SLX1_YEAST
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 03-AUG-2022, entry version 158.
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}; OrderedLocusNames=YBR228W;
GN 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}.
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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 AlphaFoldDB; P38324; -.
DR SMR; P38324; -.
DR BioGRID; 32923; 99.
DR ComplexPortal; CPX-1355; RTT107-SLX4-SLX1 complex.
DR ComplexPortal; CPX-3159; Slx1-Slx4 complex.
DR DIP; DIP-1770N; -.
DR IntAct; P38324; 4.
DR MINT; P38324; -.
DR STRING; 4932.YBR228W; -.
DR PaxDb; P38324; -.
DR PRIDE; P38324; -.
DR EnsemblFungi; YBR228W_mRNA; YBR228W; YBR228W.
DR GeneID; 852529; -.
DR KEGG; sce:YBR228W; -.
DR SGD; S000000432; SLX1.
DR VEuPathDB; FungiDB:YBR228W; -.
DR eggNOG; KOG3005; Eukaryota.
DR GeneTree; ENSGT00390000013368; -.
DR HOGENOM; CLU_030739_1_1_1; -.
DR InParanoid; P38324; -.
DR OMA; LQFEHAW; -.
DR BioCyc; YEAST:G3O-29161-MON; -.
DR PRO; PR:P38324; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38324; protein.
DR GO; GO:0000228; C:nuclear chromosome; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IC:SGD.
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 endodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IC:ComplexPortal.
DR GO; GO:1902681; P:regulation of replication fork arrest at rDNA repeats; IC:ComplexPortal.
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 SMART; SM00465; GIYc; 1.
DR SUPFAM; SSF82771; SSF82771; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc; 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"
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
