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EIF3D_USTMA
ID   EIF3D_USTMA             Reviewed;         579 AA.
AC   Q4PEZ2; A0A0D1CYN5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit D {ECO:0000255|HAMAP-Rule:MF_03003};
DE            Short=eIF3d {ECO:0000255|HAMAP-Rule:MF_03003};
GN   ORFNames=UMAG_01321;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: mRNA cap-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation. In the
CC       eIF-3 complex, eif3d specifically recognizes and binds the 7-
CC       methylguanosine cap of a subset of mRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_03003}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- DOMAIN: The RNA gate region regulates mRNA cap recognition to prevent
CC       promiscuous mRNA-binding before assembly of eif3d into the full
CC       eukaryotic translation initiation factor 3 (eIF-3) complex.
CC       {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit D family. {ECO:0000255|HAMAP-
CC       Rule:MF_03003}.
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DR   EMBL; CM003141; KIS71423.1; -; Genomic_DNA.
DR   RefSeq; XP_011387230.1; XM_011388928.1.
DR   AlphaFoldDB; Q4PEZ2; -.
DR   SMR; Q4PEZ2; -.
DR   STRING; 5270.UM01321P0; -.
DR   EnsemblFungi; KIS71423; KIS71423; UMAG_01321.
DR   GeneID; 23562386; -.
DR   KEGG; uma:UMAG_01321; -.
DR   VEuPathDB; FungiDB:UMAG_01321; -.
DR   eggNOG; KOG2479; Eukaryota.
DR   HOGENOM; CLU_024521_2_0_1; -.
DR   InParanoid; Q4PEZ2; -.
DR   OMA; PDGWGPC; -.
DR   OrthoDB; 1030308at2759; -.
DR   Proteomes; UP000000561; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IBA:GO_Central.
DR   GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
DR   GO; GO:0098808; F:mRNA cap binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0002191; P:cap-dependent translational initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   HAMAP; MF_03003; eIF3d; 1.
DR   InterPro; IPR007783; eIF3d.
DR   PANTHER; PTHR12399; PTHR12399; 1.
DR   Pfam; PF05091; eIF-3_zeta; 1.
DR   PIRSF; PIRSF016281; EIF-3_zeta; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..579
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D"
FT                   /id="PRO_0000364180"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..321
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
SQ   SEQUENCE   579 AA;  62882 MW;  BF686192EE085654 CRC64;
     MASFKLPELQ PDNDLWGPAS GSNALPAELK DIPFAPYAKN DKVGRIADWN NASGASNDAA
     NARGGRQGRA RDVQQNFGTS AASSAFAYFH GDDEASFSVV DNTRTVASRR GGLGQMSQRG
     GRGGRGGAGG AGAAGGRGAS KFGAGAGRGA RGGRGGAAGA RRGGGRFGWK EWDKPQRIRE
     ASVTVGQDWE QVEEIDFVRL GKLRLEVEEP QDISSYGSLF EYDRSYDRVT VKTAQSLSSI
     DRIRYNTTTS EDPVIHDISA KEDAQIYMTD SILALLMCAT RSVYSWDVII TKTADGKVFF
     DKRDGGAFDY LTVNENAADP PSEASEGKEN EAAAKANAIN TPSALSLEAT YINQNFAFQV
     VNEKNVYKLE HENPFYSSDE TAPLASCAYR YRKFNLSSEE SDPVELVVRT EVDAYTVGAS
     KEKQLITIKS LNEFDARAQG AGGALDWRLK LDSQRGAVVA TEMKNNSFKL ARFAVQSLLA
     GADSMKLGYI SRANPKDTSR HMILGTSWLK PRELAAQMAV NLSNGWGIVR TVADLARKAE
     QGKYVLLKDP NKQTIRMYRV PANFGEENDE IVEEDEADE
 
 
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