SND1_DROME
ID SND1_DROME Reviewed; 926 AA.
AC Q9W0S7; Q8T0F1;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Staphylococcal nuclease domain-containing protein 1 {ECO:0000305};
DE EC=3.1.31.1 {ECO:0000269|PubMed:14508492};
DE AltName: Full=Tudor staphylococcal nuclease {ECO:0000312|FlyBase:FBgn0035121};
GN Name=Tudor-SN {ECO:0000312|FlyBase:FBgn0035121};
GN Synonyms=p100 {ECO:0000303|PubMed:19232356},
GN SND1 {ECO:0000303|PubMed:19232356}, TSN {ECO:0000312|FlyBase:FBgn0035121};
GN ORFNames=CG7008 {ECO:0000312|FlyBase:FBgn0035121};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL39506.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39506.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL39506.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:AAO25027.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO25027.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAO25027.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ASSOCIATION WITH THE RISC COMPLEX,
RP INTERACTION WITH AGO2; FMR1 AND VIG, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14508492; DOI=10.1038/nature01956;
RA Caudy A.A., Ketting R.F., Hammond S.M., Denli A.M., Bathoorn A.M.,
RA Tops B.B., Silva J.M., Myers M.M., Hannon G.J., Plasterk R.H.;
RT "A micrococcal nuclease homologue in RNAi effector complexes.";
RL Nature 425:411-414(2003).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PIWI, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ILE-282;
RP GLU-320; GLY-368; 437-ILE--ARG-926 AND GLY-501.
RX PubMed=26808625; DOI=10.1371/journal.pgen.1005813;
RA Ku H.Y., Gangaraju V.K., Qi H., Liu N., Lin H.;
RT "Tudor-SN Interacts with Piwi Antagonistically in Regulating
RT Spermatogenesis but Synergistically in Silencing Transposons in
RT Drosophila.";
RL PLoS Genet. 12:E1005813-E1005813(2016).
RN [7] {ECO:0007744|PDB:2WAC}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 700-916, AND DOMAIN.
RX PubMed=19232356; DOI=10.1016/j.jmb.2009.02.018;
RA Friberg A., Corsini L., Mourao A., Sattler M.;
RT "Structure and ligand binding of the extended Tudor domain of D.
RT melanogaster Tudor-SN.";
RL J. Mol. Biol. 387:921-934(2009).
CC -!- FUNCTION: Endonuclease which shows activity towards both DNA and RNA
CC substrates (PubMed:14508492, PubMed:26808625). Has a role in
CC translation regulation throught its association with the with the RNA-
CC induced silencing complex (RISC) (PubMed:14508492, PubMed:26808625).
CC Plays a role in spermatogenesis probably by negatively regulating piwi
CC expression in the germline (PubMed:26808625). Together with piwi, might
CC be involved in transposon repression in the germline (PubMed:26808625).
CC {ECO:0000269|PubMed:14508492, ECO:0000269|PubMed:26808625}.
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:0000269|PubMed:14508492};
CC -!- SUBUNIT: Associates with the RNA-induced silencing complex (RISC)
CC (PubMed:14508492). Interacts with the RISC components AGO2, Fmr1 and
CC vig (PubMed:14508492). Interacts with piwi (PubMed:26808625).
CC {ECO:0000269|PubMed:14508492, ECO:0000269|PubMed:26808625}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14508492,
CC ECO:0000269|PubMed:26808625}. Nucleus {ECO:0000269|PubMed:14508492,
CC ECO:0000269|PubMed:26808625}. Note=Associates with ribosomes.
CC {ECO:0000269|PubMed:14508492}.
CC -!- TISSUE SPECIFICITY: Expressed in adult ovaries and testis (at protein
CC level). {ECO:0000269|PubMed:26808625}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both germline and somatic cells
CC during oogenesis and spermatogenesis (at protein level).
CC {ECO:0000269|PubMed:26808625}.
CC -!- DOMAIN: Tudor domain specifically binds peptides with symmetrically
CC dimethylated arginines (sDMA) and may facilitate protein-protein
CC interactions. {ECO:0000269|PubMed:19232356}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in defective
CC spermatogenesis. {ECO:0000269|PubMed:26808625}.
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DR EMBL; AE014296; AAF47366.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB93890.1; -; Genomic_DNA.
DR EMBL; AY069361; AAL39506.1; -; mRNA.
DR EMBL; BT003270; AAO25027.1; -; mRNA.
DR RefSeq; NP_001261195.1; NM_001274266.1.
DR RefSeq; NP_612021.1; NM_138177.3.
DR PDB; 2WAC; X-ray; 2.10 A; A/B=700-916.
DR PDBsum; 2WAC; -.
DR AlphaFoldDB; Q9W0S7; -.
DR SMR; Q9W0S7; -.
DR IntAct; Q9W0S7; 24.
DR MINT; Q9W0S7; -.
DR STRING; 7227.FBpp0304417; -.
DR PaxDb; Q9W0S7; -.
DR PRIDE; Q9W0S7; -.
DR DNASU; 38045; -.
DR EnsemblMetazoa; FBtr0072519; FBpp0072419; FBgn0035121.
DR EnsemblMetazoa; FBtr0332107; FBpp0304417; FBgn0035121.
DR GeneID; 38045; -.
DR KEGG; dme:Dmel_CG7008; -.
DR UCSC; CG7008-RA; d. melanogaster.
DR CTD; 38045; -.
DR FlyBase; FBgn0035121; Tudor-SN.
DR VEuPathDB; VectorBase:FBgn0035121; -.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00510000047270; -.
DR HOGENOM; CLU_005966_0_0_1; -.
