ID   A0A3Q1CGN8_AMPOC        Unreviewed;       910 AA.
AC   A0A3Q1CGN8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Staphylococcal nuclease domain-containing protein {ECO:0000256|PIRNR:PIRNR017179};
DE            EC=3.1.31.1 {ECO:0000256|PIRNR:PIRNR017179};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000026100.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000026100.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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   AlphaFoldDB; A0A3Q1CGN8; -.
DR   STRING; 80972.ENSAOCP00000026100; -.
DR   Ensembl; ENSAOCT00000016855.1; ENSAOCP00000026100.1; ENSAOCG00000014166.1.
DR   GeneTree; ENSGT00510000047270; -.
DR   OMA; EKTCCTV; -.
DR   OrthoDB; 375531at2759; -.
DR   Proteomes; UP000257160; Unplaced.
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; 4.
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   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          17..166
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          193..327
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          340..496
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          525..660
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          729..787
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
SQ   SEQUENCE   910 AA;  101945 MW;  68BF38D2960A3C2D CRC64;
     MASVSAPSQT APAPTAPLQR GIVKMVLSGC AIIVRGQPRG GPPPERQINL SNIRAGAMAR
     RAAQGQPDTK DTPDEPWAFQ AREFLRKKLI GKEVCFTVEI RTALGREYGM VYLGKDTTGE
     NIAESLVNEG LATVRREGIR GNNPEQARLC ELEDQAKSSK KGMWSEGGGT HTIRDIKYTI
     ENPRNFVDSL HQKPINAIIE HVRDGSVVRA LLLPDYYLVT VMLSGVKCPT FKREADVETP
     EPFAAEAKFF TESRLLQRDV QIILESCPNQ IILGTILHPN GNITELLLKE GFARCVDWSM
     AVYTQGAEKL RAAERSAKER KVRIWKDYVA PTANLDQKDR QFVAKVMQVV NADAMVVKLN
     SGEYKTIHLS SIRPPRNEGE EKNKDKDKRF RPLYDIPYMF EAREFLRKKL IGKKVNVTVD
     YIRAATGPGE GTPAFPERTC ATVTIGGINI AEALVSKGLA TVIRYRQDDD QRSSHYDELL
     AAEARAIKNG KGLHSKKEVP IHRVADISGE TQKAKQFFPF LQRAGRSEAV VEYVFSGSRL
     KLYMPKETCL ITFLLAGIEC PRSSRNLPGG MQVAEPFSDE AMLFTKELVL QREVEVEVES
     MDKAGNFIGW LHIEGVNLSV ALVENALSKV HFTAERSAYY KTLVSAEDAC RQRKEKIWAN
     YEEKPVEEVV HVSEEKERVA NYRPVYVTEI ADTLHFYTQD VETGGQLESL METMRAEIAA
     QPPVEGSYSA RRGDYCIAKF ADGEWYRARV EKVESPAKVH VFYIDYGNRE VVSSTRLAAI
     PPAFSTRTLP AQATEYAFAF IQVPQDEDAR ADVVDCVVRD IQNSQCLLNV EYSGATCPHV
     TIQFGDTKDD VGLGLVKEGL VMVDVRKEKH LQKMVTEYLN SQESAKSARL NIWRYGDFRA
     DDADEFGYSR
//