ID   A0A3Q2VY02_HAPBU        Unreviewed;       908 AA.
AC   A0A3Q2VY02;
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   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000017086.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000017086.1}
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}.
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DR   RefSeq; XP_014191613.1; XM_014336127.1.
DR   AlphaFoldDB; A0A3Q2VY02; -.
DR   STRING; 8153.ENSHBUP00000017086; -.
DR   Ensembl; ENSHBUT00000025763.1; ENSHBUP00000017086.1; ENSHBUG00000019135.1.
DR   GeneID; 102298229; -.
DR   CTD; 27044; -.
DR   GeneTree; ENSGT00510000047270; -.
DR   OMA; EKTCCTV; -.
DR   OrthoDB; 375531at2759; -.
DR   Proteomes; UP000264840; 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; 3.
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:UP000264840};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          15..163
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          190..325
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          338..494
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          523..658
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          727..785
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
SQ   SEQUENCE   908 AA;  101844 MW;  6BAB2D88AD0A4998 CRC64;
     MASVSGPAQT ASAPPLQRGI VKMVLSGCAI IVRGQPRGGP PPERQINLSN IRAGALARRA
     AQGQPDSKDT PDEPWAFQAR EFLRKKLIGK EVCFTVEYKN MHREYGMVYL GKDTTGENIA
     ESLVSEGLAT VRREGFRGNN PEQARLCDLE DQSKASKKGL WSEGGGAQTI RNIKYTIENP
     RNFVDSLHQK PINAIIEHVR DGSVVRALLL PDYYLVTVML SGIKCPTFKR EGDGTETPEP
     FAAEARFFTE SRLLQRDVQI ILESCPNQII LGTILHPNGN ITELLLKEGF ARCVDWSMAV
     YTQGAEKLRA AERSAKERKV RIWKDYVAPT ANLDQKDRQF VAKVMQVVNA DAMVVKLNSG
     EYKTIHLSSI RPPRNEGEEK NKDKDKRFRP LYDIPYMFEA REFLRKKLIG KKVNVTVDYI
     RAATGPGEGT PAFPERTCAT VTIGGINIAE ALVSKGLATV IRYRQDDDQR SSHYDELLAA
     EARAIKNGKG LHSKKEVPIH RVADISGETQ KAKQFLPFLQ RAGRSEAVVE YVFSGSRLKL
     YMPKETCLIT FLLAGIECPR SSRNTPGGVQ VAEPFSDEAM LFTKELVLQR EVEVEVESMD
     KAGNFIGWLH IEGVNLSVAL VENALSKVHF TAERSAYYKT LVAAEEGCRQ RKEKVWANYE
     EKPVEEVVHL SEEKERVANY KPVYVTEITD TLHFYAQDVE TGSQLENLME TMRAEIAAQP
     PVEGSYSPRR GDYCIAKFAD GEWYRARVEK VESPAKVHVF YIDYGNREVV SSTRLAPIPP
     AFSTRTLPVQ ATEYTFAFIQ VPQDEDARAD VVDCVVRDIQ NSQCLLNVEY SGATCPHVTI
     QFGDTKEDVG LGLVKEGLVM VDVRKEKHLQ KMVTEYLNSQ ESAKSARLNI WRYGDFRADD
     ADEFGYSR
//