ID   SLX1_TALMQ              Reviewed;         389 AA.
AC   B6QFH5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
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; ORFNames=PMAA_082160;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; DS995901; EEA24210.1; -; Genomic_DNA.
DR   RefSeq; XP_002147721.1; XM_002147685.1.
DR   AlphaFoldDB; B6QFH5; -.
DR   SMR; B6QFH5; -.
DR   STRING; 441960.B6QFH5; -.
DR   EnsemblFungi; EEA24210; EEA24210; PMAA_082160.
DR   GeneID; 7025347; -.
DR   KEGG; tmf:PMAA_082160; -.
DR   VEuPathDB; FungiDB:PMAA_082160; -.
DR   HOGENOM; CLU_030739_1_0_1; -.
DR   OrthoDB; 844266at2759; -.
DR   PhylomeDB; B6QFH5; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
DR   GO; GO:0033557; C:Slx1-Slx4 complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:InterPro.
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   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; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..389
FT                   /note="Structure-specific endonuclease subunit slx1"
FT                   /id="PRO_0000383793"
FT   DOMAIN          17..99
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         227..281
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   REGION          38..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   389 AA;  43387 MW;  EE6523C9E50B915E CRC64;
     MISTAPADLP SPKPIPAFYC CYLLRSVKKP SSLYIGSTPD PARRLEQHNG FTKGGAKRTE
     RDTLRPWEMI TIIEGFTSRT GALQFEWSWQ HVHTTRHIGA VETDQLNRRR KDPPVDQGSG
     IWTSTPKVLG NLHQLLRSTY FGTWPLTVRF LSTEAHSHWQ RWTERADGLL PDTIHVELDF
     HAEGASVLDS NLPANDMTHI NATYSGIQDH LEKSASLLND SAKTLACEVC KKLLSPHGDV
     IVVCSQPHCH AVSHVKCLSQ LFLRDEGSSG LVPTLGDCPA CKREVTWVAL MKELSMRLHG
     AKIATKLLKK ERKSKAISDS RKSSKSGKKT ANTYADILGN DYDDLDEDWM NSVNVDSGSE
     PLDHKFTNAN NSTGRVEIVI EDSEEETFD