ID A0A1J4JTS7_9EUKA Unreviewed; 260 AA.
AC A0A1J4JTS7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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=TRFO_07425 {ECO:0000313|EMBL:OHT01848.1};
OS Tritrichomonas foetus.
OC Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC Tritrichomonas.
OX NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT01848.1, ECO:0000313|Proteomes:UP000179807};
RN [1] {ECO:0000313|Proteomes:UP000179807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA Tasca T., Bogo M.R., de Souza W.;
RL Submitted (OCT-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHT01848.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLAK01000893; OHT01848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4JTS7; -.
DR VEuPathDB; TrichDB:TRFO_07425; -.
DR OrthoDB; 276644at2759; -.
DR Proteomes; UP000179807; 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 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; 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; SSF57903; FYVE/PHD zinc finger; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000179807}.
FT DOMAIN 4..88
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
SQ SEQUENCE 260 AA; 30201 MW; 6B368FCA0315E3F4 CRC64;
MQSSFAGCYL LRSKNPSYRE ACYVGFTVNP TRRLRQHNGD RSGGAYKTHA KRPWEMTIVV
YGFPTRKQAL KFEWCWQHPT QSTRLKEIHW HEVFQQTGGP TKYKSHIRIL KEMLNIPPWN
RLDLLICVTC PDVLDLLNTE PKIDPHHTVK LGRLEDIPIE TQLIPTPSEK NHPTCLICHN
DHESIGEKLN WIVCPFCSTF FHLRCLARRF IEKTSNSTST LIPTEGTCPT CNEKLLWRNV
VELRNQISDK DSLLHLANDK
//