SLX1_YEAS1
ID SLX1_YEAS1 Reviewed; 304 AA.
AC B3LMT5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 45.
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}; ORFNames=SCRG_02743;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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; CH408048; EDV11888.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LMT5; -.
DR SMR; B3LMT5; -.
DR EnsemblFungi; EDV11888; EDV11888; SCRG_02743.
DR HOGENOM; CLU_030739_1_1_1; -.
DR Proteomes; UP000008335; Unassembled WGS sequence.
DR GO; GO:0033557; C:Slx1-Slx4 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
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; 3.30.40.10; -; 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 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Nucleus; Zinc; Zinc-finger.
FT CHAIN 1..304
FT /note="Structure-specific endonuclease subunit SLX1"
FT /id="PRO_0000383804"
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; 35778 MW; 09E5B56C9240B9C3 CRC64;
MSQKIQQHQF PDFYCCYLLQ SINKRQSFYV GSTPNPVRRL RQHNGKLAVG GAYRTKRDGS
RPWEMIMIVR GFPSKIAALQ FEHAWQHGYQ THYIAEKDRV VKHKAGGRTL HHKVALMKLL
LKHEFFQRMN LIVDVFNIKA WEVWKQDKFF IERDRFPINI QINENALEEP KEKTVDVLMD
HSDENLKVVE AVYTKVIENE RNIFETFEKK LTTGVVRCEI CEKEIDYTSE EQNLKPFVAL
CNNKDCGSVN HLKCLHRYFL DDEQLIVGRR NLIPRGGKCP KCDTFCDWTT LVKFSTRMKL
AHGK