ID   SLX1_GIAIC              Reviewed;         359 AA.
AC   A8B2Z8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=GL50803_16475;
OS   Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=184922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50803 / WB clone C6;
RX   PubMed=17901334; DOI=10.1126/science.1143837;
RA   Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA   Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA   Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA   Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E.J., Palm D.,
RA   Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA   Svard S.G., Sogin M.L.;
RT   "Genomic minimalism in the early diverging intestinal parasite Giardia
RT   lamblia.";
RL   Science 317:1921-1926(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 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; AACB02000001; EDO82414.1; -; Genomic_DNA.
DR   RefSeq; XP_001710088.1; XM_001710036.1.
DR   AlphaFoldDB; A8B2Z8; -.
DR   SMR; A8B2Z8; -.
DR   STRING; 5741.EDO82414; -.
DR   EnsemblProtists; EDO82414; EDO82414; GL50803_16475.
DR   GeneID; 5703014; -.
DR   KEGG; gla:GL50803_0016475; -.
DR   VEuPathDB; GiardiaDB:GL50803_16475; -.
DR   HOGENOM; CLU_772612_0_0_1; -.
DR   InParanoid; A8B2Z8; -.
DR   OMA; FCITCAG; -.
DR   OrthoDB; 844266at2759; -.
DR   GO; GO:0033557; C:Slx1-Slx4 complex; IBA:GO_Central.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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; IPR001841; Znf_RING.
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; Zinc; Zinc-finger.
FT   CHAIN           1..359
FT                   /note="Structure-specific endonuclease subunit SLX1
FT                   homolog"
FT                   /id="PRO_0000383762"
FT   DOMAIN          9..91
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         192..238
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   REGION          256..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   359 AA;  39448 MW;  9CF10429C83A43AE CRC64;
     MTIFSGPRGL FACYCLVAES SESPKRCYIG FTNNPLRRIR QHNRKIAGGA RKTSRYGPWR
     MVLFVGGFST KVSALKFEYI WTYPTRSRYV NCISATSQKL RLACPRSIST ALDVLVTLLI
     HPPFSLQPLY VVLLDAEGNR VKSQLEQHSV PVFVSTMEAL QIEPGVRAPS DIIYAQCTSS
     NGTTDTTFTD VCPICQDGVS PSNVQCMQCS ARFCITCAGK LFTRRNTLIP CFGKCPICKR
     EFQWKEMLRK RAEELVAGRK SVPHKTQAVD GQSSLSQNSS YDDYDTISLL SSSSEPEKDD
     ISRDESGTVA SVQPVSSVAL SDSSRSPATT SPTKPLAIDP LLSSPRPCAL PSDVISITD