SLX1_DROPE
ID SLX1_DROPE Reviewed; 291 AA.
AC B4GEU1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=GL22073;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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}.
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DR EMBL; CH479182; EDW34126.1; -; Genomic_DNA.
DR RefSeq; XP_002017026.1; XM_002016990.1.
DR AlphaFoldDB; B4GEU1; -.
DR SMR; B4GEU1; -.
DR STRING; 7234.FBpp0186180; -.
DR EnsemblMetazoa; FBtr0187688; FBpp0186180; FBgn0159665.
DR GeneID; 6591982; -.
DR KEGG; dpe:6591982; -.
DR eggNOG; KOG3005; Eukaryota.
DR HOGENOM; CLU_030739_0_0_1; -.
DR OMA; LQFEHAW; -.
DR PhylomeDB; B4GEU1; -.
DR Proteomes; UP000008744; 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 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..291
FT /note="Structure-specific endonuclease subunit SLX1
FT homolog"
FT /id="PRO_0000383758"
FT DOMAIN 15..101
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT ZN_FING 189..242
FT /note="SLX1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT REGION 261..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..291
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 33261 MW; 4F3BE2BC68E7F2B2 CRC64;
MPPPPEDEAI AHKGHFYGVY LLCSQSLDSR YRAKCYVGFT VNPKRRIKQH NRGCDFGGAK
KTSKKGPWQM VMIVHGFPNN ISALQFEWAW QQPTLSTRLK IFPDLKRKKP KETHFDYNFR
ILNRMLGVGP WHRLALTIRW LETDYERAFD LPIPCHMEIV SGKVSISASQ RKLEEATGTA
PPVAWAHECH LCMQSIEQPE RSRLGCTNPT CRLTCHMLCL ASYLLGDEPG QYIPIGGECP
LCETRLSWSA LLQRKRLQLG VPEEMQDNEE EDLSDDGPDV DSDVEVQEFS D