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Database: UniProt
Entry: A0A0D2EQ64_9EURO
LinkDB: A0A0D2EQ64_9EURO
Original site: A0A0D2EQ64_9EURO 
ID   A0A0D2EQ64_9EURO        Unreviewed;       406 AA.
AC   A0A0D2EQ64;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=GIY-YIG domain-containing protein {ECO:0000259|PROSITE:PS50164};
GN   ORFNames=PV05_02347 {ECO:0000313|EMBL:KIW57788.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW57788.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW57788.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW57788.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) 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. {ECO:0000256|HAMAP-Rule:MF_03100}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03100};
CC   -!- SUBUNIT: Forms a heterodimer with SLX4. {ECO:0000256|HAMAP-
CC       Rule:MF_03100}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03100}.
CC   -!- SIMILARITY: Belongs to the SLX1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03100}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03100}.
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DR   EMBL; KN847318; KIW57788.1; -; Genomic_DNA.
DR   RefSeq; XP_013318372.1; XM_013462918.1.
DR   AlphaFoldDB; A0A0D2EQ64; -.
DR   STRING; 348802.A0A0D2EQ64; -.
DR   GeneID; 25324255; -.
DR   HOGENOM; CLU_030739_1_0_1; -.
DR   OrthoDB; 276644at2759; -.
DR   Proteomes; UP000054342; 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   CDD; cd10455; GIY-YIG_SLX1; 1.
DR   Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR048749; SLX1_C.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR20208; STRUCTURE-SPECIFIC ENDONUCLEASE SUBUNIT SLX1; 1.
DR   PANTHER; PTHR20208:SF10; STRUCTURE-SPECIFIC ENDONUCLEASE SUBUNIT SLX1; 1.
DR   Pfam; PF01541; GIY-YIG; 1.
DR   Pfam; PF21202; SLX1_C; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50164; GIY_YIG; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_03100};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_03100};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_03100};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_03100};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03100};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03100};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03100};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          8..90
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000259|PROSITE:PS50164"
FT   REGION          100..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   406 AA;  45616 MW;  051E22A4BF12B9DB CRC64;
     MDIKPIPAFY CCYLLRSTVR HASVYVGSSP DPARRLGQHN GRVQGGAVRT SRATLRPWEV
     TCIVAGFPSN IAALQFEWAW QNSHLTRHIT PNDRISFATT RTKTSRSGKT TKRPGRPRTS
     LMDKLSNLHL LLRASYFSKW PLEVRFFNQD AYRSWETWCE RVDTNISPDI KVHFDPSQTQ
     PHQDQDEFTS AQPLQKRRKA DLIGKGGVDG VDPTYARLRG VFEKSQFLLD EDDEQKCTVC
     HSGIDLKKGL FVICHTDHCR SISHVTCLAE TSLKQLGSAS LVPRTGYCPS CKLEHSWQDL
     MQQVTLRMRG VKEIKRLLGK KGKGTAATAA EILEAESEES EAEEEVLTAQ EVVDEELGDD
     QDCDDAASIA STDSYISRAS DFEAGEKPVV SQPRLEIVIE DSEDER
//
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