ID   SLX11_TRYCC             Reviewed;         529 AA.
AC   Q4D7L5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Structure-specific endonuclease subunit SLX1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03100};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
GN   ORFNames=Tc00.1047053509453.60;
OS   Trypanosoma cruzi (strain CL Brener).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=353153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL Brener;
RX   PubMed=16020725; DOI=10.1126/science.1112631;
RA   El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA   Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA   Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA   Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA   Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA   da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA   Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA   Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA   Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA   Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA   Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA   Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA   Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA   Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA   Andersson B.;
RT   "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT   disease.";
RL   Science 309:409-415(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}.
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DR   EMBL; AAHK01000875; EAN88519.1; -; Genomic_DNA.
DR   RefSeq; XP_810370.1; XM_805277.1.
DR   AlphaFoldDB; Q4D7L5; -.
DR   SMR; Q4D7L5; -.
DR   STRING; 5693.XP_810370.1; -.
DR   PaxDb; Q4D7L5; -.
DR   PRIDE; Q4D7L5; -.
DR   EnsemblProtists; EAN88519; EAN88519; Tc00.1047053509453.60.
DR   GeneID; 3541122; -.
DR   KEGG; tcr:509453.60; -.
DR   eggNOG; KOG3005; Eukaryota.
DR   OrthoDB; 1170897at2759; -.
DR   Proteomes; UP000002296; Unassembled WGS sequence.
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; 3.40.1440.10; -; 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   Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..529
FT                   /note="Structure-specific endonuclease subunit SLX1 homolog
FT                   1"
FT                   /id="PRO_0000383768"
FT   DOMAIN          4..89
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         231..364
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   REGION          275..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  59775 MW;  230BC53342425DFE CRC64;
     MDTRFHCVYL LTSLDPQCAG EYYIGYTVDP IRRLRQHNGE IVSGAWRTKR RGRPWELLCC
     VSGFGEDRIA LKFEWCWQHP TKSTRLKTQM TQLRGVHRLP YAVGVLHLLL RADLFARLQL
     TLHIFEPERV GRVVAELQGR VPSISPLVAT SLLRIEEITK ERFMSLYLDG VSGDGTAGDG
     CVYFVTAPLS SQPDVDAPSR RVRSCRYLSE EDVFRQHARV KELLEANQCP CALCSLPLRS
     PYFVRCYRTP FCALRAHLAC LAMWFTYETM QKRDVTMGQS TRNERSGEYS NKIKDDSNDG
     TMDAHASGRQ LHSLSVNNAD FSSSRDAGSI LDSSGHISAF EESRCASSPS LTLLPCQPCP
     CPLCDEPLQW GALVHDLKRR AVLEKRWMER QRREKIEAAL AERLQRLQNS SLTERKSRRK
     ATPALGQKRN RGEYCGDTVG DGGKEAVTNW RARAMDGCDS WNDTNDFSHS VSLPPSRDEG
     YACDSSRRGV GGSKHTTRMT DEGKNDSITD ICDCVLQLTE FNLDEWLDA