DR InParanoid; Q9W0S7; -.
DR OMA; FGQEAHD; -.
DR OrthoDB; 227839at2759; -.
DR PhylomeDB; Q9W0S7; -.
DR SignaLink; Q9W0S7; -.
DR BioGRID-ORCS; 38045; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Pep; fly.
DR EvolutionaryTrace; Q9W0S7; -.
DR GenomeRNAi; 38045; -.
DR PRO; PR:Q9W0S7; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035121; Expressed in ovary and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0016442; C:RISC complex; IDA:FlyBase.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0010529; P:negative regulation of transposition; IGI:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR CDD; cd04508; TUDOR; 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 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; SSF50199; 5.
DR PROSITE; PS50830; TNASE_3; 4.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Nuclease; Nucleus;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..926
FT /note="Staphylococcal nuclease domain-containing protein 1"
FT /id="PRO_0000445085"
FT DOMAIN 23..167
FT /note="TNase-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 195..333
FT /note="TNase-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 346..505
FT /note="TNase-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 535..674
FT /note="TNase-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 749..807
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..788
FT /note="Involved in dimethylarginine binding"
FT /evidence="ECO:0000269|PubMed:19232356"
FT MUTAGEN 282
FT /note="I->F: Normal spermatogenesis."
FT /evidence="ECO:0000269|PubMed:26808625"
FT MUTAGEN 320
FT /note="E->K: Defective spermatogenesis."
FT /evidence="ECO:0000269|PubMed:26808625"
FT MUTAGEN 368
FT /note="G->E: Normal spermatogenesis."
FT /evidence="ECO:0000269|PubMed:26808625"
FT MUTAGEN 437..926
FT /note="Missing: Defective spermatogenesis."
FT /evidence="ECO:0000269|PubMed:26808625"
FT MUTAGEN 501
FT /note="G->R: Defective spermatogenesis."
FT /evidence="ECO:0000269|PubMed:26808625"
FT STRAND 703..710
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 714..720
FT /evidence="ECO:0007829|PDB:2WAC"
FT HELIX 721..723
FT /evidence="ECO:0007829|PDB:2WAC"
FT HELIX 724..740
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 755..759
FT /evidence="ECO:0007829|PDB:2WAC"
FT TURN 761..763
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 766..775
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 778..783
FT /evidence="ECO:0007829|PDB:2WAC"
FT TURN 784..786
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 789..793
FT /evidence="ECO:0007829|PDB:2WAC"
FT HELIX 794..796
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:2WAC"
FT HELIX 802..804
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 805..807
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 810..816
FT /evidence="ECO:0007829|PDB:2WAC"
FT HELIX 825..839
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 843..850
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 857..862
FT /evidence="ECO:0007829|PDB:2WAC"
FT TURN 864..866
FT /evidence="ECO:0007829|PDB:2WAC"
FT HELIX 870..876
FT /evidence="ECO:0007829|PDB:2WAC"
FT STRAND 879..882
FT /evidence="ECO:0007829|PDB:2WAC"
FT HELIX 888..890
FT /evidence="ECO:0007829|PDB:2WAC"
FT HELIX 891..906
FT /evidence="ECO:0007829|PDB:2WAC"
FT HELIX 910..912
FT /evidence="ECO:0007829|PDB:2WAC"
SQ SEQUENCE 926 AA; 103100 MW; 432321EBD8FCAE27 CRC64;
MATAANTATA AGAAKDAPPA PTKSLSGIVK QVLSGDTVVI RATKGAPPPE KQITFSHVLA
PKLARRPGAG GDETKDEPWA WESREFLRKK LIGVEVTFTF DKPANSNREY GFVWIGKDKE
TGENVVESIV REGLVSVRRE GRPTAEQQTL IELEDQARAA GRGKWSPTAS AADKVRNIKW
SHENPAHLVD IYGGNPVKAI IEHVRDGSTV RAFLLPDFHY ITLMISGIRC PGVKLDADGK
PDLSVKVPFA DEARYYVETR LLQRDVEIRL ESVNNSNFIG TILYPKGNIA ESLLREGLAK
CVDWSMAVMK TGTDKLRAAE RFAKEKRLRQ WQDYQAKTPA FNSKEKDFSG TVVEVFNGDA
INVRLSNGQV KKVFFSSIRP PRDQRAVVGT DGEEIVKAPP RGKNYRPLYE IPHMFDAREF
LRKKLINKKV QCNLDYISPP RENFPEKYCY TVSIGGQNVA EAMVAKGLAT CVRYRQDDDQ
RSSAYDQLIA AEQQAIKGLK GLHAKKDNAT LRVNDLTVDH SRIKVQYLPS WQRALRTEAI
VEFVASGSRL RIFVPKDSCL VTFLLAGISC PRSSRPALNG VPAQEGEPFG DEALTFTRER
VLQRDVSVHI DTTDKAGSSV IGWLWTDSGA NLSVALVEEG LAEVHFSAEK SEYYRQLKIA
EDRAKAAKKN IWTNYVEEVP KEKTVTEEEK EDKVVAERKV NYENVIVTEI TETLTFFAQS
VESGSKLESL MSKLHADFQS NPPIAGSYTP KRGDLVAAQF TLDNQWYRAK VERVQGSNAT
VLYIDYGNKE TLPTNRLAAL PPAFSSEKPY ATEYALALVA LPTDNEDKEE ALRAFSEDVL
NHKVQLNVEL KVTGSPNLAT LRDPTTKVDF GKQLVAEGLV LAEQRGERKL KELVDQYKAA
QEAARVAHLA IWKYGDITQD DAPEFR
