ID   A0A3B0KSQ5_DROGU        Unreviewed;       927 AA.
AC   A0A3B0KSQ5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Staphylococcal nuclease domain-containing protein {ECO:0000256|PIRNR:PIRNR017179};
DE            EC=3.1.31.1 {ECO:0000256|PIRNR:PIRNR017179};
GN   ORFNames=DGUA_6G009231 {ECO:0000313|EMBL:SPP86928.1};
OS   Drosophila guanche (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP86928.1, ECO:0000313|Proteomes:UP000268350};
RN   [1] {ECO:0000313|Proteomes:UP000268350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endonuclease that mediates miRNA decay of both protein-free
CC       and AGO2-loaded miRNAs. {ECO:0000256|PIRNR:PIRNR017179}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC         phosphooligonucleotide end-products.; EC=3.1.31.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR017179};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR017179}.
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DR   EMBL; OUUW01000012; SPP86928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0KSQ5; -.
DR   STRING; 7266.A0A3B0KSQ5; -.
DR   OMA; EKTCCTV; -.
DR   OrthoDB; 375531at2759; -.
DR   Proteomes; UP000268350; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016442; C:RISC complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0016894; F:endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters; IEA:UniProtKB-EC.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:InterPro.
DR   CDD; cd00175; SNc; 1.
DR   CDD; cd20433; Tudor_TDRD11; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 2.40.50.90; -; 5.
DR   InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR047386; Tudor_TDRD11.
DR   PANTHER; PTHR12302; EBNA2 BINDING PROTEIN P100; 1.
DR   PANTHER; PTHR12302:SF2; STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00565; SNase; 4.
DR   Pfam; PF00567; TUDOR; 1.
DR   PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
DR   SMART; SM00318; SNc; 4.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF50199; Staphylococcal nuclease; 5.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50830; TNASE_3; 4.
DR   PROSITE; PS50304; TUDOR; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR017179};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          24..168
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          196..334
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          347..506
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          536..675
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          750..808
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
SQ   SEQUENCE   927 AA;  103298 MW;  8408164C691D9242 CRC64;
     MATAANTVAA AGAPKDGVPP APAKTLSGIV KQVLSGDTLV IRATKGAPPP EKQITFSHVL
     APKLARRPGA GGDETKDEPW AWESREFLRK KLIGVEVTFT FDKPANSNRE YGFVWIGKDK
     ETGENVVESI VREGLVSVRR EGRPTPEQQT LIELEDQARA AGRGKWSHNV NAVEKVRNIK
     WAHENPAHIV DVYGGKPVKA IIEHVRDGST VRAFLLPDFH YITLMISGIR CPGVKLDADG
     KPDLSVKVPF ADEARYYVET RLLQRDVEIR LESVNNSNFI GSILYPKGNI AESLLREGLA
     KCVDWSMAVM KTGADKLRAA ERVAKEKRLR QWQDYQAKTP AFNSKEKDFG GTVIEVFNGD
     AVNVRLSNGH VKKVFFSSIR PPRDQRAVVG TDGEEIVKAP PRGKNYRPLY EIPHMFDARE
     FLRKKLINKK VQCNLDYISP PRENFPEKYC YTVLIGGQNV AEAMVAKGLA TCVRYRQDDD
     QRSSAYDQLI AAEQQAIKGL KGLHAKKDNA TLRVNDLTVD HSRIKVQYLP SWQRALRSEA
     IVEFVASGSR LRIFVPKDSC LVTFLLAGIS CPRSSRPALN GVPAQEGEPF GDEALTFTRE
     RVLQRDVSVH IDTTDKAGSS VIGWLWTDAG ANLSVALVEE GLAEVHFSAE KSEYYRLLKS
     AEDRAKAAKK NIWANYVEQV PEEKVVVEEE KEEKILVERK VNYENVIVTE ITETLTFFAQ
     SVENGPKLET LMSKLHADFH GNPPIAGSYT PKRGDLVAAQ FTLDNQWYRA KVERIQGSNA
     TVLYIDYGNK ETLPTNRLAA LPPAFSSEKP YATEYALALV ALPADNEDKE EALRAFSEDV
     LNHKVQLNVE LKVAGAPNLA TLHDPTTKTD FGKQLVAEGL VLAEKRRERK LKDLVEQYRA
     AQEAALASHL AIWKYGDITQ DDTPEFR
//