ID A0A2G5UZC7_9PELO Unreviewed; 913 AA.
AC A0A2G5UZC7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, 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};
GN Name=Cni-tsn-1 {ECO:0000313|EMBL:PIC44887.1};
GN Synonyms=Cnig_chr_II.g5098 {ECO:0000313|EMBL:PIC44887.1};
GN ORFNames=B9Z55_005098 {ECO:0000313|EMBL:PIC44887.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC44887.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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:PIC44887.1}.
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DR EMBL; PDUG01000002; PIC44887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5UZC7; -.
DR Proteomes; UP000230233; Chromosome ii.
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; 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:UP000230233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 22..168
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 193..328
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 341..491
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 523..667
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 739..797
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 100662 MW; 3B74F4077C13A948 CRC64;
MSDAAATASP TAPPPASSAT PAVRRGLVKS VLSGDAVILQ GQPQNGPPPE WTVYLSNVSA
PRLGRRPTDS APATPDEPYA WEAREFLRGK LVGQFVTFVR DFTASSGRDH GRVYLGGTSP
ADAENVAEEA VAAGLLEVRQ GKITDDYTTK LLELQEQAKA SGKGKWSSTP GTIREIRWVI
DNPRELVDKY AQKPIDAVIE MVRDGSTVRA FLLPNYEYIT LQLSGVRAPS TKNPTSHDSR
AEPFSEEAKF FVESRLLQRD VQIILESTSN QNFVGSIIHP KGNIAESLLR EGYAKCVDWS
IGLCTGGAQK LRDAERQAKE KRVRLWKSYT PAASGYSGDR KAFSAKVVEV VLNDAVVVQK
EDGTEMKLHL SSIRLPRETG EDKQPSVGRQ FRPLYDVPFM FQAREFLRKR IHGKKVQVQI
DYVQPKSDNF PEKTCATIKH GDLNIAEGLI SRGLSKVVRH RADDENRSCE YDLLLAAEAN
AEKGKKGLFA DKTAEKKDTL RIQEITGDVA KSKQFLPYLQ RGGRAEGVVE FLSGGSRLRI
YIPKETVLIT FLLGGINCPK GSRVGPGGVT IGAAEPFADE AAAFTRKLVL QHEVQLEVES
TDKNGNFVGY LFVSPDGNTS RGINLSEALV EAGLATLHFT AERSGHYNAL LAAENRAKKA
KKNIWANYTE EQHQEEVEVQ QADTSERKQN YRQVAVTDLA PGALRFSAQN IEDGAKIEKM
TSEMRQAIAD HPPLAGSYAA KRGDLCVAKF SEDGLWYRAK VESVRQGQAE IVYIDYGNRE
TVEAAKLAQI PGGFASFPAG VKEYNLALVK LPNEDYVQLT LDAFAQYLYG HSSVFVNSEY
KVGTAEYVTV YFDSGNKKVD IGKSLVEEGL ALADSRREPR LQTLCNEYKS AEDKARKSRK
NIWEYGDFTG NDI
//
