SLX1_YARLI
ID SLX1_YARLI Reviewed; 288 AA.
AC Q6C0W7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Structure-specific endonuclease subunit SLX1 {ECO:0000255|HAMAP-Rule:MF_03100};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
GN Name=SLX1 {ECO:0000255|HAMAP-Rule:MF_03100};
GN OrderedLocusNames=YALI0F21131g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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. {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 SLX4. {ECO:0000255|HAMAP-
CC 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; CR382132; CAG78504.1; -; Genomic_DNA.
DR RefSeq; XP_505695.1; XM_505695.1.
DR AlphaFoldDB; Q6C0W7; -.
DR SMR; Q6C0W7; -.
DR STRING; 4952.CAG78504; -.
DR EnsemblFungi; CAG78504; CAG78504; YALI0_F21131g.
DR GeneID; 2908279; -.
DR KEGG; yli:YALI0F21131g; -.
DR VEuPathDB; FungiDB:YALI0_F21131g; -.
DR HOGENOM; CLU_030739_1_1_1; -.
DR InParanoid; Q6C0W7; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0033557; C:Slx1-Slx4 complex; IBA:GO_Central.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:EnsemblFungi.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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 SUPFAM; SSF82771; SSF82771; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..288
FT /note="Structure-specific endonuclease subunit SLX1"
FT /id="PRO_0000383803"
FT DOMAIN 7..90
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
SQ SEQUENCE 288 AA; 32838 MW; 2149A9B695E004E1 CRC64;
MTHQYPPFYG VYLLQSTKKP LSCYVGSTPN PFRRIRQHNG DLKAGGAWRT KRAHLRPWSM
VLIVNGFPSK ISALKFEHAL QHPNMTRLIT TKDIKRKVPQ KARALGTHLA FIRLLVRCSY
FRRMHLRITF FRSHAHEAWE KNDYDVGSLP PQFQVETDYP SDEAEAPPST VGSGELDINN
RSIEEYLQKC RDAVSNDKQL TCYLSEKTLN ISEGNVALCH NCDGAFDVAE LAERFLNEEI
PEELPFTTPS RHIIPIGGDC PSCLARMEWS NVIKGVLAMR PVLEDNKE