ID SLX1_YEAST Reviewed; 304 AA. AC P38324; D6VQM3; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 04-NOV-2026, entry version 177. DE RecName: Full=Structure-specific endonuclease subunit SLX1 {ECO:0000255|HAMAP-Rule:MF_03100}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100}; DE AltName: Full=Synthetic lethal of unknown function protein 1; GN Name=SLX1 {ECO:0000255|HAMAP-Rule:MF_03100}; GN OrderedLocusNames=YBR228W; ORFNames=YBR1525; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP FUNCTION, AND INTERACTION WITH SLX4. RX PubMed=11139495; DOI=10.1093/genetics/157.1.103; RA Mullen J.R., Kaliraman V., Ibrahim S.S., Brill S.J.; RT "Requirement for three novel protein complexes in the absence of the Sgs1 RT DNA helicase in Saccharomyces cerevisiae."; RL Genetics 157:103-118(2001). RN [4] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12832395; DOI=10.1101/gad.1105203; RA Fricke W.M., Brill S.J.; RT "Slx1-Slx4 is a second structure-specific endonuclease functionally RT redundant with Sgs1-Top3."; RL Genes Dev. 17:1768-1778(2003). CC -!- FUNCTION: Catalytic subunit of the SLX1-SLX4 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. Has a preference for simple Y, 5'-flap CC and replication fork-like structures. It cleaves the strand bearing the CC 5'-non-homologous arm at the branch site junction and generates CC ligatable, nicked products from the 5'-flap or replication fork CC substrates. Plays a critical role in maintaining the integrity of the CC ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled CC replication forks. Has Holliday junction resolvase activity in vitro. CC {ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000269|PubMed:11139495, CC ECO:0000269|PubMed:12832395}. 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 SLX4. CC -!- INTERACTION: CC P38324; Q12098: SLX4; NbExp=6; IntAct=EBI-21016, EBI-37788; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100, CC ECO:0000269|PubMed:12832395}. 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; Z36097; CAA85191.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07343.1; -; Genomic_DNA. DR PIR; S46104; S46104. DR RefSeq; NP_009787.3; NM_001178576.3. DR PDB; 7CQ2; X-ray; 2.50 A; A/B=1-304. DR PDB; 7CQ3; X-ray; 1.45 A; A=1-304. DR PDB; 7CQ4; X-ray; 3.29 A; A=1-304. DR AlphaFoldDB; P38324; -. DR SMR; P38324; -. DR BioGRID; 32923; 103. DR ComplexPortal; CPX-1355; RTT107-SLX4-SLX1 complex. DR ComplexPortal; CPX-3159; SLX1-SLX4 structure-specific endonuclease complex. DR DIP; DIP-1770N; -. DR FunCoup; P38324; 502. DR IntAct; P38324; 4. DR STRING; 4932.YBR228W; -. DR PaxDb; 4932-YBR228W; -. DR PeptideAtlas; P38324; -. DR EnsemblFungi; YBR228W_mRNA; YBR228W; YBR228W. DR GeneID; 852529; -. DR KEGG; sce:YBR228W; -. DR AGR; SGD:S000000432; -. DR SGD; S000000432; SLX1. DR VEuPathDB; FungiDB:YBR228W; -. DR eggNOG; KOG3005; Eukaryota. DR HOGENOM; CLU_030739_1_1_1; -. DR InParanoid; P38324; -. DR OMA; AAHIFCL; -. DR OrthoDB; 24645at2759; -. DR BioCyc; YEAST:G3O-29161-MONOMER; -. DR BioGRID-ORCS; 852529; 2 hits in 10 CRISPR screens. DR PRO; PR:P38324; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P38324; protein. DR GO; GO:0000228; C:nuclear chromosome; NAS:ComplexPortal. