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Database: UniProt
Entry: Q7ZY98_XENLA
LinkDB: Q7ZY98_XENLA
Original site: Q7ZY98_XENLA 
ID   Q7ZY98_XENLA            Unreviewed;       906 AA.
AC   Q7ZY98;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 96.
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.L {ECO:0000313|RefSeq:NP_001080500.1,
GN   ECO:0000313|Xenbase:XB-GENE-6254060};
GN   Synonyms=2e999 {ECO:0000313|RefSeq:NP_001080500.1}, snd1
GN   {ECO:0000313|RefSeq:NP_001080500.1,
GN   ECO:0000313|Xenbase:XB-GENE-6254060}, snd1-a
GN   {ECO:0000313|RefSeq:NP_001080500.1}, snd1-b
GN   {ECO:0000313|RefSeq:NP_001080500.1}, tdrd11
GN   {ECO:0000313|RefSeq:NP_001080500.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH43884.1};
RN   [1] {ECO:0000313|RefSeq:NP_001080500.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH43884.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH43884.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001080500.1}
RP   IDENTIFICATION.
RG   RefSeq;
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; BC043884; AAH43884.1; -; mRNA.
DR   RefSeq; NP_001080500.1; NM_001087031.1.
DR   STRING; 8355.Q7ZY98; -.
DR   PaxDb; 8355-Q7ZY98; -.
DR   DNASU; 380192; -.
DR   GeneID; 380192; -.
DR   KEGG; xla:380192; -.
DR   AGR; Xenbase:XB-GENE-6254060; -.
DR   CTD; 380192; -.
DR   Xenbase; XB-GENE-6254060; snd1.L.
DR   OMA; EKTCCTV; -.
DR   OrthoDB; 375531at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 380192; Expressed in pancreas and 20 other cell types or tissues.
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:0003676; F:nucleic acid binding; IEA:InterPro.
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; 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; 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; PS01284; TNASE_2; 1.
DR   PROSITE; PS50830; TNASE_3; 4.
DR   PROSITE; PS50304; TUDOR; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR017179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          14..162
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          189..324
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          337..492
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          521..656
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          725..783
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
SQ   SEQUENCE   906 AA;  101281 MW;  E2066B7434F46374 CRC64;
     MASSGAQTGP VAPALQRGIV KMVLSGCAII VRGQPRGGPP PERQINLSNI RAGALARRAA
     ASQQDSKDTP DEPWAFPARE FLRKKLIGKE VCFTVEYKTP QGREYGTVYL GKDTSGENIA
     ESLVAEGLAS RREGVRANTP EQSRLAELEE QARSAKKGVW SEGTGSHTVR DVKYTIENPR
     HFVDSMHQKP VNAVIEHVRD GSVVRALLLP DCYLVTVMLS GIKCPTFKRE ADGTESPEAF
     AAEAKFFTES RLLQRDVQII LESCHNQNIL GTILHPNGNI TELLLKEGFA RCVDWSIAVY
     TQGSEKLRAA ERFAKEHKTR IWRDYVAPTA NLDQKDKQFV AKVVQILNAD AMVVKLNSGD
     YKTIHLSSIR PPRLEGEGAQ DKNKKLRPLY DIPYMFEARE FLRKKLIGKK VNVNVDYIRS
     ASTATETVPA FSERTCATVT IGGINIAEAL VSKGLATVIR YRQDDDQRSS HYDELLAAEA
     RAIKNAKGLH SKKEVPIHRV ADISGDTQKA KQFLPFLQRA GRSEAVVEYV FSGSRLKLYM
     PKETCLITFL LAGIECPRGS RNMPSGVQEG EPFSEEAMLF TKELVLQREV EVEVEAMDKA
     GNFIGWLHID GVNISVALVE HALSKVHFTA ERSNYYKTLL AAEEGPKQRK EKVWSKFEEQ
     PVEEVVTVVE EKERNANYKP VLVTEITDEL HFYIQDVETG TQLEKLMESM RSEIASNPPL
     EGSFSPRRGD YCIAKYMDGE WYRARVEKVE STAKVHVFYI DYGNREVLPS TRLGTLPQSF
     SISTLPAQAI EYCFAFIQVP ADEDARADVV DNVVRDIQNT QCLLNVEYSG AGCPHVTLQF
     TDSKDDVGLG LVKEGLVMVE VRKEKQFHKL IGEYVAAQES AKAARLNLWR YGDFRADDAA
     EFGYSR
//
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