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SLX1_VANPO
ID   SLX1_VANPO              Reviewed;         319 AA.
AC   A7TTE6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Kpol_223p3;
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: 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; DS480564; EDO14460.1; -; Genomic_DNA.
DR   RefSeq; XP_001642318.1; XM_001642268.1.
DR   AlphaFoldDB; A7TTE6; -.
DR   SMR; A7TTE6; -.
DR   STRING; 436907.A7TTE6; -.
DR   EnsemblFungi; EDO14460; EDO14460; Kpol_223p3.
DR   GeneID; 5542452; -.
DR   KEGG; vpo:Kpol_223p3; -.
DR   eggNOG; KOG3005; Eukaryota.
DR   HOGENOM; CLU_030739_1_1_1; -.
DR   InParanoid; A7TTE6; -.
DR   OMA; LQFEHAW; -.
DR   OrthoDB; 844266at2759; -.
DR   PhylomeDB; A7TTE6; -.
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: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; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..319
FT                   /note="Structure-specific endonuclease subunit SLX1"
FT                   /id="PRO_0000383802"
FT   DOMAIN          20..103
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         233..297
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
SQ   SEQUENCE   319 AA;  36874 MW;  B24BD14747DABDF7 CRC64;
     MMNSSQFSDS QTTSLHRIPT FYCCYLLQSI NKKQSFYIGS TPNPVRRLRQ HNGNLSNGGA
     YRTKREGTRP WEMVLVVYGF TSKIAALQFE HAWQHGYKTH YIPMDDRIMK NANSGRTVHH
     KLGLVRQLLA NVYFRHMNLK VHFFSMPILD VWNLNKFNIK MGSNEISVDV SQVSQETKTN
     LEQASDDDDD NGACSRDERN LQLVTELYDN TVTKENEIKE IIKDILVLGE RNCNLCGQCY
     DYTSEDDTMK MHIFICPNST CHYEAHLNCL YEKFIEEESG IDSKNILLPN FCMCPGCLDE
     MSWSDFVKIS TMIKNSFSN
 
 
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