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:0033557; C:Slx1-Slx4 complex; IPI:SGD. DR GO; GO:0017108; F:5'-flap endonuclease activity; IDA:SGD. DR GO; GO:0008821; F:crossover junction DNA endonuclease activity; IBA:GO_Central. DR GO; GO:0006261; P:DNA-templated DNA replication; IGI:SGD. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central. DR GO; GO:2000001; P:regulation of DNA damage checkpoint; NAS:ComplexPortal. DR GO; GO:0031297; P:replication fork processing; NAS:ComplexPortal. DR CDD; cd10455; GIY-YIG_SLX1; 1. DR FunFam; 3.40.1440.10:FF:000006; Structure-specific endonuclease subunit SLX1; 1. DR Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR048749; SLX1_C. DR InterPro; IPR050381; SLX1_endonuclease. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR20208; STRUCTURE-SPECIFIC ENDONUCLEASE SUBUNIT SLX1; 1. DR PANTHER; PTHR20208:SF10; STRUCTURE-SPECIFIC ENDONUCLEASE SUBUNIT SLX1; 1. DR Pfam; PF01541; GIY-YIG; 1. DR Pfam; PF21202; SLX1_C; 1. DR SMART; SM00465; GIYc; 1. DR SUPFAM; SSF82771; GIY-YIG endonuclease; 1. DR PROSITE; PS50164; GIY_YIG; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA damage; DNA recombination; DNA repair; Endonuclease; KW Hydrolase; Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1..304 FT /note="Structure-specific endonuclease subunit SLX1" FT /id="PRO_0000202517" FT DOMAIN 12..95 FT /note="GIY-YIG" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100" FT ZN_FING 218..282 FT /note="SLX1-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100" FT STRAND 15..23 FT /evidence="ECO:0007829|PDB:7CQ3" FT STRAND 28..34 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 36..44 FT /evidence="ECO:0007829|PDB:7CQ3" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 53..56 FT /evidence="ECO:0007829|PDB:7CQ3" FT TURN 58..60 FT /evidence="ECO:0007829|PDB:7CQ3" FT STRAND 62..70 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 75..86 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:7CQ3" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:7CQ2" FT HELIX 110..122 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 124..127 FT /evidence="ECO:0007829|PDB:7CQ3" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:7CQ3" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 138..146 FT /evidence="ECO:0007829|PDB:7CQ3" FT TURN 152..154 FT /evidence="ECO:0007829|PDB:7CQ2" FT STRAND 159..167 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 175..211 FT /evidence="ECO:0007829|PDB:7CQ3" FT TURN 219..221 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:7CQ3" FT STRAND 238..240 FT /evidence="ECO:0007829|PDB:7CQ3" FT TURN 244..246 FT /evidence="ECO:0007829|PDB:7CQ3" FT STRAND 249..251 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 252..267 FT /evidence="ECO:0007829|PDB:7CQ3" FT STRAND 275..278 FT /evidence="ECO:0007829|PDB:7CQ3" FT TURN 280..282 FT /evidence="ECO:0007829|PDB:7CQ3" FT STRAND 285..287 FT /evidence="ECO:0007829|PDB:7CQ3" FT HELIX 288..302 FT /evidence="ECO:0007829|PDB:7CQ3" SQ SEQUENCE 304 AA; 35857 MW; 4C676E877FDF7A7A CRC64; MSQKIQQHQF PDFYCCYLLQ SINKRQSFYV GSTPNPVRRL RQHNGKLAVG GAYRTKRDGS RPWEMIMIVR GFPSKIAALQ FEHAWQHGYQ THYIAEKDRV VKHKAGGRTL HHKVALMKLL LKHEFFQRMN LIVEVFNIKA WEVWKQDKFF IERDRFPINI QINENALEEP KEKTVDVLMD HSDENLKVVE AVYTKVIENE RNIFETFEKK LTTGVVRCEI CEKEIDYTSE EQNLKPFVAL CNNKDCGCVN HLKCLHRYFL DDEQLMVGRR NLIPRGGKCP KCDMFCDWTT LVKFSTRMKL AHGK //