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EIF3D_ASPFU
ID   EIF3D_ASPFU             Reviewed;         585 AA.
AC   Q4X054;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=AFUA_2G14670;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000001; EAL93761.1; -; Genomic_DNA.
DR   RefSeq; XP_755799.1; XM_750706.1.
DR   AlphaFoldDB; Q4X054; -.
DR   SMR; Q4X054; -.
DR   STRING; 746128.CADAFUBP00002969; -.
DR   EnsemblFungi; EAL93761; EAL93761; AFUA_2G14670.
DR   GeneID; 3513495; -.
DR   KEGG; afm:AFUA_2G14670; -.
DR   VEuPathDB; FungiDB:Afu2g14670; -.
DR   eggNOG; KOG2479; Eukaryota.
DR   HOGENOM; CLU_024521_2_0_1; -.
DR   InParanoid; Q4X054; -.
DR   OMA; PDGWGPC; -.
DR   OrthoDB; 1030308at2759; -.
DR   Proteomes; UP000002530; 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..585
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D"
FT                   /id="PRO_0000364169"
FT   REGION          110..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..314
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
FT   REGION          560..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..585
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   585 AA;  65231 MW;  769F461E52DC0C39 CRC64;
     MAPMSIADLV AALPAEDTWG PATPSDNMLD GVPYAPFSKG DKLGRMADWT GDGKDRDRSG
     RQAYNRNYRD QQVYGAGTSS LFNIQVAEDE SSFSVVDNTR TSTKRTFARG GGTVFRGRGQ
     RGVGQRGGRA GFQRVGAGRG QGGDRYYDNR SARSNRGRRF GWKDYDKPQR TREPSVNVRP
     DWTMLEEVDF NRLSKLNLEA PEGEDLDSYG FLYYYDRSYD KAPVKNAERK LQALERAAYN
     VTTSQDPVIQ ELAEKNEATV FATSDILSML MCAPRSVYSW DIVIVHQGDK IYFDKREGAS
     IDLVTVNENA ADAPVETADS SGKQESINTP SALALEATFI NHNFALQTVV ESEESKVTFN
     HPNPFYNAAE ETEPLASKGY KYRRFDLSLQ DDEEPLNMIV RTEVDAVMKN PVGGEDQHLI
     VKALNEFDSK APGSGGALDW RSKLWSQRGA VVATEMKNNS IKLARWTTQA ILAKADAMKL
     GFVSRANPRS ATSHVILGVV GYKPREFAAQ MNLNLGNGWG IVRTIVDRIR ALDAEEEEDK
     VKKYVLIKDP NRPVIRLYSV PPNTFEEDDE AAEEQEEKAE DESEE
 
 
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