ID A0A3B3RZQ3_9TELE Unreviewed; 267 AA.
AC A0A3B3RZQ3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Structure-specific endonuclease subunit slx1-like {ECO:0000313|Ensembl:ENSPKIP00000023959.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000023959.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000023959.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Ensembl; ENSPKIT00000004649.1; ENSPKIP00000023951.1; ENSPKIG00000007396.1.
DR Ensembl; ENSPKIT00000004657.1; ENSPKIP00000023959.1; ENSPKIG00000007396.1.
DR GeneTree; ENSGT00390000013368; -.
DR OrthoDB; 276644at2759; -.
DR Proteomes; UP000261540; Unplaced.
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 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; 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 SUPFAM; SSF82771; GIY-YIG endonuclease; 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 Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03100};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03100}.
FT DOMAIN 7..90
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
SQ SEQUENCE 267 AA; 30564 MW; 717A4A2356224BC6 CRC64;
MVVEVESFFG VYMLYCTNPK FKGRIYIGFT VNPERRIGQH NAGRHKGGAK RTSGRGPWEM
ILIIHGFPSD IAALRFEWAW QHPHSSRRLS HVGRRSRRES SLQFHWRVLS HMLQVAPWNR
LPLTARWLRQ EYRLEFEPGL QPPLHVPVVF GSVRAKKQQP PVPTEQERGE EGPGGRCHLC
LDAVKAADRV SCFRPSCEMV AHLICLAKHF LKSEPSHLLP VEGKCPGCRH SMLWGNLIRH
KTGCYGDLEE IASSATSREH WADELQV
//
