subunit SLX1
FT                   homolog"
FT                   /id="PRO_0000383760"
FT   DOMAIN          22..108
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         196..249
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   REGION          275..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..291
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   298 AA;  34191 MW;  1B222E04B8F9931F CRC64;
     MNSYDPQDTG SQQEETVALK GHFYGVYLLC SQSLDPRYRG KCYVGFTVNP KRRIRQHNLG
     CDFGGARKTS RKGPWLMVMI VHGFPNNTVA LQFEWAWQQP SLSTRLKMYP ELKRKLPRET
     FFDYNFRILS HMLGVGPWNR LPLTVRWLET DYERPFSKTL PNHMEIVSGK VSISASQRRR
     PDDAVPPPPV AWASECHLCM QQIEQPEKSR LGCTNQMCRL TCHMVCLANY LLGDETGHYI
     PVGGECPLCE TRLSWAALLQ RKRLLMGVPE ELQDHDEDLS DDIDVDSDIE DGAQELSN