ID   EIF3D_NEMVE             Reviewed;         563 AA.
AC   A7SMR1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
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};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 7 {ECO:0000255|HAMAP-Rule:MF_03003};
GN   ORFNames=v1g235689;
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6;
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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; DS469711; EDO35013.1; -; Genomic_DNA.
DR   RefSeq; XP_001627113.1; XM_001627063.1.
DR   AlphaFoldDB; A7SMR1; -.
DR   SMR; A7SMR1; -.
DR   STRING; 45351.EDO35013; -.
DR   EnsemblMetazoa; EDO35013; EDO35013; NEMVEDRAFT_v1g235689.
DR   GeneID; 5506418; -.
DR   KEGG; nve:5506418; -.
DR   eggNOG; KOG2479; Eukaryota.
DR   HOGENOM; CLU_024521_2_0_1; -.
DR   InParanoid; A7SMR1; -.
DR   OMA; PDGWGPC; -.
DR   OrthoDB; 1030308at2759; -.
DR   PhylomeDB; A7SMR1; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
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: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..563
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D"
FT                   /id="PRO_0000364166"
FT   REGION          95..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..308
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
FT   REGION          528..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..563
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  64192 MW;  CB0CAFC844F76A74 CRC64;
     MAGKAKFCAP EIQDNPDGWG PCSVPTAFKD IPYQPFSKAD RLGKVSDWTG SVYQDRRYAN
     KYQSQFGTGN QMFSYYHEED ETSFQLVDTS RTQRPGYMRN RNRFNQRGGY RRDNRGGRFQ
     GQGGNMGMQN LSRGRDTRNK FQRKMQRNWG GGRHWSDKKT GGMHKRVASV TVREEWKVLE
     DGELDFPRLS KLNLPNVEEP ETLYECGSVE YYDKAYDRVT TKNEVPLVGV NRVFHKVTTT
     DDPIISKLLS QGNVFATDAI ISTLMTCTRS NYSWDIVVQR VGSKLFFDKR DDSEFDLLTV
     GETANDLNID ETSGINTPTN LSLEATFINQ NFSQQVLKRG EVKTFDHPNP FVTDEDDSTV
     ASVCYRYRKW DLGDGIQLIV RCEHDAIMQG PRGETCLVNI KTLNEWDPKM TGVDWRQKLD
     SQRGAVLATE LKNNSCKLAK WTANSILAGS EYLKLGYVSR VNFLDTSKHT ILGTQQFRPR
     EFATQIALNM DNAWGVLRCI IDICMKQPEG KLLILKDPSK GVIRIYDIPN STFETDEEDD
     DDDEDDVEND DGDDEKDEGD GED