ID   SLX1_LEIMA              Reviewed;         704 AA.
AC   Q4Q9W0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=LmjF25.1330, LmjF_25_1330;
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin;
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B.G., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(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 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FR796421; CAJ05240.1; -; Genomic_DNA.
DR   RefSeq; XP_001683888.1; XM_001683836.1.
DR   AlphaFoldDB; Q4Q9W0; -.
DR   SMR; Q4Q9W0; -.
DR   STRING; 5664.LmjF.25.1330; -.
DR   EnsemblProtists; CAJ05240; CAJ05240; LMJF_25_1330.
DR   GeneID; 5652544; -.
DR   KEGG; lma:LMJF_25_1330; -.
DR   VEuPathDB; TriTrypDB:LmjF.25.1330; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_250020300; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_250020100; -.
DR   eggNOG; KOG3005; Eukaryota.
DR   InParanoid; Q4Q9W0; -.
DR   OMA; CSRAPFC; -.
DR   Proteomes; UP000000542; Chromosome 25.
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; 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..704
FT                   /note="Structure-specific endonuclease subunit SLX1
FT                   homolog"
FT                   /id="PRO_0000383764"
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          157..180
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          354..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..671
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   704 AA;  74798 MW;  55E47B08853FE55E CRC64;
     MDTRFHCVYL LTSLDPQCEG DFYIGYSVNP LRRLRQHNGE LVNGARRTGR RGRPWTIVCC
     VSGFPDDRTA LKFEWCWQHP TASARLRHTI DILTGLRRLP YAVATLHLLV RASLFCQLDL
     TLHIFESAFL QEAAARAEVF LARRRGAFAV GGGLQAESPR VGTQQHSQRS SSLQGQADGV
     VTPPLPALDS QGELQGASTA AALATTTAAS HLLPPLTPSL LLHVENTTRE AFEDAYLSHD
     RCLLLPSAGM GVVVGEAGKE DSHMSASAGT SCPYDVSLLS QAARAEWSNA SFASDSDDED
     TRRLAPYCPS AGSSTPSPQR VRTAASPALL GYRSEERAGD GVWEASPGSS VGCGAALRSF
     SSPPPPRESS PRSASRPPVC TGINASASLA VDAPHGDVTA ACPSSPAAAP APQPRIPLRF
     ADYGEVDFAR AHAEEQHRLH HGLLPCSLCA LPLQPSCLVY CSRAPFCTLR CHLSCLAMWM
     LYAEAEAAAT IDGTDKSPAL LSHAPPAPIS PLRRLIPSQP CPCPLCGVLL HWGSLVKELK
     KRVVVERRLH AVQRRIRMEQ RWQARLAHIE PTKRSTGAAM RRRQRARVGA AAALAKGAGK
     VPGAASTVPA PTMHAGPARR DAPRVSSPIS FGEPTLTSFA AAASCPSPSA SLAALSPTSA
     SPISRHNGHS NTVTATHTAA AAAAASDASL LSLTDFCEED WLLP