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Database: UniProt
Entry: A0A445EVL4_ARAHY
LinkDB: A0A445EVL4_ARAHY
Original site: A0A445EVL4_ARAHY 
ID   A0A445EVL4_ARAHY        Unreviewed;       384 AA.
AC   A0A445EVL4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 11.
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=Ahy_A01g004277 {ECO:0000313|EMBL:RYR79463.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR79463.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR79463.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR79463.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) 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:RYR79463.1}.
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DR   EMBL; SDMP01000001; RYR79463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445EVL4; -.
DR   STRING; 3818.A0A445EVL4; -.
DR   Proteomes; UP000289738; Chromosome a01.
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   SMART; SM00465; GIYc; 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:UP000289738}.
FT   DOMAIN          32..117
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000259|PROSITE:PS50164"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  41954 MW;  749021415F195ED7 CRC64;
     MRKRKGSSKS LASSASTSSS TSSSSSTPQE HGFFACYLLA SLNPRFKGHT YIGFTVNPRR
     RIRQHNGEIG CGAWRTKKKR PWEMVLCIYG FPTNVAALQF EWAWQHPVES LAVRKAAANF
     KSLSGVANKI KLAYTMLTLP SWQSMDMTVN FFSTKYMKHS AGCPSLPEHM TIEMGEMDEL
     PCYTGRIDGL VSDNDDIDEG EFGKNNSNSD IVPDMCGGVS IAHDSDQNNG DKISESIAQN
     QKSEAAGEQT THPLASQDSS DSIMTGEDTN LVSAMNNGGS NISDGLSQSE CDQPLPATSP
     KRVEIIVMNK SNSCAVLAAN NNNNQESRRM FLVPHEAEII DLSTPSPSCS RRVLDSNKKR
     RVSSSLCVGA DFIDLTKSPN FVQL
//
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