ID   SLX1_ASPCL              Reviewed;         434 AA.
AC   A1C4Z4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=ACLA_001730;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027004; EAW14762.1; -; Genomic_DNA.
DR   RefSeq; XP_001276188.1; XM_001276187.1.
DR   AlphaFoldDB; A1C4Z4; -.
DR   SMR; A1C4Z4; -.
DR   STRING; 5057.CADACLAP00000116; -.
DR   EnsemblFungi; EAW14762; EAW14762; ACLA_001730.
DR   GeneID; 4708623; -.
DR   KEGG; act:ACLA_001730; -.
DR   VEuPathDB; FungiDB:ACLA_001730; -.
DR   eggNOG; KOG3005; Eukaryota.
DR   HOGENOM; CLU_030739_1_0_1; -.
DR   OMA; LQFEHAW; -.
DR   OrthoDB; 844266at2759; -.
DR   Proteomes; UP000006701; 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..434
FT                   /note="Structure-specific endonuclease subunit slx1"
FT                   /id="PRO_0000383772"
FT   DOMAIN          14..97
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         259..314
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   REGION          96..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  49121 MW;  8557251D3015EA13 CRC64;
     MENIQLEHSK PIPAFYCCYL LRSTVRHASL YIGSTPNPAR RLTQHNGVVK GGARRTAAEK
     LRPWEMVMIV EGFMSRLGAL QFEWAWQNPG YSRHLRSEEE GLEAPGTTST TKPKTTRRAK
     SQTPQPLEFE RDPSVSKSLG TPKRKNQRRR RPQRSLTTHF ADLHRLLQSP YFSNWPLRIR
     FFSADVYQSW KAWYDRVDIF LPGHVNILLD GSCPENSAQC SAVGARFGSV EQAKVNYDII
     QDYLEKAMFL LDDPKDLSCR VCQTQIAPKE QLAVVCPQAG CHCTCHLLCL SKKFLDAMPE
     PDCLIPRHGA CPACKATVQW SLMMQELSFR SRGEQEALAI LKRKRRLDRR QQVISKAKCA
     GKGVDSSDVR PTSVDLDRSN NNASDDLLLD DDWFDEFASE SDSDTGHRSK ALSKAAPNLE
     TVVEDSEGDD LEFL