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Database: UniProt
Entry: A0A0V1LUP0_9BILA
LinkDB: A0A0V1LUP0_9BILA
Original site: A0A0V1LUP0_9BILA 
ID   A0A0V1LUP0_9BILA        Unreviewed;       933 AA.
AC   A0A0V1LUP0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Staphylococcal nuclease domain-containing protein {ECO:0000256|PIRNR:PIRNR017179};
DE            EC=3.1.31.1 {ECO:0000256|PIRNR:PIRNR017179};
GN   Name=SND1 {ECO:0000313|EMBL:KRZ63231.1};
GN   ORFNames=T02_8175 {ECO:0000313|EMBL:KRZ63231.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ63231.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ63231.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ63231.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ63231.1}.
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DR   EMBL; JYDW01000002; KRZ63231.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1LUP0; -.
DR   Proteomes; UP000054721; 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; 2.
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; 5.
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:UP000054721};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          20..168
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          195..331
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          343..495
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          541..679
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          762..820
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   933 AA;  104450 MW;  8D885622E7F172F2 CRC64;
     MYPNNVSSQT PQPAPVSSPP LMRGIGKMAL GGDSIVIRGQ PKGGPPPERL INLSNVISPK
     LARRQADSTA TDSQDEPYAW EAREALRKLV VGHELLFTVD YKVPTSGREY GSVFVTIDGK
     RQNVAETLVS QGWLEVRQSG VKSNDDAVKR LLELQNTAKA NSKGKWQADD ATKHVRQIIW
     STANPRSLVE SFNRSRIKAV IEHVRDGCTV RAFLLPSFHY VTIMISGIRT PTFKLGEGGM
     IQDPEPFAEE AKFFTECRLL QNDVEVILEG ASNQNFLGTV LHKHGNIAEA LLKEGFAKCV
     DWSMPLVTSG PEKLREAERQ AKERRLRLWK NYEPSHAKAA GENSFQAKVV EITLGDSMII
     KKQDGMYQKI FLSSIRPPRL EDAGLVRETQ SGRQFRPLYD IPFMFAAREV LRKKLIGKKV
     NVTIDYVQPS VNQLPERTCC TVVFGGQNMA ELLVSKGLAA VVRNRQGDEN RSPFYDNLLT
     AEAAAEKARL GIHSLKHSVD ANHMETANIY NTSEKQIVRL QELQGNVAKS KQFLPFLIRS
     GRTDGLVEFV VTGSRLRIFV PKESIMITLL LGGVSCPRPG RMTKGGGAAE AEDEPFSQEA
     LQFTKDFCLQ REVEFEVESV DKAGNFIGWC FFHGKNLSEL LVENGLAAVH FTADRSKYGP
     ALRAAELRAK EAKLKIWTLA YYDDETEELN DADDLDKGPS AAPSAGIVPE RVPQYRAVLV
     TEICENLKFY IQYFDQGSQL EQMMKEMRTA LNADPGRQGA FVPKKGDVCA ALFSADQQWY
     RARVEAVRKD EIDVFYIDFG NRETRKQNEL ASLPAGFASR PPGARECAFA LLKLPDDADY
     CTAAVKHFYK EVNGEQCLMN MEYRLGGVEY VTLLRADQSD IGKSLIRNGY CLVEQRRDRK
     MQLQLADYLQ AQESAKSERL NIWQYGDFTG NEL
//
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