ID   SLX1_LEIIN              Reviewed;         705 AA.
AC   A4I1H7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=LinJ25.1380, LinJ_25_1370;
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5;
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(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; FR796457; CAM68607.1; -; Genomic_DNA.
DR   RefSeq; XP_001466168.1; XM_001466131.1.
DR   AlphaFoldDB; A4I1H7; -.
DR   SMR; A4I1H7; -.
DR   STRING; 5671.XP_001466168.1; -.
DR   GeneID; 5069603; -.
DR   KEGG; lif:LINJ_25_1370; -.
DR   VEuPathDB; TriTrypDB:LINF_250019500; -.
DR   eggNOG; KOG3005; Eukaryota.
DR   InParanoid; A4I1H7; -.
DR   OMA; CSRAPFC; -.
DR   Proteomes; UP000008153; Chromosome 25.
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   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..705
FT                   /note="Structure-specific endonuclease subunit SLX1
FT                   homolog"
FT                   /id="PRO_0000383763"
FT   DOMAIN          4..90
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         446..526
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   REGION          155..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   705 AA;  74919 MW;  28703CD0DC1B4D71 CRC64;
     MDTRFHCVYL LTSLDPQCEG DFYIGYTVNP LRRLRQHNGE LVNGARRTSR RGRPWTIVCC
     VSGFPDDRAA LKFEWCWQHP TASARLRHAI DILTGLRRLP YAVATLHLLV RASLFCRLDL
     TLHIFESALL QEAAARAEVL LARRRGAFAV GGGLRASSPR VGTQQHSQRS SSLQGQADGV
     ATPPLPALDS KGELQDASTA AALATTTAAS HLLPPLTPSL LFHVEDTTRQ AFEDAYLSHD
     RCLLLPSVGM GVDVGEAGKE GSHMSASAGT SCPYDVSLLS QAARAEWSNA SFASDSDDED
     TRRFAPYCPS TGSRTPSPQR VHTAASPALL GYRSEERAGD GVLEASPGSS IGCGAALRSF
     SSPPPPRASS PRSASCPPLY TGINASASLA VDAPHGGVTD ACTSSPAAAP APQPRIPLRF
     ADYGEVDFAR AHAEEQHRLH HGLLPCSLCT LPLQPSCVAY CSRAPFCTLR CHLSCLAMWM
     LYAEAEAAAT VDGTDKSPAL LSQAPPAPIS PLRRLIPSQP CPCPLCGVLL HWGSLVKELK
     KRVVVERRLH AAQRRIRMEQ RWQARLAHID HTKRSTSAAM RRRQRTRVGA AALAKGAGEA
     PGAASTVRAS TMHVGPARRD APRVSSPSCL GEPTLTSFAA AASCPSPSTS LAALSPAASA
     SPISRHNGHS NTVTATNTAV AAAAAVSDAS LLSLTDFCEE DWLLP