ID   U4UHV3_DENPD            Unreviewed;       878 AA.
AC   U4UHV3;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Staphylococcal nuclease domain-containing protein {ECO:0000256|PIRNR:PIRNR017179};
DE            EC=3.1.31.1 {ECO:0000256|PIRNR:PIRNR017179};
GN   ORFNames=D910_09920 {ECO:0000313|EMBL:ERL92607.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL92607.1, ECO:0000313|Proteomes:UP000030742};
RN   [1] {ECO:0000313|EMBL:ERL92607.1, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
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; KB632330; ERL92607.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4UHV3; -.
DR   STRING; 77166.U4UHV3; -.
DR   Proteomes; UP000030742; 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; 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:UP000030742};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..101
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          128..267
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          280..452
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          479..616
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          686..744
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
FT   REGION          317..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   878 AA;  98328 MW;  97BCB02BA61FA8B8 CRC64;
     MLKDVPCTDE PWAWEAREFL RKKLVGQEIL FISEKPPNST REYGTVFLGK DINTAENITE
     SLVSEGLVSV RREGVRPTAE LTRLGELEDE AKRAGKGKWS SSPLSEHVRD VKWSIDNLQV
     FVEKSGGKPI NAVIEHVRDG STVRAFLLPD FHYVTLMITG IRCNGYKFDD QGKPDPTQKV
     EFADEARYFV EVRLLQQDVE IILNSANNTT LSGSIIHPKG NIAEKLLSEG FARCVDWSIS
     ALPTAEIQQL RAAEAKARSE NKRIWKTYQA KTPQITGKEK EFTATVVEVV NGDALQLKLA
     NGAFKKVFLA SIRPPREAGR AAPEDGKPAP RPKGELLSKN SSIPFNEYAL GFRPLYDIPW
     MFEAREYLRK KLIGKKVHVV IDYIQEARDT FPEKSCATVT ISGKNIAEAL VSKGLATVVR
     YRPDDEQRST RYDELLKAES KAEKSQLGVH SKKDSAPLRV TEIDAARAKL ELSAFQRVQT
     IDAIVEFVAS GSRFRVYIPK SNSLATFLLG GISCPRATRP ATGNLPASEG EEFGDEALLF
     TKEKCLQREV TIKVDTHDKA GNFIGWLWVD NLNMSVELVR AGFASVHFTG EKSAYASLLK
     QAEDSAKSQK LRRWKNYVEE EPKEKHVEEE RHVDRKVNYE EVVVTEVSAE GTFFAQKFAD
     GPKAVALLAK LRQEFEANPP LPGAYTPKRG DIAAAKFTLD DEWYRVKVEK VAAGNAVVHY
     IDYGNRETIP TTRLASLPAA YSSEKPFAVE YSLPYVILPK DEEFREIALK YFREDISVPK
     LYLNVESRGA HPQSASLHKD ESGTTDIIRA LIAEGLLLVE NIKSKRPNKL LEDYRAAQDE
     AKKAHLNIWE YGDITEDDAK EFGLGNCKAY FTGDGTIK
//