ID A0A2G5EV80_AQUCA Unreviewed; 467 AA.
AC A0A2G5EV80;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Structure-specific endonuclease subunit SLX1 homolog {ECO:0000256|HAMAP-Rule:MF_03100};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_03100};
GN ORFNames=AQUCO_00400493v1 {ECO:0000313|EMBL:PIA59634.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA59634.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA59634.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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: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 a member of the SLX4 family.
CC {ECO:0000256|HAMAP-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; KZ305021; PIA59634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5EV80; -.
DR STRING; 218851.A0A2G5EV80; -.
DR InParanoid; A0A2G5EV80; -.
DR OrthoDB; 276644at2759; -.
DR Proteomes; UP000230069; 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 CDD; cd10455; GIY-YIG_SLX1; 1.
DR Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 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 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 PROSITE; PS50164; GIY_YIG; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069}.
FT DOMAIN 37..121
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT REGION 201..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..33
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 208..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 53350 MW; 8BE0046E2B726FB8 CRC64;
MGKRKERRIE RLLEEQENKE EEEVGVEEEV EEETTKGFFA CYLLCSLCPR FKGQTYIGFT
VNPRRRIRQH NGELRSGAWR TKSKRPWEMI LCIYGFPTNI IALQFEWAWQ HPRESLAVRN
AAASLKSLSG IVGKIKLAYT MLTLPPWQRL NLTVNFFSTK YMNNANGCKS LPKQMKVQFG
PMDELPCYTD GSQIFDEMDD QDDEDEYSKN GTNDRHLQGT LKKSDHHHSR LEAVNDALKV
IEKESDRQPG EQFTLGVEDK SNEPLSLLGE DSFEEEFTLR GYDHRLPYHV DDSPLITSSR
STCLVNIEEI VEDRLADTTT SREHQLSSNH GYLHSPELSC RETNELLAGA DDCDGLHYPL
VDLPVKTSLS SDCGLVKTVQ DQDSSQLNQE TYNLEVLSPK QCSKIPSVTD INRPLSGKSL
LASPEVIDIS TPTSSYMISS FRRKKRRNNW ISQKIIDLTN SPDFVQL
//
