SLX1_CANGA
ID SLX1_CANGA Reviewed; 312 AA.
AC Q6FML9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=CAGL0K06941g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380957; CAG61486.1; -; Genomic_DNA.
DR RefSeq; XP_448525.1; XM_448525.1.
DR PDB; 4XLG; X-ray; 1.78 A; A=1-312.
DR PDB; 4XM5; X-ray; 2.34 A; A=1-312.
DR PDBsum; 4XLG; -.
DR PDBsum; 4XM5; -.
DR AlphaFoldDB; Q6FML9; -.
DR SMR; Q6FML9; -.
DR STRING; 5478.XP_448525.1; -.
DR EnsemblFungi; CAG61486; CAG61486; CAGL0K06941g.
DR GeneID; 2890413; -.
DR KEGG; cgr:CAGL0K06941g; -.
DR CGD; CAL0134685; CAGL0K06941g.
DR VEuPathDB; FungiDB:CAGL0K06941g; -.
DR eggNOG; KOG3005; Eukaryota.
DR HOGENOM; CLU_030739_1_1_1; -.
DR InParanoid; Q6FML9; -.
DR OMA; LQFEHAW; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0033557; C:Slx1-Slx4 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:EnsemblFungi.
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 GO; GO:0006261; P:DNA-templated DNA replication; IEA:EnsemblFungi.
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 3D-structure; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW Hydrolase; Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..312
FT /note="Structure-specific endonuclease subunit SLX1"
FT /id="PRO_0000383780"
FT DOMAIN 9..92
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT ZN_FING 219..282
FT /note="SLX1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:4XLG"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:4XLG"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:4XLG"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:4XLG"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:4XLG"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4XM5"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:4XM5"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:4XLG"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:4XLG"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:4XLG"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:4XLG"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:4XLG"
FT HELIX 176..213
FT /evidence="ECO:0007829|PDB:4XLG"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:4XLG"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:4XLG"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4XLG"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:4XLG"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:4XLG"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:4XM5"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:4XLG"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:4XLG"
SQ SEQUENCE 312 AA; 36433 MW; 5485DFD46860AD40 CRC64;
MEEFQQIPDF YGCYLLQSIS KRQSFYIGST PNPVRRLRQH NGSLSRGGAY RTKRDGTRPW
EMVAIVYGFP SRIAALQFEH AWQHGYQTRY IKSQDRVVKT RKGGRSIHHK LAMITSLLKN
EYFRYMDLTL HFFNQKVEEI WKNDKFNVSQ TQESIDNNYT VSLSQDALTE INNDTIDDIM
DVNEKNMELV QNLYSTTLAE KTKTLLLYKE KIDTGINTCQ FCNKIIKHNL SGNISENLFA
FCRDTSCTFV SHLACAYRYF MSNTELPKED TIIPQSPKCP KCYTLLKWCD VIYYSIKLNK
DNTTADDKKK TI
