ID   SLX4_VANPO              Reviewed;         680 AA.
AC   A7TEM0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=Kpol_1036p73;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: Regulatory 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_03110}.
CC   -!- SUBUNIT: Forms a heterodimer with SLX1. {ECO:0000255|HAMAP-
CC       Rule:MF_03110}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03110}.
CC   -!- PTM: Phosphorylated in response to DNA damage. {ECO:0000255|HAMAP-
CC       Rule:MF_03110}.
CC   -!- SIMILARITY: Belongs to the SLX4 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03110}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS480380; EDO19327.1; -; Genomic_DNA.
DR   RefSeq; XP_001647185.1; XM_001647135.1.
DR   AlphaFoldDB; A7TEM0; -.
DR   SMR; A7TEM0; -.
DR   STRING; 436907.A7TEM0; -.
DR   PRIDE; A7TEM0; -.
DR   EnsemblFungi; EDO19327; EDO19327; Kpol_1036p73.
DR   GeneID; 5547668; -.
DR   KEGG; vpo:Kpol_1036p73; -.
DR   eggNOG; ENOG502RYEW; Eukaryota.
DR   HOGENOM; CLU_022388_0_0_1; -.
DR   InParanoid; A7TEM0; -.
DR   OMA; FMNTQIQ; -.
DR   OrthoDB; 1009961at2759; -.
DR   PhylomeDB; A7TEM0; -.
DR   Proteomes; UP000000267; 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:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR   HAMAP; MF_03110; Endonuc_su_Slx4; 1.
DR   InterPro; IPR027784; Slx4_ascomycetes.
DR   InterPro; IPR018574; Structure-sp_endonuc_su_Slx4.
DR   Pfam; PF09494; Slx4; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..680
FT                   /note="Structure-specific endonuclease subunit SLX4"
FT                   /id="PRO_0000388050"
FT   REGION          15..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..170
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   680 AA;  77170 MW;  692545C4F163D1DF CRC64;
     MDFRQAQRNL ELIEEVAKNS QDSDEPIIDE DDLKEGKVEE EGEGTQIPSM PFSDDDDSDN
     NSKDTFKETP LELVDKEEAI EDKAPNDDEP VVSVEEKIAT QEPEPEEQIF MNTQIQGQLD
     DIEQEDNLRS KLSNFKYASE ESSSVQVIKR SNERKLKSKK ITKPKLTKTS KRTKTNSNPS
     TQQTLDEIKI SRSENILKLL SGKHGKVKDM INHQRNVEKK VKLVKNKNSN IITYDTYNSE
     EWLRIMKLIL EKFPSANDME VKQVYHYIYG EEQEQEYDNL WEASQIPLAS MREEAYNEDN
     QIDRKIPNIP NSTQTRVEVM SLSQVMDDVS IIEESKKTTI DSEREMHIYE VPDSTDDEDS
     RIIRVISGSD EVASIVAESE FSTETESTST QFFTADGNMV DGVIDLTQGS FKAVTKLFSP
     LKVDTLLSIN KNKEKVQVAV TRTSTRFSNL GSGPVGLEET PRLAPDEAAT PPTVISRSPQ
     STRTPQATRL PNPNITVMYE VNKCELQSSN SYQSRSSEDI RIVNQYDIDV RDSQDEYDSA
     TEKCLIEFAV TNSATPSVQP EDVMNVISSQ SVQKLRQDLK TIGLKPVRTK AKMIEALMAA
     SQVLDTDNVD QEQTREALYD QLTSMIKQIP ELVSKISRFE PITMEELVLQ LIEVNPFADH
     IDESTIKEWA DIQGITLRNN