SLX1_DROER
ID SLX1_DROER Reviewed; 294 AA.
AC B3P230;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Structure-specific endonuclease subunit SLX1 homolog {ECO:0000255|HAMAP-Rule:MF_03100};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
GN Name=slx1; ORFNames=GG12527;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Catalytic subunit of a heterodimeric 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 mus312/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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDV47803.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH954181; EDV47803.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001978845.2; XM_001978809.2.
DR AlphaFoldDB; B3P230; -.
DR SMR; B3P230; -.
DR STRING; 7220.FBpp0131073; -.
DR EnsemblMetazoa; FBtr0132581; FBpp0131073; FBgn0104815.
DR GeneID; 6552290; -.
DR KEGG; der:6552290; -.
DR eggNOG; KOG3005; Eukaryota.
DR OrthoDB; 844266at2759; -.
DR Proteomes; UP000008711; 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; IPR026850; FANCL_C.
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; PF11793; FANCL_C; 1.
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; Zinc; Zinc-finger.
FT CHAIN 1..294
FT /note="Structure-specific endonuclease subunit SLX1
FT homolog"
FT /id="PRO_0000383754"
FT DOMAIN 23..109
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT ZN_FING 197..250
FT /note="SLX1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
SQ SEQUENCE 294 AA; 33993 MW; 3E3D652B07C312DF CRC64;
MNSYDPQDTA SEQQEETVAL KGHFYGVYLL CSQSLDPRFR GKCYVGFTVN PKRRIRQHNL
GCDFGGARKT SRRGPWLMVM IVHGFPNNTV ALQFEWAWQQ PSLSTRLKMY PELKRKLPRE
TFFDYNFRIL SHMLGVGPWN RLPLSVRWLE TDYERPFNMP LPNHMDIVSG KVSISASQRK
RTDDAEVPPP VAWASECHLC MQQIEQPERS RLGCTNQMCR LTCHMMCLAN YLLGDEPGHY
IPVGGQCPLC ENRLSWAALL QRKRLLLGVP KELRDYDEDL IEDIDVDSNI EDTP
