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SLX12_TRYCC
ID   SLX12_TRYCC             Reviewed;         530 AA.
AC   Q4CTY5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Structure-specific endonuclease subunit SLX1 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03100};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
GN   ORFNames=Tc00.1047053511881.30;
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; AAHK01001928; EAN83738.1; -; Genomic_DNA.
DR   RefSeq; XP_805589.1; XM_800496.1.
DR   AlphaFoldDB; Q4CTY5; -.
DR   SMR; Q4CTY5; -.
DR   STRING; 5693.XP_805589.1; -.
DR   PaxDb; Q4CTY5; -.
DR   EnsemblProtists; EAN83738; EAN83738; Tc00.1047053511881.30.
DR   GeneID; 3535356; -.
DR   KEGG; tcr:511881.30; -.
DR   eggNOG; KOG3005; Eukaryota.
DR   OMA; CSRAPFC; -.
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..530
FT                   /note="Structure-specific endonuclease subunit SLX1 homolog
FT                   2"
FT                   /id="PRO_0000383769"
FT   DOMAIN          4..89
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         232..365
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   REGION          276..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  59703 MW;  B01C66AA1D9B1A7F CRC64;
     MDTRFHCVYL LTSLDPQCAG EYYIGYTVDP IRRLRQHNGE IVSGAWRTKR RGRPWELLCC
     VSGFGEDRIA LKFEWCWQHP TKSTRLKTQM TQLRGVHRLP YAVGVLHLLL RADLFARLQL
     TLHIFEPEHV GRVVAELQGR VPSIPPLVAT SLLRIEEITK ERFMSLYLDG VSGGDGTAGD
     GCVYFVTAPL SSQPEADAPS RRVRSCRYLS EEDIFRQHAR VKELLEANQC PCALCSLPLR
     SPYFVRCSRT PFCTLRAHLA CLAMWFTYET MQKRDATMGQ STRNERSGEY SNKIKDDSND
     GTMDAHASGR QLHSLSVNNA DFSSSRDAGS ILDSSGHISA FEESRCASSP SLTLLPSQPC
     PCPLCDEPLQ WGALVHDLKR RAVLEKRWME RQRREKIEAA LAERLQRLQN SSLTERKSRR
     KAKPALGQKR NRGEYCGDTV GDGGKEAITN WRARVMDGCD SWNDTNDFSH SVSLPPSGDE
     GYACDSSRRG VGGSKHTTRM TDEGKNDSIT DICDCVLQLT EFNLDEWLDA
 
 
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