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Database: UniProt
Entry: A0A1S3E8F4_CICAR
LinkDB: A0A1S3E8F4_CICAR
Original site: A0A1S3E8F4_CICAR 
ID   A0A1S3E8F4_CICAR        Unreviewed;       383 AA.
AC   A0A1S3E8F4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   27-MAR-2024, entry version 27.
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   Name=LOC101498619 {ECO:0000313|RefSeq:XP_012571281.2};
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_012571281.2};
RN   [1] {ECO:0000313|RefSeq:XP_012571281.2}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_012571281.2};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_012571281.2; XM_012715827.2.
DR   AlphaFoldDB; A0A1S3E8F4; -.
DR   KEGG; cam:101498619; -.
DR   Proteomes; UP000087171; Chromosome Ca5.
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   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:UP000087171}.
FT   DOMAIN          45..130
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000259|PROSITE:PS50164"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   383 AA;  42436 MW;  12BAA96BE5207E60 CRC64;
     MRKRKGATRS ETNFNSASSC AEEEQSVQVE LQHNQNENEG GDGEGFFACY LLASLNPRFK
     GHTYIGFTVN PRRRIRQHNG EIGCGAWRTK KKRPWEMVLC IYGFPTNVSA LQFEWAWQHP
     VESLAVRKAA VGFKSLSGIA NKIKLAYTML TLPSWQSMNM TVNFFSTKYM KHCAGCPNLP
     QHMTVEMGSM DELPCYTERI DGLLENEDDS TDEVEFDDSN NASTSGGSVP DASDDSITAD
     SPKNMNHIDK VSEPFGWNEE SEAREPPGHS FTPQEQSESF GSISSPKGKS SSTTSSKRGV
     IEDTDFVSSM KTSNGESSKP DSEQTGAVDV RGAFFVPRHA EIIDLSTPSP SCRNVIDRKK
     KRVSSSVSSE FIDLTMSPNF IQL
//
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