ID   SLX1_XENLA              Reviewed;         282 AA.
AC   Q0IH86;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Structure-specific endonuclease subunit slx1 {ECO:0000255|HAMAP-Rule:MF_03100};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
DE   AltName: Full=GIY-YIG domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03100};
GN   Name=slx1a; Synonyms=giyd1, slx1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; BC123264; AAI23265.1; -; mRNA.
DR   RefSeq; NP_001090376.1; NM_001096907.1.
DR   AlphaFoldDB; Q0IH86; -.
DR   SMR; Q0IH86; -.
DR   MaxQB; Q0IH86; -.
DR   DNASU; 779287; -.
DR   GeneID; 779287; -.
DR   CTD; 779287; -.
DR   Xenbase; XB-GENE-6252778; slx1a.L.
DR   OrthoDB; 844266at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 779287; Expressed in oocyte and 19 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   2: Evidence at transcript level;
KW   DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW   Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..282
FT                   /note="Structure-specific endonuclease subunit slx1"
FT                   /id="PRO_0000332123"
FT   DOMAIN          7..97
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         191..243
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
SQ   SEQUENCE   282 AA;  32576 MW;  B21EEA96BC713FE9 CRC64;
     MVVEVEGFYG VYLLFCTNPK YKGRIYIGFT VNPERRIQQH NGGKHKGGAW KTSGRGPWDM
     VLIVHGFPND IAALRFEWAW QHPHVSRRLT HVPRKTKKQS SFDFHLLVLC HMLRVAPWNR
     LPLTLRWLRQ EYRRELPLLL QPPLHMPLAF GQVRARPIPK GEKEKGRLGE NRAEETEQEV
     ILLGDAVVQR CRVCYERVQD KDDSLHCFHP GCTLTAHIMC LAKLFLLNEP QNLIPVEGLC
     PSCGHSLLWG DLIRHRNGCY GDLEEISSSQ AHWGDELHRC SD