ID   SLX1_CRYPI              Reviewed;         410 AA.
AC   Q5CT62;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 61.
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   ORFNames=cgd2_4280;
OS   Cryptosporidium parvum (strain Iowa II).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=353152;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa II;
RX   PubMed=15044751; DOI=10.1126/science.1094786;
RA   Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA   Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA   Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA   Anantharaman V., Aravind L., Kapur V.;
RT   "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL   Science 304:441-445(2004).
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 a member of the SLX4 family.
CC       {ECO:0000255|HAMAP-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; AAEE01000005; EAK88615.1; -; Genomic_DNA.
DR   RefSeq; XP_626607.1; XM_626607.1.
DR   AlphaFoldDB; Q5CT62; -.
DR   SMR; Q5CT62; -.
DR   STRING; 353152.Q5CT62; -.
DR   EnsemblProtists; EAK88615; EAK88615; cgd2_4280.
DR   GeneID; 3373476; -.
DR   KEGG; cpv:cgd2_4280; -.
DR   VEuPathDB; CryptoDB:cgd2_4280; -.
DR   InParanoid; Q5CT62; -.
DR   OMA; CPPRRIK; -.
DR   Proteomes; UP000006726; Chromosome 2.
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:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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   Pfam; PF01541; GIY-YIG; 1.
DR   PROSITE; PS50164; GIY_YIG; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW   Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..410
FT                   /note="Structure-specific endonuclease subunit SLX1
FT                   homolog"
FT                   /id="PRO_0000383761"
FT   DOMAIN          6..89
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
SQ   SEQUENCE   410 AA;  47943 MW;  F4241C7FD16BB459 CRC64;
     MKSNIQLHYC YFLLSEAKKK ASYIGYSVNP CRRLRQHNGE IKKGAKKTKS GVPWNLGICV
     GGFPDRVAAL RFEWAWQHPN ICKVTRDNIE SWKIVKTKKT SENKRILNKR QWSIQQRVSI
     LLCMTTLEPW KNMNLTVFVF KDELENTIKE VIEGIKKIKI SPNFTSPNIL NKDYLLMFLY
     FGEDSFYEKG IKFLRCDYET FKEFQKPSFD CDSDSNIEDN SNVFNPEEII SHEDSFSIKC
     FLCQKDIGIG RNYLEFPCCT EIKVHLSCIQ LWGESNNHLE TVIDELFPLK EFVAPLIPLN
     ISCPCCFKDF EWEEAKKNYI KTKNVPTESL ELGEDFPVLS NGEKENYSQE ENSQNKVIED
     GFLEMDIDNH RNRLSYAHET KQKRDILFSD DEFSEISQKC EFIDLTVDSD