SLX1_DROPS
ID SLX1_DROPS Reviewed; 291 AA.
AC B5DXG8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=GA27368;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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; CM000070; EDY68263.1; -; Genomic_DNA.
DR RefSeq; XP_002137705.1; XM_002137669.3.
DR AlphaFoldDB; B5DXG8; -.
DR SMR; B5DXG8; -.
DR STRING; 7237.FBpp0284332; -.
DR EnsemblMetazoa; FBtr0285894; FBpp0284332; FBgn0248735.
DR GeneID; 6897560; -.
DR KEGG; dpo:Dpse_GA27368; -.
DR eggNOG; KOG3005; Eukaryota.
DR HOGENOM; CLU_030739_0_0_1; -.
DR InParanoid; B5DXG8; -.
DR OMA; LQFEHAW; -.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0248735; Expressed in female reproductive system and 2 other tissues.
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..291
FT /note="Structure-specific endonuclease subunit SLX1
FT homolog"
FT /id="PRO_0000383759"
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; 33307 MW; FA3FF2F861AF7F2B CRC64;
MPPPPEDEAI AHKGHFYGVY LLCSQSLDSR YRAKCYVGFT VNPKRRIKQH NRGCDFGGAK
KTSKKGPWQM VMIVHGFPNN ISALQFEWAW QQPTLSTRLK IFPDLKRKKP KETHFDYNFR
ILNRMLSVGP WHRLALTIRW LETDYERAFD LPIPCHMEIV SGKVSISASQ RKLEEATGTA
PPVAWAHECH LCMQSIEQPE RSRLGCTNPT CRLTCHMLCL ASYLLGDEPG QYIPIGGECL
LCETRLSWSA LLQRKRLQLG VPEEMQDNEE EDLSDDGPDV DSDVEVQEFS D