SMG_DROYA
ID SMG_DROYA Reviewed; 999 AA.
AC P60320; B4PFF7;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Protein Smaug;
GN Name=smg; ORFNames=GE21267;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 861-986.
RX PubMed=14525923; DOI=10.1101/gr.1311003;
RA Domazet-Loso T., Tautz D.;
RT "An evolutionary analysis of orphan genes in Drosophila.";
RL Genome Res. 13:2213-2219(2003).
CC -!- FUNCTION: Translation regulator that binds to the 3'-UTR of specific
CC mRNAs such as nanos (nos) and prevent their translation. Prevents
CC translation of unlocalized nos in the bulk cytoplasm via the
CC recruitment of cup (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with oskar (osk). Binds to the 3'-UTR of nos.
CC Interacts with cup, which in turn recruits eIF4-E, leading to an
CC indirect interaction between smg and eIF4-E that prevents mRNA
CC translation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The SAM domain mediates the association with the 3'-UTR of
CC specific mRNAs.
CC -!- SIMILARITY: Belongs to the SMAUG family. {ECO:0000305}.
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DR EMBL; CM000159; EDW93083.1; -; Genomic_DNA.
DR EMBL; AY231956; AAR09979.1; -; mRNA.
DR RefSeq; XP_002093371.1; XM_002093335.2.
DR AlphaFoldDB; P60320; -.
DR SMR; P60320; -.
DR STRING; 7245.FBpp0266277; -.
DR EnsemblMetazoa; FBtr0267785; FBpp0266277; FBgn0067927.
DR GeneID; 6532627; -.
DR KEGG; dya:Dyak_GE21267; -.
DR eggNOG; KOG3791; Eukaryota.
DR HOGENOM; CLU_003304_0_0_1; -.
DR OMA; HHSQHAQ; -.
DR OrthoDB; 670335at2759; -.
DR PhylomeDB; P60320; -.
DR ChiTaRS; smg; fly.
DR Proteomes; UP000002282; Chromosome 3L.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0034655; P:nucleobase-containing compound catabolic process; IEA:UniProt.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd09557; SAM_Smaug; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.170; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015327; PHAT_dom.
DR InterPro; IPR037093; PHAT_dom_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037634; Smaug_SAM.
DR Pfam; PF09246; PHAT; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Phosphoprotein; Repressor; RNA-binding;
KW Translation regulation.
FT CHAIN 1..999
FT /note="Protein Smaug"
FT /id="PRO_0000071973"
FT DOMAIN 600..654
FT /note="SAM"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..763
FT /note="Interaction with cup"
FT /evidence="ECO:0000250"
FT REGION 773..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 905
FT /note="Q -> H (in Ref. 2; AAR09979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 999 AA; 109049 MW; 2BBD2FA4D1A876A3 CRC64;
MKYATGTDNA MTSGISGQTN NSNSVSNEMQ PTTSTPTAVH KEATSTATTT ATYANGNPNS
NANPSQSQPS NALFCEQVTT VTNLFEKWND CERTVVMYAL LKRLRYPSLK FLQYSIDSNL
TQNLGTSQTN LSSVVIDINA NNPVYLQNLL NAYKTFQPCD LLDAMSSSSS DKDSMPCYGS
DFQITTSAQC DERKLYARKE DILHEVLNML PLLKPGNDEA KLIYLTLIPV AVKDTMQQIV
PTELVQQIFS YLLIHPAITS EDRRSLNIWL RHLEDHIQAA AAGLTNRSYF LQPSPQLVAG
GSSTGSGSCS SSATSSSTAS CSSVASSSMC PASGSRSSRT NDWQTIAPPS KQLQNKLAGD
WRGSGGGSSS GSINPLCDNL NGITLNELAS SQNSLGLSLE GSSSLVNGVV AGAGSMLGIG
GGDDHDTSFS KNGTEILDFD PVTADMGEAC SLASSSLCGR SGGNPVEDRS QPPPNLQQQL
LQPPPYASIL MGNVGDQFGE INRWSLDSKI AALKTRRSNS LTTQTISSCS SSSNSSVITV
NDNCSNSTEN LAQFANKPRS FSLSIEHQRG ALINSGSDTR LDEFKPNYIK FHTRNVGMSG
IGLWLKSLRL HKYIELFKNM TYEEMLLITE DFLQSVGVTK GASHKLALCI DKLKERANIL
NRVEQDLLTG QMELSTAVEE LTNIVLTPMK PLESPGPPEE NIGLRFLKVI DIVTNTLQQD
PYAAQDDETL GVLMWILDRS IHNEAFMNHA SQLKDLKFKL SKMKISMVPK MHHVKPAGVG
PNNGNINKPR WNGKTRKCDT KNGSNDRINN RKNSNDMLNF SLNCLPHPLP HHSQQPPPPL
PQFDYNGYGG GPSHQPQYKS SSYPSFMGNP QQQPPPPPPS KAHHHAQQMQ QMLQQHNHFP
ALPQQTPPQS HRRSLNNLIL VTGGPQQPQQ MIFKPGQGVL TNNGSNDNLG LERNQQPQQQ
QQQRKLSGGV SSVEQQPKKT MAAVVMENLA KFDQHFTLF
