SLX1_DROAN
ID SLX1_DROAN Reviewed; 299 AA.
AC B3M0F3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=GF16665;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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; CH902617; EDV43159.1; -; Genomic_DNA.
DR RefSeq; XP_001954598.2; XM_001954562.2.
DR AlphaFoldDB; B3M0F3; -.
DR SMR; B3M0F3; -.
DR STRING; 7217.FBpp0119857; -.
DR EnsemblMetazoa; FBtr0121365; FBpp0119857; FBgn0093686.
DR GeneID; 6499459; -.
DR KEGG; dan:6499459; -.
DR eggNOG; KOG3005; Eukaryota.
DR HOGENOM; CLU_030739_0_0_1; -.
DR InParanoid; B3M0F3; -.
DR OMA; LQFEHAW; -.
DR OrthoDB; 844266at2759; -.
DR PhylomeDB; B3M0F3; -.
DR Proteomes; UP000007801; 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..299
FT /note="Structure-specific endonuclease subunit SLX1
FT homolog"
FT /id="PRO_0000383753"
FT DOMAIN 23..109
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT ZN_FING 197..250
FT /note="SLX1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT REGION 273..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 299 AA; 34299 MW; 30D49FE5E5B31132 CRC64;
MSFRKFTATA DPEKDETIAR KGHFYGVYLL CSQSLDSRYR GKCYVGFTVN PKRRIKQHNR
GCDFGGAKKT SRKGPWQMVM IVHGFPNNIV ALQFEWAWQQ PTLSTRLKIF PELKRKNPRE
SHFDYNFRIL NRMLGVGPWN RLALKIRWLE TDYERGFEVP LPRHMEIVSG KVSISSSQRR
KGEDAAATVP VAWAPECHLC MQRIDQPERS RLGCTNPTCR LTCHMLCLAN YLLGDEPGHY
IPVGGECPLC ETRLSWSALL QRKRLLNGIP EELLDQEEAD EDLSDGPDVD SDVEVLESD