ID W5NER7_LEPOC Unreviewed; 923 AA.
AC W5NER7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Staphylococcal nuclease domain-containing protein {ECO:0000256|PIRNR:PIRNR017179};
DE EC=3.1.31.1 {ECO:0000256|PIRNR:PIRNR017179};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000019126.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000019126.1}
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 EMBL; AHAT01029099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NER7; -.
DR STRING; 7918.ENSLOCP00000019126; -.
DR Ensembl; ENSLOCT00000019158.1; ENSLOCP00000019126.1; ENSLOCG00000015537.1.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00510000047270; -.
DR InParanoid; W5NER7; -.
DR OMA; EKTCCTV; -.
DR Proteomes; UP000018468; Linkage group LG8.
DR Bgee; ENSLOCG00000015537; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004518; F:nuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
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; IPR002071; Thermonucl_AS.
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 SUPFAM; SSF50199; Staphylococcal nuclease; 5.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS01284; TNASE_2; 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:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 18..167
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 194..329
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 342..506
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 535..670
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 739..800
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 103545 MW; FBDFF042A2D0DA75 CRC64;
MASSSSSQAQ ANAAPSLPLQ RGIVKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGALA
RRAAQNQPDT KDTPDEPWAW PAREFLRKKM IGKEVCFTVE NKTPQGREYG MVYLGKDTSG
ENIAESLVSE GLATVRREGI RGNNPDQVRL CDLEDQAKGA KKGIWSDGSG SHSIRDLKYT
IENPRHFVDS LHQKPVNAII EHVRDGSVVR ALLLPDYYLV TVMLSGVKCP TFKREPDGTE
TPESFAAEAK FFTESRLLQR DVQIILESCP NQVILGTILH PNGNITELLL KEGFARCVDW
SMAVYTQGGE KLRAAERSAK ERKVRIWKDY VAPTANLDQK DKQFVAKVMQ IVNADAIVVK
LNSGEHKTIH LSSIRPPRIE GESNQQEKNK DKDKRFRPLY DIPYMFEARE FLRKKLIGKK
VNVTVDYIRA ATTGADLGTG TGPSFPERTC STVTIGGINI AEALVSKGLA TVIRYRQDDD
QRSSHYDELL AAEARAIKNG KGLHSKKEVP IHRVADISGE TQKAKQFLPF LQRAGRSEAV
VEYVFSGSRL KLYMPKETCL ITFLLAGIEC PRGSRNTPGG VQEAEPFSDE ATLFTKELVL
QREVEVEVES MDKAGNFIGW LHIDGVNLSV ALVEHALSKV HFTAERSSYY KTLLSAEDSA
RQKKEKIWAN YEEQPTEEVV QMTEEKERIA NYKPVYVTEI TDELHMYVQD VGTGTQLEKL
METMRSEIAA HPPVEGSYSP RRGDYCISKF ADGEWYRART SYVNEIQIPN KSYIFKSTYN
KRETVPSTRL AALPPAFNIR TLPAQATEYA FAFIQVPQDE DARADVVDSV VRDIQNTQCL
LNLEYMVGSC PHVTLQFSDS KDDVGLGLVK EGMVMVDVRK EKHLQKMITE YLNAQESAKS
ARLNIWRYGD FRADDADEFG YRR
//
