EIF3D_CHAGB
ID EIF3D_CHAGB Reviewed; 584 AA.
AC Q2H5T8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 53.
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=CHGG_05977;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408031; EAQ89358.1; -; Genomic_DNA.
DR RefSeq; XP_001222072.1; XM_001222071.1.
DR AlphaFoldDB; Q2H5T8; -.
DR SMR; Q2H5T8; -.
DR STRING; 38033.XP_001222072.1; -.
DR EnsemblFungi; EAQ89358; EAQ89358; CHGG_05977.
DR GeneID; 4391386; -.
DR eggNOG; KOG2479; Eukaryota.
DR HOGENOM; CLU_024521_2_0_1; -.
DR InParanoid; Q2H5T8; -.
DR OMA; PDGWGPC; -.
DR OrthoDB; 1030308at2759; -.
DR Proteomes; UP000001056; 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 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW RNA-binding.
FT CHAIN 1..584
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D"
FT /id="PRO_0000364172"
FT REGION 118..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..326
FT /note="RNA gate"
FT /evidence="ECO:0000250|UniProtKB:K7IM66"
FT REGION 563..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..584
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 64534 MW; E823F4EB43B38C58 CRC64;
MAEYTAGTSP LVDLINSLPD SDGTWGPPIT NETTLNGVPY APFSKSDKLG RMADWTDAKD
GRDGRGRQQY NRNYRDQQVY GAGSASLFAP PAAEDEASFS VVSNVRDTGK TRFGRGAIFT
RGRGQRGRGG QDTRGGGRQQ FQRGGRGGQQ YGGGGYSDRG GGRGGGARGR RFGWKDYDKP
QRNRDASVNI RPDWKLLEEI DYNRLSKLNL DTDEGEDVDS YGFLYYYDRS YDKPPVKSAE
RKLAVVDRAV YNVTTSSDPI IQELAEKDEA TIFATDSILS MLMCAPRSMY PWDIIIVRQG
NKVFLDKRDN AALDMVTVNE NAADAPLEAS EGSKDVINQP GALAEEATYI NHNFVNQVVL
ESSNQKVDMA NENPFHSASE ETEPPASKAY KYRRFDLSTS EETPTYLVVR TELDAVQKNP
TSGEDQFVTV HALNEFDSKA QGSGGALDWR TKLVSQRGAV VATEMKNNSC KLARWTVQSI
LAKADVMKLG FVSRVTPKAN DKHVILGCVG WKPKDFANQM NLQLSNGWGI VRTIADMCLQ
REEGKYVLVK DPNKNILRLY EVPANGLDDD DEGPEPEGVA EEED
