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EIF3D_EMENI
ID   EIF3D_EMENI             Reviewed;         586 AA.
AC   Q5AVZ0; C8VBM6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=AN7540;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000129; EAA62120.1; -; Genomic_DNA.
DR   EMBL; BN001304; CBF79596.1; -; Genomic_DNA.
DR   RefSeq; XP_680809.1; XM_675717.1.
DR   AlphaFoldDB; Q5AVZ0; -.
DR   SMR; Q5AVZ0; -.
DR   STRING; 162425.CADANIAP00000646; -.
DR   EnsemblFungi; CBF79596; CBF79596; ANIA_07540.
DR   EnsemblFungi; EAA62120; EAA62120; AN7540.2.
DR   GeneID; 2869682; -.
DR   KEGG; ani:AN7540.2; -.
DR   VEuPathDB; FungiDB:AN7540; -.
DR   eggNOG; KOG2479; Eukaryota.
DR   HOGENOM; CLU_024521_2_0_1; -.
DR   InParanoid; Q5AVZ0; -.
DR   OMA; PDGWGPC; -.
DR   OrthoDB; 1030308at2759; -.
DR   Proteomes; UP000000560; Chromosome IV.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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..586
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D"
FT                   /id="PRO_0000364175"
FT   REGION          107..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..315
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
FT   REGION          566..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..586
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  64872 MW;  1B5949AD48342AFF CRC64;
     MAPISIADIV AALPAEDTWG PVTSADNMLD GVPYAPFSKG DKLGRMADWT ADSKDRDRGG
     RQAYNRNYRD QQVYGAGSSS LFAVQVAEDE STFSVVDNTR TSAKRTFGRG GGTVFRGRAQ
     RGGAGQRGGR AGFQRVGAGR GQGGDRYYDN RGARGNRGRR FGWKDYDKPQ RTREPSVNIR
     PDWSMLEEVD FNRLSKLNLQ APEGEDVDTY GFLYYYDRSY DKAPVKNAER RLQALDRAAY
     NVTTSQDPVI QELAEKNQAT IFATSDILSM LMCAPRSVYS WDIVIVHQGN KIYFDKREGA
     SLDLVTVNEN AADAPLEVAE SSGKQESINT PSALALEATF INHNFALQTV VEANNAKVDF
     NHPNPFYNAE EETEPLASKG YKYRRFDLSL ESDEEPLNMI VRTEVDALVK NPVNGEDQQL
     VVKALNEFDS KAQGSGGSLD WRSKLYSQRG AVVATEMKNN SCKLARWTTQ AILAKADGMK
     LGFVSRANPR SAAAHVVLGV AGYKPREFAA QMNLNLGNGW GIVRTIVDRI RALDADEEED
     KVTKYILVKD PNRPVLRLYS VPANAFEEDD EAAEEEQEAK GEVEEA
 
 
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