ID A0A158NIG0_ATTCE Unreviewed; 268 AA.
AC A0A158NIG0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=105620436 {ECO:0000313|EnsemblMetazoa:XP_012057318.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012057318.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012057318.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) 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 EMBL; ADTU01016457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012057318.1; XM_012201928.1.
DR AlphaFoldDB; A0A158NIG0; -.
DR STRING; 12957.A0A158NIG0; -.
DR EnsemblMetazoa; XM_012201928.1; XP_012057318.1; LOC105620436.
DR GeneID; 105620436; -.
DR KEGG; acep:105620436; -.
DR eggNOG; KOG3005; Eukaryota.
DR InParanoid; A0A158NIG0; -.
DR OMA; HNRGCDF; -.
DR OrthoDB; 276644at2759; -.
DR Proteomes; UP000005205; 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; 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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022771};
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:UP000005205};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 11..96
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
SQ SEQUENCE 268 AA; 31379 MW; 793455326DDF1C06 CRC64;
MMEEESEVIE HFFGVYLLYC MNPRYKGRTY IGYTVDPRRR IKQHNAGKKH GGAWKTSNRG
PWNMILIVHG FPNSTSALRF EWAWQHPDVS RRLKHVPRKK SSQKILDFQL IVLSEMLKIG
PWYRLPLTIR WLDYQFSKNY YEYISPPLHM PICYSKVTSC KVKQTQKTNE DNILSQLPIK
KSLIFCSLCD SNIIEKDSVT CIKPKCFLIV HLICLAKEFC KDDMILPIEG ICPMCKSNVL
WGDLIKKRMV IIKALEEINI NFSNNDAI
//