EIF3A_ASHGO
ID EIF3A_ASHGO Reviewed; 921 AA.
AC Q75DT8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 110 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Translation initiation factor eIF3, p110 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
GN Name=TIF32 {ECO:0000255|HAMAP-Rule:MF_03000}; OrderedLocusNames=ABL065W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: RNA-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.
CC {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
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; AE016815; AAS50706.1; -; Genomic_DNA.
DR RefSeq; NP_982882.1; NM_208235.2.
DR AlphaFoldDB; Q75DT8; -.
DR SMR; Q75DT8; -.
DR STRING; 33169.AAS50706; -.
DR PRIDE; Q75DT8; -.
DR EnsemblFungi; AAS50706; AAS50706; AGOS_ABL065W.
DR GeneID; 4618963; -.
DR KEGG; ago:AGOS_ABL065W; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; Q75DT8; -.
DR OMA; VMYQTTA; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0010494; C:cytoplasmic stress granule; 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; IBA:GO_Central.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR Pfam; PF01399; PCI; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..921
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366349"
FT DOMAIN 319..493
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 497..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 562..647
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 693..868
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 505..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 105926 MW; 90BFF60797F62103 CRC64;
MAPPVLRPEN ALKRADELIS VGEPQAALQS LLDYITSRRI RFADPAAIEP IVFKFLELGV
ELKRGKVIKD GLYQYRKHVQ SSTEGLKSVG AVSRRFIDLI EKKMSSEQAK ANAEESTEED
LEGGVTPENL LISVYEQDQS VGGFNDEAVT SWLRFTWESY RTVLDLLRNN SQLEITYSGV
VNRAMQFCLK YNRKNEFKRL ADMLRQHLDA ANYQQQKSKQ YTVDLSDPDT LQRYLDQRIL
QVNVSVKLGL WHEAFRSIED VHHLLSMSTR DPKPSVLANY YQNMAKVFFV SSNYLLNSVA
LQKFYDLYQQ NPKATDEDFK FYASQLVLSA LSIQQDDLPV VGYDPLARLA GFLNLESKPT
RSQVIEAVSD SKIFSRADEP VKKLYELLNS DFDVNTLKES LASLLPELNS KSYFTQYVEP
LKSFTIRKAF ISASKQFGSI KLDELFEHTS LPSPFDLSPL DLEKSLLQAA MNDYVSFSID
HDAGVVSFME DPFELLGGST ATNADDEQRN DDGYEETHVE EEPEPILTRN SAVRTQLIEL
AKALKETEGF PHASYVDKVR MARNELIRQN NAIIASEKEA AEERARQLEY EKQSASGVPL
TAEQVVEERQ RRMKEEKEAA EARMEAEARR RAEEKREREL AAINEKTMLK MIEDINAKGL
IFIDPKEAKN MTLEKFKKLT VELVSKDKKD LDERMSHAFK RVDHIERAYR KLEAPLWEKD
AQKQKERDLE SYNKLKQMMV EKAKKDHEEN LRIHDRLVKI YPSYLHFREK VIAAQKSQIE
ALRAENAAKL EAAKNARLQE VRQQRYNELI ARRKEELAAK EHDDRQRMLQ DRLTKERKER
ERVNKEKDEA ARKQREIEEA VERTIKRNVS ATPAPPVRSA PPARAAPPPR ASNEQVASPA
PQPEKKLTYA EKMKLRRAGR A
