EIF3D_BOMMO
ID EIF3D_BOMMO Reviewed; 549 AA.
AC Q0ZB77;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 51.
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 Name=eIF3-S7 {ECO:0000255|HAMAP-Rule:MF_03003};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang L.-L., Chen K.-P., Yao Q., Hu Z.-G., Chen H.-Q.;
RT "Translation initiation factors in Bombyx mori.";
RL Submitted (MAY-2006) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ645459; ABG54287.1; -; mRNA.
DR RefSeq; NP_001037656.1; NM_001044191.1.
DR AlphaFoldDB; Q0ZB77; -.
DR SMR; Q0ZB77; -.
DR STRING; 7091.BGIBMGA005592-TA; -.
DR GeneID; 733085; -.
DR KEGG; bmor:733085; -.
DR CTD; 733085; -.
DR eggNOG; KOG2479; Eukaryota.
DR HOGENOM; CLU_024521_2_0_1; -.
DR InParanoid; Q0ZB77; -.
DR OrthoDB; 1030308at2759; -.
DR Proteomes; UP000005204; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0098808; F:mRNA cap binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
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 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 2: Evidence at transcript level;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW RNA-binding.
FT CHAIN 1..549
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D"
FT /id="PRO_0000364140"
FT REGION 101..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..291
FT /note="RNA gate"
FT /evidence="ECO:0000250|UniProtKB:K7IM66"
FT REGION 521..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 62432 MW; 5B6DBBA0DDF2238A CRC64;
MSEHVLPAEG PMRFISPIIQ DNPTGWGPYE MPDQFRDMPY QPFSKGDRLG KISDWTMVQD
KKYQNKYASQ FGAGSSYAYF HDEDESTFHL VDTTRVQKPY QSYQRGRARG QRGRGARGAR
TPGGMTTLNK PRERKLGKRW GQRGAPMKIR DASVTVRPTW VTIEDMDFPR LAKLSLPGIK
EGEDIVSCGT LEYYDKAYDR VNVKHEKPLQ RIDRIFHTVT TTDDPVIRRL SKTAGTVYAT
DAILATIMCC TRSNYSWDIV IEKIGDKLFL HKRDNTEFDL LTVNETSVEP PADDGNSINS
PRNLALEATF INHNFSQQVL KSGPTEPKYK FQEPNPFVSE QEDGEVASVG YRYRKWILNN
GVVLIARCEH DAVMQGPQGE TQFLTIKALN EWDSKLANGV EWRQKLDTQR GAVLANELRN
NSCKLAKWTV QALLAGSDQI KFGYVSRAQV RDNSRHVILG TQQFKPHEFA AQINLSMDNA
WGILRCIIDI CMKQKDGKYL IMKDPNKPLI RLYDIPDNTF ESDASEESGD EQADTPFAPL
YSYGNSKRV