EIF3D_BOTFB
ID EIF3D_BOTFB Reviewed; 576 AA.
AC A6SJW6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 60.
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=BC1G_12797;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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 -!- SEQUENCE CAUTION:
CC Sequence=EDN18951.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476951; EDN18951.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001548500.1; XM_001548450.1.
DR AlphaFoldDB; A6SJW6; -.
DR SMR; A6SJW6; -.
DR World-2DPAGE; 0005:A6SJW6; -.
DR PRIDE; A6SJW6; -.
DR VEuPathDB; FungiDB:Bcin15g04490; -.
DR OrthoDB; 1030308at2759; -.
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: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; 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 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; RNA-binding.
FT CHAIN 1..576
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D"
FT /id="PRO_0000366887"
FT REGION 103..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..318
FT /note="RNA gate"
FT /evidence="ECO:0000250|UniProtKB:K7IM66"
FT COMPBIAS 161..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 63969 MW; 131D6CF4D12E25E9 CRC64;
MAPISLSDII SALPSEDSWG PSTTSETTLN GVPYAPYSKG DKLGRMADWT AEGKDGRDGR
GGRQQYNRNY RDQQVYGAGT SSLFAVQLAE DESTFSVVSN TRDSTKTRFG RGGLARGRGQ
RGGRGDTRGG RGQFQRVGGR GGQQGYNSYD TRGGRGGARG GRKFGWKDYD KPQRNRDASV
NIKPDWKMLE EIDFNRLAKL NLDTDDGEDI DSYGFLYYYD RSFDKQPVKA AERKLNVVDR
ASYNVTTSSD PVIQELAEKD EATIFATDSI LSMLMCSPRS VYPWDIVIVR QGNKVFLDKR
DNATLDMVTV NENAADAPMD ASEGSKDAIN QPSALAEEAT YINHNFANQV MKESDSQKVE
MENENPFYNS AEETDPPASK AYKYRKFDLS LNDEDPVHLV VRTELDAVSK NAISGEDQFL
TVKALNEFDS KAQGSGGALD WRTKLVSQRG AVVATEMKNN SCKLARWTVQ SIIAKADVMK
LGFVSRANPK LNDRHVVLGV IGWKPRDFAS QMNLSLSNGW GIVRTIVDMC LKREEGKYVL
VKDPNKPILR LYQVPAGSFE DDGEHDVIEE NVEEDD
