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