SMG_DROSE
ID SMG_DROSE Reviewed; 998 AA.
AC B4HKJ7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Protein Smaug {ECO:0000250|UniProtKB:Q23972};
GN Name=smg {ECO:0000250|UniProtKB:Q23972}; ORFNames=GM24897;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW40800.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW40800.1};
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).
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|UniProtKB:Q23972}.
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|UniProtKB:Q23972}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q23972}.
CC -!- DOMAIN: The SAM domain mediates the association with the 3'-UTR of
CC specific mRNAs. {ECO:0000250|UniProtKB:Q23972}.
CC -!- SIMILARITY: Belongs to the SMAUG family. {ECO:0000255}.
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DR EMBL; CH480815; EDW40800.1; -; Genomic_DNA.
DR RefSeq; XP_002029814.1; XM_002029778.1.
DR AlphaFoldDB; B4HKJ7; -.
DR SMR; B4HKJ7; -.
DR STRING; 7238.B4HKJ7; -.
DR EnsemblMetazoa; FBtr0207882; FBpp0206374; FBgn0179759.
DR GeneID; 6604971; -.
DR KEGG; dse:6604971; -.
DR HOGENOM; CLU_003304_0_0_1; -.
DR OMA; HHSQHAQ; -.
DR PhylomeDB; B4HKJ7; -.
DR ChiTaRS; smg; fly.
DR Proteomes; UP000001292; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Cytoplasm; Developmental protein; Phosphoprotein; Reference proteome;
KW Repressor; RNA-binding; Translation regulation.
FT CHAIN 1..998
FT /note="Protein Smaug"
FT /id="PRO_0000395317"
FT DOMAIN 600..654
FT /note="SAM"
FT /evidence="ECO:0000255"
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 329..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..763
FT /note="Interaction with cup"
FT /evidence="ECO:0000250|UniProtKB:Q23972"
FT REGION 773..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..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|UniProtKB:Q23972"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q23972"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q23972"
SQ SEQUENCE 998 AA; 108806 MW; C91B9D248A423E90 CRC64;
MKYATGTDNA MTSGISGQTN SSNSASNEMQ PTTSTPTAVH KEATSTATTT ATYANGNPNP
SANPSQSQPS NALFCEQVTT VTNLFEKWND CERTVVMYAL LKRLRYPSLK FLQYSIDSNL
TQNLGTSQTN LSSVVIDINA NNPVYLQNLL NAYKTFQPCD LLDAMSSSSS DKDSMPCYGS
DFQITTSAQC DERKLYARKE DILHEVLNML PLLKPGNEEA KLIYLTLIPV AVKDTMQQIV
PTELVQQIFS YLLIHPAITS EDRRSLNIWL RHLEDHIQAA AAGLTNRSYF LQPSPQLVAG
GSSTGSGSCS SSATSSSTAS CSSVASSSLC PASGSRSSRT NDWQTIAPPS KQLQNKLAGD
WRGSGGGSSS GSINPLCDNL NGITLNELAS SQNSLGLSLE GSSSLVNGVV AGAGSMLGIG
GGDDHDTSFS KNGTEILDFD PVTANMGEAC SLASSSLCGR NGGNPVEDRS QPPPNLQQQL
LQPPPYASIL MGNVGDQFGE INRWSLDSKI AALKTRRSNS LTTQTISSCS SSSNSSVITV
NDNCSNSTEN LAQFANKPRS FSLSIEHQRG ALMNSGSDTR LDEFKPNYIK FHTRNVGMSG
IGLWLKSLRL HKYIELFKNM TYEEMLLITE DFLQSVGVTK GASHKLALCI DKLKERGNIL
NRVEQELLTG QMELSTAVEE LTNIVLTPMK PLESPGPPEE NIGLRFLKVI DIVTNTLQQD
PYAVQDDETL GVLMWILDRS IHNEAFMNHA SQLKDLKFKL SKMKISMVPK MHHVKPAGVG
PNNGNINKPR WNGKTRKCDS KSGSNDRINN RKNSNDMLNF SLNCLPHPLP HHSQQAPPPL
PQFDYNGYGG GPSHQPQYKS SSYPSFMGNP QQQPPPPPSS KSHHHPQQMQ QMLQQHNHFP
ALPQQTPPQS HRRSLNNLIL VAGGPQQPQQ LIFKPGQGVL TNNGSNDNLG LERNQQPQQQ
QQRKLSGGVS SAEQQPKKTM AAVVMENLAK FDQHFTLF
